diff --git a/api_routes/routes.js b/api_routes/routes.js index 5e96ed56..4e8f55c3 100644 --- a/api_routes/routes.js +++ b/api_routes/routes.js @@ -1,3 +1,6 @@ +const fs = require('fs'); +const path = require('path'); + const router = require('express').Router(); const axios = require('axios'); @@ -6,12 +9,23 @@ const { handleAxiosError } = require('./utils'); const services = require('./services'); const external_apis = require('./external'); +const samples = JSON.parse(fs.readFileSync(path.join(__dirname, './sample-query-cache.json'))); + router.use('/', external_apis); router.use('/robokache', robokache.router); router.route('/quick_answer') .post(async (req, res) => { + // if this is a sample query, load the response from the cache JSON: + for (let i = 0; i < samples.length; i += 1) { + const { query, response } = samples[i]; + if (JSON.stringify(req.body) === JSON.stringify(query)) { + res.send(response); + return; + } + } + const { ara } = req.query; const ara_url = services[ara]; const config = { @@ -37,12 +51,11 @@ router.route('/quick_answer') }); } } catch (err) { - //res.send(handleAxiosError(err)); - res.send({ - status: 'error', - message: `Error from ${ara_url}`, - }); - } + res.send({ + status: 'error', + message: `Error from ${ara_url}`, + }); + } }); router.route('/answer') diff --git a/api_routes/sample-query-cache.json b/api_routes/sample-query-cache.json new file mode 100644 index 00000000..7559b478 --- /dev/null +++ b/api_routes/sample-query-cache.json @@ -0,0 +1,7677 @@ +[ + { + "name": "Chemicals that might ameliorate Huntington's Disease", + "query": { + "message": { + "query_graph": { + "nodes": { + "n0": { + "categories": ["biolink:ChemicalEntity"], + "name": "Chemical Entity" + }, + "n1": { + "name": "Huntington disease", + "categories": ["biolink:Disease"], + "ids": ["MONDO:0007739"] + } + }, + "edges": { + "e0": { + "subject": "n0", + "object": "n1", + "predicates": ["biolink:ameliorates"] + } + } + } + } + }, + "response": 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In vitro and in vivo recordings of epileptiform activity from the hippocampus have shown that levetiracetam inhibits burst firing without affecting normal neuronal excitability, suggesting that levetiracetam may selectively prevent hypersynchronization of epileptiform burst firing and propagation of seizure activity. Levetiracetam at concentrations of up to 10 uM did not demonstrate binding affinity for a variety of known receptors, such as those associated with benzodiazepines, GABA (gamma-aminobutyric acid), glycine, NMDA (N-methyl-D-aspartate), re-uptake sites, and second messenger systems. Furthermore, in vitro studies have failed to find an effect of levetiracetam on neuronal voltage-gated sodium or T-type calcium currents and levetiracetam does not appear to directly facilitate GABAergic neurotransmission. 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with intramuscular zuclopenthixol and medroxyprogesterone acetate in the treatment of agitation and aggression in Huntington's disease.|PMID:24026736|Experience with intramuscular zuclopenthixol and medroxyprogesterone acetate in the treatment of agitation and aggression in Huntington's disease|PMC6618900|Experience with intramuscular zuclopenthixol and medroxyprogesterone acetate in the treatment of agitation and aggression in Huntington?s disease |PMC7489774|Use of zuclopenthixol in the treatment of aggression in Huntington's disease.|PMID:28483083|Use of zuclopenthixol in the treatment of aggression in Huntington's 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an in vivo rat quinolinic acid model of Huntington's disease, simvastatin (2.4 ?mol/kg i.p./day, 2 or 8 weeks) was neuroprotective.|PMC3779518|Effects of simvastatin on neuroprotection and modulation of Bcl-2 and BAX in the rat quinolinic acid model of Huntington?s disease |PMC4492422|Effects of simvastatin on neuroprotection and modulation of Bcl-2 and BAX in the rat quinolinic acid model of Huntington's disease|PMC3779518|Effects of simvastatin on neuroprotection and modulation of Bcl-2 and BAX in the rat quinolinic acid model of Huntington's disease.|PMID:18938217","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"28530496":{"subject":"PUBCHEM.COMPOUND:10836","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"MTM has been shown to prolong the survival of Huntington's disease model mice and to attenuate dopaminergic neurotoxicity in mice after repeated administration of 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reduces soluble mutant huntingtin and protects striatal neurons through dopamine D3 receptors in a genetic model of Huntington's disease.|PMID:29056363|Pramipexole reduces soluble mutant huntingtin and protects striatal neurons through dopamine D3 receptors in a genetic model of Huntington?s disease |PMC7584015|Pramipexole ameliorates neurologic and psychiatric symptoms in a Westphal variant of Huntington?s disease |PMC2951749|Pramipexole ameliorates neurologic and psychiatric symptoms in a Westphal variant of Huntington's 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expression of mutant huntingtin protein alters mitochondrial and cell viability through mPTP opening in striatal cells and cortical neurons (Quintanilla, Jin, von Bernhardi, & Johnson, 2013) and CsA showed protecting effects in a Huntington's disease mouse model (Kumar & Kumar, 2009).|PMC6052406|Cyclosporine-A (CsA) is neuroprotective in animal models of Parkinson's disease (PD), Huntington's disease and stroke.|PMID:12445688|Cyclosporine-A (CsA) is neuroprotective in animal models of Parkinson's disease (PD), Huntington's disease and stroke.|PMID:12445688|The current study was conducted to explore the therapeutic potential of cyclosporine A against 3-nitropropionic acid (3-NP)-induced neurotoxicity, an animal model of Huntington disease (HD).|PMID:20448265|The patient with Huntington?s disease received an immunosuppressive therapy with cyclosporine A (CsA) for 12?months after the surgery to avoid graft rejection.|PMC3204002","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"40434983":{"subject":"PUBCHEM.COMPOUND:11125","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:1822806423e460a800f52c470be52de9bf1619c26372288e59dcdb96aff8efcd"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Lithium carbonate has been reported to have beneficial effects in different models of Huntington?s disease (HD) and 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a semisynthetic second-generation tetracycline, was reported to have neuroprotective effects in models of global and focal cerebral ischemia, the R6/2 mouse model of Huntington disease, as well as glutamate-induced neurotoxicity in mixed neuronal/glial cultures.|PMID:11711215|In addition, several studies have reported that minocycline, a tetracycline analog, has neuroprotective and anti-apoptotic effects in several neurodegenerative disorders including Huntington?s disease, amyotrophic lateral sclerosis and multiple sclerosis.|PMC2785448|Tetracycline (enrichment score = 0.673 and p-value = 9.75 ? 10?3) is reportedly one of the antibiotics that could act as neuroprotective molecules in neurological diseases such as Huntington?s disease, Parkinson?s disease, stroke, and multiple sclerosis.|PMC8004271|Minocycline, a semisynthetic derivative of tetracycline, displays beneficial activity in neuroprotective in models including, Parkinson disease, spinal cord injury, amyotrophic lateral sclerosis, Huntington disease and stroke.|PMID:15964487|Minocycline and other tetracycline derivatives: a neuroprotective strategy in Parkinson's disease and Huntington's 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inhibitors, such as suberoylanilide hydroxamic acid (SAHA) [14], sodium butyrate (SB) [15] and trichostatin (TSA) [16], have been demonstrated to be effective in upregulating histone acetylation and in ameliorating motor impairments in mouse models of Huntington's disease (HD), spinal and bulbar muscular atrophy (SBMA) and dentatorubral-pallidoluysian atrophy (DRPLA).|PMC3557284|In previous studies, HDAC inhibitors (HDACi) such as sodium butyrate or trichostatin A (TSA) were reported to rescue memory deficits in both aged and gene-mutant mice by elevating the level of hippocampal histone acetylation, and these compounds also showed therapeutic potential for depression and some neurodegenerative disorders such as Huntington?s disease (HD), Parkinson's disease (PD), and Alzheimer?s disease (AD).|PMC4415954|The HDAC inhibitors trichostatin-A (TSA) and sodium butyrate (NaB) have been shown to increase contextual fear conditioning and extinction, and both NaB and SAHA, another HDAC 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30 signaling pathways were upregulated by cyclophosphamide treatment, including seven metabolic pathways (e.g., glycolysis/gluconeogenesis, the pentose phosphate pathway, starch and sucrose metabolism, and oxidative phosphorylation), seven human disease pathways (e.g., Parkinson?s disease, Huntington?s disease, and Alzheimer?s disease), four cell growth and death pathways (e.g., the cell cycle and p53 signaling pathway), four replication and repair pathways (e.g., DNA replication and homologous recombination), and other critical pathways (e.g., the cell cycle and DNA replication) ( Supplementary Table?1 ).|PMC8239396","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"38093011":{"subject":"CHEMBL.COMPOUND:CHEMBL569713","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Acute effects of scopolamine in Huntington's 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groups have reported similar benefits of geldanamycin in fly and mouse models of Huntington's disease, supporting the benefits of this compound in protein misfolding disorders.|PMC3921213|Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease.|PMC3359295|Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease.|PMC2622762|Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease.|PMC2807466|Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's 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several studies have found that berberine is a potential neuroprotector for several neurodegenerative pathogenesis, including Parkinson?s disease, Huntington?s diseases and Alzheimer?s disease (AD) through ameliorating the ?-amyloids deposition, or enhancing the degradation of mutant huntingtin by autophagic pathway.|PMC5073438|This review attempts to summarize the current state of knowledge regarding the therapeutic potential of berberine against neurodegenerative diseases, with a focus on the molecular mechanisms that underlie its effects on Alzheimer's, Parkinson's and Huntington's diseases.|PMID:29676231|The therapeutic potential of Berberine in different neurodegenerative diseases such as Alzheimer, Parkinson and Huntington disease has been brought to evidence by numerous studies.|PMID:26398393|The therapeutic activity of berberine has been widely examined in various neurological conditions including cerebral ischemic injury, AD, Parkinson?s disease, depression, anxiety, Huntington?s disease, epilepsy and convulsions.|PMC6533761","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"18256062":{"subject":"PUBCHEM.COMPOUND:5983","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Intravenous physostigmine improved the involuntary movements of all of four patients with tardive dyskinesia and three of six patients with Huntington's disease.|PMID:146524|In order to assess whether this test is also sensitive to drugs influencing the symptoms of Huntington's disease, the effect of the dopamine antagonists haloperidol and pimozide, the acetylcholinesterase inhibitor physostigmine and the anticholinergics atropine and dexetimide were investigated as well.|PMID:2978064|The hypotheses of relative cholinergic underactivity in Huntington's disease, 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further investigations on the role of brain vasculature and hemostatic factors, e.g., thrombin, fibrin(ogen), contributing to neurodegeneration in other amyloidosis, such as Parkinson?s disease, Huntington?s disease, and amyotrophic lateral sclerosis, might lead to the hypothesis that DOACs, such as dabigatran, could be helpful also in treating vascular dysfunction in these neurodegenerative diseases.|PMC8125318","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"78358629":{"subject":"PUBCHEM.COMPOUND:6518","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:0b12bb94bbfe28a0ef9cd57a48307119a7269b43c4d1ac1bb234a605e165e049"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9941658","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Ten patients with Huntington's disease took Ch orally (8 to 20 gm per day) after the extent of their disabilities had been documented by clinical examination, movies, and combined electromyogram-accelerometer recordings.|PMID:152596","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:152596"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"99147498":{"subject":"PUBCHEM.COMPOUND:121492004","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7032046","PMC7373156"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In contrast, Ionis Pharmaceuticals, the company that developed inotersen, has several products in different stages of development for proteinopathies, including Huntington?s disease (targeting huntingtin), ALS (targeting SOD1 or C9ORF72), and Alzheimer?s disease and frontotemporal dementia (targeting tau).|PMC7032046|Investigational ASOs for Huntington?s disease (HD), amyotrophic lateral sclerosis (ALS) and transthyretin (TTR) amyloidosis, such as RG6042, tofersen and inotersen, respectively, are currently in phase III clinical 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study evaluated and compared the potential protective effects of probucol and succinobucol, two lipid-lowering compounds with anti-inflammatory and antioxidant properties, on oxidative stress and mitochondrial dysfunction induced by 3-nitropropionic acid (3-NP, a succinate dehydrogenase (SDH) inhibitor largely used as model of Huntington's disease) in rat brain mitochondria-enriched 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compound ranked highest on average was tanespimycin, an HSP-90 inhibitor, shown to acts as a senolytic agent by killing human senescent cells without affecting the viability of healthy cells and to ameliorate disease phenotypes in Drosophila models of Huntington?s disease and spinocerebellar ataxia.|PMC6342327|Likewise, 17-AAG suppressed neurodegeneration in an HSF-1-dependent manner in a Drosophila model of Huntington?s disease and in a mouse model of spino bulbar muscular atrophy caused by expression of the androgen receptor (mAR) with a polyQ-expansion.|PMC3955168|17-AAG has also been found to be neuroprotective in preclinical studies of Huntington?s disease and SCAs.|PMC3364514|17-AAG is also neuroprotective in preclinical studies of Huntington?s disease and spinocerebellar ataxia.|PMC3364517|17-AAG is currently in phase II trials as an antitumor compound, showing neuroprotective effects in preclinical models of Huntington's disease and spinocerebellar 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(Dimebon; dimebolin) is a neuroactive compound that was associated with enhanced cognition, neuroprotection and neurogenesis in laboratory animals, and has entered phase II clinical trials for both Alzheimer's disease and Huntington's disease (HD).|PMID:22869031|Together with the demonstration of neuroprotective effects in Alzheimer's disease (AD) and Huntington's disease models, these observations supported the potential of dimebon as a treatment for AD - although the plausibility of dimebon's mechanism of action has been queried.|PMC2983434|This mechanism seems to underlie the protective properties of the Alzheimer's and Huntington's disease drug Laterpirdine/Dimebon, which can also activate AMPK, promote GLUT3 translocation and protect neurons from glutamate excitotoxicity (Weisova et?al.|PMC4855681|Observations from our study and others suggesting dimebon might improve cognition in wild type mice and rats raises the possibility that dimebon might be able to benefit cognitive function in patients with other neurodegenerative disorders, such as Huntington's disease, or in the aging population.|PMC3035024|Observations from our study and others suggesting dimebon might improve cognition in wild type mice and rats raises the possibility that dimebon might be able to benefit cognitive function in patients with other neurodegenerative disorders, such as Huntington's disease, or in the aging 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effects of probenecid in a transgenic animal model of Huntington's disease.|PMID:19551467|Neuroprotective effects of probenecid in a transgenic animal model of Huntington?s disease |PMC7423862|Neuroprotective effects of probenecid in a transgenic animal model of Huntington?s disease |PMC3706206|Neuroprotective effects of probenecid in a transgenic animal model of Huntington?s disease |PMC3922661|Neuroprotective effects of probenecid in a transgenic animal model of Huntington?s disease 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one of the alkaloids of the Rauwolfia species, had been used for the management of hypertension, schizophrenia and psychiatric disorders and even thought to be beneficial in cases of Huntington disease.|PMC3336935|Insofar as reserpine has been used with some clinical efficacy in hyperkinetic movement disorders such as Huntington's disease and tardive dyskinesia, it may be that potentiation of reserpine's hypokinetic effect by a drug such as THC could greatly increase the clinical value of reserpine or related drugs in the treatment of these disorders.|PMID:6273940|Insofar as reserpine has been used with some clinical efficacy in hyperkinetic movement disorders such as Huntington's disease and tardive dyskinesia, it may be that potentiation of reserpine's hypokinetic effect by a drug such as THC could greatly increase the clinical value of reserpine or related drugs in the treatment of these disorders.|PMID:6273940|[Haloperidol, reserpine, l-dopa and amantidine in the treatment of Huntington chorea (author's transl)]|PMC5975251|[Haloperidol, reserpine, l-dopa and amantidine in the treatment of Huntington chorea (author's transl)].|PMID:134449","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"113572128":{"subject":"UMLS:C0525094","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"For example, Ginkgo biloba extract EGb 761 has been reported to increase proteasome activity and enhance degradation of aggregated protein in a Huntington's disease (HD) cellular model.|PMC6800904|Various studies have reported that ginseng and ginkgo protect against injury in numerous neurological diseases, including Parkinson?s disease, Alzheimer?s disease and Huntington?s 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trials are underway using green tea extract or EGCg in diseases other than DMD (Alzheimer?s disease, Huntington?s disease, multiple sclerosis, HIV, small cell carcinoma; http://www.Clinicaltrials.gov).|PMC3486431|It was previously demonstrated that (-)-epigallocatechin-3-gallate, one of the major polyphenols present in green tea, has a suppressing effect on various aspects of pathogenesis in models of Huntington's disease (HD), an inherited neurodegenerative disorder.|PMID:29973113","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"38139521":{"subject":"UMLS:C2740799","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3349345","PMC4140724","PMID:22031240","PMC6549163","PMID:31165723"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0d5bc56bfeac71409702adbdd4efbd5649d30df28b11fd424e8fe61fb7fdba37","tmkp:d9e43bf4cf4aa9d977cfbf186ae56aacbb2047a056850fec6ccaada6c4ee3297","tmkp:c41727c3784ac48323ac06a5d1e1f63a9b08193860e8be72bc2844929fa9618e","tmkp:7b6a905a75b3bf30ac5f83338aac020cc035e70ba655a97f65905e71822a0dac","tmkp:bc0c67004c02984ce69387fe5bc11edadf782fae97db00db7895fcd1d20d96ce"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.994993135","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"For example, they are among the most effective therapeutic compounds tested to date in animal models of Huntington's disease as well as in stroke.|PMC3349345|To date its efficacy has been proved in several pre-clinical rodent trials for diseases such as Huntington's disease (HD), familial forms of amyotrophic lateral sclerosis (ALS) and spinocerebellar ataxia type 1 (SCA1) as well as in familial forms of Alzheimer disease (AD).|PMC4140724|To date, a therapy for Huntington's disease (HD), a genetic, neurodegenerative disorder, remains elusive.|PMID:22031240|Huntington disease is a neurodegenerative condition for which there is no cure to date.|PMC6549163|Huntington disease is a neurodegenerative condition for which there is no cure to date.|PMID:31165723","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"103129650":{"subject":"PUBCHEM.COMPOUND:5314","object":"MONDO:0016621","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:10632921"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a38a90efdacb13b2b704dd906936619ce3191f657a3f48f20dab2f7ca9920e0b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"We describe the management of a 12-year-old girl with JHD scheduled for gastroscopy under general anaesthesia necessitating the use of suxamethonium.|PMID:10632921","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99824035","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"106442422":{"subject":"PUBCHEM.COMPOUND:27400","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6785943","PMC5606996","PMC6976599","PMC3856079","PMC6628568"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995065000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Pizotifen activates ERK and provides neuroprotection in vitro and in vivo in models of Huntington's disease|PMC6785943|Pizotifen activates ERK and provides neuroprotection in vitro and in vivo in models of Huntington?s disease |PMC5606996|Pizotifen activates ERK and provides neuroprotection in vitro and in vivo in models of Huntington?s disease |PMC6976599|Pizotifen activates ERK and provides neuroprotection in vitro and in vivo in models of Huntington?s disease |PMC3856079|Pizotifen activates ERK and provides neuroprotection in vitro and in vivo in models of Huntington?s disease 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importantly, previous studies by our group and others have demonstrated that Fasudil exhibited protective effect in models of Parkinson's disease (PD),4 amyotrophic lateral sclerosis (ALS),4 Alzheimer's disease (AD),5, 6 Huntington disease,7 and spinal muscular atrophy (SMA).8|PMC6930827|Furthermore, significant therapeutic effects were also observed in a mouse model of Huntington's disease, both with Y-27632 and Fasudil treatment (Li et al.,), and in a model of spinal muscle atrophy, a condition with high similarity to ALS.|PMC5281550|In a previous study, fasudil hydrochloride (fasudil), a potent ROCK inhibitor, was found to improve the pathology in brain ischemia, Alzheimer?s disease, Parkinson?s disease, and Huntington?s disease, as well as brain neurotrauma.|PMC4951004|In a previous study, fasudil hydrochloride (fasudil), a potent ROCK inhibitor, was found to improve the pathology in brain ischemia, Alzheimer?s disease, Parkinson?s disease, and Huntington?s disease, as well as brain neurotrauma.|PMC4951004","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:76b67f94f0861515aeac2f85effee3dbde673da72488f91dfb2fe9e793be125b","tmkp:a5cefe9dca13e31f2d9b9dc600fb33a31fbf95b1809b68a90a53de1aa283f89b","tmkp:cc68f42b02ed458650368042c976535c2f51f45d4ea8afa1ab986dfbf92212ce","tmkp:a73184d6870f69a379307d8808fe542985226dcb965f7799e4699bb8fc97553d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"59807835":{"subject":"PUBCHEM.COMPOUND:446925","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"In the CNS, lycopene also acts as a prophylactic and therapeutic agent in other disorders, such as Alzheimer's disease, Parkinson's disease, Huntington's disease, cerebral ischemia, epilepsy, and depression.|PMC8106523|The present study investigates synergistic effect of combination treatment of lycopene, quercetin and poloxamer188 in 3-nitropropionic acid (3-NP)-induced Huntington?s disease (HD).|PMC4576812|The present study investigates synergistic effect of combination treatment of lycopene, quercetin and poloxamer188 in 3-nitropropionic acid (3-NP)-induced Huntington's disease (HD).|PMID:26401371","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9804432666666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:791b4994c52d8b9341185ce70acbbd23e37bf027ac4f198f3079465162a60d71","tmkp:1af19c07441bbfbc00bbb830fec7a6c7b675aacb50028853896d9a4552310730","tmkp:fdc1256995bae94a309e4b5d1fd95f48798c41f7d31903e33ed48817ab20e548"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8106523","PMC4576812","PMID:26401371"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"43147130":{"subject":"PUBCHEM.COMPOUND:2771","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Results of the citalopram to enhance cognition in Huntington disease trial.|PMID:24375941|Results of the citalopram to enhance cognition in Huntington disease trial|PMC7337146|Results of the citalopram to enhance cognition in Huntington disease trial|PMC5671629|Results of the citalopram to enhance cognition in Huntington disease trial|PMC5597227|Results of the citalopram to enhance cognition in Huntington disease trial|PMC4353372","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:24375941","PMC7337146","PMC5671629","PMC5597227","PMC4353372"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c83027197f1d26dc80478d5766a321263ea7b4d93b5d8a0294196edfe5ac9f78","tmkp:158cdd9b1eb42c8fdcd2e1607c5995703f9a19ebcbad3df516d1e639801c275c","tmkp:78373d7fe9851cfc788177cb39dca17bfb050baf403ec3388fad47b9989c7b0e","tmkp:9273551d5f83a3b351347f6c3197b566e0d3214f37be725ca95a4405e5c7281b","tmkp:ac2119415423334b53f2df48ed046efdec5d49c1da63bd34e6aa06e5db9955bf"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999336449","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"84210353":{"subject":"PUBCHEM.COMPOUND:6324599","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7427508"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:346084f08a6842906a6f98a2179598691f41fdf6713d21d711e4979ea16451c3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Thus, based on the previous observations that the blood-brain barrier permeable and selective P2X7R antagonist, brilliant blue G (BBG), attenuated motor incoordination in a model of Huntington?s disease (D?az-Hern?ndez et al.,), we now evaluated if this P2X7R antagonist alleviates LID in a rat model.|PMC7427508","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99945325","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"87246169":{"subject":"PUBCHEM.COMPOUND:12035","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2916709","PMC5906610","PMC5906610","PMC4349202","PMID:25562842"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9962902692857143","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"NAC and vitamin E can inhibit autophagic flux and increase aggregation in a zebrafish model of Huntington's disease.|PMC2916709|Earlier we showed that the antioxidant N-acetylcysteine (NAC) relieves behavioral abnormalities associated with Huntington?s disease, and others observed similar beneficial effects of NAC in AT mice.|PMC5906610|Earlier we showed that the antioxidant N-acetylcysteine (NAC) relieves behavioral abnormalities associated with Huntington?s disease, and others observed similar beneficial effects of NAC in AT mice.|PMC5906610|This CSE model of Huntington?s disease is supported by the therapeutic effects of cysteine and N-acetylcysteine in mice with Huntington?s disease.|PMC4349202|In conclusion, NAC is able to delay the onset of motor deficits in the R6/1 model of Huntington's disease and it may do so by ameliorating mitochondrial dysfunction.|PMID:25562842","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a6670d7c632df886185974acfdc3c3e8c422e3d0dba9aed231dfe71f61020408","tmkp:026dc5c1e59787e42be9292d81e0c907c399191d935caf298f7e095d59c7a784","tmkp:cec126da8fc07ea92d7ba65436bb2e090fde49d20276f162b941e411af847246","tmkp:3fec3d27610c4f75a7fd6be485df6cdd0df0a4c8ccff014bb77d3ec9f5aeaa1e","tmkp:7f086cc7255eb97cc574ca03c3018f676247a46d24a5d662a04a48c72c16d3f3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"70390729":{"subject":"PUBCHEM.COMPOUND:4775","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5117222","PMC4204527","PMC3275566","PMC2684627","PMID:15494404"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9992533633653846","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:563a5c1c76df031d3c6110baaf93d0d586077b4145a0941806d078f846860f03","tmkp:71953d3832514b77ac0fb221a37a3bc5a4a452f174066dcc653ddf0bc97f9823","tmkp:846084b7bc2d6a435fd4be8640d2a637b0eb128604011c9642a1786d5c21cac6","tmkp:8a2b749de3816350f94d3012560bc2c208d6046e1ba98f94729bad5c8af2c543","tmkp:96ef62ca300d0b4674bc3705f26e2b1c9540c6a657b42ffac87e71574bcbe9a8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Such approaches have shown success in the laboratory for a variety of genetic diseases including ?1-anti-trypsin deficiency, cystic fibrosis, and Huntington's disease, using compounds such as 4-phenylbutyrate (4PBA), carbamazepine and celastrol.|PMC5117222|Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington?s disease.|PMC4204527|Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease.|PMC3275566|Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease.|PMC2684627|Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease.|PMID:15494404","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"111657441":{"subject":"PUBCHEM.COMPOUND:135398570","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Raising cGMP levels promotes the clearance of mutant proteins in zebrafish models of a tauopathy and Huntington?s disease.|PMC8224753|Because cGMP can also activate proteasomes and enhance protein degradation, we tested whether raising cGMP might also help clear these aggregation-prone proteins and thus reduce the resulting pathology in zebrafish models of tauopathies and Huntington?s 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of 5-hydroxy-L-tryptophan to individuals with Huntington's 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for Treatment of Chorea in Huntington Disease.|PMID:27380339|The newer agent, deutetrabenazine, an inhibitor of vesicular monoamine transporter type 2 (VMAT2) depletes presynaptic dopamine and is FDA approved for treatment in Huntington disease and tardive dyskinesia patients.|PMC7111125|Indirect tolerability comparison of Deutetrabenazine and Tetrabenazine for Huntington disease.|PMID:28265459|Deutetrabenazine: Treatment of hyperkinetic aspects of Huntington's disease, tardive dyskinesia and Tourette syndrome.|PMC6107994|Deutetrabenazine: Treatment of hyperkinetic aspects of Huntington's disease, tardive dyskinesia and Tourette syndrome.|PMID:28387387","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"65337315":{"subject":"PUBCHEM.COMPOUND:446284","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9991062433333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC2926984","PMC2926984","PMID:16777669","PMC2926984","PMID:26175332"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In a murine model of Huntington disease, supplementation with essential fatty acids such as eicosapentaenoic acid (EPA) is associated with improved motor manifestations.|PMC2926984|In a murine model of Huntington disease, supplementation with essential fatty acids such as eicosapentaenoic acid (EPA) is associated with improved motor manifestations.|PMC2926984|These techniques have been applied to the investigation of the effects on cerebral structure of intervention with fatty acids, particularly the long-chain polyunsaturated n-3 fatty acid eicosapentaenoic acid (EPA), in disorders such as schizophrenia, treatment-resistant depression, chronic fatigue syndrome (myalgic encephalomyelitis or ME), and Huntington's disease.|PMID:16777669|However, since Huntington disease is characterized by insulin resistance and hypertriglyceridemia is one characteristic of insulin resistance, a beneficial effect of EPA on triglycerides in Huntington disease may be a manifestation of this omega-3 fatty acid?s protective effects on the central nervous system.|PMC2926984|It has been suggested that treatment with ethyl-eicosapentaenoic acid (EPA) may improve motor function in patients with Huntington's disease (HD) with cytosine-adenine-guanine repeat numbers of <45.|PMID:26175332","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ec8844c4dd8330405703c0c79548ea04818f79ec0bebcf10350a8f6ca88380ad","tmkp:0b8d2d08c9384283ea8bebda4e74936d3eba4a6a5d84f40b5c0ae70747535a13","tmkp:4952c0029abb937eef818b7488aff85a79a752a3babdd546011be95604919d15","tmkp:9aa9c9489965f683a964a0d9eb94cead773a7066f3955c3686e0b6061fe4f5ff","tmkp:53b6816a28081d8f12e4212515ca2bd86d9dfc2eabf09cb9a83c672529d1d484"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"91801789":{"subject":"PUBCHEM.COMPOUND:71811910","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99951637","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In addition to dimethyl fumarate, Nrf2 activators such as curcumin, resveratrol, sulforaphane, masatinib, methylene blue, omaveloxolone, tideglusib, Dl-3-n-butylphthalide ide, ALKS-8700, benfotiamine, and ketogenic diet undergoing clinical trials for treating various neurodegenerative disease such as Alzheimer?s disease, Parkinson?s disease, Huntington?s disease, Friedreich?s ataxia, multiple sclerosis, amyotrophic lateral sclerosis, cataract, schizophrenia, bipolar disorder, mild cognitive impairment, depression, autism, obstructive sleep apnea, 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order to assess whether this test is also sensitive to drugs influencing the symptoms of Huntington's disease, the effect of the dopamine antagonists haloperidol and pimozide, the acetylcholinesterase inhibitor physostigmine and the anticholinergics atropine and dexetimide were investigated as 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objective was to investigate the effect of a high-dose vitamin D3 supplementation on a transgenic mouse model of Huntington's disease.|PMID:27685770","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994579","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"15111421":{"subject":"PUBCHEM.COMPOUND:2585","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"These results also provided evidence supporting the hypothesis that carvedilol and melatonin can be useful for treating neurodegenerative diseases, such as Huntington's 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particular, Nec?1 is reported to have neuroprotective effects in several brain disease models by reducing tissue damage in brain injury, alleviating functional deficits in Huntington's disease and inhibiting neural cell degeneration induced by aluminium (Zhu et?al, 2011; Wang et?al, 2012; Qinli et?al, 2013; Su et?al, 2015).|PMC5210088","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5210088"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9995384","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:35246624adf1de476c4516e874a3ff270a5923f8051f4385c60b58ba7cc0da95"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"82203620":{"subject":"PUBCHEM.COMPOUND:43815","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:519c66088e129a00509e6f1e13833ddd7e8b1637c778979948b5bf381fa4bc57"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:15048901"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"We report that administration of paroxetine, a widely prescribed antidepressant drug that acts by inhibiting reuptake of the neurotransmitter serotonin, suppresses the neurodegenerative process and increases the survival of huntingtin mutant mice, an animal model of Huntington's disease (HD).|PMID:15048901","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994711","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"71290406":{"subject":"PUBCHEM.COMPOUND:23925","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"In vivo assessment of iron in Huntington?s disease and other age-related degenerative brain diseases |PMC2955824|Fer-1?s ability to mitigate the deleterious events associated with ferroptosis has previously been demonstrated in various cellular models, including Huntington?s disease, and likely accounts for improved islet viability.|PMC5964226|In 2014, Skouta et al. found that Fer-1 inhibited cell death in three in vitro models of Huntington?s disease (HD), periventricular white matter (PVL), and renal insufficiency.|PMC6997353|We found that Fer-1 inhibited cell death in cellular models of Huntington's disease (HD), periventricular leukomalacia (PVL), and kidney dysfunction; Fer-1 inhibited lipid peroxidation, but not mitochondrial reactive oxygen species formation or lysosomal membrane permeability.|PMID:24592866|We found that Fer-1 inhibited cell death in cellular models of Huntington?s disease (HD), periventricular leukomalacia (PVL), and kidney dysfunction; Fer-1 inhibited lipid peroxidation, but not mitochondrial reactive oxygen species formation or lysosomal membrane permeability.|PMC3985476","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9916724736","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f2fbd874d864521c0c348657f74cf8cd4ec6f278f7cecfa9293d7229815284c3","tmkp:de41c277917c013962c736ab17eb9cb87bcdbaf7ffce48d0d1fcd0e7998e3d52","tmkp:05beac38cf7f38fa9e30ff8c8973befc06daadc9ece15284115f1874a1b80f4c","tmkp:2fce2d128549773867bba19b0ed263a07c0413baa90fe7db03ac2013d87b5a53","tmkp:d5146bb340cf8046a2365b83e80dd85f60d709d9640c50e1be9da1f2497a1d13"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2955824","PMC5964226","PMC6997353","PMID:24592866","PMC3985476"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"91180676":{"subject":"PUBCHEM.COMPOUND:47936","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:f106216e6f08a4d322a97ea29168b79bdeaa5d865c036a9915607c801ea2e18c","tmkp:10af2e09ca6a9d39913d9ef85c54e76951b9fac2ac8f23693818ac2fcc30f455","tmkp:6f6148a77c28339deb0a5c3b79eed1d5444038b5bd6b2fd7af6db109917821ab","tmkp:975668c974b690e55c94e792e242946c557ba1e6e033694be78853e79cd66422"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:28400813","PMC5361515","PMC6364342","PMC7996534"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995198275","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Adenyl cyclase activator forskolin protects against Huntington's disease-like neurodegenerative disorders.|PMID:28400813|Adenyl cyclase activator forskolin protects against Huntington's disease-like neurodegenerative disorders |PMC5361515|Adenyl cyclase activator forskolin protects against Huntington's disease-like neurodegenerative disorders|PMC6364342|Adenyl cyclase activator forskolin protects against Huntington?s disease-like neurodegenerative disorders |PMC7996534","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"47714436":{"subject":"PUBCHEM.COMPOUND:4236","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"We examined whether modafinil induced similar effects in individuals with Huntington's disease (HD).|PMID:18516718|The effects of modafinil on mood and cognition in Huntington's disease.|PMID:18516718|The effects of modafinil on mood and cognition in Huntington?s disease |PMC6474183|The effects of modafinil on mood and cognition in Huntington?s disease |PMC8116411|The effects of modafinil on mood and cognition in Huntington's 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proven by human post-mortem and animal model studies, the histaminergic system becomes altered in the CNS when neuroinflammation exacerbates the outcome for instance of traumatic brain/spinal cord injury, multiple sclerosis, Alzheimer?s, Parkinson?s and Huntington?s diseases, and several histamine-related drugs are in clinical trial for these pathologies.|PMC6696457|Dimebon, originally developed as an anti-histamine drug, is being re-purposed for new indications as an effective treatment for patients suffering from Alzheimer's and Huntington's diseases, albeit with an as-yet unknown mechanism of action.|PMID:19939222|Studies outlining the significance of anti-histamine drugs in treating neurodegenerative disorders and the neuroprotective functions of latrepirdine in animal models initiated interest for repurposing latrepirdine as a potential therapy for AD and Huntington's disease (HD).|PMC4030329","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:43532e2e65229f57d40a49f9840a3b49cfbc282fcd781c281e45ccf59f3aad60","tmkp:2e57365592105b82b4a9bc61e86628e6b93d7f3b59f1fbbfe6f23d11b6e81c86","tmkp:6c877146c53be6d5ed849624ebe211a3a47d70e68d097757f44afdc5da974db1"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9955674333333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"32616846":{"subject":"PUBCHEM.COMPOUND:161166","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.98522472","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Despite these concerns, major advances are being made in kynurenine-related treatments for Huntington's disease and schizophrenia, and the range of conditions potentially amenable to kynurenine-related therapy continues to escalate.|PMC7066259|Our goal was to simultaneously identify tryptophan and kynurenines in the brain's extracellular compartment, to determine the effects of systemic kynurenine administration on these analytes, and to evaluate these features in a widely used animal model of the neurodegenerative disorder, Huntington's disease (HD).|PMC3274646|Despite these concerns, major advances are being made in kynurenine-related treatments for Huntington's disease and schizophrenia, and the range of conditions potentially amenable to kynurenine-related therapy continues to 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particular, the use of compounds containing phenol structural moiety in the treatment of Alzheimer?s disease, Parkinson?s disease, Huntington?s disease, and cancer have been extensively studied in the last two 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together, taurine neuroprotection in a current Huntington's disease model is due, at least partially, to its indirect antioxidant activity and GABA agonistic action.|PMC6536745|In nervous system disorders, taurine has a broader role, showing protective activity against toxicity in different neurodegenerative disease models for Parkinson's, Alzheimer's and Huntington's diseases.|PMC6536745|Taurine has been shown to provide protection against neurological diseases, such as Huntington's disease, Alzheimer's disease, and stroke.|PMID:23392887|In this review, we describe the mode of action of taurine and its clinical application in the neurological diseases: Alzheimer's disease, Parkinson's disease and Huntington's disease.|PMID:22903433|Neuroprotective effect of taurine in 3-nitropropionic acid-induced experimental animal model of Huntington?s disease 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example, quercetin (QE), a 3,5,7,3?,4?-pentahydroxyflavone, has been reported to attenuate motor coordination deficits and anxiety, decrease the proliferation of microglia and increase the number of astrocytes in lesion core in a 3-nitropropionic acid-induced rat model of Huntington's disease (Chakraborty et al., 2014).|PMC5361505|Quercetin also exhibits a neuro-protective function in several central nervous system disorders, including seizures and Huntington's disease.|PMC7388369|Although anti-carcinogenic, anti-inflammatory and vasodilating effects of quercetin are well documented, it has been found effective in the management of nervous system disorders including Parkinson?s and Huntington?s diseases.|PMC5802731|Several studies have reported on the neuroprotective effects of quercetin, both in vitro and in vivo models of neurodegenerative disorders, such as cognitive impairment, ischemia, traumatic injury, Parkinson?s disease (PD), and Huntington?s disease (HD).|PMC7023116|Quercetin 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felodipine is being investigated as an inducer of autophagy in Huntington?s disease and Parkinson?s disease models.|PMC8235459|The efficacy of felodipine has been further assessed in zebrafish models of tauopathy, a class of neurodegenerative disease involving the aggregation of Tau protein in the human brain, mouse models of Huntington?s disease, and mouse models of PD.|PMC8235459|We selected felodipine as the most suitable candidate for further assessment and validated its effects in in vivo models of tauopathy, Huntington?s disease and Parkinson?s disease (A53T ?-synuclein mutation) to test whether this autophagy-inducing drug had relevance to multiple neurodegenerative 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is unique amino acid which readily crosses blood brain barrier and possesses neuroprotective potential against neurodegenerative disorders including Huntington disease (HD).|PMID:26957301|The present study has been designed to investigate the protective effect of L-theanine against 3-nitropropionic acid (3-NP)-induced Huntington's disease (HD)-like symptoms in rats.|PMID:24325390","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.996027725","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"41548456":{"subject":"PUBCHEM.COMPOUND:445154","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"A recent study published in Experimental Neurology examined the therapeutic potential of a micronised proprietary resveratrol formulation, SRT501 in the N171?82Q transgenic mouse model of Huntington?s disease (HD).|PMC6081196|ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington's disease|PMC3098728|ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington?s disease |PMC3711381|ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington?s disease |PMC4380832|ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington's 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activity.|PMC7224297","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c1ec6a9cd42c245430265703826af9ce989edea887e56c31c0530ee1cc7bda8d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC7224297"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"29866309":{"subject":"PUBCHEM.COMPOUND:444795","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"CA150 also has been found by DD to be up-regulated in all-trans retinoic acid (ATRA)-induced apoptosis of H9 and SR-786 T cell lymphoma cell lines and 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effects of apomorphine in an animal model of Huntington's disease.|PMID:156535|The sedative effectiveness of apomorphine in a newly developed animal model of Huntington's disease was examined.|PMID:156535|Acute challenge with apomorphine in Huntington's disease: a double-blind study.|PMID:8665556|Acute challenge with apomorphine in Huntington?s disease: a double-blind study |PMC5995787|We evaluated tolerability and the efficacy of continuous infusion of apomorphine hydrochloride on involuntary movements and mood disorder in Huntington's disease (HD) patients in a pilot, single center, double-blind, randomized, crossover, and controlled versus placebo 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CD, Rodrigues CM, Eich T, Chhabra MS, Steer CJ, et al. (2002) Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease.|PMC3882322|TUDCA acts as a mitochondrial stabilizer and anti-apoptotic agent in several models of neurodegenerative diseases, including AD, Parkinson's diseases (PD), and Huntington's diseases (HD).|PMC4030606|Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic model of Huntington's disease|PMC6259142|Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease.|PMC3178513|Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease.|PMC3031519","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9993961622222223","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3882322","PMC4030606","PMC6259142","PMC3178513","PMC3031519"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"104588290":{"subject":"PUBCHEM.COMPOUND:4507","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Nitrendipine is a calcium channel blocker that declines the incidences of dementia (upto 50%) in HD in a period of 2 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striatum.|PMID:30284227","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:30284227"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"75519741":{"subject":"PUBCHEM.COMPOUND:2803","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3518431"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99952924","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:435aff9b2726e5dad38e13fcd0cd58d2573fce54bd9cbde2447136008a122a0a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"For instance, imidazoline receptor agonists such as clonidine and rilmenidine induce autophagy and have protective effects in cell culture, D. melanogaster and zebrafish models of Huntington?s disease.|PMC3518431","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"33697006":{"subject":"PUBCHEM.COMPOUND:3958","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"During the trial, patients will be permitted to receive lorazepam as needed up to 1 mg per day for anxiety/insomnia, and non-benzodiazepine hypnotics, e.g., zolpidem.Current clinical diagnosis of schizophrenia, schizoaffective disorder, other psychosis, or bipolar 1 disorder (DSM-IV TR criteria).Current or recent (past 6 months) alcohol or substance dependence (DSM-IV TR criteria).Current major depression or suicidality as assessed by the study psychiatrist.Suicidal behavior or dangerous behavior with serious safety risk or risk of physical harm to self or others.Parkinson?s disease, Lewy body disease, multiple sclerosis, CNS infection Huntington?s disease, amyotrophic lateral sclerosis, other major neurological disorder.Clinical stroke with residual neurological 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chorea.|PMID:145212","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"124805287":{"subject":"PUBCHEM.COMPOUND:3117","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:26baabf9202dfdb02acc95dbc31b58da72bb71a75bc2adeb0e025d1b1e5ea2ba"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:18479220"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9991522","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Our encouraging findings in recent studies reveal anticancer activities of several copper-binding ligands including disulfiram (an antialcoholism drug), clioquinol (used to treat Alzheimer's and Huntington's diseases) and diethyldithiocarbamate (an agent for HIV-1 infection treatment).|PMID:18479220","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"23740235":{"subject":"PUBCHEM.COMPOUND:6099","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:22875942","PMC5215751","PMC4001318","PMC7710872","PMC3825132"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9994974691666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8be8367b736ed0401b8b5659f1e2c50ca46dedc23bf3dc10ed82d8a00fa3993e","tmkp:5b94cfe11b4524c237f0c56adc0cfaf1299cc9d5401a9947b3b0f96f37f7618a","tmkp:76e36424d06478a056aee317f1520d1b8068f651110e4b2064555db026c4c02b","tmkp:94c014eec6566bc82fa4cbb598d722f5f1be4bcda131f8c1e00fe9ed691cdb2a","tmkp:aed56c0c367f834a8f776f8b4c7b2096507bb3bebaef5ce2b713878450f0fc49"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models.|PMID:22875942|Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models|PMC5215751|Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models|PMC4001318|Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models|PMC7710872|Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models|PMC3825132","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"34292772":{"subject":"UNII:1VS4X81277","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:e657d80bba6d9c9fe15f86384cb08c8a640b2a14ffa13c5862b5a3152eaa9c26"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99938476","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Likewise, scyllo-inositol reduces 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present study was carried out to evaluate the beneficial effect of mitochondrial cofactors; alpha-lipoic acid (ALA) and acetyl-l-carnitine (ALCAR) in 3-nitropropionic acid (3-NP) induced experimental model of Huntington's disease (HD).|PMID:24393741","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:fc7151d8917950d0b86275455aa93f9393c399a71178e4322e160dc7a83ffafd"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"99359416":{"subject":"PUBCHEM.COMPOUND:3830","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99934524","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC7865834"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, kinetin treatments furnished a visible improvement including curing the severe neurological conditions of Huntington?s 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adenosine (Ado) and non-Ado nucleosides, such as guanosine (Guo), inosine (Ino) and uridine (Urd), modulate both physiological and pathophysiological processes in the brain, such as sleep, pain, memory, depression, schizophrenia, epilepsy, Huntington's disease, Alzheimer's disease and Parkinson's disease.|PMID:23992313|Moreover, all these findings are opening new avenues to study the motor system and the effects of damage to the mechanism of motor function in neurological and neurodegenerative diseases such as Parkinson disease (Rickards), multiple sclerosis (Mehanna and Jankovic), Huntington disease (Guo et al.) and spino-cerebellar ataxia (Klinke et 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chloride in the treatment of Huntington's disease and tardive dyskinesia: a preliminary report.|PMID:142261|Oral choline administration to patients with Huntington?s disease |PMC5181681|Effects of oral choline administration on serum and CSF choline levels in patients with Huntington's disease.|PMID:137960|Choline chloride was administered orally (3 to 15 gm per day) to five patients with Huntington chorea.|PMID:142929|Effects of oral choline administration on serum and CSF choline levels in patients with Huntington?s disease 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with intramuscular zuclopenthixol and medroxyprogesterone acetate in the treatment of agitation and aggression in Huntington's disease.|PMID:24026736|Experience with intramuscular zuclopenthixol and medroxyprogesterone acetate in the treatment of agitation and aggression in Huntington's disease|PMC6618900|Experience with intramuscular zuclopenthixol and medroxyprogesterone acetate in the treatment of agitation and aggression in Huntington?s disease 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effects of quetiapine (QTP), valproate (VPR), lithium (Li), fluoxetine (FLX), donepezil (DNP), and memantine (MMT) are displayed for specific steps in the neuropathic process, derived from preclinical models relevant to Alzheimer's disease (AD), Parkinson's disease (PD), and Huntington's disease (HD) regarding both pre-symptomatic and early clinical stages of these diseases.|PMC5204212|Effect of donepezil on motor and cognitive function in Huntington disease.|PMC3677041|Effect of donepezil on motor and cognitive function in Huntington disease.|PMC4718719|Effect of donepezil on motor and cognitive function in Huntington disease.|PMID:17030764|Cognitive deficits in the R6/2 mouse model of Huntington?s disease and their amelioration with Donepezil 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disease: novel therapeutic perspectives hanging in the balance.|PMID:29671352","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"52662485":{"subject":"PUBCHEM.COMPOUND:131801471","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99923292","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3b45781937dd603be842c4b0a3b6c2ec925b133aafc74625ab9d5d553a1060ee","tmkp:e4a473ab3ec2c4dbffe7d34a7c5095317d776c32654fad7c92f23dce8e6a9928","tmkp:b622c51489c7f7ec6c881fa5f2b3eb5c937f9e0fa67428c733bc07f0bf1c0471","tmkp:6532a3e1611a0278f8c2746845227b20231d290355014745e81c87dd336ad470"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5573879","PMC6290705","PMC7438883","PMC6290705"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Indeed, nusinersen (SPINRAZA; Biogen), a centrally delivered ASO drug, was approved by the Food and Drug Administration (FDA) for treatment of spinal muscular atrophy, together with several other centrally delivered ASO therapeutics that are in clinical phase I trials for familial amyotrophic lateral sclerosis and Huntington?s disease (ClinicalTrials.gov:|PMC5573879|The recently demonstrated clinical benefit and subsequent FDA approval of intrathecal anti-sense oligonucleotide therapy (nusinersen, Spiranza?) to correct a genetic mutation causing spinal muscular atrophy in pediatric patients, as well as promising results of the Ionis-Roche anti-sense oligonucleotide (RG6043) in phase I/IIa clinical trials for Huntington?s disease, leading to PRIME (PRIority MEdicines) designation by the European Medicines Agency, sparked a renewed promise that a broader application of gene therapy to correct devastating monogenetic neurological diseases, including lysosomal storage disease, ALS and Huntington?s disease, could be realized if appropriate brain delivery technologies were introduced in gene therapy designs.|PMC6290705|Several ASO therapeutics are already in clinical phase 1 trials for familial amyotrophic lateral sclerosis and Huntington?s disease, and Nusinersen has been approved by the FDA for the treatment of spinal muscular atrophy (ClinicalTrials.gov:|PMC7438883|The recently demonstrated clinical benefit and subsequent FDA approval of intrathecal anti-sense oligonucleotide therapy (nusinersen, Spiranza?) to correct a genetic mutation causing spinal muscular atrophy in pediatric patients, as well as promising results of the Ionis-Roche anti-sense oligonucleotide (RG6043) in phase I/IIa clinical trials for Huntington?s disease, leading to PRIME (PRIority MEdicines) designation by the European Medicines Agency, sparked a renewed promise that a broader application of gene therapy to correct devastating monogenetic neurological diseases, including lysosomal storage disease, ALS and Huntington?s disease, could be realized if appropriate brain delivery technologies were introduced in gene therapy designs.|PMC6290705","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"57452793":{"subject":"PUBCHEM.COMPOUND:5281915","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:sri-reference-kg","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"74330127":{"subject":"PUBCHEM.COMPOUND:119","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Cell lines that produce large amounts of GABA may be useful for transplantation into the brain in conditions such as Huntington's disease or epilepsy, where localized application of GABA may be of therapeutic value.|PMID:10686067|The mixed findings concerning GABA administration in clinical populations suffering from epilepsy or Huntington?s disease are insufficient to rule out a possible effect of GABA in the brain.|PMC4594160|Patients with Huntington?s disease also have reduced GABA levels in the brain, but administration of GABA to remedy this deficiency has shown mixed results with regards to the reduction of symptoms.|PMC4594160|Muscimol, a gamma-aminobutyric acid (GABA) analogue that exerts potent and specific agonist effects on GABA receptors, was administered orally to 10 patients with Huntington's disease.|PMID:152602|GABA-releasing polymer matrices or control matrices without GABA were implanted either unilaterally or bilaterally in the vicinity of the ventromedial thalamic nucleus of normal rats and of rats with unilateral or bilateral excitotoxic striatal lesions (rat model of Huntington's disease), to study the effects of these GABA-releasing matrices on amphetamine-induced rotational behavior (unilateral implants in unilaterally lesioned rats) and on overnight spontaneous locomotor activity (bilateral implants in bilaterally lesioned rats).|PMID:8934563","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2507bcf31267b8bff332ce6dd5a474ed5b9ede305c30d6e826d383455d368c98","tmkp:19234d69372adc497d831111840a565f4994bf3aaaaeb53a43c91d66dd15ed10","tmkp:1f3f8ec2b67e8e76b4d53e215dcca22c68b8f0e79a5cb849bdda061011617140","tmkp:2ddab3c72fbec84137dde92a2b4f2d29d540da6d2cff3f50524a0945c71d99f8","tmkp:5d798c794cb924a8ca0375a67e15eb4517664e03a2a702eda386fc216b75eb20"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9931780399999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:10686067","PMC4594160","PMC4594160","PMID:152602","PMID:8934563"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"107838715":{"subject":"PUBCHEM.COMPOUND:1923","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Indeed, 8-hydroxyquinoline analogs are in phase 2 testing for patients with AD or Huntington?s disease, supporting the safety of this chemical backbone in human applications.|PMC5341138|The hydroxyquinoline PBT2 has been developed as a potential treatment for Alzheimer?s and Huntington?s disease and has progressed to phase 2 human clinical trials, with a daily dose of 250?mg over 6?months being safe and well tolerated.|PMC6299484|Hydroxyquinoline has been developed as a potential drug for Alzheimer?s and Huntington?s disease, however it failed efficacy checkpoints in the phase 2 human clinical trials.|PMC7558363|PBT2 {5,7-dichloro-2-[(dimethylamino)methyl]quinolin-8-ol} is a hydroxyquinoline-based ionophore that was developed as a treatment for Alzheimer?s disease and Huntington?s disease, and it progressed to phase 2 human clinical 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rotenone and 3-NP treatments mimic the mitochondrial impairment and oxidative stress that contribute to development of Parkinson's disease and Huntington's disease, these data suggest that induction of hsp70 might represent a possible neuroprotective mechanism against the pathophysiological chain of events implicated in these neurodegenerative disorders.|PMID:19580850|We employed rotenone and 3-nitropropionic acid (3-NP), mitochondrial CoI and CoII inhibitors, respectively, widely used in modeling central facets of the neurodegenerative disorders Parkinson?s disease (PD) and Huntington?s disease (HD), respectively.|PMC7881114","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:19580850","PMC7881114"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"63008214":{"subject":"CHEMBL.COMPOUND:CHEMBL559147","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Furthermore, significant therapeutic effects were also observed in a mouse model of Huntington's disease, both with Y-27632 and Fasudil treatment (Li et al.,), and in a model of spinal muscle atrophy, a condition with high similarity to ALS.|PMC5281550|Y-27632, an inhibitor of the Rho-associated kinase ROCK, is a therapeutic lead for Huntington disease (HD).|PMID:18573880|Interestingly, Y-27632 was shown to improve degradation of mutant huntingtin as well as motor performance in the R6/2 mouse model of Huntington?s disease.|PMC4840958|In regard to neuroprotection, Y-27632 has been applied to animal models of Huntington?s disease and spinal muscular atrophy where it improved rotarod performance and prolonged survival, respectively (Li et al.,; Bowerman et al.,).|PMC3207219|In a model of Huntington's disease, the ROCK inhibitor Y-27632 improved rotarod performance without influencing survival time at a dosage of 100 mg/kg (Li et 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oxidase contributes to neurotoxicity in an excitotoxic/prooxidant model of Huntington's disease in rats: protective role of apocynin.|PMID:19795371","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9990108","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"45397829":{"subject":"PUBCHEM.COMPOUND:54677946","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Laquinimod is an orally dosed immuno-modulator currently under development for Huntington's disease (HD).|PMID:30191262|Laquinimod treatment improves myelination deficits at the transcriptional and ultrastructural levels in the YAC128 mouse model of Huntington disease|PMC6824292|Laquinimod treatment improves myelination deficits at the transcriptional and ultrastructural levels in the YAC128 mouse model of Huntington disease|PMC7676421|Laquinimod Treatment Improves Myelination Deficits at the Transcriptional and Ultrastructural Levels in the YAC128 Mouse Model of Huntington Disease|PMC7699283|Laquinimod treatment improves myelination deficits at the transcriptional and ultrastructural levels in the YAC128 mouse model of Huntington disease|PMC7052383","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994247888679245","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:30191262","PMC6824292","PMC7676421","PMC7699283","PMC7052383"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0c7be1677f9ddbfef1159bb33c1c2ab5192e4d921372e46871be1e658d0d547d","tmkp:029a63ac4e2ad6a59460039c81ec09381d9d2ba6c624328b6cf0db34ad242652","tmkp:0c1c263fb90316941d0219fa952ae837f2298f0021e9332f2a9c8c2a6da68270","tmkp:3f2ad471fe04f731eae4ba18327805a6c90137dc12b28625b3fd08cbee13008a","tmkp:c022d9be397ff676d8dbe62e5f77c73b71e9130ef16e3f0946c760c4d1567947"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"105085273":{"subject":"PUBCHEM.COMPOUND:16078","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC8134483","PMC4818362","PMID:12858038","PMID:6273940"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Previously, we demonstrated that ?arrestin1-biased cannabinoids, such as CP55940 and THC, reduce cellular viability in a cell culture model of Huntington?s disease .|PMC8134483|Many studies report that THC provides protection against neuronal injury in a cell culture model of Parkinson disease and experimental models of Huntington disease, exhibits anti-oxidative action and mitigates the severity of the autoimmune response in an experimental model of diabetes.|PMC4818362|In this study, we examined whether a treatment with Delta9-tetrahydrocannabinol, a non-selective cannabinoid receptor agonist, or with SR141716, a selective antagonist for the cannabinoid CB(1) receptor subtype, could affect the toxicity of the complex II reversible inhibitor malonate injected into the striatum, which replicates the mitochondrial complex II deficiency seen in Huntington's disease patients.|PMID:12858038|Insofar as reserpine has been used with some clinical efficacy in hyperkinetic movement disorders such as Huntington's disease and tardive dyskinesia, it may be that potentiation of reserpine's hypokinetic effect by a drug such as THC could greatly increase the clinical value of reserpine or related drugs in the treatment of these disorders.|PMID:6273940","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:054552722d34d77abb9b9bded5bcd180077de390faf6c442dcbe3c7d7b6e8181","tmkp:2e498bfc71718eee93b10c942b738a6ba7ac3f8812b66a2cee5cfcc803f85071","tmkp:967c7bae046493f5ea2ac6a46ce04ed87772bdc7a81ae0dfb0fc88ca414c9153","tmkp:8ab2b757e866377184ef8fb360e5d69c8050d0abfb2fdf3921e887b781877836"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9976380675000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"30546901":{"subject":"PUBCHEM.COMPOUND:91666318","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:1dfc551a91e18f51d0e1c1a88c71244d04e9011b6aea5c263b64d2e5d730ca53"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC4927912"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"CPECs encapsulated in alginate- and poly-ornithine-coated materials exerted neuroprotection in a rodent model of Huntington?s disease.|PMC4927912","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99038494","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"117751773":{"subject":"PUBCHEM.COMPOUND:170361","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:2f145ea8f7f1620531c4ed790827be9f27359da4fec3831f9b752334afaefdb9"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"We have investigated whether chronic administration of the selective nicotinic partial agonist varenicline improved motor, cognitive and affective symptoms in a transgenic mouse model of Huntington's disease.|PMID:28025093","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:28025093"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9995223","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"60857384":{"subject":"PUBCHEM.COMPOUND:5997","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"We have revealed new cholesterol-targeting therapeutic strategies in Huntington?s disease, and presumably in other neurodegenerative diseases where dysregulation of cholesterol homeostasis has been clearly identified.|PMC4766376|In addition, in animal experiments, the cholesterol infusion to striatum of Huntington's disease mice prevented cognitive decline (Birolini et al.,).|PMC8248815|Cholesterol-loaded nanoparticles ameliorate synaptic and cognitive function in Huntington's disease mice.|PMID:26589247|Cholesterol-loaded nanoparticles ameliorate synaptic and cognitive function in Huntingtons disease mice.|PMC5543677|Cholesterol-loaded nanoparticles ameliorate synaptic and cognitive function in Huntington's disease mice|PMC6490702","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9983558840000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0eaf0136e6370657732597fcaed6ffa882cc85ba8255011803d9867801c0a39c","tmkp:b814f3fbcd6463f18cba9281b12327b201829a213844ce5d47caddfbaad606af","tmkp:463b4c81acf378b4be6dc1080188eb79f7f72aaefa197e565ff0a7ffb9bc864c","tmkp:e5f22d63a8fe5e0d5719b572972ec82793d8d5fd019730bbde17b0d2341f6c76","tmkp:7d05112385809d6d0720f56a84a516502df86812ae5b2b160a6cd5cd7e5bda25"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4766376","PMC8248815","PMID:26589247","PMC5543677","PMC6490702"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"65155087":{"subject":"PUBCHEM.COMPOUND:5113032","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3772001","PMID:25223731","PMID:25223836","PMC4265300","PMC7464235"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"One compound (Selisistat or SEN196) is in Phase II clinical trials for Huntington's disease.|PMC3772001|Selisistat, a selective SirT1 inhibitor is being developed as a potentially disease-modifying therapeutic for Huntington's disease (HD).|PMID:25223731|Selisistat (SEN0014196), a first-in-class SirT1 inhibitor, is being developed as a disease-modifying therapy for Huntington's disease.|PMID:25223836|Safety and tolerability of selisistat for the treatment of Huntington's disease: results from a randomized, double-blind, placebo-controlled phase II trial (S47.004)|PMC4265300|On the other hand, selisistat (Ex527), a SIRT1 inhibitor, has been studied in healthy individuals and patients with Huntington?s disease, and has also been shown to be 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research also indicates that cannabis and cannabinoids have therapeutic potential for multiple sclerosis, Huntington?s disease, Parkinson?s disease, glaucoma, hypertension, stress and psychiatric disorders, Alzheimer?s disease and dementia, and anti-neoplasia, many of which have not been described in traditional use.|PMC7039888|In addition, the study found there was little evidence that marijuana had any effect on movement disorders such as Parkinson?s disease or Huntington?s disease, but it was effective in combating the muscle spasms associated with MS.|PMC3628147|Medical cannabis is increasingly used as a treatment or adjunct treatment with different levels of efficacy in several neurological disorders or related symptoms (such as multiple sclerosis, autism, Parkinson and Alzheimer disease, Tourette's syndrome, Huntington's disease, neuropathic pain, epilepsy, headache), as well as in other medical conditions (e.g.|PMID:28412919|A total of 24 reports that evaluated the use of medical cannabis for Alzheimer's disease, anorexia nervosa, anxiety, dementia, dystonia, Huntington's disease, Parkinson's disease, post-traumatic stress disorder (PTSD), psychosis and Tourette syndrome were included in this review.|PMID:29073741|Studies have looked at the potential benefits of medical marijuana and cannabinoids for the treatment of Huntington's disease (HD).|PMC5165161","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"53357010":{"subject":"PUBCHEM.COMPOUND:6326970","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Rutin and selenium co-administration reverse 3-nitropropionic acid-induced neurochemical and molecular impairments in a mouse model of Huntington's disease|PMC7085382|Rutin and selenium co-administration reverse 3-nitropropionic acid-induced neurochemical and molecular impairments in a mouse model of Huntington?s disease |PMC7455605|Rutin and selenium co-administration reverse 3-nitropropionic acid-induced neurochemical and molecular impairments in a mouse model of Huntington?s disease 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diseases.|PMID:19417220","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994165633333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC8146903","PMC7245554","PMID:19417220"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:201e90c21769e7f99a56ee523e567536a8d369b9b7b1547e31dfd5b789a6d01e","tmkp:0ff80be389df08909a10922f1077c28cd0452b485065138542bfab2c7a2910c0","tmkp:581ee469f04a9472effd77d48dd3960208bc499cd211fe60c41dfed657cca015"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"59375095":{"subject":"PUBCHEM.COMPOUND:9926832","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994642","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b562d29ba0d5bb6b614ee674be4c89ab4be32bc9b83007e9944411c6be5b5eed"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"This study investigated the hypothesis that AFQ056 (mavoglurant), a selective metabotropic glutamate receptor 5 antagonist, reduces chorea in Huntington's disease (HD).|PMID:25689146","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:25689146"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"106111282":{"subject":"PUBCHEM.COMPOUND:5961","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:d86a7cd45cff6998c26e2a264e053f3e992730bb4e5ef8d3911322e3554975ce"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99703014","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6320634"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In clinical practice, some scholars have increased glutamine content in the diet of patients with Alzheimer?s disease, Huntington?s disease, and amyotrophic lateral sclerosis, so as to reduce oxidative stress damage.|PMC6320634","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"90932190":{"subject":"PUBCHEM.COMPOUND:108144","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4713307","PMC4713307","PMID:26581638"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ab2084e68bd53d8b94834e495ced645fbf00eadc1dfc8a297f25f784336960e6","tmkp:08b6334757ec04721b4611f6d1252ca3cc4b2d330ec64464abd2db567c32ba0b","tmkp:39325c64906d17c593d95037b2be7b7037130d281ccecaed75ddcbe767ac819e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"A number of drugs that are able to inhibit CytC release from isolated mitochondria have been identified; among them, the carbonic anhydrase inhibitor (CAI) methazolamide (MTZ), proved to be neuroprotective in models of Huntington's Disease (HD) and ischemic injury.|PMC4713307|The carbonic anhydrase inhibitor (CAI) methazolamide (MTZ) was identified among a library of drugs as an inhibitor of CytC release and proved to be neuroprotective in Huntington's disease and stroke models.|PMC4713307|The carbonic anhydrase inhibitor (CAI) methazolamide (MTZ) was identified among a library of drugs as an inhibitor of CytC release and proved to be neuroprotective in Huntington's disease and stroke models.|PMID:26581638","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995120333333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"112711366":{"subject":"PUBCHEM.COMPOUND:5280793","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:27685770"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:846baa5f7158adef1376f55e419b754123fc09441ff99cfa4076db0949c386fd"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9995047","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Our findings support the potential influence of vitamin D deficiency on the disease course and propose that vitamin D may be an effective supplementary treatment to beneficially influence clinical features of Huntington's disease.|PMID:27685770","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"55841907":{"subject":"PUBCHEM.COMPOUND:24795069","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:d5f2183d505b7313c46e514f0832bd6aa8fdf104d835e43aa38f03f060d7841f","tmkp:b3e5603e407699f61434e0cb843f1d9c183bd6af73cd9e1ef9f952bb218f74ba"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:29455579","PMC6283785"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"In April 2017, the Food and Drug Administration (FDA) approved 2 new vesicular monoamine transporter 2 (VMAT2) inhibitors, deutetrabenazine and valbenazine, for chorea related to Huntington's disease and tardive dyskinesia, respectively.|PMID:29455579|Although tolerability was not a major issue in these studies, clinical experience with side effects of tetrabenazine that occur in more than 5% of patients in persons with Huntington?s disease (such as sedation, insomnia, depression, akathisia, parkinsonism, instability, irritability), and the requirement to dose the medication up to 3 times per day, and assessing for CYP 2D6 poor/extensive metabolizers if doses greater than 50?mg/day need to be used, led to the development of the two tetrabenazine alternatives, valbenazine and deutetrabenazine, discussed previously.|PMC6283785","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.973018945","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"55936288":{"subject":"PUBCHEM.COMPOUND:5284583","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Efficacy of levetiracetam in Huntington disease.|PMID:16340384|Open-label pilot study of levetiracetam (Keppra) for the treatment of chorea in Huntington's disease.|PMID:16941461|The objective of this study is to evaluate the tolerability and preliminary efficacy of levetiracetam (LEV) in reducing chorea in Huntington's disease (HD) patients in a prospective open-label pilot study.|PMID:16941461|Efficacy of levetiracetam in Huntington disease|PMC5216093|Efficacy of levetiracetam in Huntington disease|PMC3643297","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dca1ff342a019afaec7705f89c72058a00ee9582a905825ec230dd3e2c18612b","tmkp:3c615735eb6055712e828be7602fb36928dc860433f27ad16fb7ad72878c3704","tmkp:38f02b0e7385527f74836f903d9a2ff50910b8c43a789342f99f414c511b5230","tmkp:6b33568554d37d160653140484e8298f9b0468687858a080f4360bd221510b1c","tmkp:93793087c09fb19945064fbab4d4495fc656cfe4d6ba45215b6fd33c0336e5eb"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999460006","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:16340384","PMID:16941461","PMID:16941461","PMC5216093","PMC3643297"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"42436896":{"subject":"PUBCHEM.COMPOUND:445580","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2926984","PMID:20802793"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:926d45d1ef44e7567a84d475d12edb64a7891584d9b702dfd6aebe596e214fac","tmkp:a4c542732ffa5c02373d687dd822ef79ebdfa2ab9fb5e13f06a5922599aa1afc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"The fish-derived omega-3 fatty acids, eicosapentaenoic acid and docosahexaenoic acid, have been examined in clinical trials of Huntington disease patients.|PMC2926984|The fish-derived omega-3 fatty acids, eicosapentaenoic acid and docosahexaenoic acid, have been examined in clinical trials of Huntington disease patients.|PMID:20802793","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995427","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"122078011":{"subject":"PUBCHEM.COMPOUND:6862","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:7562269"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994611","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Currently, NAA is being studied in many other brain disorders, such as Alzheimer disease, Huntington disease, and stroke.|PMID:7562269","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b964b04140f59bae59abb4a81d867446e5680c03e8f6704a04b97e8a9d3b3c66"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"103056677":{"subject":"PUBCHEM.COMPOUND:586","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9993931471111112","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:896ab8aa8fa4bae2be8ee15228971e400807ff0a5d4ec3abaa2eab6810727c96","tmkp:a95b30c7866b25e0f03cccaa694727d67f6a47a9b37caa42828075d6fb65c70d","tmkp:739ff4b9be8c6ae1c242826a22d332b2a802d196487b2a93d3b8f1ddf87b35f8","tmkp:c86b718010e6dd3511c3903d54795fdc2fdb4e25b4043e7b9e6137ef716a0f2d","tmkp:2c015ea9796dde274a06aa0523d027cbab06882b5a8cd53fb003ea31adab4098"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"To evaluate the effect of creatine (Cr) supplementation (5 g/day) in Huntington's disease (HD).|PMID:14557561|One of the first groups to investigate the antioxidant properties of creatine was Matthews et al.. Using an animal model of Huntington?s disease, Matthews et al. examined whether creatine could protect against the formation of striatal lesions (tissue damage) in the brain, induced either by intrastriatal injections of malonate or intraperitoneal injections of nitropropionic acid (3-NP); both of which are inducers of neurotoxicity.|PMC7551337|Several studies have suggested that creatine supplementation may also reduce oxidative DNA damage and brain glutamate levels in Huntington disease patients.|PMC3205506|The evidence presented in this review suggests that creatine supplementation improves bioenergetic deficits and may exert neuroprotective effects in Parkinson?s and Huntington?s disease.|PMC2886719|Several studies have investigated the short- and long-term therapeutic benefit of creatine supplementation in animals, children, and adults with various neuromuscular diseases like Huntington?s disease (HD); Parkinson?s disease (PD); mitochondria-related diseases; amyotrophic lateral sclerosis (ALS); spinal and bulbar muscular atrophy; and, muscular dystrophies (MD).|PMC7910963","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:14557561","PMC7551337","PMC3205506","PMC2886719","PMC7910963"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"111420486":{"subject":"PUBCHEM.COMPOUND:5665","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Gamma-vinyl GABA treatment of Huntington's disease|PMC6303784|Gamma-vinyl GABA treatment of Huntington's disease.|PMID:6228746|In a double-blind, crossover study gamma-vinyl GABA, 2 g/day, and placebo were administered orally for 2 weeks each to six patients with Huntington's 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data suggest that the currently approved CNS drugs, sertraline, chlorprothixene, and chlorpromazine are likely to have polypharmacological activity against the mSin3B PAH1 domain, which binds to REST/NRSF, whose dysregulation is related to glioblastoma, Huntington?s disease, and neuropathic pain in addition to medulloblastoma.|PMC6137095|Treatment of depressive-like behaviour in Huntington's disease mice by chronic sertraline and exercise|PMC3394391|Treatment of depressive-like behaviour in Huntington's disease mice by chronic sertraline and exercise|PMC5347981|Treatment of depressive-like behavior in Huntington's disease mice by chronic sertraline and exercise|PMC4005937|Sertraline slows disease progression and increases neurogenesis in N171-82Q mouse model of Huntington's 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neuroprotective effect of Met has been demonstrated in different neurological disorders such as Alzheimer?s disease, Parkinson?s disease, Huntington?s disease, and seizures.|PMC5776431|Numerous studies have shown that Met exerts beneficial effects on a variety of neurological disorders, including Alzheimer?s disease (AD), Parkinson?s disease (PD) and Huntington?s disease (HD).|PMC7601223|Moreover, Met has been found to rescue the early brain changes and abnormal behaviors in Huntington?s disease (HD)-modeled in 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early-onset convulsions, and diabetic encephalopathy.|PMC5845642|Because caffeine (a nonselective adenosine receptor antagonist) and selective adenosine A2A receptor (A2A R) blockade alleviate neurodegeneration in different brain diseases, namely at early stages of another polyglutamine-related disorder such as Huntington's disease, we now tested their ability to control MJD-associated neurodegeneration.|PMID:23625556|Other disease in which caffeine exerts positive effects includes stroke, traumatic brain injury, Alzheimer's disease, Huntington's disease and multiple sclerosis.|PMC3918252|The positive impact of caffeine on a worm model of polyglutamine disease suggests that chronic caffeine consumption may generally enhance resistance to proteotoxic stress and may be relevant to assessing risk and developing treatments for human diseases like Alzheimer's and Huntington's disease.|PMID:24764514|The positive impact of caffeine on a worm model of polyglutamine disease suggests that chronic caffeine consumption may generally enhance resistance to proteotoxic stress and may be relevant to assessing risk and developing treatments for human diseases like Alzheimer?s and Huntington?s 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pharmacokinetics of tiapride were determined at steady-state in 5 patients with tardive dyskinesia and 2 patients with Huntington's disease given tiapride 100 mg t.i.d. for 7 days.|PMID:2948825|The pharmacokinetics of tiapride were determined at steady-state in 5 patients with tardive dyskinesia and 2 patients with Huntington's disease given tiapride 100 mg t.i.d. for 7 days.|PMID:2948825|Single oral dose pharmacokinetics of tiapride in patients with Huntington's disease.|PMID:2958291|A patient with Huntington's disease developed acute dystonia whilst treated with tiapride.|PMID:2523309|Single oral dose pharmacokinetics of tiapride in patients with Huntington's 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mimetics (such as exendin-4 and liraglutide) have been shown to exert neuroprotective effects, being beneficial in Parkinson?s disease (PD), Huntington?s disease (HD) and Alzheimer?s disease (AD) mouse models, and in clinical studies involving PD and AD patients.|PMC5997749|Neurons throughout the brain express GLP-1 receptors and recent studies have shown that GLP-1 and the longer-lived GLP-1 analog Exendin-4 can act directly on neurons to promote their resistance to dysfunction and degeneration in animal models of AD, Parkinson?s disease (PD), and Huntington?s disease (HD).|PMC3084367|Prior studies with exendin-4 have demonstrated that it provides neurotrophic and neuroprotective actions in cellular and animal models of a host of neurological disorders, including AD, Parkinson?s disease, Huntington's disease, motor neuron disease, peripheral neuropathy, stroke and traumatic brain injury.|PMC5947865|Exendin-4 improves glycemic control, ameliorates brain and pancreatic pathologies and extends survival in a mouse model of Huntington?s disease |PMC2753676|Exendin-4 improves glycemic control, ameliorates brain and pancreatic pathologies and extends survival in a mouse model of Huntington?s disease 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result stands in line with other studies where fenofibrate improved cognition in Huntington's disease and cerebral ischemia models.|PMC3945208|Fenofibrate has shown neuroprotective action in animal models of stroke and Huntington's disease.|PMC3420697|Clinical trials are ongoing for unanticipated diseases, such as sexual dysfunction (NCT00923676) and Huntington?s disease (NCT03515213) using 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stimulating factor attenuates striatal degeneration with activating survival pathways in 3-nitropropionic acid model of Huntington's disease.|PMID:18166168|Granulocyte-colony stimulating factor attenuates striatal degeneration with activating survival pathways in 3-nitropropionic acid model of Huntington?s disease |PMC5770429|Granulocyte-colony stimulating factor attenuates striatal degeneration with activating survival pathways in 3-nitropropionic acid model of Huntington?s disease |PMC5220237|Granulocyte-colony stimulating factor attenuates striatal degeneration with activating survival pathways in 3-nitropropionic acid model of Huntington's disease|PMC3711389|Granulocyte-colony stimulating factor attenuates striatal degeneration with activating survival pathways in 3-nitropropionic acid model of Huntington?s disease 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to degeneration of striatal neurons patients suffering from Huntington's disease react early with development of extrapyramidal side effects after therapy with amisulpride.|PMID:16220421|This case study shows the treatment of a patient with Huntington's disease, verified by genetic analysis, with the atypical antipsychotic drug amisulpride.|PMID:12524580","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:16220421","PMID:12524580"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"76369833":{"subject":"PUBCHEM.COMPOUND:9651","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:18938211","PMC5181681","PMID:15101572","PMC4365284","PMID:15101572"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Galantamine reduces striatal degeneration in 3-nitropropionic acid model of Huntington's disease.|PMID:18938211|Galantamine reduces striatal degeneration in 3-nitropropionic acid model of Huntington?s disease |PMC5181681|Treatment of Huntington's disease with galantamine.|PMID:15101572|Galanthamine is a registered drug for treating Alzheimer?s and Huntington?s diseases, and huperzine A is sold as a procognitive food supplement.|PMC4365284|We present the case of a patient with Huntington's disease and psychosis, whose motor and psychiatric symptoms improved after administration of galantamine, an acetylcholinesterase 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postnatal Days 1?15).Inflammation:significant inhibition of the expressions of NOS, COX-2 and the production of NO; increased expression of heme oxygenase-1 and EPO in microglia in in vitro tests.Anticancer Activity:reduction of NO, intracellular Ca2+ levels, and CAT activity in C6 glioma cells when combined with Dasatinib (Bcr-abl tyrosine kinase inhibitor), in comparison to Dasatinib applied alone.Huntington Disease:reduction of striatal damage, immunoreactivity to glial GFAP and lymphocyte common antigen (CD45) (markers of astrocyte and microglia activation); reduced behavioral deficits tested on the rotarod in the chemical model of Huntington disease (male C57BL/6 mice); reduced mortality of cultured striatal neurons of male C57BL/6 mice after the induction of the inflammation by 3NP.|PMC5452207","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9586461","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"61603194":{"subject":"PUBCHEM.COMPOUND:135398641","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.979322225","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:23992313","PMID:23992313"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:5dea6b2e8f49df0b62288ad0c32c7ea07660e2365cd801ee4459b1edaaea4a19","tmkp:a44e9ec92cd490eb7eaf0767164a519347a4af105c93d002d82267efa43bad01"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Indeed, adenosine (Ado) and non-Ado nucleosides, such as guanosine (Guo), inosine (Ino) and uridine (Urd), modulate both physiological and pathophysiological processes in the brain, such as sleep, pain, memory, depression, schizophrenia, epilepsy, Huntington's disease, Alzheimer's disease and Parkinson's disease.|PMID:23992313|Indeed, adenosine (Ado) and non-Ado nucleosides, such as guanosine (Guo), inosine (Ino) and uridine (Urd), modulate both physiological and pathophysiological processes in the brain, such as sleep, pain, memory, depression, schizophrenia, epilepsy, Huntington's disease, Alzheimer's disease and Parkinson's 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evidence indicates that mithramycin A (MA), an anti-cancer drug, has neuroprotective effects in ischemic brain injury and Huntington's disease (HD).|PMID:29048243|Chemotherapy for the brain: the antitumor antibiotic mithramycin prolongs survival in a mouse model of Huntington's disease.|PMC2916021|Chemotherapy for the brain: the antitumor antibiotic mithramycin prolongs survival in a mouse model of Huntington's disease.|PMC3001865|Chemotherapy for the brain: the antitumor antibiotic mithramycin prolongs survival in a mouse model of Huntington?s disease.|PMC7925995|Chemotherapy for the brain: the antitumor antibiotic mithramycin prolongs survival in a mouse model of Huntington?s 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uridine pro-drug 2',3',5'-tri-O-acetyluridine (PN401) was shown to be protective in the mitochondrial complex II inhibitor 3-nitropropionic acid model of Huntington's disease (HD).|PMID:17011205|Oral uridine pro-drug PN401 is neuroprotective in the R6/2 and N171-82Q mouse models of Huntington's disease.|PMID:17011205|Oral uridine pro-drug PN401 is neuroprotective in the R6/2 and N171-82Q mouse models of Huntington?s disease |PMC3505265|Oral uridine pro-drug PN401 is neuroprotective in the R6/2 and N171-82Q mouse models of Huntington?s disease |PMC3461214|Oral uridine pro-drug PN401 is neuroprotective in the R6/2 and N171-82Q mouse models of Huntington's 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since a large body of evidence exists regarding the effects of omega-3 fatty acids on cardiovascular risk, their beneficial effects on lipid metabolism could potentially be associated with improved clinical outcomes in individuals with Huntington disease.|PMC2926984|Omega-3 fatty acid dietary supplementation may also decrease the incidence or improve the clinical outcome of patients with other neurode-generative disorders such as multiple sclerosis, Parkinson's disease and Huntington's disease.|PMC2884051|To determine whether ethyl-eicosapentaenoic acid (ethyl-EPA), an omega-3 fatty acid, improves the motor features of Huntington disease.|PMID:19064745|However, since Huntington disease is characterized by insulin resistance and hypertriglyceridemia is one characteristic of insulin resistance, a beneficial effect of EPA on triglycerides in Huntington disease may be a manifestation of this omega-3 fatty acid?s protective effects on the central nervous 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induction by mutant huntingtin via Cdx2 modulates heterochromatin condensation and pathology in Huntington?s disease.|PMC5883374|ATRX induction by mutant huntingtin via Cdx2 modulates heterochromatin condensation and pathology in Huntington's disease.|PMID:22240898","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"12904894":{"subject":"PUBCHEM.COMPOUND:5311","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Vorinostat was also shown to cross the blood?brain barrier in a mouse model of Huntington's disease.|PMC4040511|Also the conversion of cysteamine to hypotaurine was inhibited when purified ADO was incubated with Vorinostat, possibly shedding light on the reported efficacy of Vorinostat in Huntington?s disease.|PMC4950666|HDAC inhibitors, such as suberoylanilide hydroxamic acid (SAHA) [14], sodium butyrate (SB) [15] and trichostatin (TSA) [16], have been demonstrated to be effective in upregulating histone acetylation and in ameliorating motor impairments in mouse models of Huntington's disease (HD), spinal and bulbar muscular atrophy (SBMA) and dentatorubral-pallidoluysian atrophy (DRPLA).|PMC3557284|For example, high-performance liquid chromatography-mass spectrometry (HPLC-MS) was used to analyze the active constituents of Xiao-Xu-Ming decoction; drosophila transgenic models were used to identify combinatorial drug, such as suberoylanilide hydroxamic acid (SAHA) and geldanamycin, for the treatment of Huntington's disease; cell-based assays technology was used to screen two-component combinations for the treatment of cancer, infectious diseases, and CNS disorders.|PMC3878852|Mielcarek M, Benn CL, Franklin SA, Smith DL, Woodman B, .. 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general, when high doses of dextromethorphan are given alone (>100 mg per day), the resultant higher dextromethorphan/dextrorphan concentrations than those associated with DM/Q have been tolerated in epilepsy (up to 150 ng/mL), neurosurgery (up to 193 ng/mL), and Huntington?s disease patients (up to 275 ng/mL) (see Table 3).|PMC4079824","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"54456638":{"subject":"PUBCHEM.COMPOUND:12881464","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9990756592307692","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC4487815","PMID:8866496","PMC2605644","PMC3303936","PMC2605644"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"A controlled trial of idebenone in Huntington's 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MDSCs were treated with JHD and oxaliplatin in vitro, 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antagonism by kynurenic acid is thought to be a mechanism for recovery and protection from stroke, epilepsy, and Huntington?s disease.|PMC8213022|Neuroprotective effects of a novel kynurenic acid analogue in a transgenic mouse model of Huntington?s disease.|PMC4825950|Neuroprotective effects of a novel kynurenic acid analogue in a transgenic mouse model of Huntington?s disease.|PMC6119962|Neuroprotective effects of a novel kynurenic acid analogue in a transgenic mouse model of Huntington's disease.|PMID:21194001|Neuroprotective effects of a novel kynurenic acid analogue in a transgenic mouse model of Huntington?s disease 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patients with Huntington disease were treated with aminooxyacetic acid (AOAA), an inhibitor of gamma-aminobutyric acid aminotransferase (GABA-T), in an effort to alleviate symptoms by increasing brain GABA content.|PMID:6446691|Seven patients with Huntington disease were treated with aminooxyacetic acid (AOAA), an inhibitor of gamma-aminobutyric acid aminotransferase (GABA-T), in an effort to alleviate symptoms by increasing brain GABA content.|PMID:6446691|For inhibition of hydrogen sulfide (H2S) production, the cystathionine-?-synthase (CBS) inhibitor aminooxyacetic acid (AOAA) has already been tested in humans in the contexts of Huntington disease and tinnitus.|PMC5319818|AOAA was in clinical trials several decades ago for non-oncological indications (including Huntington disease and tinnitus) Box 2, and as such, could potentially be repurposed.|PMC5319818|For inhibition of hydrogen sulfide (H2S) production, the cystathionine-?-synthase (CBS) inhibitor aminooxyacetic acid (AOAA) has already been tested in humans in the contexts of Huntington disease and tinnitus.|PMC5319818","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.999278046","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"55767002":{"subject":"PUBCHEM.COMPOUND:9577379","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:26096705","PMID:27589053","PMC7696015","PMC6433839","PMC4096754"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:aa7b84a865915fb78ec2c995b8dbb909e14d0b762161a0b7f92a6c098284bca1","tmkp:c03ac1e64d06638ee666c2a4f66e59c7e81bbd76e75f791dad6b4865040f45c9","tmkp:b75c7bf809ff5fb2572ed8d1e19a7eb5cf5c5eddf537159dcb6974a79765bc0a","tmkp:dc16fc61c37965c79c25665b37b76a1b71cc71871e9a50a5ab8922abaedaf45c","tmkp:a15c5e6f60841e81b2daba33c9f8e2c0af00c99880143b2ace59930e616f053a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The potential neuroprotective value of sulforaphane (SFN) in Huntington's disease (HD) has not been established yet.|PMID:26096705|In this work, we determined whether the sulforaphane-neuroprotective effect in the rodent experimental model of Huntington's disease induced by QA is associated with mitochondrial function preservation.|PMID:27589053|In addition to dimethyl fumarate, Nrf2 activators such as curcumin, resveratrol, sulforaphane, masatinib, methylene blue, omaveloxolone, tideglusib, Dl-3-n-butylphthalide ide, ALKS-8700, benfotiamine, and ketogenic diet undergoing clinical trials for treating various neurodegenerative disease such as Alzheimer?s disease, Parkinson?s disease, Huntington?s disease, Friedreich?s ataxia, multiple sclerosis, amyotrophic lateral sclerosis, cataract, schizophrenia, bipolar disorder, mild cognitive impairment, depression, autism, obstructive sleep apnea, etc..|PMC7696015|Sulforaphane enhances proteasomal and autophagic activities in mice and is a potential therapeutic reagent for Huntington?s disease.|PMC6433839|Liu Y, Hettinger CL, Zhang D, Rezvani K, Wang X, .. (2014) Sulforaphane enhances proteasomal and autophagic activities in mice and is a potential therapeutic reagent for Huntington's disease.|PMC4096754","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9326475472","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"52734739":{"subject":"PUBCHEM.COMPOUND:36811","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:24744818","PMC5471434"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:bc93166472ca89ad8c59a2192f85d6d453eb9f2a7f87418ecdeb441aecdbef4d","tmkp:64515a9b6d10fc34194701b2f7b34e6941d35fc2b729108ee3f7addf0a381706"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99939865","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Right ventricular dysfunction in the R6/2 transgenic mouse model of Huntington's disease is unmasked by dobutamine.|PMID:24744818|Right ventricular dysfunction in the R6/2 transgenic mouse model of Huntington's disease is unmasked by dobutamine|PMC5471434","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"74519983":{"subject":"PUBCHEM.COMPOUND:4912","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9993246875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:30186318","PMC6696321","PMC6112232","PMID:23333792"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Antidepressant Effects of Probucol on Early-Symptomatic YAC128 Transgenic Mice for Huntington's Disease.|PMID:30186318|Antidepressant effects of probucol on early-symptomatic YAC128 transgenic mice for Huntington?s disease |PMC6696321|Antidepressant Effects of Probucol on Early-Symptomatic YAC128 Transgenic Mice for Huntington's Disease |PMC6112232|This study evaluated and compared the potential protective effects of probucol and succinobucol, two lipid-lowering compounds with anti-inflammatory and antioxidant properties, on oxidative stress and mitochondrial dysfunction induced by 3-nitropropionic acid (3-NP, a succinate dehydrogenase (SDH) inhibitor largely used as model of Huntington's disease) in rat brain mitochondria-enriched synaptosomes.|PMID:23333792","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:110c01c7fd6b6200f608196670cdb08d5ba5f439978383bb0abe8ced7bdfdd30","tmkp:956e7e9eca231c6af8bfeab1906dd1d64834b9510619c599e71732d1bfc864e3","tmkp:a29cdf8ab146e8b6384d62486814845e9588247a4934bf3b72cbf637a318741d","tmkp:5dda1fcf631f7418946ad24ae9ae68da653ae87c8876c59fc73bd7a53850fc23"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"65320318":{"subject":"PUBCHEM.COMPOUND:750","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"The clinical effects of milacemide, a glycine prodrug, were studied in seven patients with Huntington's disease under double-blind, placebo-controlled 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treatment reduces motor and neuropsychiatric phenotypes in the zQ175 mouse model of Huntington disease|PMC7755709|Metformin treatment reduces motor and neuropsychiatric phenotypes in the zQ175 mouse model of Huntington disease|PMC7369111|Metformin treatment reduces motor and neuropsychiatric phenotypes in the zQ175 mouse model of Huntington disease |PMC6549163|Metformin treatment reduces motor and neuropsychiatric phenotypes in the zq175 mouse model of huntington disease|PMC8160983|Metformin treatment reduces motor and neuropsychiatric phenotypes in the zQ175 mouse model of Huntington disease|PMC7401865","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9970732679090909","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"27628836":{"subject":"PUBCHEM.COMPOUND:3032771","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"In addition to dimethyl fumarate, Nrf2 activators such as curcumin, resveratrol, sulforaphane, masatinib, methylene blue, omaveloxolone, tideglusib, Dl-3-n-butylphthalide ide, ALKS-8700, benfotiamine, and ketogenic diet undergoing clinical trials for treating various neurodegenerative disease such as Alzheimer?s disease, Parkinson?s disease, Huntington?s disease, Friedreich?s ataxia, multiple sclerosis, amyotrophic lateral sclerosis, cataract, schizophrenia, bipolar disorder, mild cognitive impairment, depression, autism, obstructive sleep apnea, etc..|PMC7696015","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7696015"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e7bd7b9546da99414b0d52c34fbc82a1fbb1eb8e41748014b6be7632fd1433ee"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995178","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"93801176":{"subject":"PUBCHEM.COMPOUND:1614","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:ad8ec65da25f1d94fa526a2240af7a42afb2fc0e39b0e832a82a7c3166845331","tmkp:1b6cf36b3bc8f4394aedec7ed1ef044a351b77914256c16c8a8832cebcecc689"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9743446499999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4539940","PMC5361515"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Schematic diagrams show published protocols for the generation of midbrain dopamine (mDA) neurons for the potential treatment of Parkinson's disease, striatal neurons for the treatment of Huntington's disease and glial precursors for the treatment of demyelinating disorders.|PMC4539940|MDA, the end product of lipid peroxidation is considered as an effective target for ameliorating Huntington's disease-like disorders (Dalle-Donnea et al., 2003).|PMC5361515","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"44269376":{"subject":"PUBCHEM.COMPOUND:896","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Melatonin treatment has been used in a rat model of Huntington disease induced by 3-nitropropionic acid, a mycotoxin that inhibits the mitochondrial succinate dehydrogenase or complex II.|PMC3001212|Melatonin can easily cross the blood-brain barrier (BBB), and many pre-clinical and clinical studies hypothesize that it can act as a novel neuroprotective agent, and mitigate brain injuries in a variety of neurological diseases such as Alzheimer's disease (AD), traumatic brain injury, stroke and Huntington's disease.|PMC8207287|It is not yet known, however, whether melatonin provides neuroprotection in genetic models of Huntington's disease (HD).|PMID:21994366|It is not yet known, however, whether melatonin provides neuroprotection in genetic models of Huntington?s disease (HD).|PMC3213696|In this article, the several mechanisms through which melatonin exerts neuroprotective actions in neurodegenerative disorders such as Parkinson's disease (PD), Alzheimer's disease (AD), and Huntington's disease (HD) and in a number of mitochondrial dysfunction related conditions such as aging, ischemia/reperfusion (I/R), or septic shock, are 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in Huntington's disease (chorea): effect on weight, dyskinesia, and mental 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treatment for other diseases, including but not limited to neurodegenerative diseases like Parkinson disease and Huntington disease as well as several highly-prevalent mental health disorders such as depression and anxiety, any cardiac remodeling involving 5-HT represents clinically significant processes with important ramifications.|PMC7288848|Additionally, SSRIs or serotonin alone, have been neuroprotective in animal models of Parkinson?s disease, Alzheimer?s disease, and Huntington?s disease.|PMC4267991|In addition, the downstream metabolite 3-hydroxykynurenine has also been widely reported to be increased in multiple serotonin deficiency-related neurodegenerative disorders including Alzheimer?s disease, Parkinson?s disease and Huntington?s 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also found that the ?dopaminergic stabilizer? pridopidine (structurally similar to the S1R agonist R(+)-3-PPP), is a high-affinity S1R agonist and is synaptoprotective in a mouse model of Huntington disease.|PMC6363865|Pridopidine (ACR16) belongs to a novel class of central nervous system compounds in development for the treatment of Huntington disease.|PMID:21586914|To assess the 1-year safety profile of the dopaminergic stabilizer pridopidine in patients with Huntington disease.|PMID:23446684|Squitieri F, Di Pardo A, Favellato M, Amico E, Maglione V, Frati L. Pridopidine, a dopamine stabilizer, improves motor performance and shows neuroprotective effects in Huntington disease R6/2 mouse model.|PMC5963017|The sigma-1 receptor mediates the beneficial effects of pridopidine in a mouse model of Huntington disease.|PMID:27818324","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6363865","PMID:21586914","PMID:23446684","PMC5963017","PMID:27818324"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"74614812":{"subject":"PUBCHEM.COMPOUND:4649","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"An interaction between PAS and human movements suggests that neuroplasticity induced by PAS could be related to motor learning in such clinical conditions as Parkinson's disease (Morgante et?al.; Ueki et?al.), schizophrenia (Daskalakis et?al.; Frantseva et?al.), and Huntington's disease (Orth et?al.).|PMC4212109|Euthanasia and physician-assisted suicide (PAS) by request and/or based on an advance directive are legal in The Netherlands under strict conditions, thus providing options for patients with Huntington's disease (HD) and other neurodegenerative diseases to stay in control and choose their end of life.|PMID:23264360|In the literature there are few reports on euthanasia or physician-assisted suicide (PAS) or other matters concerning the end-of-life in patients with Huntington's disease (HD), although clinical experience suggests these issues do arise.|PMID:25062680","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c6998795dab2a3ca19f0342d9c84d9684ea3bea59ea934798e79cddae6e54032","tmkp:0d6519e785175cd7b3c51509ff000de316cfd094ce3ba5f89f826dadae092f22","tmkp:d3805573587c44b39cc3fc2bb905aebed7e09bcd1db230091fe248c9d9417b6b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9974031466666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC4212109","PMID:23264360","PMID:25062680"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"82572425":{"subject":"PUBCHEM.COMPOUND:2913","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Apomorphine, 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one hand, minimal studies involved the neuroprotective effect of agmatine reported in some areas, such as brain hemorrhage, or Huntington's disease.|PMC6251039","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"18576016":{"subject":"PUBCHEM.COMPOUND:2477","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:8140199","PMC3677041","PMC3677041","PMID:9217410","PMID:8010374"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Treatment of aggression in juvenile-onset Huntington's disease with buspirone.|PMID:8140199|Treatment of aggression in juvenile-onset Huntington's disease with buspirone.|PMC3677041|Buspirone in the management of disruptive behaviors due to Huntington's disease and other neurological disorders.|PMC3677041|Buspirone in the management of disruptive behaviors due to Huntington's disease and other 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alteration in circulating levels of PRL, GH, TSH, and cortisol was studied after the oral administration of muscimol (3-hydroxy-5-aminomethylisoxazole) to human subjects with Huntington's disease (n = 4) and chronic schizophrenia (n = 5).|PMID:162520|Huntington's disease: Treatment with muscimol, a gaba-mimetic drug|PMC2854970|Muscimol, a gamma-aminobutyric acid (GABA) analogue that exerts potent and specific agonist effects on GABA receptors, was administered orally to 10 patients with Huntington's disease.|PMID:152602","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c37aba4f26492cbf60ae6bff7ab906d9e476d26a1af455cb5057bc3c2e3f013c","tmkp:adb4c92d5417a2e00e4414bb13b3ee81f99ad6b4d7fcdafb0ff95e319324bb83","tmkp:60d400cfcaedf4b70d4c8f085f30ca77f22a9890cc93b5dfba3feebef0f284aa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"105061379":{"subject":"PUBCHEM.COMPOUND:6305","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9709909299999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:27114543","PMID:16573644"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Here, we find that increased levels of KYNA relative to 3-HK are likely central to the protection conferred by TDO inhibition in a fruit fly model of Huntington's disease and that TRP treatment strongly reduces neurodegeneration by shifting KP flux toward KYNA synthesis.|PMID:27114543|The tryptophan load restored 5-HIAA to baseline levels in controls and patients with brain injury, but not in those with Huntington's disease, in whom 5-HIAA remained significantly 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is now being tested clinically for treating a number of disorders including L-dopa induced dyskensias in Parkinson's disease and in Huntington's disease (see 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a mouse model of Huntington's disease, which has progressive disruption of sleep/wake rhythms with age, reversal of the cognitive decline and survival rate can be achieved by a timed delivery of the benzodiazepine alprazolam, which reinstitutes a daily cycle of sleep [, 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Moussa serves as an investigator on Nilotinib trials in Parkinson?s diseases, Alzheimer?s disease, and Huntington?s disease.|PMC6417280|Besides AD, low dose of Nilotinib also being tested for Amyotrophic Lateral Sclerosis and Huntington?s disease.|PMC7092971|Interestingly, Nilotinib (Tasigna?) is in clinical trials for Parkinson?s disease and Huntington?s disease, but its potency has not been evaluated in any of the rodent models of neurodegenerative illnesses.|PMC7794371","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994338866666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6417280","PMC7092971","PMC7794371"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:1a797d9b79c961731300a833e71cd8b3b1dbabb6197b8fa81f16cf77b03270de","tmkp:f88a37bc9850703ec1147297f7adb1f959a158be482a9b34c7501d176151f494","tmkp:26fa3aaa321af0ab94a92695b2b2b395a09c9da6e9dcb08bfe49a4a99cb66a21"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"69219201":{"subject":"PUBCHEM.COMPOUND:7151","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:11571498"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The response to topical aqueous methyl nicotinate solution was recorded at 5 min intervals over 20 min in six in-patients with advanced (stage III) Huntington's disease and in 14 age- and sex-matched normal individuals with no history of this or any other major neurological disorder.|PMID:11571498","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9993387","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:bace339cb161f960c3144b5b0b48e22d67d43d07d5b1ee432e708d27d6fd6e95"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"91669141":{"subject":"PUBCHEM.COMPOUND:445154","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:sri-reference-kg","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"70793328":{"subject":"PUBCHEM.COMPOUND:681","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:93533256db65235ce1a4c8059f5dd6a3a09b74d7c1bedbe5d0aadf913b60162b","tmkp:9c07f5fce9a15cbb025e3d039255439b4e4592ad47a0f0dc80b374e4481ce732","tmkp:cf2cd0379568d23c94149e722dbc069606ab4cc74c59df2e422bd3283c949267","tmkp:18993fe1e8f3998d862c39441d30416d85d4f7f639a9c60e241147ee3961f9a5","tmkp:bee2981df6ac198e0f8997c1085507cdf89dce5f281636f0d6252e6416f18581"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Dopamine receptors are the primary targets in the treatment of schizophrenia, Parkinson's disease, and Huntington's chorea, and are discussed in this review by Philip Seeman and Hubert Van Tol.|PMID:7940991|Dopamine-related drugs may be therapeutic to patients with striatal neurodegeneration, such as Huntington's disease (HD) and Parkinson's disease (PD), but these drugs have unwanted side effects.|PMC5142824|Dopamine modulates the susceptibility of striatal neurons to 3-nitropropionic acid in the rat model of Huntington's disease.|PMID:9822765|Dopamine modulates the susceptibility of striatal neurons to 3-nitropropionic acid in the rat model of Huntington's disease|PMC5361515|Dopamine modulates the susceptibility of striatal neurons to 3-nitropropionic acid in the rat model of Huntington's disease|PMC4176035","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:7940991","PMC5142824","PMID:9822765","PMC5361515","PMC4176035"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.994003208","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"51741534":{"subject":"PUBCHEM.COMPOUND:5284616","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:sri-reference-kg","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"103698156":{"subject":"UMLS:C0032254","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Combination of lycopene, quercetin and poloxamer188 alleviates anxiety and depression in 3-nitropropionic acid-induced Huntingtons disease in rats|PMC7401865|The present study investigates synergistic effect of combination treatment of lycopene, quercetin and poloxamer188 in 3-nitropropionic acid (3-NP)-induced Huntington?s disease (HD).|PMC4576812|The present study investigates synergistic effect of combination treatment of lycopene, quercetin and poloxamer188 in 3-nitropropionic acid (3-NP)-induced Huntington's disease (HD).|PMID:26401371","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:5d6a15066b06ab0d3da947fbb774b0c6ce46a63d8ff1f34dbcde128c946d985e","tmkp:3e86377259c65716c646a03345330b5fc12a9104f14dea8448a5b43d7d863128","tmkp:82bd75dd0c9cf920092322c9adede9bb9062de48fce45ec698f030dafb33c93a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9984888999999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7401865","PMC4576812","PMID:26401371"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"72005444":{"subject":"PUBCHEM.COMPOUND:2520","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC3955168","PMC6472390","PMC6472390"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994842833333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Nearly all of these compounds are FDA-approved drugs for different indications, and of these, verapamil, had been identified in a screen for drugs that induced autophagy with beneficial effects in cell, fly and zebrafish models of Huntington?s disease.|PMC3955168|We have previously observed that verapamil was beneficial in our zebrafish model of Huntington?s disease.|PMC6472390|Furthermore, verapamil rescued mutant huntingtin toxicity in Drosophila and zebrafish models of Huntington?s disease, where it also reduced huntingtin aggregate numbers.|PMC6472390","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:998dbcac1cb8006d9e3bc19de1bf000f47df2173d9fa2b269cce6765937adf2d","tmkp:2d7e5f8eadaf9640b95e8f2978ba17a973587a69f51557a0caa61dbe2fa0cff8","tmkp:2724c8e561126c660b38f7c55397cbff4a826de96e521ab0acdf4d5090fd7ffa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"127170556":{"subject":"PUBCHEM.COMPOUND:65064","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9990569976190476","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The polyphenol (-)-epigallocatechin-3-gallate (EGCG) has recently attracted much research interest in the field of protein-misfolding diseases because of its potent anti-amyloid activity against amyloid-beta, alpha-synuclein and huntingtin, the amyloid-fibril-forming proteins involved in Alzheimer's, Parkinson's and Huntington's diseases, respectively.|PMID:19616561|Green tea (?)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models.|PMC2835767|EGCG is a naturally occurring flavonoid extracted from green tea that has shown promise as a possible therapeutic for amyloid related diseases, entering early clinical trials for the prevention of Alzheimer's, Parkinson's, and Huntington's disease and is currently one of the best studied natural products against amyloid aggregation.|PMC4662995|Clinical trials are underway using green tea extract or EGCg in diseases other than DMD (Alzheimer?s disease, Huntington?s disease, multiple sclerosis, HIV, small cell carcinoma; http://www.Clinicaltrials.gov).|PMC3486431|EGCG also reduces photoreceptor degeneration and improves motor function in a Drosophila model of Huntington?s disease.|PMC4697862","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9aebec23e9fe6a685ad675a7b09e6b3b26de0b9f5017c2e2fd5e621935a2f991","tmkp:30475420b4562af6055735e4dbb0de3978754826ae982b1f7b6817346fbe7c1d","tmkp:4d19ad845a0f1d17610df34280df59e6061c34782dcab82491a1b6a774a6cc8c","tmkp:ea71e735e808dfb640ab3fa52a89a0c32c4cc20f0abc7459e14c9b86168e9956","tmkp:146f6674580ff652b71f6a860e1b91b1ceb32356d9fab0076623b71b0bf7da1b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:19616561","PMC2835767","PMC4662995","PMC3486431","PMC4697862"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"89919516":{"subject":"PUBCHEM.COMPOUND:5281040","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Several experimental reports have also demonstrated the neuroprotective effects for montelukast and other members of the same class of drugs in various neurodegenerative conditions such as acute and chronic ischemic brain injury, traumatic brain injury, Huntington disease-like symptoms, ischemia-reperfusion-induced vasculitic neuropathic pain, spinal cord injury, and experimental autoimmune encephalomyelitis.|PMC4384514","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4384514"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b0183703f06176e811fb0f031c8487385e2224916c67d3e41dd2250409552dc2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9994854","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"35650320":{"subject":"UMLS:C0873138","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Gintonin, a ginseng-derived ingredient, as a novel therapeutic strategy for Huntington's disease: Activation of the Nrf2 pathway through lysophosphatidic acid receptors.|PMID:30853569|Various studies have reported that ginseng and ginkgo protect against injury in numerous neurological diseases, including Parkinson?s disease, Alzheimer?s disease and Huntington?s disease.|PMC6929202|Different studies have revealed that the components of Panax ginseng, especially the ginsenosides Rb1, Rb2, Rb3, Rc, Rd, Re, Rg1, Rg2, and Rg3, have significant therapeutic effects (Fig. 9) in various neurological disorders, such as memory, anxiety, depression, epilepsy, stroke, amyotrophic lateral sclerosis, AD, PD, and Huntington disease (Table S9).|PMC8020288|Gintonin, a ginseng?derived ingredient, as a novel therapeutic strategy for Huntington's disease: Activation of the Nrf2 pathway through lysophosphatidic acid receptors |PMC6974717|This review considers publications dealing with the various actions of P. ginseng that are indicative of possible neurotherapeutic efficacies in neurodegenerative diseases and neurological disorders such as Parkinson?s disease, Alzheimer?s disease, Huntington?s disease, and amyotrophic lateral sclerosis and multiple sclerosis.|PMC3659610","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:30853569","PMC6929202","PMC8020288","PMC6974717","PMC3659610"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:bc5e301f5320180af9dec8701b703c5a378b988f55d5cb735fd2ed4971884f55","tmkp:4a0e1a46ed9e0b5373037f461520f8b1035cf9645bd7da39d9722103e0d12322","tmkp:3c374cebee1c179e30dc1a4e87e9dd96fa501d1d5fa52925f555f5b50678922e","tmkp:187b176e86d3fa901d4a68dfc1d70b253b9b73c1781c2d81339241036121f303","tmkp:7bcd7461e2714c8e809130b97554ceee0c8b2e55db544db06c542149bb60318e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.996294504375","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"27921651":{"subject":"PUBCHEM.COMPOUND:5090","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:2bbe4e282b5bcefa812186eec6ef0372f984e904cc47a754aabbe271ec3da399","tmkp:a19ecfc52c0e07ff37e49b0dcc3ee467d83c10b9965aaf4ddd53add7b36c49b1","tmkp:31800e2b0fe35026b703b900bb62abc12c4a2821c259152784f84f9fbf61b2f7","tmkp:d5b20fa45d8d5ac9e96d6364085ce0c60342c884936d2481dd19f6370d640798","tmkp:113011aaf705150a49d0902a7318ab8e3447d3529f8098a60865151370e5f628"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:15474369","PMC4604084","PMC7581113","PMC4604084","PMID:23562615"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.988754092","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"We examined the effectiveness of acetylsalicylate and rofecoxib as treatments for the R6/2 and N171-82Q transgenic mouse models of Huntington's disease.|PMID:15474369|One study in rats have shown that statins, together with rofecoxib, exert a synergistic neuroprotective effect against malonic acid induced Huntington's disease and related cognitive dysfunction.|PMC4604084|Synergistical neuroprotection of rofecoxib and statins against malonic acid induced Huntington's disease like symptoms and related cognitive dysfunction in rats|PMC7581113|Synergistical neuroprotection of rofecoxib and statins against malonic acid induced Huntington's disease like symptoms and related cognitive dysfunction in rats|PMC4604084|Synergistical neuroprotection of rofecoxib and statins against malonic acid induced Huntington's disease like symptoms and related cognitive dysfunction in rats.|PMID:23562615","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"120131672":{"subject":"PUBCHEM.COMPOUND:16043","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Dietary supplementation with tert-butylhydroquinone (tBHQ) was shown to attenuate the effects of 3-nitropropionic acid, a mitochondrial complex II inhibitor, in a mouse model of Huntington?s disease.|PMC3322307|Dietary supplementation with tert-butylhydroquinone (tBHQ) was shown to attenuate the effects of 3-nitropropionic acid, a mitochondrial complex II inhibitor, in a mouse model of Huntington?s 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findings reveal that exogenous administration of GPE selectively prevents excitotoxin induced phenotypic degeneration of striatal projection neurons and cholinergic and NADPH diaphorase interneurons in an animal model of Huntington's disease.|PMID:10486177|More importantly, GPE has been shown to have potent neuroprotective effects in numerous animal models of hypoxic-ischemic brain injury and neurodegenerative diseases such as Parkinson's, Alzheimer's and Huntington's diseases.|PMID:22070686|The IGF-I amino-terminal tripeptide glycine-proline-glutamate (GPE) is neuroprotective to striatum in the quinolinic acid lesion animal model of Huntington's disease.|PMID:10486177|The involvement of CPu, GPe, and SNr in movement disorders in neurological diseases, such as Parkinson's disease and Huntington's disease was widely investigated.|PMC5342481|The IGF-I amino-terminal tripeptide glycine-proline-glutamate (GPE) is neuroprotective to striatum in the quinolinic acid lesion animal model of 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aggressive effect of propranolol in a patient with Huntington?s disease |PMC4051721|Paradoxical aggressive effect of propranolol in a patient with Huntington?s disease |PMC2918785|Paradoxical aggressive effect of propranolol in a patient with Huntington's disease.|PMC3677041|Paradoxical aggressive effect of propranolol in a patient with Huntington's disease.|PMID:2957363|Episodic aggressive behavior that responded poorly to neuroleptics was reduced by a carefully titrated dose of propranolol in three patients with advanced Huntington's 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carbonic anhydrase inhibitor (CAI) methazolamide (MTZ), proved to be neuroprotective in models of Huntington's Disease (HD) and ischemic injury.|PMC4713307|The carbonic anhydrase inhibitor (CAI) methazolamide (MTZ) was identified among a library of drugs as an inhibitor of CytC release and proved to be neuroprotective in Huntington's disease and stroke models.|PMC4713307|The carbonic anhydrase inhibitor (CAI) methazolamide (MTZ) was identified among a library of drugs as an inhibitor of CytC release and proved to be neuroprotective in Huntington's disease and stroke models.|PMID:26581638|One of these drugs, methazolamide, is neuroprotective in vivo in a transgenic mouse model of Huntington disease.|PMC2674528|Nevertheless, it should be noted that methazolamide has been successfully employed previously in a transgenic mouse model of Huntington?s disease, in which intraperitoneal inoculation of the drug resulted in a significant dose-dependent delay of disease onset and mortality, 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we previously observed in a mouse model of Huntington?s disease (Ravikumar et al.,), mice treated with temsirolimus showed a decrease in immunoreactivity for phosphorylated S6 ribosomal protein, a downstream target of the mTOR pathway, whilst immunoreactivity for total S6 ribosomal protein did not change (Fig. 2A).|PMC2801325|Recent findings suggested that temsirolimus also provided beneficial effects in animal models of Huntington's disease and spinocerebellar ataxia type 3, two neurodegenerative diseases caused by accumulation of aberrant proteins within brain.|PMID:24880087|Despite this, our study demonstrates that temsirolimus may have additional therapeutic values beyond the effect previously demonstrated by pre-symptomatic treatment in a mouse model of Huntington?s disease (Ravikumar et 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particular, rapamycin protects in Huntington's disease models and evidence suggests that this is due to stimulation of autophagy.|PMC2880868|For instance, rapamycin and its analogues can increase autophagy through inhibition of the mammalian target of rapamycin (mTOR), and have recently shown beneficial effects when tested in mouse models of Huntington's disease, tuberous sclerosis, and spinocerebellar ataxia type 3. Chronic treatments with rapamycin are tolerated, and even extend lifespan in mice.|PMC2948554|However, induction of autophagy by treatment with rapamycin has proven effective in enhancing the clearance of aggregate-prone proteins in vitro and in vivo, in Drosophila models of Huntington's disease and tauopathy and mouse models of Huntington's disease and spinocerebellar ataxia type 3.|PMC3060341|However, induction of autophagy by treatment with rapamycin has proven effective in enhancing the clearance of aggregate-prone proteins in vitro and in vivo, in Drosophila models of Huntington's disease and tauopathy and mouse models of Huntington's disease and spinocerebellar ataxia type 3.|PMC3060341|Moreover, the rapamycin analog CCI-779 decreased aggregate formation and improved performance on behavioral tasks in a mouse model of Huntington?s 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urate has also been associated with Huntington?s disease (HD), and amyotrophic lateral sclerosis (ALS) 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all, these results suggest an in vivo neuroprotective role of nicotinamide in different animal models of AD and Huntington?s disease.|PMC7438969|Nicotinamide improves motor deficits and upregulates PGC-1a and BDNF gene expression in a mouse model of Huntington?s disease |PMC3722255|Nicotinamide improves motor deficits and upregulates PGC-1a and BDNF gene expression in a mouse model of Huntington?s disease |PMC3376646|Nicotinamide as a beneficial treatment for AD complements a number of emerging studies showing that Sir2 inhibitors improve pathology in other neurodegenerative diseases including Huntington?s disease and other models of polyglutamine repeat disorders and Parkinson?s disease.|PMC2617713|Comparative mitochondrial-based protective effects of resveratrol and nicotinamide in Huntington's disease 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term treatment of Huntington disease with L-glutamate and pyridoxine.|PMID:153484|In patients with Huntington's disease, on administration of isoniazid at 900 mg/day, along with pyridoxine at 100 mg/day, a 4-fold increase of both free (P less than 0.005) and conjugated GABA (P less than 0.0025) was seen.|PMID:6235893|During a randomized, double-blind, crossover, placebo-controlled clinical trial of isoniazid (plus pyridoxine) in Huntington's disease (HD), amino acids and related amino compounds were measured in both cerebrospinal fluid (CSF) and plasma utilizing a newly developed high-performance liquid chromatography ion-exchange/fluorometric assay 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open label trial of dextromethorphan in Huntington's disease.|PMID:2529964|Because of its interactions at N-methyl-D-aspartate and haloperidol specific sigma receptors, dextromethorphan may have symptomatic or protective effects in Huntington's Disease (HD).|PMID:2529964|In general, when high doses of dextromethorphan are given alone (>100 mg per day), the resultant higher dextromethorphan/dextrorphan concentrations than those associated with DM/Q have been tolerated in epilepsy (up to 150 ng/mL), neurosurgery (up to 193 ng/mL), and Huntington?s disease patients (up to 275 ng/mL) (see Table 3).|PMC4079824|An open label trial of dextromethorphan in Huntington?s disease |PMC3714141|An open label trial of dextromethorphan in Huntington?s disease 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diseases.|PMC4915971|Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases.|PMC2842438|Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases.|PMC4857623|Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases.|PMID:19476553","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:da57a1e4226e291605e8425ef1c076bf85ef06daabc748b4e725dbaf40ea8a61","tmkp:29965dbfd0d4ee53fa088e5d0dfcbb5ef29939046bd6f0044a94324541e43802","tmkp:6689e94e6ab235fb133f0d61ffb71a3c5c9b2c865b1ef8318adb3a3a8468528a","tmkp:cd4c61ea999c516ac2fb252369e83b5b8bf8d55847eeed44bebb3a11ad421734","tmkp:dccc1ec9ea198456be122bc511423dee4a5f6e987c1a4ecc352c0947652b9417"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9991521007655502","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6627360","PMC4915971","PMC2842438","PMC4857623","PMID:19476553"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"58187473":{"subject":"PUBCHEM.COMPOUND:2244","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7477891","PMC6122250","PMID:15474369"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3cb107aa62d321ae23c79854b9b932d2008533e4be0fe40d5ba6a236ba21f8e5","tmkp:1d5193d10f262349f81489b803c4afdbfe1cac3534f09110ea441147fca3957c","tmkp:d38e3c2c89dc70bd51b3533faf5d85a0eb26dc861e0ef7d9b9ec8cb4759257c8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"More broadly, aspirin reduces protein aggregation in several amyloid-based, neurodegenerative diseases, and this protection was directly linked to its ability to acetylate proteins in C. elegan models of Huntington?s disease and AD.|PMC7477891|There is also evidence to show that aspirin may play a role in fighting neurodegenerative diseases such as Parkinson, Alzheimer, Huntington disease, and mood disorders.|PMC6122250|We examined the effectiveness of acetylsalicylate and rofecoxib as treatments for the R6/2 and N171-82Q transgenic mouse models of Huntington's 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level of brain-derived neurotrophic factor mRNA is progressively reduced in rodent models of Huntington?s disease: restoration by the neuroprotective compound CEP-1347 |PMC6506160|Blood level of brain-derived neurotrophic factor mRNA is progressively reduced in rodent models of Huntington?s disease: restoration by the neuroprotective compound CEP-1347 |PMC5916827|Blood level of brain-derived neurotrophic factor mRNA is progressively reduced in rodent models of Huntington?s disease: restoration by the neuroprotective compound CEP-1347 |PMC5762114|Blood level of brain-derived neurotrophic factor mRNA is progressively reduced in rodent models of Huntington?s disease: restoration by the neuroprotective compound CEP-1347 |PMC3922377|Blood level of brain-derived neurotrophic factor mRNA is progressively reduced in rodent models of Huntington's disease: restoration by the neuroprotective compound CEP-1347|PMC4881765","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0a5592f7ec87acc4ac67fac9d46c2fa69539dc2fe17911007ad301f741061696","tmkp:5cde734a20621f2ea9483a0a8bd6f1aef96fdb2311e2127fc0220e4abe712685","tmkp:67f60ae2b6c044756a163ba366b81fedf09f35427094911e9b15338aaca4c097","tmkp:6dee66eb895e75dd327b9b48add8d959130b840b3a41f4efedd9c0b3d5950755","tmkp:a64d584a9915f68ab678cce04c63b2ef827e57610942bc53e062cdd88f7ac6be"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9994960081818182","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"21564812":{"subject":"PUBCHEM.COMPOUND:9831415","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Ethyl-eicosapentaenoic acid treatment in Huntington's disease: A placebo-controlled clinical trial|PMC5975251|Ethyl-eicosapentaenoic acid treatment in Huntington's disease: A placebo-controlled clinical trial.|PMID:26175332|Preliminary evidence suggests beneficial effects of pure ethyl-eicosapentaenoate (ethyl-EPA) in Huntington disease (HD).|PMID:16043801|Efficacy of ethyl-EPA as a treatment for Huntington disease: a systematic review and meta-analysis.|PMID:30890195|Ethyl-EPA treatment improves motor dysfunction, but not neurodegeneration in the YAC128 mouse model of Huntington disease|PMC4685469","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:03792a0687d9b5b5fa0d21ea01793dec0330f9dd6b28b3f2305a6bc4ad6dab37","tmkp:05f963244311fdbde7749f37160adc496fe97d05e87f36ff7796e3ef87786f33","tmkp:c0629bc6e29b5b5812ebcd8aa15dc4248d33ab05f7ff9a49a34a2958aa532e58","tmkp:3efa2af224bbc8369817114a4adb1155b675b6ad30221ca2320c0b64120a3037","tmkp:06c0559a9e8fccf0b156c3dc8315ec3400c8bceceaa5d8bfe9e8ab3c9f5e1961"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9992969385882353","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5975251","PMID:26175332","PMID:16043801","PMID:30890195","PMC4685469"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"87995580":{"subject":"PUBCHEM.COMPOUND:11764719","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6340342"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9993474","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"SS-31 (elamipretide) is currently being tested in clinical trials for rare disease indications, including mitochondrial myopathy, Barth syndrome, Leber hereditary optic neuropathy, and Huntington disease (stealthbt.com/clinical).|PMC6340342","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:31e58ae5d33252cb1fe1d8a81c2fc0111976cd8def0d0d9e37bbd083eadd37c3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"127017176":{"subject":"PUBCHEM.COMPOUND:708857","object":"MONDO:0016621","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"(A) C57BL/6 and ?MT mice or (B) BALB/c and JHD mice were exposed to two rounds of L3 Hp infection and drug treatment with pyrantel pamoate.|PMC2745290","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2745290"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9991652","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8996f5944f88ab91322de29b4ec3c6793c508ac18a9e0c8a8177fafde805a071"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"32479954":{"subject":"PUBCHEM.COMPOUND:108018","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:95a5818696c16f72eb4b0f4d276b96e25d36b6d9adba60d6237226cb2bcc4b57","tmkp:336fe39f4eb894b2dd4bd89c2f17383354212ab0728a72f1eea21ae09a867f7a","tmkp:c9f7108e5c2099a90e1faa4eebfdff20847fbf7b6802eea317cfd2bc7dacccd5","tmkp:b921ffe37c792035274fc0a0b9dd3460e59ae4e8d544423104fc984859f6f1f8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5743427","PMC4101776","PMC5595947","PMC3346261"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"This small molecule lead, NCT-504, is important because it appears to trigger the degradation of huntingtin, and thus falls into the hypotheses of therapies for HD designed to _specifically_ reduce or eliminate huntingtin protein in Huntington's disease, which include AAV siRNAs, and anti-sense oligonucleotides, which are either pending or are in clinical trials currently.|PMC5743427|identifier: NCT00471211) and are now under phase II clinical trial for Huntington disease as well.|PMC4101776|Pridopidine (4?[3?(methylsulfonyl)phenyl]?1?propylpidperidine; formerly known as ACR16, is an investigational drug under development by Teva Pharmaceutical Industries for treatment of Huntington's disease (HD; e.g., PRIDE?HD, NCT02006472).|PMC5595947|NCT00920946: A safety and efficacy study of Dimebon in patients with huntington disease (HORIZON)|PMC3346261","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9936421","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"29883567":{"subject":"PUBCHEM.COMPOUND:10954115","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.973631","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:87895b5adc830fdb98476a4c8887a05e6ddcb8c1eb2a266a7d0724949a56a72f","tmkp:ae718f4cb126cb0a9aae05fd4489730b1a0f1e5ec06fe4a3874fc910f5afdd77"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4706313","PMC5676851"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Normal glucose, insulin, and growth hormone responses to oral glucose in Huntington's disease|PMC4706313|Normal glucose, insulin, and growth hormone responses to oral glucose in Huntington's disease|PMC5676851","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"128064343":{"subject":"PUBCHEM.COMPOUND:31101","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Effects of bromocriptine in Huntington chorea.|PMID:7938569|The authors tested the effects of 2-Br-ergocriptine (bromocriptine, CB-154), a drug which exerts a mixed agonist-antagonist activity on the dopaminergic receptors, in 12 patients with Huntington Chorea in a double-blind crossover trial.|PMID:141860|Apomorphine, bromocryptine, lysuride, diazepam and cyproheptadine were administered to 11 patients with Huntington's disease (HD).|PMID:6210644|The effects of bromocriptine (BC) on choreiform movement were compared with those of bromperidol (BP) and fluphenazine (FLZ) in a patient with Huntington 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N, Peng Q, Li Q, Jiang M, Liang Y, Wang X, Zhao M, Wang W, Ross CA, Duan W (2008) Tiagabine is neuroprotective in the N171-82Q and R6/2 mouse models of Huntington's disease.|PMC2945295|Tiagabine is neuroprotective in the N171?82Q and R6/2 mouse models of Huntington?s disease.|PMC3404089|Tiagabine is neuroprotective in the N171-82Q and R6/2 mouse models of Huntington's disease.|PMID:18395459|Tiagabine is neuroprotective in the N171-82Q and R6/2 mouse models of Huntington's disease.|PMC3031519|Tiagabine is neuroprotective in the N171-82Q and R6/2 mouse models of Huntington?s disease 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ameliorates behavioral, biochemical and cellular alterations in quinolinic acid induced neurotoxicity: Possible role of peroxisome proliferator activated receptor-? 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(RG) is a drug of thiazolidinediones (TZDs) class that has demonstrated positive effects in various investigations related to brain pathologies, including in vivo studies of Alzheimer?s disease, models of Parkinson?s disease and Huntington?s disease.|PMC5796062|Neuroprotective effects of PPAR-gamma agonist rosiglitazone in N171-82Q mouse model of Huntington?s disease.|PMC6722212|Neuroprotective effects of PPAR-gamma agonist rosiglitazone in N171-82Q mouse model of Huntington?s disease |PMC4901333|Neuroprotective effects of PPAR-gamma agonist rosiglitazone in N171-82Q mouse model of Huntington?s disease |PMC6941053|Neuroprotective effects of PPAR-gamma agonist rosiglitazone in N171-82Q mouse model of Huntington's 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phase II, open-label evaluation of cysteamine tolerability in patients with Huntington's disease.|PMID:25475049|Cysteamine is known to target active site cysteine residues and has been launched as a potential therapeutic for a broad range of disease indications including cystic fibrosis, neurodegenerative diseases, and Huntington?s disease, amongst others by Raptor pharmaceuticals, Mylan, and the European Institute for Cystic Fibrosis Research.|PMC6313797|CYTE?I?HD: Phase I dose finding and tolerability study of cysteamine (Cystagon) in Huntington's disease |PMC4864334|Recent work has found that cysteamine and a related agent, cystamine, have neuroprotective effects in Huntington's disease (HD) mice, through enhancing central BDNF levels.|PMID:16797865|CYTE-I-HD: phase I dose finding and tolerability study of cysteamine (Cystagon) in Huntington's 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we demonstrate as a proof-of-principle that suppression of GPCR signaling by AMD3100 can activate autophagy to reduce the accumulation of expanded polyglutamine repeats, extend survival, and ameliorate neurodysfunction in a mouse model of Huntington's disease.|PMC4421748|Finally, they demonstrate that AMD3100, a GPCR antagonist, increases the level of ATG14L and autophagic flux, and has a therapeutic effect in a Huntington disease mouse model.|PMC4421748|Lysosomal efficiency declines with age, and this decline has been implicated in age-related diseases, such as Parkinson's and Huntington's diseases, and recently, AMD.|PMC6058694|Accumulating evidence demonstrates that ferroptosis is a potential cause of many human disorders such as Alzheimer?s disease, Huntington?s disease, Parkinson?s disease, and age-related macular degeneration 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is in line with prior work showing that the same molecule was neuroprotective in a mouse model of Huntington?s disease.|PMC5466080|Several experimental reports have also demonstrated the neuroprotective effects for montelukast and other members of the same class of drugs in various neurodegenerative conditions such as acute and chronic ischemic brain injury, traumatic brain injury, Huntington disease-like symptoms, ischemia-reperfusion-induced vasculitic neuropathic pain, spinal cord injury, and experimental autoimmune encephalomyelitis.|PMC4384514|Soon after this, the EBST was employed by the same research group also in animal studies of Huntington?s disease and ischemic stroke.|PMC4525734|Also, in a mouse model of Huntington?s disease, the same inhibitor prevented striatal neuron 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patients below 60 and above 90 years, suffering from psychiatric and neuropsychiatric diseases such as Schizophrenia, Parkinsonism, Huntington's disease, Pick's disease etc, persistent endocrine disorders and other systemic disorders; and who were on psychotropic drugs including alcohol were excluded from the study.|PMC3296335|GLT-1 functional efficiency was not directly tested in this study, nevertheless, deficient glutamate uptake was observed in postmortem brain tissue taken from Huntington?s disease patients, and in ethanol-treated rats despite no changes observed in glutamate transporter levels in either 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JH, Connor T, Chopra V, Dorsey K, Kama JA, et al. (2010) The mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is not neuroprotective in the R6/2 mouse model of Huntington's disease.|PMC3882322|The mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is not neuroprotective in the R6/2 mouse model of Huntington's disease.|PMC3479314|The mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is not neuroprotective in the R6/2 mouse model of Huntington's disease.|PMC4355620|The mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is not neuroprotective in the R6/2 mouse model of Huntington's disease.|PMID:20569486|The mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is 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huntingtin (that causes Huntington's disease) or mutant forms of alpha-synuclein that cause familial Parkinson's disease.|PMC2597715","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:948e621108ea45ccd249ed07828c0f543421311216c871c8cec4094d7fbb7621"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9985662","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"27730385":{"subject":"PUBCHEM.COMPOUND:60511","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"A controlled trial of remacemide hydrochloride in Huntington's disease.|PMID:8723144|Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease.|PMID:11880489|Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington?s disease.|PMC6433839|Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease.|PMC2645678|Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's 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from medicinal plants such as triterpene, polyphenol, flavonoid, alkaloid, and glycosides have been reported to have neuroprotective effects against stroke, Alzheimer?s disease, Parkinson?s disease, and Huntington?s disease, while resveratrol, curcumin, and ginsenoside were demonstrated to possess an anti-PD effect.|PMC7779621|Improvement of neuropathology and transcriptional deficits in CAG 140 knock-in mice supports a beneficial effect of dietary curcumin in Huntingtons disease.|PMC5543676|Improvement of neuropathology and transcriptional deficits in CAG 140 knock-in mice supports a beneficial effect of dietary curcumin in Huntington's disease.|PMID:22475209|Improvement of neuropathology and transcriptional deficits in CAG 140 knock-in mice supports a beneficial effect of dietary curcumin in Huntington's disease|PMC5768890|Improvement of neuropathology and transcriptional deficits in CAG 140 knock-in mice supports a beneficial effect of dietary curcumin in Huntington?s disease 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and Cambinol are drugs in the preclinical stage of investigation, and EX-527 is in phase I and II trial for Huntington's disease and glaucoma.|PMC6505634","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99935395","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6505634"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d8d6b092c94037d16b4c34fce3a1c7ea7cad9faffb1925b0e547c0a3409bb760"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"47500837":{"subject":"PUBCHEM.COMPOUND:8481","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2f28b15e3a212de62f2d74f68bb4ca5af7dbbb0074113abb4163511a04b1a78e","tmkp:97e20d3baaef46dc7bb88d99e0c2cdddbc1753d311886fcbe4567daeff185c0d","tmkp:9dbd73f2843b7260cacf0dd019f4406687c82faed1598ad82c88c7a708dfe9b3","tmkp:e01345558b2f076062c50d77f5a7c78145e6bec5959abdad3253ff89befe3194"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9992998625","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Also, injection of ASC-E in the mouse model slowed progression of the Huntington?s disease phenotype, including weight loss and declining rotarod performance; although the molecular contents of the ASC-E that exerted these therapeutic effects was not assessed in this study.|PMC7062679|Moreover, exosomes derived from ASC ameliorated the disease progression in an in vitro model of Huntington?s disease, reducing huntingtin protein aggregates and the level of apoptotic proteins (Lee et al.,).|PMC5359305|Here, we show that ASC transplantation rescues the striatal pathology of Huntington disease (HD) models.|PMID:19938161|Im et al. investigated the influences of cell-free extracts of human ADSC (ASC-E) on R6/2 mice, which developed Huntington?s disease, and found that ASC-E induced activation of the p-CREP-PGC1? pathway and amelioration of mHtt aggregates as well as striatal atrophy in the brain of R6/2 mice.|PMC7062679","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7062679","PMC5359305","PMID:19938161","PMC7062679"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"61015005":{"subject":"PUBCHEM.COMPOUND:5360373","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.997548275","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8082113d554bf0684464de2ea14ca015b8d3ecc7efd3136d6508469432453bb6","tmkp:ac52faee87bbbdfe92d1f81538d5c0174601ce37e2718343732821c2ebe73756"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:6197197","PMID:6197197"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Ionizing radiation sensitive, mutant human lymphoblastoid cell lines derived from patients with Huntington's disease (HD), or ataxia telangiectasia (AT) both showed cross sensitivity to bleomycin, as assayed by reduced cell viability and increased frequency of chromosome aberrations compared to normal controls.|PMID:6197197|Responses of Huntington's disease and ataxia telangiectasia lymphoblastoid cells to bleomycin.|PMID:6197197","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"80731287":{"subject":"PUBCHEM.COMPOUND:5092","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9995081662068965","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:19291221","PMC4623357","PMC5962650","PMC3027647","PMID:18424161"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, we investigated whether rolipram treatment altered the degeneration of parvalbuminergic interneurons typical of Huntington's disease (Fusco et al., 1999).|PMID:19291221|Underscoring the importance of PDE4 inhibitors in disease, the PDE4 inhibitor rolipram has been reported to have potential as a neuroprotectant, as well as enhance cognition and rescue memory deficits in models of Huntington?s disease, Alzheimer?s disease, diabetes, or following brain injury.|PMC4623357|Beneficial effects of rolipram in the R6/2 mouse model of Huntington?s disease.|PMC5962650|Beneficial effects of rolipram in the R6/2 mouse model of Huntington's disease.|PMC3027647|Beneficial effects of rolipram in the R6/2 mouse model of Huntington's disease.|PMID:18424161","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:428865e4fcb2b3a3c08112dc31ed74f50438fe558794fc1ffdc05e612f6918db","tmkp:c8967939b662df5055a7ba74830ff1b810d78b1038bf2e8d545c478c87150cbd","tmkp:4d1eee858f964df8ad7ed09ec8c20f24823dc4b57984855aafe9762251996e9c","tmkp:c25ae1e352021aa78fd6f63209d9a95668748b65944eaffb7f61f1cc205c6527","tmkp:cf3b0ee4c8c4d9b39c1e48a9b6bfb1cb23dcfc1042cf77f263ec68f70dde13d9"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"44131052":{"subject":"PUBCHEM.COMPOUND:6047","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"The effects of levodopa in chronic progressive hereditary chorea (Huntington's chorea): case report.|PMID:127129|This is the first report of a patient with adult onset Huntington's disease with parkinsonism responsive to levodopa.|PMID:9771791|[Haloperidol, reserpine, l-dopa and amantidine in the treatment of Huntington chorea (author's transl)]|PMC5975251|[Haloperidol, reserpine, l-dopa and amantidine in the treatment of Huntington chorea (author's transl)].|PMID:134449|Levodopa is recommended as a therapeutic approach for patients with the hypokinetic-rigid, Westphal variant of Huntington's disease, but no guidelines are available for the case of nonrespondence to levodopa.|PMID:11852299","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e0e9b661769ee02e98c3b62d6db8223fed9e6517a20882da9142b484883dfb7b","tmkp:e316fd1c30a9e5e60f84792cabbf3d244c15fddc7069b4e211e51336a415494c","tmkp:d896660503b4366aeee800ae1689b62482746a3945174069d0b8d6020b45c53e","tmkp:5ee668c51088069be505b17d5b24950dfd8445d74cc354933332ea40ade343ec","tmkp:65e385ee888f82883f08a547c36574261faafd5e01e559593d4f5d5787fe753a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9886947511111112","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:127129","PMID:9771791","PMC5975251","PMID:134449","PMID:11852299"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"53215307":{"subject":"PUBCHEM.COMPOUND:23725625","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:53b6282b0364c4310d1dd7c67cdc244a5c77c4dbdc95e169df1c9bcaf0d57c77","tmkp:07cfee38b9f51fd63d5ba9674d4d7f440a07ee95a50761459711919e24b05943"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99930655","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC7602058","PMC7602058"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In this study, we investigated the neuroprotective effect of Olaparib, an inhibitor of PARP-1, in the mouse model of Huntington?s disease.|PMC7602058|In the present study, we used another PARP-1 inhibitor, namely, Olaparib, a drug already in use for patients with ovarian cancer, in the transgenic model of Huntington?s disease.|PMC7602058","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"22392268":{"subject":"PUBCHEM.COMPOUND:2099","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:a0994880537d87794c54ebc2ba1ee9be4ee6891743d0aa50858b4bf994192af2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Among the few prominent examples are latrepirdine (former name: dimebolin; C), a candidate for treatment of Huntington disease, the antihistaminic mebhydrolin (D), and the serotonin receptor antagonist alosetron (E) (Figure 1).|PMC3097496","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC3097496"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9987765","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"31572730":{"subject":"PUBCHEM.COMPOUND:3767","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:6458778","PMID:6235893","PMID:6460947","PMID:156313","PMC7878033"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4e2b2336d3a766992eadf88f4c8e7eed1c8d51d4a3eb3428460641c37b333f3e","tmkp:ad8402097743e34f935907cd3e53ed62746756dbdb8c3d3abfde46398f8d9cb5","tmkp:ba3aeba55845c6ab0c3b8ab67ebe3e804f3e0f5e2ed817aaa217c13fa0f9b437","tmkp:a0d813221ed31ea28810598480277bce77c712888df3656016b04123b6c0ce73","tmkp:886efdf94a54891d82649a2f421f233bd6ef5e66619e34e84e72ada751ee4140"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Isoniazid therapy for Huntington disease.|PMID:6458778|In patients with Huntington's disease, on administration of isoniazid at 900 mg/day, along with pyridoxine at 100 mg/day, a 4-fold increase of both free (P less than 0.005) and conjugated GABA (P less than 0.0025) was seen.|PMID:6235893|A double-blind clinical trial of isoniazid in Huntington disease.|PMID:6460947|Nevertheless, results are sufficiently promising to warrant further controlled trials of INH or other GABA-T inhibitors in Huntington disease.|PMID:156313|Isoniazid therapy of Huntington disease|PMC7878033","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9972813895238095","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"53785623":{"subject":"PUBCHEM.COMPOUND:2284","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c8c4b05a91869109719dfcd6080d3f77c34631f5601cbe85ce410502d18d59b4","tmkp:7c214983e36aa0fd3ebb36f598a88364bed81a992080a8919d4853f09f90d0d9","tmkp:6d53aafa2a1db45245a1e9c0f43e14ab7feb94f4f5ba249dfdd32e7d38db9635","tmkp:c3f20f07b56f8a872ea498be4d3fce40a22231dd658bd4e3949c4fc64c2c87f4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9989727350000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6549409","PMID:2524992","PMID:24333873","PMID:8501265"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Recently, a very low dose (0.01 mg/kg) of baclofen was shown to promote cell survival in a mouse model of Huntington?s disease which exhibited an improvement in behavior and enhanced activity of the ubiquitin-proteasome system.|PMC6549409|We carried out a controlled clinical trial to examine the potential of baclofen to slow the functional decline of patients with early Huntington's disease (HD).|PMID:2524992|Baclofen, a GABAB receptor agonist, enhances ubiquitin-proteasome system functioning and neuronal survival in Huntington's disease model mice.|PMID:24333873|While participating in a controlled study of baclofen as protective therapy, 39 Huntington's disease (HD) patients underwent measurements of horizontal saccade latency and velocity, repeated longitudinally over a 2-year 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disorders and neurogenesis deficits in Huntington's disease mice are rescued by fluoxetine|PMC4000963|Cognitive disorders and neurogenesis deficits in Huntington's disease mice are rescued by fluoxetine|PMC5204212|Cognitive disorders and neurogenesis deficits in Huntington's disease mice are rescued by fluoxetine|PMC2991413|Cognitive disorders and neurogenesis deficits in Huntington's disease mice are rescued by fluoxetine|PMC3251944|Cognitive disorders and neurogenesis deficits in Huntington's disease mice are rescued by 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we will overview available literature data on the neuroprotective role of niacin and its derivatives, especially focusing especially on its involvement in neurodegenerative diseases (Alzheimer's, Parkinson's, and Huntington's diseases), as well as in other neuropathological conditions (ischemic and traumatic injuries, headache and psychiatric disorders).|PMID:30813414|Animal models show niacin?s role in Huntington?s disease (HD), Parkinson?s disease, and Alzheimer?s disease.|PMC6888477","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"59222120":{"subject":"PUBCHEM.COMPOUND:119570","object":"MONDO:0042980","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:sri-reference-kg","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"60398339":{"subject":"PUBCHEM.COMPOUND:10917","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:22294053","PMID:19932584","PMC5266860","PMC7401865","PMC4163371"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:30b1c8c402f5670d41385bf26567d1366736bc85aac3faf5f3e31bd3f736ae73","tmkp:fda2d4cbb2144811ccaebc12c394427155de2fcb7c57b3c51639b6b9c8007bf6","tmkp:106cbd3dacc2ad6fff4dcd28b1d114f45adcdcacf6c9ec33a1b8a3f55e9df775","tmkp:10bd505d1872767097b37416ebbc819b6403b95352983f6081cc4d4cecebeeb7","tmkp:14ba9f4653d7d4a95756d7133736c342496b370426a4a83ba796d556554e2730"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99794484875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"While beneficial effects of carnitine have been demonstrated in animal models of Huntington's disease (HD), metabolism of carnitine has not been studied in humans with this illness.|PMID:22294053|Neuroprotective effects of L-carnitine in a transgenic animal model of Huntington's disease.|PMID:19932584|Neuroprotective effects of L-carnitine in a transgenic animal model of Huntington's disease|PMC5266860|Neuroprotective effects of L-carnitine in a transgenic animal model of Huntington?s disease |PMC7401865|Neuroprotective effects of L-carnitine in a transgenic animal model of Huntington's disease|PMC4163371","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"15280203":{"subject":"PUBCHEM.COMPOUND:3291","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:e0fd292b123058b5da1c30c366e6430496a80c0e0d0df0009e4eada690e2486f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6097874"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99952626","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Importantly, ethosuximide's neuroprotective effects are not limited to worms, as it has also been shown to be protective in a mammalian neuroblastoma cell culture model of Huntington's disease.|PMC6097874","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"11959304":{"subject":"PUBCHEM.COMPOUND:6468","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Overall, the present results suggest that pridopidine exerts anti-amnesic effects in subchronically PCP-treated mice, which may be relevant to the therapeutic potential of this compound not only in Huntington's disease (e.g., slowing functional decline) but also in other pathological conditions characterized by cognitive impairment.|PMC5902730","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3af3968840c4eb31f797dd90f6f09aa00b56029ede8074a3ecf3c699b453f84b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC5902730"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9977506","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"85020352":{"subject":"PUBCHEM.COMPOUND:6076","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:12165554"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.98352355","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Previous analyses of gene expression in a mouse model of Huntington's disease (R6/2) indicated that an N-terminal fragment of mutant huntingtin causes downregulation of striatal signaling genes and particularly those normally induced by cAMP and retinoic acid.|PMID:12165554","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f6e4d51c0812e57b186896b5db79f5f84a24cb1a8b5def106a24868e3069dd16"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"57047045":{"subject":"PUBCHEM.COMPOUND:44115","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:sri-reference-kg","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"62961621":{"subject":"PUBCHEM.COMPOUND:11272610","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5539174","PMID:28824383"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In fact, we have previously shown that, INO-1001, a PARP-1 inhibitor, displays a neuroprotective effect in the R6/2 model of Huntington?s disease (HD).|PMC5539174|In fact, we have previously shown that, INO-1001, a PARP-1 inhibitor, displays a neuroprotective effect in the R6/2 model of Huntington's disease (HD).|PMID:28824383","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9994972","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:04c0226c4d6112586749c8436d558e115a52f59163c1209f68373a6b4ef38110","tmkp:3c41c11d1eddaf15ccab2e61bb22de823313ece81595bef1c7d1c32a3ec422df"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"97302979":{"subject":"PUBCHEM.COMPOUND:1061","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.98082846","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"To our knowledge, this is the first database analysis that examines the contribution of phosphate in medications to the overall phosphate burden in HD patients from a large dialysis organization 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in Huntington's disease: the first case reports|PMC3701870|Ziprasidone in Huntington?s disease: the first case reports |PMC3705171|Ziprasidone in Huntington?s disease: the first case reports |PMC4051721|Ziprasidone in Huntington's disease: the first case reports.|PMC3677041|Ziprasidone in Huntington's disease: the first case 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JMF1907, an adenosine analog, has been demonstrated to be ENT-1 inhibitor that can increase brain extracellular adenosine levels in the striatum of mice by intraperitoneal administration and produces beneficial effects on transgenic mice with Huntington disease (HD).|PMC7773772|Targeting ENT1 and adenosine tone for the treatment of Huntington's disease.|PMID:28069792|As an inhibitory neuromodulator in the brain, adenosine modulates a variety of physiological functions including sleep, nociception, cerebral blood flow and respiration as well as many neurological disorders such as epilepsy, Parkinson disease and Huntington disease.|PMC3628342|Targeting ENT1 and adenosine tone for the treatment of Huntington's disease|PMC5869924|Targeting ENT1 and adenosine tone for the treatment of Huntington's 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cysteamine was able to reproduce the lipid-lowering effect obtained by pantethine administration to human fetal fibroblasts or rabbits and rats and was shown to have important neuroprotective effects in models of Parkinson's disease and Huntington's disease, it is possible that pantethine effect in mice is at least in part mediated by this metabolite.|PMC4684146","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9153417b8180fae65a76a6a5703a54f73cb5f0821280d917efa5678a2b0dc0ba"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"103270437":{"subject":"PUBCHEM.COMPOUND:107970","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC7902029","PMID:24301680","PMC5649462","PMC7734581","PMC8021391"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9987590194736843","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3e38b9b615fecd1fee74e8e869770357cef23f99030e6c5fd2b43eee6bbbc1f1","tmkp:a2be15cd5a858b4d11f53be1f1fc48a0d13d45c0f3a39d1c9fc824a1c4a21fff","tmkp:0095b804100dd1926ebc777bc199c04bc5e5128db330ac6ca9f5b5c93f0a43cc","tmkp:031cf024c64fd414d6b30fbfd554b0fc49a74c37bc986da18b9a62dfe4f58c24","tmkp:0c1e08fb9a64b395c3266defd54eed7158d026fde01c3ab8f672807f4be9cff0"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, other neurodegenerative or neuro-inflammatory diseases such as Parkinson?s disease, Huntington?s disease, and epilepsy also explore the use of Fingolimod as possible treatment because of its diverse anti-inflammatory and neuroprotective effects.|PMC7902029|FTY720 (fingolimod) is a neuroprotective and disease-modifying agent in cellular and mouse models of Huntington disease.|PMID:24301680|FTY720 (fingolimod) is a neuroprotective and disease-modifying agent in cellular and mouse models of Huntington disease|PMC5649462|FTY720 (fingolimod) is a neuroprotective and disease-modifying agent in cellular and mouse models of Huntington disease|PMC7734581|FTY720 (fingolimod) is a neuroprotective and disease-modifying agent in cellular and mouse models of Huntington 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repaglinide on Huntington's 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neuroprotective properties of SRT2104, an activator of SIRT1, were reported in mouse models of Huntington disease.|PMC4992043|In this study, we report that SRT2104, a small molecule Sirtuin 1 activator, penetrated the blood?brain barrier, attenuated brain atrophy, improved motor function, and extended survival in a mouse model of Huntington's disease.|PMC4284130|In this study, we report that SRT2104, a small molecule Sirtuin 1 activator, penetrated the blood-brain barrier, attenuated brain atrophy, improved motor function, and extended survival in a mouse model of Huntington's 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of intrastriatal injections of quinolinic acid and 3-nitropropionic acid for use in animal models of Huntington's disease.|PMID:9829299|The present study compared the effects of acute intrastriatal administration of quinolinic acid (QA) and 3-nitropropionic acid (3-NP), two neurotoxins used in animal models of Huntington's disease (HD), on the following behavioral and histological measures: (1) open field activity levels; (2) performance on balance beam and grip strength tasks; (3) acquisition of a radial-arm-water-maze (RAWM) task; (4) size of striatum and lateral ventricles; (5) amount of cytochrome oxidase (CYO) labeling; and (6) counts of Nissl-stained neurons and NADPH-diaphorase-labeled neurons in the striatum.|PMID:9829299|Lesioning of the striatum in rodents using the excitatory amino acid agonist, quinolinic acid (QA), effectively mimics the human neuropathology seen in Huntington's disease.|PMID:10486177|Comparison of intrastriatal injections of quinolinic acid and 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collaborators, Prof David Rubinsztein and coworkers at Cambridge University, using their zebrafish larvae models of tauopathies and Huntington?s disease, showed that treatment of these fish with sildenafil for four days reduced the levels of the mutant tau and huntingtin.|PMC8224753|In this study we tested whether phosphodiesterase 5 (PDE5) inhibitors, sildenafil and vardenafil, would afford protection against 3-nitropropionic acid (3NP), which produces striatal lesions that closely mimic some of the neuropathological features of Huntington's Disease (HD).|PMID:20109548","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"15527754":{"subject":"PUBCHEM.COMPOUND:1646","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7358344"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dd5dae480fd46dcf61f6b2c5451089e9cffe71c7d66360529d92816c705bad7e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"In addition, it would be helpful to explore tramiprosate benefits in other neurodegenerative disorders which present dysfunction in cholinergic neurons and cholinergic transmission in the brain, such as Huntington's disease.|PMC7358344","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995016","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"23095942":{"subject":"PUBCHEM.COMPOUND:54675783","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Minocycline crosses the blood brain barrier, and its use as a neuroprotectant has been explored in several neurodegenerative conditions as well as in rheumatoid arthritis and Huntington disease.|PMC7470188|The efficacy of minocycline in Huntington disease treatment has been extensively debated over the last decade.|PMC3461214|These actions of minocycline are thought to be responsible for the success of the compound in reducing the ultimate brain injury in models of Parkinson?s disease, Huntington?s disease, amyotrophic lateral sclerosis (ALS), and ischemic events such as traumatic brain injury, focal cerebral ischemia, and global cerebral ischemia.|PMC3169090|Minocycline and other tetracycline derivatives: A neuroprotective strategy in Parkinson?s disease and Huntington?s disease |PMC6400111|Minocycline and other tetracycline derivatives: a neuroprotective strategy in Parkinson?s disease and Huntington?s disease 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example, the FDA recently granted IND approval for DNP to re-enter the clinic as a potential therapeutic for patients with Huntington?s disease, and niclosamide and nitazoxanide are FDA-approved anti-parasitic drugs that were discovered to have mitochondrial uncoupling 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have recently attracted much research interest because of the effects on aging diseases, which are always associated with amyloid fibril formation, for example, Alzheimer's, Parkinson's, and Huntington's diseases.|PMID:25934110|Ginsenosides protect striatal neurons in a cellular model of Huntington's disease.|PMC3659610|Ginsenosides protect striatal neurons in a cellular model of Huntington's disease.|PMID:19185022|Ginsenosides protect striatal neurons in a cellular model of Huntington?s disease |PMC4299449|Ginsenosides protect striatal neurons in a cellular model of Huntington?s disease 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a non-selective blocker of GJs, carbenoxolone, is in preparation for clinical trials for neuroprotection in Huntington?s disease.|PMC5805564|Finally, while carbenoxolone is FDA approved for the treatment of gastrointestinal ulcers and inflammation and is widely known to block pannexin channels, it also blocks connexin channels at high concentrations and has even entered clinical trials for Huntington?s disease (see Oxalys Pharmaceuticals, http://drugprofiles.informa.com/drug_profiles/24384-oxd-4|PMC6461534","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c81648a019390ef7a5fa114eefd3604836dd1e73b43a8889ca962a30db23906b","tmkp:d42a5365f056e23475802afb040bcaf7ad0697007083a358ac376c69b99adc11"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"3461839":{"subject":"PUBCHEM.COMPOUND:5437","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:aa6353c627f0b15dcdac2b0b698a13e794ed2fc3bb2f3831709aee9dfc95404d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9790051","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:26362846"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Using 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striatum).|PMID:26362846","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"110026562":{"subject":"MESH:D008094","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:sri-reference-kg","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"117736617":{"subject":"PUBCHEM.COMPOUND:4843","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:71781849dd3dd90a2c4fcdb1cf5f86c507eea42631820f26d5821ebce91cb1e8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"[The 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dantrolene has been shown to have neuroprotective effects in multiple models of neurodegenerative disorders like Huntington?s disease (Chen et al.,) and Alzheimer?s disease (Wang et al.,; Liang and Wei,).|PMC7378956|Dantrolene is neuroprotective in Huntington's disease transgenic mouse model.|PMC4543576|Dantrolene is neuroprotective in Huntington's disease transgenic mouse model.|PMID:22118545|Dantrolene is neuroprotective in Huntington's disease transgenic mouse model.|PMC6585245|Dantrolene has been demonstrated to be neuroprotective in many neurodegenerative diseases, including cerebral ischemia, Alzheimer?s disease, Huntington?s disease, spinocerebellar ataxia type 3, seizure, and trauma.|PMC7505009","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"39706228":{"subject":"PUBCHEM.COMPOUND:10114","object":"MONDO:0007739","predicate":"biolink:ameliorates","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:21909362"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"16723108":{"subject":"PUBCHEM.COMPOUND:54670067","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9987665985714286","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC3037964","PMC3037964","PMC3944243","PMID:19162177","PMC3866341"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3dedff84e83ec5209dc8b9cf42698a072aef394409a4ee947e18a546f293a85c","tmkp:558640bcff1ead247760703d18f1fac496ff092d98a23fc628e9a5bfd6d9d28b","tmkp:b2099bc6d43f2dbfa37faececb24fb8bf880bc03a8ecb7b84d4a097859ef97d2","tmkp:9df423b2816c7d374deb9807c788605de05869f6ab193e0c2d8c48d27b19123e","tmkp:eb2b7369f90a3728ab83c79c2c37cfd687b9fb8d75e75821c8c759e808720344"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Ascorbic acid ? also known as Vitamin C ? has shown neuroprotective effects in neuronal cell cultures and animal models of Alzheimer, Parkinson and Huntington disease.|PMC3037964|Ascorbic acid ? also known as Vitamin C ? has shown neuroprotective effects in neuronal cell cultures and animal models of Alzheimer, Parkinson and Huntington disease.|PMC3037964|As vitamin C acts as a vital antioxidant molecule in the brain and neurodegenerative diseases typically involve high levels of oxidative stress, a number of reports have suggested that vitamin C has potential therapeutic roles against AD, ischemic stroke, Parkinson's disease and Huntington's disease.|PMC3944243|Neurodegenerative diseases typically involve high levels of oxidative stress and thus ascorbate has been posited to have potential therapeutic roles against ischemic stroke, Alzheimer's disease, Parkinson's disease, and Huntington's disease.|PMID:19162177|Several experiments using animal models of excitotoxic neurological disorders, such as Huntington's disease, showed neuroprotective effects of vitamin C. Vitamin C protected cultured neurons from the toxic effects of excessive glutamate action, which is also related to nociception, by acting at the NMDA receptor reduction-oxidation 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provides a unique opportunity to explore novel treatment strategies and design future drugs for the effective treatment of lysosome-related diseases especially lysosomal storage disorders (LSD), cancer, inflammatory, neurodegenerative conditions (Parkinson's, Alzheimer's and Huntington's diseases) and autoimmune diseases.|PMID:28862054|Here, we review how our understanding of microglia's involvement in promoting or limiting the pathogenesis of diseases such as amyotrophic lateral sclerosis, Alzheimer's disease, Huntington's disease, multiple sclerosis, X-linked adrenoleukodystrophy (X-ALD) and lysosomal storage diseases (LSD) has changed over time.|PMID:25107477|Here, we review how our understanding of microglia?s involvement in promoting or limiting the pathogenesis of diseases such as amyotrophic lateral sclerosis, Alzheimer?s disease, Huntington?s disease, multiple sclerosis, X-linked adrenoleukodystrophy (X-ALD) and lysosomal storage diseases (LSD) has changed over time.|PMC4131134|Furthermore, these impairments are associated with several disorders, such as amyotrophic lateral sclerosis, Alzheimer?s disease, Huntington?s disease, multiple sclerosis, X-linked Adrenoleukodystrophy (X-ALD), and Lysosomal Storage Diseases (LSD).|PMC7253822","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0f521705c024812b08e635147eac504f9ff0b4e3be91a171b653734b88323993","tmkp:0691ff262f714756418b4267bd4c322fa562b4301adfa8ac138507647a6267b9","tmkp:a63962854300f2ca5ceb73b99fbbea6b815c00a695bc721df595b89727f83c62","tmkp:ae8af7f8e7f67b07859243f54f6150088546d39595abaf260001bcb49b57e8ec"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"23491827":{"subject":"PUBCHEM.COMPOUND:69286","object":"MONDO:0007739","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5625655","PMC5222822","PMID:25568297","PMC6137430","PMC5289046"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:887b2dea5f85a94e7581587e7361af78c59c3caa0a870514f45f3771aa7621c0","tmkp:b9e2591ca0f452c6f02ec9007314a75e56aabaa0372168f777b640ca11bce1c3","tmkp:291e2f762cdfcb054707374c9328527154723593ac35845ef1fa21dbf0e28a1b","tmkp:235a59748381c40deb691bed12f4f8a7706155f37d5d9e3182c40c8fac8ed112","tmkp:3030d42ed21af377bec5f2b215ab8c8f0a26b4aee3529d3cfc959e9a765e92af"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Fanny Mochel holds a patent on the use of triheptanoin in Huntington disease and GLUT1 deficiency syndrome.|PMC5625655|For instance, triheptanoin alleviated metabolic disturbances associated with several neurological and neuromuscular disorders and improved symptoms in models of epilepsy (Willis et al.,; Thomas et al.,; Hadera et al.,), Canavan disease (Francis et al.,), autism disorders (Park et al.,) and Alzheimer's Disease (Aso et al.,) as well as patients and a mouse model of glucose transporter 1 deficiency (Marin-Valencia et al.,; Pascual et al.,; Mochel et al.,), and patients with Huntington's disease (Mochel et al.,; Adanyeguh et al.,).|PMC5222822|Based on our previous work in Huntington disease (HD) showing improved energy metabolism in muscle by providing substrates to the Krebs cycle, we wished to obtain a proof-of-concept of the therapeutic benefit of triheptanoin using a functional biomarker of brain energy metabolism validated in HD.|PMID:25568297|Triheptanoin improves brain energy metabolism in patients with Huntington disease|PMC6137430|Triheptanoin improves brain energy metabolism in patients with Huntington 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The antiepileptic activity of levetiracetam was assessed in a number of animal models of epileptic seizures. Levetiracetam did not inhibit single seizures induced by maximal stimulation with electrical current or different chemoconvulsants and showed only minimal activity in submaximal stimulation and in threshold tests. Protection was observed, however, against secondarily generalized activity from focal seizures induced by pilocarpine and kainic acid, two chemoconvulsants that induce seizures that mimic some features of human complex partial seizures with secondary generalization. Levetiracetam also displayed inhibitory properties in the kindling model in rats, another model of human complex partial seizures, both during kindling development and in the fully kindled state. 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).|PMC6729122","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:50dc1e79a2f4bf12ae80a31a3cdfed60ef2dff92aea17e6981e1673a485147a1","tmkp:3c4eaa034061f57f96ac85eb492318abc11c62842199f508cee874212480cbac","tmkp:e5aa4b13e5a626cb1b002a8803613f4eac95915e460457df138c9e0cd196af89","tmkp:022b02852d3bc37fe2865f4bef6dbc01e7f05a63d52271c11983a653438c2184"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6729122","PMC3682954"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9988244233333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"124734262":{"subject":"UMLS:C2740799","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:a00887888d7fae7e51e82e3fda2af3e62a093a5b819e2ba40ff16f4d7bc14085","tmkp:3c057e8b395b492bf9e5422af2bc11969bc7a87563a685dafdee0d70c4f5cd81","tmkp:df354578f64c52922a1e3428270dc970b5dffb23c2f08658818b4eb3e5e43e33","tmkp:8176e47dc955c25039542aca5af25619719b5fef0c95987bcfde1b10a86250f7","tmkp:2238965a92b6167755aee16ad0712cdf387ede2608eb6743eca425a2a73d56e6","tmkp:262c5c6130b16149ad7162ed46c9d61dc057a99c2f7f780eb1bf4bc9165b2f68","tmkp:e484fb1fce15b3f8350c558c6211dc7ed828f3b2f826cc1f2a7f99480eb78acf","tmkp:7f8c0bc4be26cf1f0ff5f81cde6c3a86e59cfa1843fccedc4b044789d4a4d76a","tmkp:2724e7f375dae357946334ae1440f257b67e23dfffd6d2c3c996aaa6859d024f","tmkp:2a56152afddb3d48f5aefad6fa94e600d5da45e44001d5a0d3e6ed0232909bc4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Up to date, more research showed P-glycoprotein (P-gp) overexpression and apoptotic resistance associated with the activation of cell growth signaling pathway, including PI3K-AKT, PTEN, MAPK, ERK and p53 signaling pathway are closely related multidrug resistance.|PMC5535724|Among the MAPK-targeting therapies’ resistance mechanisms described to date, reactivation of the MAPK pathway is the most frequent: it has been characterized in more than 70% of resistance cases in patients treated with BRAFi alone or with BRAFi + MEKi.|PMC6721518|To date, at least three major MAPK cascades have been described that involve the activation of ERK, SAPK/JNK, and p38 MAPK in the brain.|PMC4135138|The development of PB inhibitors represents a major advance in the field given that most of clinical grade RAF inhibitors to date elicit ERK1/2 hyperactivation in vitro and the formation of cuSCC/KA in vivo.|PMC3695051|GPER-mediated MAPK and/or PI3K activation have now been shown to occur upon estrogen treatment in many cells, and in all cases examined to date, to occur through the transactivation of the 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found that PCP may inhibit melanin biosynthesis through down-regulation of the p38 MAPK pathway in B16F10 cells.|PMC4632747|Tyrosine phosphorylation of GluN2B, Pyk2 and ERK1/2 was significantly reduced following an acute injection of PCP (Ps<0.05).|PMC3410627|PCP reduced the phosphorylation of p38 MAPK, but not ERK or JNK.|PMC4632747|Therefore, the decrease in phosphorylation of T386 in this dataset suggests ERK2 is less active after PCP treatment.|PMC4605830|After restoring STEP61 to KO cultures, PCP once again increased STEP61 (p < 0.05), decreased BDNF level (p < 0.05), and down-regulated ERK1/2 and CREB phosphorylation (p < 0.05, Fig. 2c; representative blots in Figure 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barrier.|PMID:18387950","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"93866113":{"subject":"PUBCHEM.COMPOUND:5206","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:b193fad3293b811627af9754358028fd98c57faa36ffb86a5676c643819c8125"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5025001"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.98788166","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"*Differences 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respectively).|PMC5025001","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"126436695":{"subject":"PUBCHEM.COMPOUND:5865","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:1ef8456c4b05ffe4c1c0d5f7663673ff0b383af2067a89c4c30ed8cd72f1200d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5107914"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99971336","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Treatment of 3T3-L1-derived adipocytes with prednisone decreased insulin-stimulated glucose uptake (Fig. 3a), phosphorylation of Akt (Fig. 3b), and the expression of IRS-1 (Fig. 3c), GLUT4 (Fig. 3d), and adiponectin (Fig. 3e).|PMC5107914","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"54136266":{"subject":"PUBCHEM.COMPOUND:2083","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Salbutamol effectively reduces the production of VEGF and IL-1β corresponds to a reduction in the angiogenesis, so that it may be considered as an angiogenesis regulator with potential therapeutic uses in inflammatory diseases.|PMC5615866|The observed IL-1β and VEGF inhibitory properties of salbutamol may be responsible for anti-inflammatory and anti-angiogenic effect of the agent.|PMC5615866|In addition, salbutamol decreased the production of VEGF and IL-1β.|PMC5615866|Here, we also introduced a new function for salbutamol as a potent inhibitor of VEGF-mediated angiogenesis.|PMC5615866","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:18430317","PMC5615866","PMC5588270"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8d565e98101c39b0a2ff75048531217f58f6cffd78300a8b1fb0b4d5e20c75a2","tmkp:6267fea327cf6b652954956747e697ab1cb7c99b83752e1f26742a2f97da36f6","tmkp:cb2318197f2fa511d620ec142f38da8f25780bba860c85eb4838dc76f088a514","tmkp:d83883352afcb29181c0da31110b619af2b2e53784f221daf7231bb3d6aa5ac3","tmkp:8ee1fba3ececea67c9e6001ea456b2cdd50793f40aef16e4e715de7bad027e6b","tmkp:a25b4d07f241d6ddf34efe2b7b946272fcd36902f08a4dcc9c43cb5feb7570f8","tmkp:616200c38ba78359a5b47c541af02467b71209541bb47892419972395e0ef891","tmkp:85d9ebb9937b01e28b7be9995fd6ee4890071d8d57c7bc0a2e9f1a887a53fbfb","tmkp:79e6f37fb9623d3bf449e5be309ae97826ace8a9d4505c4c75f65605c1482b89"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.999696535","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"27147273":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:cdab263c8012c6f59d4e174d47aeabfeb516ab11da746818a0a27a41df3159a1","tmkp:8df6f7819de792862f47e08dfd86cad4fe5bb4a9b2a186a6d3fb2c45d1251a05","tmkp:6ff625d046f7bf72d5872b36a34cdba69745c438c271d13b154167d54a860bc0","tmkp:53ca245c2a4184cd37c7ec1bb8a4a279c5f5f77240ebd9dd5aef1717c6c40f1d","tmkp:832aeab5ac348aab157836d554399a209dd6ef1d2a4e825136882fc1b681b576","tmkp:1c933c542a69edea1f112a0c907d783ed89bed70caf41088350ebc1bafa91b0d","tmkp:3b2822698bacf265f93673164be41cb9254f69e0a4f75d36d646fe2ac25b45b1","tmkp:8854b68b9664ab7c44c6839b8edef80ebf52291f5bce9900582ea21d5fad7c29","tmkp:8d24494fdb1ae879935eec66bad0b9b277923a1f79d42aff953156a1f89b985d","tmkp:23ec7949356676a770004b593d7a0d5ecdbdf111b68bcb74f9a35e7296717d65"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9978442000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6241369","PMC7248980","PMID:16339203","PMC3924971","PMC6010852"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Manilkara zapota leaf water extract significantly upregulated the ERK1/2 mRNA level at 24 μg/mL (P < 0.05).|PMC6241369|The case is similar to previous reports that eNOS/NO pathway partly mediates VEGF‐, PGE2‐, and Korean red ginseng water extract evoking ERK1/2 activation in ECs.27, 30, 31 |PMC6010852|However, upregulation of ERK1/2 mRNA level was noted in 24 μg/mL of Manilkara zapota leaf water extract (Figure 9), which is possibly associated with oxidative stress.|PMC6241369|Nevertheless, a water extract of adlay seed, but not a methanolic extract, has been demonstrated to activate the expression of COX-2, ERK1/2, and protein kinase C (PKC)-α in the pregnant female mice, leading to the uterine contraction and increased risk of abortion.|PMC3924971|In this study we demonstrated that local testicular heat treatment of adult monkey with water at 43 C for 30 min once daily for 2 consecutive days was capable of activating reexpression of ck-18 in Sertoli cells, which was coincident with activation of ERK1/2 and Akt kinases.|PMID:16339203","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"7890751":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Several years later the possible function for GPER was identified by demonstrating protein kinases Erk1 and Erk2 activation induced by E2, as well as by the ER antagonists ICI 182,780 and tamoxifen, in breast cancer cell lines expressing GPER but not in cell lines lacking GPER.|PMC4153070|To determine cellular responses to different magnitudes of ERK1/2 activity, we examined the effects of ERK1 or ERK2 overexpression in different human tumor or immortalized normal cell lines that stably express the tamoxifen-inducible ΔRaf-1:ER (i.e., LNCaP-ΔRaf-1:ER, HEK293-ΔRaf-1:ER, and U251-ΔRaf-1:ER).|PMC5732048|To analyze the role of Erk2 signaling in peripheral CD4 T cells, we crossed Erk2f/f mice to CreERT2 mice, and the deletion of the loxP-flanked exons of Erk2 was induced by tamoxifen (Fig. 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addition, quercetin exhibited anti-apoptotic effects by decreasing intracellular reactive oxygen species (ROS), restoring mitochondrial membrane potential (MMP) and inhibiting the Caspase-3 pathway in apoptotic rat chondrocytes.|PMID:31550528|Quercetin, a known PI3K inhibitor, prevented alcohol-induced liver injury through the phosphatidylinositol 3-kinase PI3K/Akt/NF-κB and STAT3 signaling pathways and also promoted B-cell lymphoma (Bcl2) and Bcl 2-associated X (Bax) apoptosis regulator, inhibited protein expression levels of caspase 3 and poly ADP ribose polymerase, and decreased apoptosis.|PMC7519454|EGb761, quercetin and bilobalide had dose-dependent inhibitory effects on the expression of caspase-3 in the hypoxia-reoxygenated cardiomyocytes.|PMC3053309|Quercetin ameliorates ischemia/reperfusion-induced cognitive deficits by inhibiting ASK1/JNK3/caspase-3 by enhancing the Akt signaling pathway|PMC6591520|Quercetin ameliorates ischemia/reperfusion-induced cognitive deficits by inhibiting ASK1/JNK3/caspase-3 by enhancing the Akt signaling 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in human ES cells differentiated into neural progenitors, hypoxic preconditioning for 12 h at 0.1% oxygen resulted in upregulation of HIF-1, VEGF, EPO, and Bcl-2.|PMC6126254|(2) Hyperbaric oxygen inhibits the apoptosis of nerve cells around the injury and hippocampal neurons, and reduces the loss of hippocampal neurons through up-regulating Bcl-2 and Bcl-xl expression and down-regulating Bax expression.|PMC4145948|In addition, the ratio of BAX/BCL2 also increased after adding vitamin C under conditions of 2% O2, while the gene expression level of BCL2 increased after adding vitamin C under increasing oxygen concentrations.|PMID:25519716|On a molecular level, hyperbaric oxygen therapy leads to activation of ion channels, inhibition of hypoxia inducible factor-1alpha, up-regulation of Bcl-2, inhibition of MMP-9, decreased cyclooxygenase-2 activity, decreased myeloperoxidase activity, up-regulation of superoxide dismutase and inhibition of Nogo-A (an endogenous growth-inhibitory factor).|PMID:19298750|BMSCs protected against neonatal rat hyperoxic lung injury during recovery as demonstrated by enhanced expression of AQP5 and SP-C, likely due to the suppression of alveolar cell apoptosis and lung inflammation responses to oxygen with up-regulation of the expression of BCL-2 gene and down-regulation of the expression of BAX gene and stimulation of vascular endothelial growth factor and so 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pilot study was conducted to prospectively compare symptomatic improvement following a single injection of intramuscular dexamethasone (IMD) to a 3-day regimen of oral prednisone (OP) for children with mild to moderate wheezing episodes that are responsive to nebulized medications in the Pediatric Emergency Department (PED).|PMID:9350159","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9994306","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"100401100":{"subject":"PUBCHEM.COMPOUND:135398737","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In the absence of insulin, phosphorylated Akt was increased following treatment with clozapine.|PMC3306790|The mechanisms responsible for clozapine effects are currently under investigation in our laboratory, and may also involve the increases of Akt.|PMC3306790|Similar as in cellular models, in the caudate-putamen and in the tibialis muscle of clozapine-treated C57/BL/KsJ mice, Akt phosphorylation and Ped/Pea-15 protein levels were increased and PKC-ζ phosphorylation was decreased.|PMID:21618539|Similar as in cellular models, in the caudate–putamen and in the tibialis muscle of clozapine-treated C57/BL/KsJ mice, Akt phosphorylation and Ped/Pea-15 protein levels were increased and PKC-ζ phosphorylation was decreased.|PMC3306790|In vivo treatment with clozapine, an atypical antipsychotic, activates Akt and significantly reduces NET surface levels in mouse cortical 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in vitro stimulation, the ratio of T cell IFN-g/IL-4 secretion was significantly higher in the dexamethasone group than in the hydrocortisone or control groups between 8 and 9 years of age.|PMC8217456|The ratio of T-cell mitogen-induced interferon-gamma/interleukin-4 secretion was significantly higher in the dexamethasone group than in the hydrocortisone group.|PMID:18381516|These results are in concordance with our findings, observing that, in the groups treated with Dexamethasone or DLE, we found an increased expression of IL-4 and a reduction in the expression of some proinflammatory cytokines such as IL-6 and IFN-γ.|PMC5366182|Interferon-gamma production and the ratios of interferon-gamma/interleukin-4 and interferon-gamma/ interleukin-10 were significantly higher in the dexamethasone group than the reference group.|PMID:18381516|In contrast, in the groups treated with Dexamethasone (2.05%) and DLE (1.76%), we observed a significant increase in IL-4 expression (P < 0.05) (Figure 5(b)).|PMC5366182","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:20649150f4054ce776755b46959a60bdeee1c88b53a18ec6751936ae9f8966ba","tmkp:02145b3758fe0888358c23c9b9653cc71e1a74e8247dffaf08fca86688d57efd","tmkp:c01d5627bf7d08c3a6450d1a4b408c6a4e41cd042f21e915de480f8895a545f2","tmkp:9f80954169ce564eb221cb4887d5d730e62e443353e5bec9faf7580339762ee3","tmkp:8babf3795b4a3d111350bb86ce14bb84208f8201aac0ef6b6b4ed1a20df26957","tmkp:c3997c4a4cd36790bfd6337380d2a8a0a28631d5c28474056c5667c5accf5442","tmkp:9107e46dcd109dd36faccd7cbaf779cad9eff0af5bf97c9502190dcc91b4c2c1","tmkp:9b870cd55ebf877a01b3cdd618d7a270eebc10f5503c117970b6cd5f76321358","tmkp:bccd658036b4b16eb0342746e5fb80f80f41924d80f8de1278056f9938b35dc9","tmkp:d691ba49268b03bcd1623ed408765b4c2e886f53e72fa6390641cd3a57016236"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9959398086111112","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:27279984","PMID:18381516","PMC2789531","PMID:22860470","PMC3881601","PMC5366182","PMC4887713","PMC8217456"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"56122152":{"subject":"PUBCHEM.COMPOUND:4946","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:a2c814a47556caf0f4aa9a81edce654041f8ca1c2a615f46efecb9b1052d8f1f","tmkp:f02561b2104acaec6e9b1a90202f145a8df876dca3c50caf9865184ef92c75d0","tmkp:799aa8b648acc60760eb25a2f29ffb68a612353cf75ab3f072584a9ebdfc5385","tmkp:a135a6e66909c2a3b7be21064138d67f275e38e2e638bf0b6d05ed651a94ae43","tmkp:bc759fbb61eaa1cdf65c8f05219eca037ea3d6bcdf9af7214286b700d80279fd","tmkp:877e7ad468208f729d0fd51de3404c2ca704a0c862662eb896b6abd18a9dcb5d","tmkp:651162c182ae8014eb3f25e820a8fcd8504e01d895458f32e26d8ff241b20f59","tmkp:338b95ccfb8b54c96e1ee8a9b687498627d186cfd90cbb0771d3bdb016bbcd0d","tmkp:8ad946d440aa9628a95e5c099e3da4c9b284a270cf89b6a1976b23c02dc1afaa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.998854015","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6261360","PMID:26617741","PMC7662752","PMC5865987","PMC3786814","PMC4704871","PMC7477428","PMC5356557"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Propranolol promoted poly (ADP-ribose) polymerase cleavage and decreased the expression of full-length caspase-3 in liver cancer cell lines; it induced S-phase arrest in HepG2 and HepG2.2.15 cell lines, while HL-7702 cells were arrested at the G0/G1 phase of the cell cycle.|PMC5865987|Propranolol treatment induced apoptosis in cultured liver cancer cells and promoted poly (ADP–ribose) polymerase cleavage, decreased the expression of full-length caspase 3, and induced S-phase arrest in both HepG2 and HepG2.2.15 cell lines.|PMC7662752|Propranolol may increase in the pro-apoptotic protein Bax and the decrease in the anti-apoptotic proteins Bcl-2 and Caspase3 in IH tissue.|PMC6261360|Furthermore, RACK1 RNAi and S-propranolol, separately and in combination, significantly reduced caspase-3 activity, cytochrome c release and JNK 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propose that GCH-1 mutations should be considered a genetic cause of familial PED, especially if additional clinical features of monoaminergic deficiency are present in affected individuals.|PMID:20187889","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"54020089":{"subject":"PUBCHEM.COMPOUND:6131","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"However, at least one-third fold decrease in GLUT-1 protein expression was seen in those cells exposed continuously for 7 days in medium containing 100 μM ARG or when combined with 30 μM of either L-NAME or CMP-C.|PMC3680329|Continuous (or chronic) cellular exposure to 100 μM ARG for 7 days in the presence or absence of 30 μM L-NAME or 30 μM CMP-C decreased 13C6 glucose uptake from the medium (A) and GLUT-1 expression (B).|PMC3680329|Long-term exposure of ARG with or without CMP-C or L-NAME suppressed NO2-/NO3-, glucose uptake, GLUT-1, AMPK expression and activity below control, and increased overall cellular glucose, O2•- and ONOO-.|PMID:23718875","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:324395009ca652228feeb9f6f4c3fdf512e4aec89f1dd85814aeff3ad73a7f0c","tmkp:735eda4ad75d2af1b44a23f4038a1dc5db49dacb081c9ca553badf70e0d5964c","tmkp:e1bb8ad182ee3e1d2575e138b7e9a6abbbfc0ac0ea728f0f0ded3e90b4141606"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC3680329","PMC3680329","PMID:23718875"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9986554","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"115719022":{"subject":"PUBCHEM.COMPOUND:3016","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"72 Barbiturates, diazepam, sodium valproate, chloralhydrate, methylxanthine, and ethanol are nonspecific inhibitors of Glut1 function in vitro.|PMC7469861|Diazepam, chloralhydrate, and ethanol are inhibitors of GLUT1 function in vitro and might potentiate the effects of GLUT1-mediated glucose transport in patients with GLUT1 deficiency syndrome.|PMID:12548383|Additionally, there are certain compounds known to inhibit Glut-1, including phenobarbital, diazepam, methylxanthines (theophylline, caffeine), and alcohol, which should be avoided.|PMC3674738|Ethanol, diazepam, and chloralhydrate significantly inhibited GLUT1 function.|PMID:12548383|Although several antiepileptic drugs, including barbiturates, diazepam, chloralhydrate, and valproic acid, have been shown to inhibit GLUT1 function, the present study demonstrated no inhibitory effect of zonisamide on GLUT1-mediated glucose 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panel).|PMC4464397","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"57114398":{"subject":"PUBCHEM.COMPOUND:4595","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Administration of ondansetron resulted in attenuated IP3 production in the washed platelets stimulated by thrombin, as determined by reduced IP1 levels, as well as diminished p38 and ERK2 phosphorylation in response to thrombin.|PMID:22818390|Thus, rather than involving the 5-HT3-dependent pathway, the negative effect of ondansetron on platelet aggregation is instead manifested through the attenuation of agonist-induced IP3 production and MAPK (p38 and ERK2) phosphorylation that results in suppressed intracellular Ca(2+) mobilization, TXB2 formation, and ATP release.|PMID:22818390|Thus, rather than involving the 5-HT3-dependent pathway, the negative effect of ondansetron on platelet aggregation is instead manifested through the attenuation of agonist-induced IP3 production and MAPK (p38 and ERK2) phosphorylation that results in suppressed intracellular Ca(2+) mobilization, TXB2 formation, and ATP 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another larger trial assessing plasma VEGF in patients with treated with anti-VEGF therapy (bevacizumab, ranibizumab, and aflibercept) for DME found that the median plasma VEGF concentration increased by +0.20 pg/ml (IQR −5.00 to +4.90) 4 weeks after the first injection of ranibizumab.|PMC7127926|After two intravitreal ranibizumab injections, reductions in the levels of circulating cytokines IL-1β, IL-13, G-CSF, IFN-γ, IP-10, MIP-1α, and TNF-α were measured, with increased levels recorded for IL-9, MIP-1b, VEGF, and sVEGFR-1, after correcting for the multiple comparisons.|PMC7127926|In addition to the reduced concentrations of certain cytokines, we found that at 28 days after two consecutive monthly intravitreal ranibizumab treatments IL-9, MIP-1b, VEGF, and sVEGFR-1 were elevated in the serum.|PMC7127926|There was then a rebound increase of 67% in total plasma VEGF levels following a further injection, which remained above baseline for 12 weeks despite two further intravitreal ranibizumab injections.|PMID:25657041|One approach to achieve this goal may be combination therapy of ranibizumab with verteporfin-PDT since after PDT the production of VEGF is 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the setting of ethanol, TQ and Met treatment resulted in a remarkable decrease in the level of PARP-1 and decreased its 89 kDa cleaved products in the cortical neurons (Figure 4F).|PMC3317821|Osmotin and osmotin plus ethanol caused a decrease in total PARP-1 levels relative to untreated and ethanol-treated groups, respectively.|PMC3973231|The results showed that, when ethanol treatment was followed by anthocyanins treatment, cellular levels of proapoptotic proteins such as Bax, activated caspase-3, and cleaved poly (ADP-ribose) polymerase 1 (PARP-1) were decreased, and the cellular level of the antiapoptotic protein Bcl-2 was increased compared to treatment with ethanol alone.|PMID:23645118|Exposure to osmotin plus ethanol or adiponectin plus ethanol resulted in a significant reduction in cleaved caspase-3 and cleaved PARP-1 levels as compared with ethanol-treated group, suggesting that osmotin and adiponectin protected against ethanol toxicity.|PMC3973231|Exposure to osmotin plus ethanol or adiponectin plus ethanol resulted in a significant reduction in cleaved caspase-3 and cleaved PARP-1 levels as compared with ethanol-treated group, suggesting that osmotin and adiponectin protected against ethanol toxicity.|PMC3973231","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"115679710":{"subject":"NCBIGene:6517","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.998026","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Transfection of PED/PEA-15 in differentiating L6 skeletal muscle cells increases the content of Glut1 transporters on the plasma membrane and inhibits insulin-stimulated glucose transport and cell-surface recruitment of Glut4, the major insulin-sensitive glucose 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of p-ERK1/2 in LC of animals treated with clonidine (60 μg/kg, i.v.) or ethanol (1 g/kg, i.v.) were increased compared to saline treated animals (Fig. 4A), though the difference was only significant for ethanol treatment.|PMC3770283|In MEFs expressing both spinophilin and arrestins, activation of the α2BAR by clonidine induced transient ERK1/2 activation, which was desensitized after 20 min of stimulation (Fig 4).|PMC4526467|The Western blot analysis showed that clonidine stimulated phosphorylation of ERK1/2 in the cultured cells; activation peeking after 10 min of exposure (Fig. 7).|PMC3933766|Moxonidine and clonidine also increased by greater than two-fold the proportion of ERK-1 and ERK-2 in the phosphorylated active form.|PMID:11739604|The results clearly show that clonidine (10−6 M) activates the phosphorylation of ERK1/2 over time; peeking after 10 min of exposure.|PMC3933766","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:29074416","PMID:25689923","PMC3770283","PMC3933766","PMID:11739604","PMC4526467"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"64419498":{"subject":"UMLS:C2740799","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7087250"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:cfdc6486a11eb83a7d2a6576001ff887217e1222736df6b42fea60f03a7f7fff"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.993932","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"From October 2013 to date, PED has occurred at about 1,000 farms throughout Japan, causing the deaths of about 440,000 pigs according to a report by the Ministry of Agriculture, Forestry and Fisheries (MAFF) (http://www.maff.go.jp).|PMC7087250","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"108039117":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:3172","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Under the same conditions, the expression of genes associated with hepatic gluconeogenesis, including phosphoenolpyruvate carboxykinase (PEPCK), glucose-6-phosphatase (G6Pase), FoxO1, PGC-1α and hepatocyte nuclear factor 4α (HNF4α) was also increased.|PMC6364177|At the same time the expression of HNF1B and HNF4A, two factors respectively essential for NGN3 induction and hepatic formation, was increased.|PMC4361612|The same holds true for re-expression of the liver identity TF network, including HNF4A, after initial suppression in acute sepsis.|PMC7600215|We observed significantly enriched binding (6-10 folds) of HNF4α protein to the CDH1 promoter at three different consensus binding regions, but only a slight (1.7-fold) increase in binding of HNF4α to the GAPDH promoter region after the same treatment.|PMC4673210|The qPCR detection of HNF4α expression in the same transfected 293 T cells revealed that the endogenous HNF4α gene expression was also significantly activated by three stick-end trans enhancers, but not activated by all blunt-ended trans enhancers (Figure 5b).|PMC6478495","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.97424964","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f6e186963a2dedcb2a39b452a8ce3467645d65a91409130e80a72925627a2525","tmkp:9eea2968860e4c6a721dd2ae62a2fb3a0affd933cf2620bc5642e024b35e0c03","tmkp:88bf7b0279bedd44a1906614b05f60343cd36fa0ae5571144e7003379d6d4f76","tmkp:76f439e0fb00c1198fccbcbce5224a3960e4063b6d7814a050828662c1e2ab43","tmkp:25610c7ab51f4ed5308309b7fbe36a0b8b093c049afd18eac63a76121e202524","tmkp:400fd72c7a0afc6169a2ccd522d2bcbcfed6a904398a1915efc5ca821d0b0774","tmkp:b3be64c558294e09db87db91a67e8782c41f670ebbbd110175e72539d40d0ea5","tmkp:1afea15d9ee7c1d86b1fdd54df0fb3ddff34c079a698472bf053dedb6528c951","tmkp:28fc44801aa5ad99fbf0c6c9123ecbf6df1e923a4c0f36098d9638489d5fd030","tmkp:bc0918306ec79a16bf1868eebb9ad7e622aaa2d5bb5df9412b4dfdc4c5bedfc3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7600215","PMC4361612","PMC6478495","PMC4445238","PMC4673210","PMC3351448","PMC7582060","PMC3251960","PMC7037729","PMC6364177"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"92724203":{"subject":"PUBCHEM.COMPOUND:247","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4189507","PMC4464397","PMC8124599","PMC7310218","PMC3443820","PMC6627700","PMC6255979","PMID:20203061","PMID:30689995"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9979976280952381","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:81de8033967fc28ee6c22d1239d335fe339aad73d6ffdf0979bcdbd59b1f0475","tmkp:8e853929e725a977a921d8bd0254747a4f5a9d165d79912b4375a433f7277f69","tmkp:a8f3add26805b259a591e3d2b2f4665bc929bb9094d145f2e7467bcbd8b82641","tmkp:cd6cf2e05e0f573c6529913b43c7bf86d2b343366430b6b095f196275f98cd4e","tmkp:e7849274ee80a9dc17e61ec4b2d17fcbf11c179a277954e69cd793ea16989e33","tmkp:459cc7b8a7f791dfd58c1e1272dce51192dc2e14c8af8d92e6f85ed148d85de6","tmkp:39f8f8a5dddb9425c6b6f9fba9b5d1afb99cf1b91e35401517712e0929428da9","tmkp:1db59b59ccc2fc9ec7d62e3390f130add096ae8f5ee7dcb3b6a08b0278e4bd14","tmkp:cc6b0a85cd11a7bb78bd47bcb46e31abc4ea9ce2eeb4081b441848d08d84c980","tmkp:46f0f66965ed50c83d7481728f648b6e394061a58fb14d06731e1799d79ea7fa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Betaine inhibits tube formation, migration and invasion in human umbilical vein endothelial cells through suppression of NF-κB and Akt signaling pathways.|PMC4189507|Betaine inhibits vascularization via suppression of Akt in the retinas of streptozotocin-induced hyperglycemic rats|PMC7310218|Betaine inhibits vascularization via suppression of Akt in the retinas of streptozotocin-induced hyperglycemic rats |PMC4464397|Betaine inhibits vascularization via suppression of Akt in the retinas of streptozotocin-induced hyperglycemic rats|PMC6627700|Betaine inhibits vascularization via suppression of Akt in the retinas of streptozotocin-induced hyperglycemic rats|PMC8124599","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"31579411":{"subject":"PUBCHEM.COMPOUND:126941","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"eye had papillitis SD-OCT of one of the eyes with intermediate uveitis disclosed cystoid macular edema (CME) with a foveal thickness of 693 ?m associated with the retina pigment epithelial detachment (PED) and epiretinal membrane formation (Figure 3A) that showed regression of CME and PED with a foveal thickness of 362 ?m associated with persistence of epiretinal membrane at the 3rd month of the methotrexate (MTX) therapy (Figure 3B).|PMC4694667|eye had papillitis SD-OCT of one of the eyes with intermediate uveitis disclosed cystoid macular edema (CME) with a foveal thickness of 693 ?m associated with the retina pigment epithelial detachment (PED) and epiretinal membrane formation (Figure 3A) that showed regression of CME and PED with a foveal thickness of 362 ?m associated with persistence of epiretinal membrane at the 3rd month of the methotrexate (MTX) therapy (Figure 3B).|PMC4694667|eye had papillitis SD-OCT of one of the eyes with intermediate uveitis disclosed cystoid macular edema (CME) with a foveal thickness of 693 ?m associated with the retina pigment epithelial detachment (PED) and epiretinal membrane formation (Figure 3A) that showed regression of CME and PED with a foveal thickness of 362 ?m associated with persistence of epiretinal membrane at the 3rd month of the methotrexate (MTX) therapy (Figure 3B).|PMC4694667","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ec89f2a6837e92411292bcb29ee6fad05051a4c1e72d0b29efd1bf8a12c74400","tmkp:41bd63b22e86a17c60848469c5045c0a07f4d59fe87c9e78e497175c27d3dcc2","tmkp:d27cae013cf225fcc7992a90b88226fd47b8da67561f4d74389a18dbf55af9c5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9974555866666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4694667","PMC4694667","PMC4694667"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"35713867":{"subject":"PUBCHEM.COMPOUND:3121","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6549927","PMC5458469","PMC4565849","PMC5746318","PMC5584960","PMID:16525652","PMC4048646","PMC6162415"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"The differentiation markers of carcinoembryonic antigen (CEA) and fibronectin (FN) were significantly increased in colon cancer cells after treatment with DPA.|PMID:16525652|The average change has been acquired from three independent assays, with VPA-induced increase of p63 (3.4-fold), Ecadherin (8-fold), MMP2 (9.8-fold), Fibronectin (15-fold) and SSTR2 (20.6-fold), and decrease of Notch1 (0.56-fold), Notch2 (0.7-fold), HES1 (0.26-fold), Twist(0.58-fold),|PMC4565849|The upregulation of profibrotic factors (TGF-β, fibronectin, and Smad3) in the PF group was significantly ameliorated by VPA.|PMC5584960|In contrast, TGF‐β‐induced fibronectin expression was repressed by de novo HIF1αdPA expression (Figure 3E).|PMC6549927","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e9a1bcb3c30d55ed1ea208ff3cdfd4f9cc66019a98b44ab6a293d6a344893393","tmkp:7ad083c29671d2b9f1c7b277d1f272c7a1f7594d74c7885d5058c30eb57d3af9","tmkp:4a42ef41b1c6a5d11e46f1f73bdb2169309911b1a7bdf676d9edbb5d566b2326","tmkp:11d9753727d9b25499a07297e266883d26ec0fea91e9b1f6c18046afbb830d46","tmkp:c851193409db8525c1579be3a2306d9ce0acedc90ddc22935b4f66d951909c70","tmkp:c099db16a2f61dd65b4d91cf2430c06679a52e0ce1ef82e9521197a806311b84","tmkp:5d3e2ebe04cade6f241d4a1d2fe18a3fa7e630c2df5fdffa35c6a5dcca7e4e11","tmkp:fe6c53853a5e85a6ff1a75c145adc896f31ca6b8ebe547fe1dd8fe10176b8ba5","tmkp:b22f8a0b3e173cd889d92ac59258885879f2b87405fee765627fb4e80153e026"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9845825175","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"27343399":{"subject":"PUBCHEM.COMPOUND:6322","object":"NCBIGene:5337","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"At later time points (48 h), LPS‐induced Arg1 expression was reduced in Pld1 LyzCre 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using an IH mouse model, we have demonstrated that propranolol rescues abnormal blood vessel development and activates ERK1/2 in vivo.|PMC4704871|In a mouse model of IH, propranolol reduced the vessel caliber and blood flow assessed by ultrasound Doppler and increased activation of ERK1/2 in IH cells.|PMC4704871|Propranolol Dose Dependently Lowered cAMP Levels and Activated MAPK Signaling in HemSCs|PMC4704871|We demonstrate that propranolol reduces cAMP levels and activates ERK1/2 in HemSCs in a dose-dependent manner.|PMC4704871|In isolated HemSCs, propranolol suppressed cAMP levels and activated extracellular signal-regulated kinase (ERK)1/2 in a dose-dependent 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effects of bosentan to reduce apoptosis have been also reported in neuronal cells through the up-regulation of bcl-2 gene expression and decreased expression of the apoptotic protein, caspase.|PMC3958611|Bosentan also decreased the expression of PDCD4, caspase 3, and Bax and increased the expression of Bcl-2 in aortic tissues, increased the expression of miRNA-21, and decreased the expression of PDCD4 mRNA.|PMC6915145|The protein expressions of Bcl-2, Bax, Caspase-8, Caspase-9 and Caspase-3 were significantly increased in response to Bosentan treatment after IR.|PMID:24276417|More importantly, mice in the ApoE−/− group exhibited higher Bcl-2 concentrations in the aortic sinus when compared with control mice, whereas bosentan treatment significantly increased the expression of Bcl-2 in the atherosclerotic plaques (Figure 6).|PMC6915145|Bosentan Treatment Reduced Caspase-3 and Bax Expression and Increased Bcl-2 Expression in the Aortic Sinuses of ApoE−/− Mice 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also significantly increased the expression of Arg-1, Ym-1, and Fizz-1 in mice.|PMC6739369|At the M2 extreme, induction of Arg1 by IL-4 requires transcription by 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relative expression of Vascular Endothelial Growth Factor (VEGF) in the propranolol group was significantly higher than that in the control group on the 2nd day (p<0.05),|PMID:31173327|The largest increase in expression was evident after 48 hours of treatment with 100 μM of propranolol (approximately 3.5-fold increase in HIF1α, approximately 15-fold increase in VEGF expression, and approximately 15-fold increase in GLUT1 expression; p < 0.0001).|PMC7265978|Propranolol leads to a discordant increase in VEGF mRNA expression while also reducing intracellular VEGF protein expression due to interference with VEGF mRNA translation.|PMC7265978|Propranolol Induces HIF, VEGF, and GLUT-1 mRNA Expression in VHL-HB Cells|PMC7265978|Some researchers indicated that isoproterenol (a β-adrenoceptors agonist) could not decrease aortic microvessel sprouting, while propranolol caused increase in VEGF-mediated microvessel 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treatment of CSC may also cause iatrogenic CNV while PDT with verteporfin has been proposed to upregulate VEGF secondary to choroidal ischemia, resulting in CNV in some patients.|PMC5701552|Visudyne eyeglass offers full protection against VEGF increases caused by verteporfin infusion but is only partially protective in eyes exposed to sensitizing light.|PMID:19220205|The presence of verteporfin at a concentration of 0.01 microg/ml did not affect the cell viability but significantly increased VEGF (p<0.001) and reduced PEDF (p = 0.03) expression.|PMID:16987905|In addition, it has been observed that PDT with verteporfin initiates an inflammatory response and up regulates VEGF and other growth factors that contribute to recurrence of CNV.|PMC2693977|In addition, anti-angiogenic agents might counteract up-regulation of angiogenic factors (including VEGF) that occur after PDT with verteporfin.|PMC2693972","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"90815005":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9808856205555555","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ee53d4e58199a092c3415fa85d16a9ecfe5538fd259e142ae9dbf746dc456038","tmkp:f97c6730ae9fec7383466a1f401f781c6e75518f359c3195bdb1a5504e845a80","tmkp:20e9eff6820c42bd8a87289aabcb60927d353c9781167b9f548d35ba90657774","tmkp:c2688affcafb08edf47a2bb80f5dc00d7d2d04aa2948b6f102e0d078ad25b05c","tmkp:3064709ed27524ed421bcac8f79173d299d82ac18824b1adda44aaf297bc3eb2","tmkp:3045b2dd46b8608861dd4a133f66f124142100e704e30e25721da0cd9f33063a","tmkp:2e8aecf467167bc366e84780aa513079548e804e14b5fdf5e872d4897163b66a","tmkp:83c77c4277c10db5cb862f7dc291f03394bab0895fcc73189f63e2041605dad6","tmkp:c12f7e60f87c404834eb64d402752afdc36ccf9689de5f9ec61c07e85c77ff95","tmkp:03186cb003e415391716f52d5c3036c172fafadc1944659dbeec41a79bd6fc62"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6757428","PMC3933653","PMC1892540","PMID:24377895","PMC3385427","PMC3560409","PMC2757744"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"(B-C) Densitometric analysis indicates increased PCNA (B) and cleaved caspase-3 (C) protein levels in the lungs of SuHx + vehicle animals vs. controls, and that AMD3100 treatment significantly reduced PCNA and cleaved caspase-3 protein levels in the lungs of SuHx animals.|PMC3933653|Similarly, administration of AMD3100 significantly decreased a) lung c-kit (+ p<0.0001), b) lung Sca-1 (+ p<0.006), c) RV c-kit (+ p< 0.01), d) RV Sca-1 (+p< 0.0001) and e) RV Isl-1 (+ p< 0.05) expressions to near baseline values as compared to Hyp PL (n=5–7/group).|PMC2757744|f AMD3100 decreased the number of Sca-1+ progenitor cells in the neointima (panel e).|PMC6757428|AMD3100 treatment significantly reduced the protein expression of PCNA and cleaved caspase-3 in the lung tissue protein lysate of SuHx animals (Figure 7A-C).|PMC3933653|More importantly, when the injured arteries were treated with AMD3100, the numbers of Sca-1+ progenitor cells were dramatically reduced in the vascular wall media and neointima 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addition, USP21 over-expression did not significantly alter FOXM1 mRNA levels in MDA-MB-231 cells transduced with a pINDUCER20 lentivirus to introduce a doxycycline-inducible USP21 transgene (Figure S3A).|PMC6425951|(A–D) Cells with stable inducible expression of wild type USP21 (A), OTUD3 (C) or inactive versions (B, D, respectively) were induced or uninduced with doxycycline (Dox, 2 μg/ml) for 16 hr followed by UV 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RT-PCR and Western blot revealed that the treatment effects of risperidone and haloperidol seemed to be mediated through activation of VEGF and MMP2.|PMID:19579000|The findings indicate a promoting effect of risperidone and haloperidol on survival of young neurons in the hippocampus by enhancing the expression of the anti-apoptotic protein BCL-2 and by activation of VEGF/MMP2, whereby an interference with ketamine and thus a priority role of the NMDA system was not evident.|PMID:19579000|Moreover, in a previous study we showed that administration of risperidone was able to increase VEGF expression and angiogenesis in the hippocampus of 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N0572, NCCTG is is evaluating the combination of the VEGF-inhibitor sorafenib and temsirolimus in treatment of recurrent GBM.|PMC6158781|The three abstracts were a discussion of a new method for quantification of the androgen receptor; the impact of high-dose vitamin D plus chemotherapy on hormone refractory disease and on the risk of thromboembolic disease; and the paradoxical effects seen with the raf-kinase and vascular endothelial growth factor inhibitor sorafenib, which produced improvement in bone scans in the absence of any prostate-specific antigen responses.|PMID:16981834|So far, three anti-VEGF inhibitors, bevacizumab, sunitinib and sorafenib, have been approved for the treatment of solid human malignancies including colorectal cancer, gastrointestinal stromal tumours and renal cell carcinoma.|PMID:17064223|Some examples are adverse effects to epidermal growth factor (EGFR) inhibitors (e.g., papulopustular exanthemas in up to 80% of patients, also xerosis, hypotrichosis, whitlow) or the hand-foot syndrome associated with the use of vascular endothelial growth factor (VEGF) inhibitors (sorafenib, sunitinib).|PMC6040010|Recently, molecularly targeted therapies, such as VEGF signaling inhibitors (sorafenib, sunitinib, bevacizumab) and mTOR inhibitors (everolimus, temsirolimus) have become FDA-approved as front-line therapy for RCC 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the mRNA level, Hnf4α mRNA abundance was decreased by 3.15 fold in the transgenic placentas of aspirin-treated mice (Hnf1α was reduced by only 13%, and Hnf1β was decreased by 27%).|PMC6510804|We propose that at least partly, aspirin action in the placenta occurs through the down-regulation of HNF4α, acting as a hub 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of HIF-1 signaling by quercetin was confirmed by qRT-PCR which showed upregulation of the HIF-1 regulated genes EPO, VEGF, PGK1 and BNIP3.|PMID:19729006|A very mild increase in VEGF mRNA expression was observed in the rats treated with quercetin.|PMID:26281317|One study reported that 0.3% quercetin treatment of wounds accelerates healing by a variety of biological effects: rapid wound contraction, modulation of inflammatory and anti-inflammatory cytokines, increased VEGF and TGF-b1, increased antioxidant status, and enhanced fibroblast proliferation, with better collagen deposition.|PMC8186379|Quercetin up-regulated vascular endothelial growth factor (VEGF), an ulcer healing factor, not only in colon epithelial cell lines but also in the inflamed colonic tissue.|PMID:17377063|The gene and protein expression data suggest that quercetin treatment (100 micro M) significantly decreased EGF and cyclin D1, whereas VEGF was up-regulated in Ishiwaka cell 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found that oxygen and glucose deprivation (OGD) in cultured neurons caused an increase in levels of cleaved (enzymatically active) caspase-3 (a marker of apoptosis) and a progressive decrease in neuronal viability.|PMC2878892|Levels of ROS, Bax, caspase-3 and BACE were increased, whereas expression of Bcl-2 was decreased, in cells treated with 95% oxygen plus 2.4% isoflurane compared with the control and 2.4% isoflurane plus air groups.|PMID:26854136|However, the expression of caspase-3 in wild type mice treated with isoflurane was clearly increased compared with FAS-knockout mice treated with pure oxygen or isoflurane, P < 0.05.|PMC4644536|Previous studies in different animal models of oxygen toxicity revealed a significant increase of effector caspase-3 activity in the brain of oxygen-treated animals.|PMC3270267|Under ischemic culture conditions (1% oxygen and glucose deprivation), caspase-3 activity significantly increased (*P<0.001).|PMC4686112","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3270267","PMID:26032740","PMC5223311","PMC4644536","PMC4734681","PMC5337362","PMID:26854136","PMC2878892","PMC6934967","PMC4686112"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"104652585":{"subject":"PUBCHEM.COMPOUND:2083","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:46cb71861c6f0857fb5365e472d0240fb42e090b0ee5de8786d6ca1e49760eb0","tmkp:6d0f47dae9a66f8347b0e0629cf9d6a5cf177b626bbd73b55427d3541ce8bfd8","tmkp:cbf1ca1cd84bb0b870fe52e790604daba1116b7a369a65a6758f98aa4649b325","tmkp:d20c619b927365bcb9798a669f9419401a56519e3ff977fce3694a7e3e606510","tmkp:20a72520a433ca2924e7b74db696d8a17525517acd59dba291b624165b1da532","tmkp:e2d095c973d3c086386f2ee8248dee3ddaa58f37523ed4e28a828da6c66ae322","tmkp:c89e0b7145541da4f6b4522fef3539a0b254a487caaa72c1558b0baaabf17e58","tmkp:394f85d4f61afb97972aef756d2069b731bcd4ded1565df5684487ca01d1b4da","tmkp:4db36c9e0ef77a60039c0e37f4817f5269231de7986d8fcdd35cdb74c5a18576"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Salbutamol effectively reduces the production of VEGF and IL-1β corresponds to a reduction in the angiogenesis, so that it may be considered as an angiogenesis regulator with potential therapeutic uses in inflammatory diseases.|PMC5615866|The observed IL-1β and VEGF inhibitory properties of salbutamol may be responsible for anti-inflammatory and anti-angiogenic effect of the agent.|PMC5615866|In addition, salbutamol decreased the production of VEGF and IL-1β.|PMC5615866|Here, we also introduced a new function for salbutamol as a potent inhibitor of VEGF-mediated angiogenesis.|PMC5615866","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:18430317","PMC5615866","PMC5588270"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999696535","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"124999259":{"subject":"PUBCHEM.COMPOUND:174","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Authors observed that Cur-PEG-PDLLA reduced cardiomyocyte apoptosis; besides, they reported a reduction in Bax, which plays a key role in mitochondrion-mediated apoptosis, and an increment in Bcl-2, which is an antiapoptotic protein that inhibits the oligomerization of Bax.|PMC7141226|Western blot analysis showed that the expression of Bax (a promoter of apoptosis) was attenuated, and the expression of Bcl-2 (an inhibitor of apoptosis) was increased in the PEG-b-PPS-Rg3 group, compared with the model group (Fig. 8B, C).|PMC7384207|In hepatocellular carcinoma, PEG10 could increase expression of the apoptosis promoting factor Bcl-2 and decrease expression of the apoptosis-inhibiting factor Bax, which induced the attenuation of apoptosis by doxorubicin.|PMC6855493|PLGA-PEG nanoparticles induced mRNA expression of apoptosis-related genes and induced poly (ADP-ribose) polymerase (PARP) cleavage, increased BAX/BCL2 ratios, and chromatin condensation indicative of apoptosis.|PMC5378405|As shown in Figure 8, both the saline and PAMAM-PEG-EpDT3/pDNA groups showed intense staining and high positive expression of Bcl-2, while both the PAMAM-PEG/pMEG3 and PAMAM-PEG-EpDT3/pMEG3 groups showed a reduced staining intensity and low expression of Bcl-2, indicating that lncRNA MEG3 potently promotes apoptosis in CRPC cells.|PMC7759727","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:61e344e67aaa8b8cd45a10effd49c5774f253402b9923084ecb84b8e7ff2842b","tmkp:910ccafd8f515839d05322984ff212add774db196be0b056e3a05411d9a366d1","tmkp:6f4872e07591dceddf6b20b8ba9acbfd86265ed7b6c824a72f5b708e87a196e1","tmkp:72726837c3034c1af77da861385e84044da0e572ba7f0a1527c4eb20e3d11431","tmkp:6afe41d1adbd77089fe3b9d47999e93006040713198bbbb25b28c4c12e1617c7","tmkp:29835497ed78a5f3a444361590ff061eb782f628045f819bfc4e88809caf84c5","tmkp:bb831edfbb263aa9457bfdb5faa922a3cd152e6f2185a8b18c61c5b0fe84edc5","tmkp:9d6f089bfbb2c15dbb1de2a850fd34c04ea729df5f058085d0780b59e9e8b073","tmkp:d350d87feacc74d3534d2f5ccde872d61317c12efdb64cb8f6589860543758b6","tmkp:5be94fcc4a0836f321d76f55d546f9fe8e6ee55f94671825d7c2cbe772e53a95"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC5378405","PMC8130275","PMC7141226","PMC7384207","PMC7759727","PMID:30125771","PMC7099792","PMC6825139","PMC6855493"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9987974971428571","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"82937722":{"subject":"PUBCHEM.COMPOUND:22833565","object":"NCBIGene:355","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:15205081"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9994672","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The highest expression of Fas protein was observed in the 20-U/mL heparin concentration at the first hour.|PMID:15205081","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:41b93664754e006a87208daed96bcf27c45280b536907b62c9db6bc29246744b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"32561998":{"subject":"PUBCHEM.COMPOUND:3672","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Consistent with the argument for an important role of VEGF in osteoarthritis, Gallelli et al. showed that ibuprofen, diclofenac and celecoxib decrease VEGF levels in the synovial fluid of the osteoarthritic joint, with a concomitant improvement in joint pain as well as joint function in osteoarthritis patients.|PMC4391471|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off at the end of week 10, delayed the development of dyskinesia, and decreased striatal cyclooxygenase-2 (COX-2) and vascular endothelial growth factor (VEGF) levels.|PMC8150526|For instance, Gallelli et al. found that diclofenac, ibuprofen, and celecoxib can decrease tumor necrosis factor-alpha (TNF-α), interleukin-6 (IL-6), and vascular endothelial growth factor in the synovial fluid of the osteoarthritic joint with a parallel improvement in joint pain and function of patients.|PMC6335784|Treatment with ibuprofen or piroxicam in combination with l-dopa preserved the effect of l-dopa at the end of week 10, delayed the development of dyskinesia and decreased striatal COX-2 and VEGF levels.|PMID:27016022|Moreover, hypoxia resulted in upregulation of hypoxia-inducible factors HIF-1alpha and HIF-2alpha that could be inhibited with the nonsteroidal anti-inflammatory drug Ibuprofen leading to cyclooxygenase-2 independent down-regulation of HIF-regulated proteins vascular endothelial growth factor (VEGF) and GLUT1.|PMC2746691","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:50f0d2f32d18f5576bd616c95d7cc2e9e7cba7cb7b5c3a5123bebfbc1152f84f","tmkp:aea4c8bf850f8642c2f20026fc1693dd190118f228dcc6b46dabdcad3430b873","tmkp:deab6bce2e9d6e25ed9020b7cbe401101b7cf8e0776e98b3e92281b5556ead86","tmkp:77aad57588e18553805e62c7ad5b3ef36af1fbbce949f61c1cee94d57857b6b1","tmkp:b69f9c1ce72199cc81581a77b4d62eb7f40c0a0c4fb451a564c44132dac735f3","tmkp:61d36393c7481ba50680ed4df9da8c9e38d481969c5ec4f696a1bcff0bfe9b86","tmkp:8f7b7e998fb1809de70eb20686cc93b5cc68c51dc221296750557bdca359ec78","tmkp:01238f410c365642c8407efab46063a14e08eba1183dca096fa587f3f9920be1","tmkp:86795c1a96f8cba309d6dfb65a3dc862af6debbf4468e26aef955a884441d114","tmkp:d7ad2a8761fb8bb5664ec203ebf25e6485057f638ca7a4d26d183234af8eb0be"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2746691","PMC4391471","PMC6566430","PMC8150526","PMID:29198223","PMID:27016022","PMC6335784"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99965926375","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"31451661":{"subject":"PUBCHEM.COMPOUND:7814","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99940294","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The expression of p-mTOR, mTOR, HIF-1α, and VEGF were significantly reduced in 10.0 mg/kg C3C12PPD group compared with control (Figure 5B).|PMC6750213|Since mTOR is one of the targets of AKT, the p-mTOR and its downstream proteins HIF-1α, VEGF were also detected, and it was observed that they were downregulated by 100.0 µmol/L C3C12PPD (Figure 4B).|PMC6750213|Within the limitations of this study, it can be concluded that, rh-IGF-I+rh-VEGF treated sites resulted in greater improvement in PPD reduction, CAL gain as well as in osseous fill after 6 months when compared with rh-VEGF, rh-IGF-I and control sites.|PMID:27790578|Although PPD-type ginsenosides, Rb1 and Rk1, have been reported to inhibit vascular permeability induced by VEGF, lipopolysaccharide, thrombin, or histamine, it is not yet clear whether pro-angiogenic ginsenosides can induce vascular leakage similar to VEGF, or act as a leakage inhibitor, similar to ANG1, FGF and HGF.|PMC6418182","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:416bf9728ed26d4273deefdb74e3a8fdb7ec37e1a38021898a6cf38cd03f5e1d","tmkp:e25e250ba063049a932be1cde191af2ce996cd3ef8a76bbbc005e1f459f7065c","tmkp:15f930e7af325208bdeae177b6307a9843693ed09beda938377fe2a8c492cdd0","tmkp:0ad3e0c6e610c1319e723e7f0acc520e8f067e0cef00e4429d888bcdc31f63df","tmkp:f6d9146970a193fea94beafc6ffdab5f2aa09c8c2ec263228de156e34b1604eb","tmkp:4b126deaff854bf84a031def1e168fcf836315e46ea98234f7e6e6ad85d34303","tmkp:7482ec1170fb9496fda0628cadd8aedd737c5173ff2123254cb939658b6b1f51","tmkp:0a87a8df84c69dbae250ccf1113e623ee376f5b6b50055659d48697d31da3fc9","tmkp:a869d2d02b9833bcab8f1c2babac1442fc9db86bbaabd25413764d84dc722492"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6750213","PMC7471442","PMID:27790578","PMID:9390328","PMC6418182","PMC5668468"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"115349166":{"subject":"PUBCHEM.COMPOUND:3016","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Conversely, diazepam treatment decreased Htr1a, Grin2a, Erk2, and Grin2b expression in the DH (see Table S9).|PMC4700274","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9997187","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4700274"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:afe01d3895ff7cb3efeffde0d043819e2d0d50738c7472e06832a7eeb73063c8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"47321702":{"subject":"PUBCHEM.COMPOUND:1775","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99946135","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6732712"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:94baf5f5712755e270b2df82cb2751cf4ebb58b390150b9a8aea64d5ee86b597"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Intragastric administration of phenytoin in epileptic mice resulted in increased expression of Caspase-3 in both the hippocampal and cortical 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administration significantly reduced Bcl2 protein expression and elevated caspase-3 protein expression as compared to normal rats, showing that adrenaline-induced MI was mediated by apoptosis.|PMC7378581|The plasma contents of Cyt C and caspase-3 in the epinephrine group and the anisodamine group gradually increased after ROSC, and were significantly higher than those in the control group.|PMID:23648158|Epinephrine also increased Fas and FasL protein expression (P < 0.01 vs. control, n = 6), and activated intracellular protease caspase-3 (P < 0.01 vs. control, n = 6).|PMID:10728402|Epinephrine induces apoptosis in HCAECs, and this effect is associated with activation of Fas-FasL and caspase-3 signal transduction 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VEGFR-2 mRNA and protein concentrations and urinary VEGF concentrations were increased in bladders of rats instilled with MMC.|PMID:20735383|It is nteresting to note that expression of angiogenic genes HGF, bFGF, and VEGF was induced at 24 h after Mitomycin C treatment.|PMC6150649|We have previously shown that VEGF111b expression is induced in SKOV3 cells after 100 μg/ml mitomycin C treatment, and VEGF111b protein was detected by our homemade VEGF111b polyclonal antibody.|PMC4480579|Our data showed that the number of fibroblast, capillary density and fibrotic tissue in the 0.5 and 0.7mg/ml MMC groups was significantly lower than the control, 0.1 and 0.3mg/ml MMC groups; while the expression of VEGF in control and 0.1mg/ml MMC groups was notably higher than 0.3, 0.5 and 0.7mg/ml MMC groups.|PMID:22056834|After culturing for 24 h, the VEGF levels in RPE cells in the BVZ and BVZ + 5-Fu groups were significantly lower than that in the control group, while the VEGF levels in the 5-Fu and 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reductions of phospho-ERK1/ERK1 (P-ERK1/ERK1) and phospho-ERK2/ERK2 (P-ERK2/ERK2) ratios were observed in 4T1-Luc cells after in vitro 100 μM dipyridamole treatment as compared to PBS-PEG-treated cells, thus resulting in an impairment of ERK1/2-MAPK pathway activation (Fig. 4b; P-ERK1/ERK1 p = 0.017; P-ERK2/ERK2 p = 0.047; Students’ t 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line with previous studies, we found that ERK1/2, a direct substrate of STEP61, was activated 24 h after the last PCP injection in WT mice but not in STEP KOs (Figure 6).|PMC3410627|Using Western blot analysis, we found no change at three days, but a significant increase in the phosphorylation of ERK1, ERK2 and MEK in the cerebellum at 10- and 20-days of continuous PCP infusion.|PMID:11166517|The improved spatial memory, ERK1/2 expression, and neuron density in dentate gyrus of hippocampus were observed in PCP-treated rats.|PMID:29847217|The PCP-induced increases in IFNγ appear to utilize both the p44/42 (ERK1/2) and p38 MAPK pathways.|PMC5453502|PCP treatment significantly increased the phosphorylation of ERK1/2 and decreased protein levels of Tau in cortical synaptosomal (P2) fractions of WT mice, but not STEP KOs 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bosentan induced a marked increase in vessel density at 3 and 28 days (1.4-fold and 1.7-fold, respectively, compared with no treatment; P<0.05), which was associated with an increase in VEGF and endothelial NO synthase levels in ischemic legs (by 31+/-8% and 45+/-23%, respectively, at 3 days and by 65+/-13% and 55+/-15%, respectively, at 28 days; P<0.05 versus nontreated 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phenothiazine drugs, trifluoperazine and promethazine, believed to inhibit calcium-sensitive proteins involved with stimulus-secretion coupling blocked insulin release and somatostatin receptor recruitment in parallel.|PMID:6190296|Some of these examples include: the trimeric chaperone system of Hsc70, Hsp110 and J-protein which together disaggregate αSyn fibrils in an ATP-dependent manner; the small molecule promethazine prevents the aggregation of human insulin and human lysozyme, and depolymerises preformed fibrils; epigallocatechin-3-gallate (EGCG) dissociates αSyn aggregates; and memantine inhibits Αβ aggregation and disassembles preformed Aβ 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also observed a significant inhibition of ERK1/2 phosphorylation by phenytoin and TTX treatment (Fig. 5) consistent with an involvement in VGSC-mediated invasion of pII cells.|PMC4734602|Blocking the Na+ current by phenytoin results in the downregulation of EGF expression and EGF-induced ERK1/2 phosphorylation, reducing the activity of MMP7, cathepsin E, and kallikrein-10, among which phenytoin showed the greatest inhibitory effect on cathepsin E. It has been proven that higher cathepsin E levels in the serum are positively correlated with poorer clinical prognosis in breast cancer patients, thus, phenytoin might serve as an effective drug for improving therapeutic efficiency and survival of patients.|PMC7393602|Phenytoin-induced suppression of MMPs/TIMPs gene expression and reduced α2β1 integrin-mediated collagen endocytosis in gingival fibroblasts through MAPK (ERK1/2) and NF-κB signaling pathways finally leads to accumulation of extracellular matrix.|PMC7195949|Phenytoin-induced suppression of MMPs/TIMPs gene expression and reduced α2β1 integrin-mediated collagen endocytosis in gingival fibroblasts through MAPK (ERK1/2) and NF-κB signaling pathways finally leads to accumulation of extracellular 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showed that the expression of VEGF in PFT-α-treated rats was significantly higher than that in vehicle-treated rats (Fig. 4C,D), and the results were confirmed with Western Blot assays (Fig. 4A,B).|PMC4876321|PFT-α induced VEGF expression in vivo and vitro |PMC4876321|Given the degree that VEGF was elevated after the administration of PFT-α, we next investigated importance of VEGF in PFT-α-induced neuroprotection after cerebral ischemia.|PMC4876321|Since upregulation of VEGF promoted angiogenesis and neurogenesis, which further improved physiological functions after cerebral ischemic injury, it is reasonable to propose that PFT-α promotes neurogenesis and angiogenesis, at least in part, through the upregulation of VEGF expression.|PMC4876321|Results demonstrated that PFT-α could improved ischemic stroke outcome by inducing neurogenesis and angiogenesis through the upregulation of VEGF expression.|PMC4876321","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC4876321"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:487911ae9fc49b833a4a231748e8537e5002f45d613ee73e303999604b60841a","tmkp:6f5d9927b1ebad630737b636a1e14823bf70849c3cac75a741a4f01555db9ad7","tmkp:cd983682bbaaa55e20d8b88acac2ac743246ac47df07bc1ccb2836b0a4915864","tmkp:65e8b1cc5d97c327387d0953bbf92f9d970615fa59eb6bdc112f7b4b31a4cc89","tmkp:2fa0747aee5a880f7ef97aa247bebc2a49bbe94925aef05f0fe31e1caec0f7f9","tmkp:1a731ef3563be7b0b157c45b5323b87c0ef111bc9901a88429eb2ad2b6dc305a","tmkp:dc7fe35cf7076221fc6cc52963ad049db3b29e81ee25454d5609b0c72d39da3d","tmkp:f6761483ea14a11950097d019122b9573093a23c30a131fca7e1b60eef52dcdd"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"84943284":{"subject":"PUBCHEM.COMPOUND:2554","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:e9802076ec1bebba0041b612813b22ad573df307d197792793980d065af7b922","tmkp:c3b72ddefb6403567ab0a1f426d4d3264123c1b746e3e2d74330b84eda306841","tmkp:28643d26d63e09e91e6105136a8b408eaf42a43a33b1631c1af135a196394e95","tmkp:515b48bab52d67ea9f0e844e88a0129fca6490cf129f53c300a3a4d113c84411"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC5291934","PMC5291934","PMC7272308","PMC5291934"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"VPA and CBZ treatments caused a decrease in β-Catenin and VEGF levels in SW480 colon cancer cell lines.|PMC5291934|We have shown here that VPA and CBZ decreased the hypoxia-mediated induction of VEGF secretion in the SW480 cell lines.|PMC5291934|CBZ is a small molecule that targets MET, AXL, and VEGF receptors and has recently been approved for treating advanced RCC patients.|PMC7272308|Treatment of SW480 cells with 5 μM of CBZ and 2.5 mM of VPA decreased the VEGF protein levels by 53.07%|PMC5291934","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996381875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"48077208":{"subject":"PUBCHEM.COMPOUND:7814","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:31353678","PMC5668468","PMC6345703","PMID:24117074","PMC7401478","PMID:29434714"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dfb6bfdbe0215452118ad8aacdfafef15c7adf98cb1d831f16fa5a6a65543694","tmkp:c124090e0cd9b3dcecd2673ecd474d0007aa456fcb027787916a3ed0d11fa63a","tmkp:d62f520f1ecf773e788b0a39cc71779fae0563034bf6506f716254362176f3c8","tmkp:799ec94519b4f53650fa3bf706b50bd8ea85baa50eff6afbbc8982cb3341487b","tmkp:f00e9f011a38736974d10a084e37bede771b742b4a182d1c16cd6ced0efd695c","tmkp:153bf3df1456525ee8224f3dc27c17560b797019681cac49aee4077b2317b85a","tmkp:b693dceb2063b403adcd0a301e5cdd43730bb71acdc7fe2edbc621c89ea1cc37","tmkp:31d40ad8d434f7e6e80c31c98910d28aaacadde1fff2c1a752c871bd13b3bc46","tmkp:dae5d736ad0ffe42317782e80440051b200cd5d77b196b19c7495f9b0a300192","tmkp:3f155fb3e21469e3f25da8443064540b03816bce98a230d52197585386ac3cee"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"The results indicate that 20(S)-PPD inhibits the viability of HepG2 cells and induces apoptosis in HepG2 cells by inhibiting the phosphoinositide-3-kinase/Akt pathway.|PMID:29434714|PPD had an inhibitory effect on macrophages by inhibiting the PDK1/Akt pathway.|PMC6345703|In addition, 20(S)-PPD inhibited the phosphorylation of protein kinase B (Akt; Ser473).|PMID:29434714|In addition, 20(S)-PPD inhibited the phosphorylation of protein kinase B (Akt; Ser473).|PMID:29434714|Furthermore, 20(S)-PPD also triggered down-regulation of phosphorylated Akt (Ser473/Thr308) and glycogen synthase kinase 3β (GSK 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levels of fibrinogen, d-dimer, coagulation inhibitors, and plasminogen decreased, whereas the levels of tissue factor pathway inhibitor and plasminogen activator inhibitor 1 increased progressively following prednisolone monotherapy, administration of vincristine plus daunorubicin, and l-asparaginase.|PMID:22751908|After 10 days of treatment, peak thrombin, velocity index, PAI-1 and VWF increased in the oral prednisolone group as compared with the placebo group (15.8 [SD 16.3] vs. -0.1 [SD 16.1], 41.2 [SD 41.3] vs. -2.3|PMID:26791678|Prednisolone increased peak thrombin, velocity index, plasminogen-activator inhibitor type-1 (PAI-1) and von Willebrand factor (VWF) compared with the placebo group, suggesting that CS treatment may contribute to thromboembolic 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results confirm and further expand recently published data, which show that epinephrine- and LPS-treated DCs enhance IL-17 and IL-4 but not IFN-γ production by CD4+ T cells in vitro.|PMC3148409|During in vitro studies using DO11.10 transgenic lymphocytes (ovalbumin-specific T cell receptor), macrophages treated with epinephrine (and cultured in the presence of ovalbumin) reduced IFN-γ secretion and enhanced IL-4 secretion by lymphocytes (Fig. 1E).|PMC4159611|Epinephrine promotes IL-4 and IL-17A, but not IFN-γ under BMDC-mediated preferential cytokine production of CD4+ T cells |PMC2939238|PBMC were stimulated by a suboptimal dose of IL-4 (10 ng/ml) cAMP inducers, adrenaline (ADR) and cholera toxin (CTx), which were found to potentiate IL-4-induced IgE production and sCD23 release after 12 days of culture.|PMID:7538334|Epinephrine-primed murine bone marrow-derived dendritic cells facilitate production of IL-17A and IL-4 but not IFN-gamma by CD4(+) T 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treatment reversed the effect of atorvastatin on radiation-induced PAI-1 production (Figure 4A,B).|PMC7917640|Furthermore, PAI-1 expression by onnamide A, theopederin B, and anisomycin was inhibited by SB202190 and SP600125, specific inhibitors of stress-activated protein kinases.|PMID:15958059","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"78560354":{"subject":"PUBCHEM.COMPOUND:5284583","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9995987","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:31102025"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:901daf70c941c525dd981e17d08b886692848b9d92604c7ac6aa5cddad4510e1"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In 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lung tissue levels of phospho-ERK1/2 and phospho-P38 MAPK expressions of heparin treatment group were markedly higher than those of normal control group, whereas markedly lower than those of ALI group.|PMID:20137277|Heparin stabilized FGF2-wt and enabled a fast and efficient ERK1/2 signaling activation also at low concentrations (0.01–1 nM).|PMC6924264|(H) Representative Western blot demonstrating increased phosphorylation of PDGFRα (Y742) and ERK1/2 (T202/T204) after heparin treatment in GBM43.|PMC7785678|Heparin was, however, found to increase Erk1/2 activation in both a time- and dose-dependent manner.|PMID:16720575|This corresponds with the activation of downstream effectors FRS2α and ERK1/2 by FGF10/heparin stimulation and inhibition by PD173074, BGJ398 and 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free PAI-1 levels of patients given MPA were significantly higher than those either given tamoxifen or post adjuvant therapy, t-PA antigen levels were not different among the three groups.|PMID:21607504|Tamoxifen was able to preserve the fibrinolytic capacity of mesothelial cells exposed to TGF-β1, and return plasminogen activator inhibitor (PAI-1)/tissue plasminogen activator (tPA) ratios to basal 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the hippocampus there was no differences in the mRNA expression level of Bax and Bcl-2 between the levetiracetam-treated and control groups (Bcl-2: 15.0±4.3 vs. 14.6±5.2|PMC5714728","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99956673","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"34901259":{"subject":"NCBIGene:9242","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"In this report, we map at nucleotide-level resolution, the critical residues which comprise PED, purify and sequence the protein that binds to it and determine that this PED 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many have identified dysregulation of ET-1 as a possible mechanism underlying this association, likely via inhibition of the Akt pathway and increased stimulation of the ERK pathway, thus leading to greater ET-1 production and decreased production of NO.|PMC4704997|These studies have shown that exposure to air pollution downregulates insulin receptor substrate 1 signaling and inhibits the Akt pathway, resulting in decreased Akt signaling while leaving the ERK pathway unaffected.|PMC4704997|As introduced early, several animal studies support potential biological mechanisms, for example, cumulative exposure to air pollution can lead to a reduction in Akt phosphorylation in the liver, skeletal muscle and white adipose tissue which influences insulin signaling pathway and apoptosis.|PMC4142518|Our study further demonstrated that inhibition of Akt activity with the selective PI3K inhibitor reduced the elevation of P-Akt in the groups treated with air, iNBO or cNBO (Figure 5); however, only the neuroprotective effect induced by iNBO was partly eliminated by pretreatment with the selective PI3K inhibitor (Figure 6).|PMC3246542|Sirtuin 1, manganese superoxide dis-mutase, and phosphatidylinositol 3-kinase (PI3K)/Akt expression decreased significantly in the smoke-exposed groups compared with the air-exposed groups and in the aging-accelerated groups compared with the normally aged 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of the CXCR4 inhibitor AMD3100 reduced the expression of the analysed myogenic markers MyoD (n = 12), Myf5 (n = 12), MyoR (n = 12), MyoG (n = 12) (A,C,E,G) in the second branchial arch of the chicken 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Akt (Ser473), phosphorylated glycogen synthase kinase-3beta (GSK-3beta) (Ser9), and heat shock transcription factor-1, which are survival-related signaling proteins, were decreased in nPC12 cells treated with 200 microM L-DOPA, but were significantly increased with combined treatment with the PI3K activator in a concentration-dependent manner.|PMID:19786063","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC5079267","PMID:24456747","PMC4122180","PMID:19786063","PMC3206544","PMC4464750"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"113389551":{"subject":"PUBCHEM.COMPOUND:9871419","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7016113","PMID:31820856","PMC6938250"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:39fc0e92d3125df95f4045f429657053fa5623f2eaf2c23937b4c094eaab421f","tmkp:3915153af6185fc763c83b676f242eb68a788683af63ac7ffd9928e8d5e159c6","tmkp:11bfe95fc0ce9622dbbc5b29010687919b781c4909de0c6d1a76f937b4fc93b7","tmkp:54ee613319946d0afb4c57f94d446f391f1b81231d543111dfdf1ed9485e92f9","tmkp:3a74a8153a96d3341e9de8202c82a66f544d14ca09452172e33ffd94ff0a44c7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9981712650000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Ticagrelor increased c-Kit, Sca-1, Ki-67, CD34, attenuated the decrease in CD105 mRNA levels, and attenuated the increase in CD31, whereas aspirin increased Ki-67, suppressed the increase in CD31 and attenuated the decrease in CD105 mRNA levels.|PMID:31820856|In our study, our results demonstrated that ox-LDL led to increased expression levels of Bax and caspase-3, and decreased the expression level of Bcl-2 in our model, and the Bcl-2/Bax ratio was significantly decreased, and these changes were improved following exposure to ticagrelor.|PMC6938250","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"71182822":{"subject":"PUBCHEM.COMPOUND:9871419","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9996805514285715","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8052144","PMC8052144","PMID:29042978","PMC8052144","PMID:29042978"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, ticagrelor treatment also significantly increased the IL-10 protein level and decreased VEGF protein level in ischemic tissues.|PMC8052144|Furthermore, ticagrelor treatment significantly increased the IL-10 protein expression and inhibited the VEGF protein expression in ischemic tissues of IL-10+/+ mice.|PMC8052144|Furthermore, the possible mechanisms underlying the effect of ticagrelor were associated with its functions of attenuating the expression levels of VEGF and EGF, as well as suppressing the phosphorylation activation of ERK1/2, P38 and nuclear factor-κB P65.|PMID:29042978|The major results of the study showed that IL-10 negatively adjusts angiogenesis induced by ischemia, and ticagrelor inhibits the angiogenesis and blood reperfusion recovery, significantly increases IL-10 level, and reduces the VEGF expression in the IL-10+/+ mouse ischemic hindlimb, which were abolished in IL-10−/− mice.|PMC8052144|In addition, ticagrelor significantly decreased the ulcer-stimulated 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addition, clenbuterol—which increases ERK1/2 activation—also reduces caspase-3 expression, and AKT activation also reduces caspase-3 activation in cardiomyocytes exposed to I/R.|PMC8217466|In addition, other studies have indicated that clenbuterol (potent and selective beta-2 adrenergic agonist) increases the phosphorylation of ERK1/2, thus inhibiting myocardial apoptosis, as indicated by the reduction of Bax/Bcl-2 mRNA and caspase-3 protein levels and that ERK1/2 inhibition exaggerates reperfusion injury in isolated rat hearts.|PMC8217466|On the contrary, it has been reported that clenbuterol increases the phosphorylation and activity of ERK1/2, members of MAPK family, to a greater extent in the TA muscle than in the soleus muscle.|PMC3633781|Clenbuterol increased the phosphorylation of ERK1/2, which resulted in inhibition of myocardial apoptosis as indicated by the reduction of terminal deoxynucleotidyltransferase end labelling-positive staining, Bax/Bcl-2 mRNA and caspase-3 protein 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evaluate the safety and to describe the use of combination IV diazepam and fentanyl in the pediatric emergency department (PED) as outpatient conscious sedation (CS) for orthopedic procedures.|PMID:8542487|At the doses given in the study, the use of combination diazepam and fentanyl for outpatient CS of PED patients during orthopedic procedures was not associated with serious 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oxygen and nitrogen species (ROS/RNS) also activate the 26S proteasome via 3-nitrotyrosine (3NT) modification leading to degradation of the tetrahydrobiopterin (BH4) synthase GTP-cyclohydrolase (GCH-1) and the BH2 to BH4 recycling enzyme dihydrofolate reductase (DHFR).|PMC6337296","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"73287543":{"subject":"UNII:15C2VL427D","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Aflibercept reduced PED height, width, and length at 48 weeks compared with baseline values (P ? 0.01 for all).|PMID:25627086|Larger studies with longer follow-up are required to determine the role of aflibercept in treatment of PED in neovascular AMD.|PMID:23558214|To analyze the efficacy of aflibercept switch treatment for regression of pigment epithelial detachment (PED) in patients previously treated with ranibizumab.|PMC6250287|To analyze the efficacy of aflibercept switch treatment for regression of pigment epithelial detachment (PED) in patients previously treated with ranibizumab.|PMID:29190241|The higher percentages of dry macula, decreased subfoveal choroidal thickness, and reduced PED in the aflibercept-treated group may be related to the pharmacological characteristics of aflibercept.|PMC5417657","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:25627086","PMID:23558214","PMC6250287","PMID:29190241","PMC5417657"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99548902016","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9e6c7a60885e384adf015ef5565da8b706d09ee322e03a25efb06ea2f691fe3a","tmkp:c2283c3f053bd86e952d8692dc2533f7ad3cb9c4866dade6110920a9c859f796","tmkp:9e0ea360f8c9f5fea929637c20128bce4b7693e7da45d750148f52667621bf3b","tmkp:b6c1bf8450a36d4356844bddbf9e3414be4d46b68bd2b65fb65f5766abd75306","tmkp:a7eab477476694549d987399e8d08e42e9fefa4e251fecc9b1cbaa37328de0c5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"57827604":{"subject":"PUBCHEM.COMPOUND:253602","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:3dcd5f07981182ab44cb2f4bf6895e9988670bdab9c79b2ecff7f2b41595af30","tmkp:8fac9858cdc6d3e704117595e13252456c464569806262382d1ccd8e357a14b9","tmkp:3767cdff5e7b6d9c51cd585a60edea3413c688bce2612605a1c65d2382a17c70"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9873018866666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Here, we demonstrate that VEGF mRNA levels are increased by anisomycin, a strong activator of stress-activated protein kinases.|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 3'-UTR).|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 3'-UTR).|PMID:10849421","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:10849421","PMID:10849421","PMID:10849421"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"56747633":{"subject":"PUBCHEM.COMPOUND:3033","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Diclofenac increased the secretion of VEGF induced by LPS and hypoxia.|PMID:24670357","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:331721b5311029130614d8113babaf3b4c3cf452acc52de948045c1b2fc0930a","tmkp:39314cd77a03e20642d100d1c6e22f97062b8059599bb7fa9cbbf7c0ca795742","tmkp:d7cb5f0a1fb899d8f20daf9708cbd3c96a241b970baf8d04fa462dbb537a0020","tmkp:4853447476e1e56093bb10765859f62282b80873b236aa982eeb93ac5fe028af","tmkp:73d549656fe61a54e4d947c27800d01a32fff0818fc08f84f550bfd49a6ffd13","tmkp:553be181f7ee69b2e374569a235e0199d129944f65c175e40c3cc457ea01a6c6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2939880","PMID:24670357","PMC6335784","PMC5539122"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9992623","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"84359051":{"subject":"PUBCHEM.COMPOUND:6957673","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996038","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dd2006ac221d92c2a5c232c7e7bf6091a9318c0fa2599812a276c4c66cf86b85","tmkp:9a01ef8bd59609706f60ad6d38a6e5026b65054ba16c3a8b7292988f2fbd0e09"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Parkin KO mice showed further impaired glucose tolerance and reduced insulin release after treatment with streptozotocin and PFTα, a p53 inhibitor, compared to control mice, suggesting a protective role of Parkin-mediated mitophagy in stressed β-cells.|PMC6768496","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC5282448","PMC6768496"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"67946056":{"subject":"PUBCHEM.COMPOUND:31307","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:31513066"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Triamcinolone acetonide intralesional injections significantly increased apoptosis in keloids, represented by increased caspase 3 protein and TUNEL expressions, supporting that steroids suppress keloids in part owing to enhancement of apoptosis.|PMID:31513066","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99949145","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9a92fa2176325ff3f7d8dfe42185ac49aab53f0f4c5943e2e54801ee7d8b9375"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"129865692":{"subject":"PUBCHEM.COMPOUND:89594","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Previous literature has suggested that nicotine down-regulates the expression of growth factors like VEGF, PDGF, TGF-β1 and TGF-β2 but has a less significant effect on inflammatory markers like TNF, IL-6 and IL-12.|PMC6411046|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Theiss et al. demonstrated that the expression of collagen type I and II genes, bone morphogenetic protein (BMP), BMP-2, BMP-4, BMP-6, basal fibroblast growth factor (FGF), and the vascular endothelial growth factor (VEGF) was decreased by a systemic nicotine administration in rabbits through a posterolateral spine fusion with the autogenous bone graft.|PMC8038608|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Plasma vascular endothelial growth factor (VEGF) levels and lung VEGF mRNA expression decreased with advancing age, and nicotine exposure insignificantly decreased plasma VEGF levels and lung VEGF mRNA expression, compared with the control rats during the study period.|PMID:22245234","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2dfde8d2ed618f7f2128d9b2cac810ba184f3cb8018ef7ca984fae1b014ef7f6","tmkp:d4796caa274fafb69fc3bdcbb7a5c9173d257ca0d36934393939d34cf957b6b5","tmkp:1d125c66619d95e956434e6999f7e4e12a3176bbf6de6b18f1ee8bd5163bb1f4","tmkp:d8a62ddfec306ccae54ef8bcb9b34f5da76f1f8bdfac698579d9480aab669937","tmkp:76c8b99dc85dd7c49549396d71dafd1fb60a08500a46961005b1e60c5004638f","tmkp:3834a18cb423625b85bb64d498aed3c64d6c428ecacba3beba011f12cfc7bcb3","tmkp:5843bab06c406add52fc3fdb31f960a238a1bb9b69305667c305f59e729ebdf7","tmkp:b754e3dbc20a044e1a835586967b20fbfce972e773f83196600eef7eeb4e9d72","tmkp:2fb52ed2babcaf8bac4bd9eba53969c37df94907d3a93d535c6c7558229e6d40","tmkp:5d588237e5c69f63b29ba817702b1049e4304f23a838457e19e1a14ccc0483e0"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC3563266","PMID:18472096","PMC6411046","PMID:11839560","PMC8038608","PMC5466671","PMC3432052","PMID:17369603","PMID:22245234"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9955639083333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"2744124":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:5594","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"molecular_modification"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"decreased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"10116","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:publications","value":["PMID:20473320","PMID:19633425","PMID:20054642","PMID:17178882","PMID:18819900","PMID:16255777","PMID:17341847","PMID:18200035","PMID:17991738","PMID:19366808","PMID:19878585","PMID:20071162","PMID:16959960","PMID:21858812","PMID:19139124"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"dct:description","value":"decreases molecular modification of","value_type_id":"EDAM:data_0006","original_attribute_name":"description"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"88722002":{"subject":"PUBCHEM.COMPOUND:3345","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Fentanyl (400 µg/kg) administered intraperitoneally to mice increased brain glucose transporter 1 (GLUT-1) and VEGF mRNA levels and concomitant use of naloxone (2.0 mg/kg) suppressed this induction within 12 h.|PMC8128984|We found that fentanyl increased the expression of key molecules (p-GSK-3β, β-catenin) and target genes (Cyclin D1, CD44, VEGF, and c-Jun) in Wnt/β-catenin signaling pathway (Figure 5A).|PMC5526971|Fentanyl augments NO concentration in wounds, which triggers VEGF synthesis in keratinocytes.|PMC5421968","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9953375000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC8128984","PMC5526971","PMC5421968"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a151bc594005abbc6dcedfcb36ac09346c68e8b4290a6d2c3505a5efa5502d6a","tmkp:a083f0735718fb7ba2f7d2cccc5c491e29edb7adc83466a725a71b3600c4c782","tmkp:861f1552f4644bb2a3bc3efddfb836d542884045bdba8191e48090fcaa1ed3af"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"124843406":{"subject":"UMLS:C2740799","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Increased expression of VEGF has been demonstrated in most human tumors examined to date, including tumors of the lung, breast, thyroid, gastrointestinal tract, kidney, bladder, ovary, and cervix, as well as angiosarcomas and glioblastomas.|PMC2783916|Similar results of upregulation of VEGF mRNA expression have been reported for the vast majority of human tumors examined to date, including carcinoma of the lung, breast, gastrointestinal tract, kidney, bladder, and ovary.|PMC3383312","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC3563266","PMC8230848","PMC3383312","PMC2669548","PMC2783916","PMID:12177445"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8d322b1a0ddf972f2ce3d2de1105211cb53d9a8ed4239b83b77b28d9e54cf8be","tmkp:a3dbeca90c25e446961a39c0ef3c3706752201407299f131f2b4b414bb2b2a8f","tmkp:04ae98a2f6f91b4729c6872f0effbe212055a2d250d4e24927edb3330fec3073","tmkp:da6cee37a0387e770c9760b60e0952a3acaa2026912ef6fe3d440203f3eb8be5","tmkp:daf4392dd9695c9c0d8d415c236aaac1dee6ef9bf5d19d75eef6eb7d1ecd024b","tmkp:77013f630ee22942b1150b7879aec9b5a63444c1eabe485152acac82245b3066","tmkp:74bef804ebb9433f5bd4fb9f0f13d559e87761f6d1741dcd9644f6accb4293df"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9987033000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"117171909":{"subject":"PUBCHEM.COMPOUND:247","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Hippocampal expression of insulin growth factor II (IGF2) and its receptors IGF1R and IGF2R were all significantly up-regulated (P < 0.05) in betaine-treated group, together with a significant activation (P < 0.01) of the downstream extracellular signal-regulated kinase 1/2.|PMID:25410747|This effect was partly attributed to an anti-inflammatory effect of betaine, which improves insulin signaling.|PMC8072273|Previous studies showed that betaine corrected abnormal adipokine (adiponectin, resistin, and leptin) levels, enhanced insulin sensitivity by improving extracellular signal-regulated protein kinase (ERK1/2) and protein kinase B, reduced endoplasmic stress, enhanced fatty acid oxidation, and restored mitochondrial function and N6-methyladenosine mRNA methylation in WAT of mice fed a high-fat diet.|PMC8224793|Betaine administration has previously been shown to enhance insulin sensitivity in diet-induced-obese mice and increases insulin signaling pathways in isolated adipocytes.|PMC6381120|It is 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nonselective endothelin receptor blocker bosentan and the selective ETA receptor blocker ambrisentan reduced the degree of mesenteric angiogenesis and portosystemic shunting in rats with biliary cirrhosis by suppressing inducible nitric oxide synthase (iNOS), cyclooxygenase 2, VEGF and VEGFR2, and Akt signaling.|PMC6127663|In addition, bosentan inhibited Gd-induced phosphorylation of ERK and Akt in hMSC.|PMID:25048859","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6127663","PMID:25048859"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"127097774":{"subject":"PUBCHEM.COMPOUND:948","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Clinical studies have shown that VEGF expression levels decrease after exposure to nitrous oxide during urological surgery.|PMC5513670|according to Pre-operative 0th min VEGF levels decreased (28%) more in the group who were given nitrous oxide than the group (11%) who were not given nitrous oxide suggests that the decrease occurred due to nitrous oxide.|PMC3955540|according to Pre-operative 0th min VEGF levels decreased (28%) more in the group who were given nitrous oxide than the group (11%) who were not given nitrous oxide suggests that the decrease occurred due to nitrous oxide.|PMC3955540|Compared with preop levels, VEGF levels were found to be low at postop 4 and 24 hours in the 30 patients who had mastectomy operation under general anasthesia using nitrous oxide but no statistically significant difference was 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HNF4α and insulin gene expression were upregulated when E47 was induced by tamoxifen in T6PNE which has a low level of insulin and HNF4α expression at baseline.|PMC3447631|Our ability to observe effects of fatty acids on HNF4α activity in T6PNE cells may be because HNF4α expression is induced in those cells by tamoxifen simultaneously with the addition of fatty acids.|PMC3447631|We found increased expression of G6p, Pepck and Hnf4α in tamoxifen-treated GHSR-null/AgRP-CreERT2 mice as compared to both GHSR-null and wild-type littermates (Figure 4C).|PMC3929914|In T6PNE cells, where HNF4α gene expression is induced by tamoxifen simultaneously with the addition of the putative fatty acid ligand, we found that 48 hour treatment with palmitate significantly inhibited HNF4α mRNA levels (Fig. 5b).|PMC3447631|Nevertheless, compared with that of WT mice, at 12 months post-tamoxifen, the expression level of Hnf4α in gastric tissues was significantly higher and structural abnormalities were observed in the gastric mucosa of Rosa26Hnf4α mice (Fig. 1c, 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the other hand, the MAP kinase ERK1/2 is modestly inhibited by paclitaxel.|PMID:15834684|Inhibition of phosphorylation of AKT and ERK1/2 by paclitaxel (PTX), fluvastatin (F), zoledronic acid (Z) and their combinations.|PMC3756383|Pristimerin and paclitaxel inhibited extracellular signal-regulated kinase (ERK)1/2/p90RSK signaling, consistent with autophagy indicators, namely p62 degradation and beclin 1 expression.|PMC6172393|Furthermore, paclitaxel-trastuzumab combination was reported to have a worsening effect on cardiomyocyte function, which might result from the inhibition of phosphorylated-ERK1/2.|PMC7283551|The effects of pristimerin were enhanced when combined with paclitaxel treatment through suppression of ERK1/2/p90 ribosomal S6 kinase (p90RSK) signaling, which in turn activated 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exposure resulted in reduced VEGF-induced cord formation on collagen and reduced capillary network structure on Matrigel in vitro.|PMID:18469146|VEGF prevents the apoptosis of primary cultured SECs induced by ethanol, through at least in part, inhibition of ethanol-induced down-regulation of Ets-1 protein expression and ethanol-induced up-regulation of Casepase-8 activity in SECs.|PMID:18269875|A model of in utero exposure of lambs to maternal alcohol was developed demonstrating reductions in lungs of preterm lambs of hypoxia-inducible factor (HIF), vascular endothelial growth factor (VEGF), and surfactant protein A (SpA) (Lazic et al.).|PMC7223741|A model of in utero exposure of lambs to maternal alcohol was developed demonstrating reductions in lungs of preterm lambs of hypoxia-inducible factor (HIF), vascular endothelial growth factor (VEGF), and surfactant protein A (SpA) (Lazic et al.).|PMC7223741|The aortic NADPH oxidase activity, ratio of oxidized to reduced glutathione (GSSG/GSH) and lipid peroxidation significantly increased, whereas nitric oxide (NO), endothelial NO synthase (eNOS), and vascular endothelial growth factor (VEGF) protein expressions were depressed in alcohol group compared to 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shown in Figure 2 , at concentrations below 40 × 10−6 m, the MF‐Lip40@PEG could significantly increase the expression level of VEGF and bFGF in a dose‐dependent manner.|PMC6364594|32 In the present study, we found that following treatment with MF‐Lip@PEG leaching liquor for 7 d, the expression levels of VEGF and bFGF in HUVECs increased significantly in a dose‐dependent manner at concentrations below 40 × 10−6 m (Figure 2b,c).|PMC6364594|In this study, vascular endothelial growth factor (VEGF)-small interfering RNA (siRNA) was encapsulated into a magnetic mesoporous silica nanoparticle (M-MSN)-based, polyethylenimine (PEI)-capped, polyethylene glycol (PEG)-grafted, fusogenic peptide (KALA)-functionalized siRNA delivery system, termed M-MSN_VEGF siRNA@PEI-PEG-KALA, which showed significant effectiveness with regard to VEGF gene silencing in vitro and in 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synthesis and preliminary bioactivity studies of indomethacin derivatives as Bcl-2/Mcl-1 dual inhibitors.|PMID:31079964|NSAIDs such as aspirin and indomethacin have long been shown to induce cancer cell apoptosis by upregulating the expression of proapoptotic Bcl-2 proteins, such as Bax and Bak, and by downregulating expression of anti-apoptotic Bcl-2 proteins such as Bcl-2 and Bcl-XL.|PMC3747411|Indomethacin treatment was associated with the disruption of mitochondrial transmembrane potential, release of cytochrome c, down-regulation of Bcl-2 and Mcl-1, upregulation of Bax, and elevation of caspases activity.|PMID:19250643|Indomethacin caused heavy destructions of the gastric mucosa, increased the expression of Bax and decreased the expression of Bcl-2, induced a certain increase in lipid peroxidation and a slight decrease in gastric PGE2 content.|PMID:31374297|Indomethacin (1 mM) and ibuprofen (1 mM) significantly reduced Bcl-2 expression in the cancer cell lines tested and might be 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date, the best-characterized synthetic lethal interactions are between BRCA1 or BRCA2 loss-of-function and inhibition of PARP1/2, both first reported in seminal papers in 2005.|PMC6097899|The majority of PARP-1 inhibitors known to date have been developed as NAD competitors.|PMC5264309|Additionally, the decrease in total PARP-1, procaspase-3 levels, and the increase of cleaved caspase-9 revealed the apoptotic effect of date seed extracts.|PMID:31721029|In fact, these molecular interactions anchoring BMN 673 to the base of the NAD+-binding pocket represent well established binding features common to many PARP1/2 inhibitors described to date (Ferraris, 2010).|PMC4157409|5-Benzamidoisoquinolin-1-one is the most PARP-2-selective compound (IC(50(PARP-1))/IC(50(PARP-2)) = 9.3) to date, in a comparative 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gene expression such as the increase in Irs1 and Glut4 expression in the heart and skeletal muscle with PPT treatment suggests that ERα may have direct effects on insulin signaling.|PMC5027347|Furthermore, the data provide evidences that ESR1-agonist PPT, as a Slc2a4/GLUT4 enhancer, can be a promising coadjuvant drug for diabetes mellitus therapy.|PMID:23167795|Activation of ERα via PPT resulted in increased GLUT4 in the EDL (fast-twitch) but not in the soleus (slow-twitch), suggesting that the ability of ERα to regulate GLUT4 may be fiber type specific.|PMC3422439|Estrogen Receptor 1 Agonist PPT Stimulates Slc2a4 Gene Expression and Improves Insulin-Induced Glucose Uptake in Adipocytes|PMC5711936|Estrogen receptor 1 agonist PPT stimulates Slc2a4 gene expression and improves insulin-induced glucose uptake in 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of PDGF-AB and VEGF increased during the first days of low dose aspirin exposition; higher concentrations led to a depletion of cytokines after an initial liberation in the case of VEGF, mRNA of which was also dose-dependently increased by aspirin.|PMID:11376496|Paradoxically, this research group also reported an increase in VEGF expression in aspirin-treated female mice.|PMC6136175|Rats treated with ASA404 also produced elevated tumor tissue concentrations of cytokines and chemokines, including TNF, VEGF, IL-6 and IL-1α, MIP-1α (CCL3), KC (CXCL1) and IP-10 (CXCL10).|PMC3583340|In summary, ASA VI promotes angiogenesis of HUVECs in vitro via up-regulating the HIF-1α/VEGF pathway, and efficiently enhances the vascularization in regenerated tissue and facilitates wound healing in vivo.|PMID:29219948|The vascular endothelial growth factor level was significantly higher in the letrozole-treated group than aspirin-treated group (0.49 ± 0.26 vs 0.42 ± 0.22, P = 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carry out the western-blot analysis, proteins in the crude tissue extracts or in the cell membrane fractions were resolved by SDS-PAGE (10% Tris-Acrylamide-Bis) and electrotransferred from the gel to nitrocellulose membranes (Hybond-ECL, Amersham Pharmacia, Piscataway, NJ) as described by Towbin et al.. Nonspecific protein binding to the nitrocellulose membrane was reduced by preincubating the filter with blocking buffer (TNT, 7% BSA); then, membranes were incubated overnight with the primary antibodies Glut4 (sc-7938, diluted 1 : 2,500), Akt (sc-7126, diluted 1 : 2,000), and phosphorylated-Ser473-Akt (sc-101629, diluted 1 : 2,500).|PMC4058098|To carry out the western-blot analysis, proteins in the crude tissue extracts or in the cell membrane fractions were resolved by SDS-PAGE (10% Tris-Acrylamide-Bis) and electrotransferred from the gel to nitrocellulose membranes (Hybond-ECL, Amersham Pharmacia, Piscataway, NJ) as described by Towbin et al.. Nonspecific protein binding to the nitrocellulose membrane was reduced by preincubating the filter with blocking buffer (TNT, 7% BSA); then, membranes were incubated overnight with the primary antibodies Glut4 (sc-7938, diluted 1 : 2,500), Akt (sc-7126, diluted 1 : 2,000), and phosphorylated-Ser473-Akt (sc-101629, diluted 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observed significantly higher mRNA levels for VEGF (1.73-fold), FGF-2 (5.6-fold) and TGFbeta receptor III (2.93-fold), PDGF receptor alpha (2.93-fold) and receptor beta (2.91-fold) in rats receiving indomethacin compared to rats given placebo (p < 0.05).|PMID:17440234|Indomethacin, a nonsteroidal anti-inflammatory drug (NSAID) with PPARγ activity, up-regulated VEGF expression, but acetylsalicylic acid, a NSAID without PPARγ activity, did not.|PMID:23542713|Infusion of fetal lambs with indomethacin for 48 hours constricted the DA and increased the thickness of the avascular zone of the DA, which in turn induced the expression of vascular endothelial growth factor, endothelial nitric oxide synthase (due to ingrowth of vasa vasorum), neointima formation, and loss of smooth muscle cells; moderate degrees of DA constriction in utero increased NO production, which inhibited DA contractility.|PMID:11282914|In addition, to determine the possible mechanism of the effect of E-cadherin on the PC invasion and metastasis, we found that the protein levels of metastasis-related factors (MMP-2, MMP-9, VEGF), which were increased in PC cells after Si-E-cad and treatment with indometacin 100 mg/L for 48 h.|PMC4085328|Indomethacin also increases the thickness of the avascular zone by causing constriction of circumferential and longitudinal muscle, decreasing blood flow in the vasa vasorum, and causing vessel wall hypoxia with release of vascular endothelial cell growth factor 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exosome-derived DNMT-targeting miRNAs enhance DNA promoter demethylation of critical CpG islets involved in the upregulation of gene expression of pivotal transcription factors (NRF2, SREBP1, FOXP3, NR4A3) and key metabolic regulators (INS, IGF1, CAV1, GLUT1, LCT) and the RNA m6A demethylase FTO.|PMC5456335","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5456335","PMC8151789"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"24059049":{"subject":"PUBCHEM.COMPOUND:6137","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9920053110526316","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC3619126","PMC5405996","PMC7694406","PMC6367544","PMC4192143","PMID:21382440","PMC6180630","PMC4068350","PMC3366283"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In addition, it was shown that Met-F-AEA is also able to block the growth of already established tumours by inhibiting the expression of vascular endothelial growth factor (VEGF).|PMC7694406|(A) Schematic of possible ways by which VEGF can block MET activation.|PMC4068350|Met-F-AEA has been shown to decrease levels of VEGF and VEGFR-1 in K-ras-transformed thyroid cells and in experimental tumors of xenografted nude mice.|PMC3366283|Finally, MET appears to have a paradox effect on angiogenesis as it promotes or inhibits expression of the pro-angiogenic vascular endothelial growth factor (VEGF) depending on breast cancer subtype.|PMC5405996|In conclusion, we found a reduced expression of VEGF and HIF-1α in the MET NVB + Endo group and a higher expression of VEGF and HIF-1α in the MTD NVB + Endo 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relative expression of Vascular Endothelial Growth Factor (VEGF) in the propranolol group was significantly higher than that in the control group on the 2nd day (p<0.05),|PMID:31173327|The largest increase in expression was evident after 48 hours of treatment with 100 μM of propranolol (approximately 3.5-fold increase in HIF1α, approximately 15-fold increase in VEGF expression, and approximately 15-fold increase in GLUT1 expression; p < 0.0001).|PMC7265978|Propranolol leads to a discordant increase in VEGF mRNA expression while also reducing intracellular VEGF protein expression due to interference with VEGF mRNA translation.|PMC7265978|Propranolol Induces HIF, VEGF, and GLUT-1 mRNA Expression in VHL-HB Cells|PMC7265978|Some researchers indicated that isoproterenol (a β-adrenoceptors agonist) could not decrease aortic microvessel sprouting, while propranolol caused increase in VEGF-mediated microvessel 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described.|PMC5338462","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3537053","PMC3795282","PMC5338462"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"1835279":{"subject":"NCBIGene:5337","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.991723743","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Over-expression 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PPT showed no significant effect on PDGF-induced proliferation, whereas WAY interestingly suppressed proliferation via inhibition of ERK1/2, Akt, and p38 signaling.|PMC6120801|Effect of U0126 (1 µM), a MEK inhibitor and LY294002 (1 µM), a PI3 K/Akt inhibitoron E2 (1 nM) and PPT (0.01 nM) induced proliferation of PASMCs (F).|PMC4615797|Estradiol's or PPT's inhibition of the fluvoxamine-induced slowing of 5-HT clearance mediated by ERα, was blocked after inhibition of either MAPK/ERK1/2 or PI3K/Akt signaling pathways.|PMID:24423185|Estradiol’s or PPT’s inhibition of the fluvoxamine-induced slowing of 5-HT clearance mediated by ERα was blocked after inhibition of either MAPK/ERK1/2 or PI3K/Akt signaling pathways.|PMC4698103|Estradiol’s or PPT’s inhibition of the fluvoxamine-induced slowing of 5-HT clearance mediated by ERα, was blocked after inhibition of either MAPK/ERK1/2 or PI3K/Akt signaling 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hormonal responses to surgery, as indicated by changes in plasma adrenaline, noradrenaline, glucagon, aldosterone, corticosterone, 11-deoxycorticosterone, and 11-deoxycortisol levels, in the insulin/glucagon, molar ratio, and in blood glucose, lactate, and pyruvate concentrations were significantly greater in the non-fentanyl than in the fentanyl group.|PMID:20928962|Major hormonal responses to surgery, as indicated by changes in plasma adrenaline, noradrenaline, glucagon, aldosterone, corticosterone, 11-deoxycorticosterone, and 11-deoxycortisol levels, in the insulin/glucagon, molar ratio, and in blood glucose, lactate, and pyruvate concentrations were significantly greater in the non-fentanyl than in the fentanyl group.|PMID:2879174|Major hormonal responses to surgery, as indicated by changes in plasma adrenaline, noradrenaline, glucagon, aldosterone, corticosterone, 11-deoxycorticosterone, and 11-deoxycortisol levels, in the insulin/glucagon molar ratio, and in blood glucose, 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contrast, the same drugs efficiently inhibited Ras-induced ERK1/2 phospshorylation in rat brain neuroblasts, as well as geranylgeranylation of Rho family GTPase in neurons, leading to an increase in apotosis and tau phosphorylation, respectively (Figure 1).|PMC3130102|Moreover, the phosphorylation of ERK1/2, c-Jun, p38 MAPK and P90RSK were inhibited to varying degrees by both MTA and SAM.|PMC3543504|Remarkably, all three compounds belonged to the same benzylidene-1H-inol-2-one (oxindole) chemical class, which were originally reported as potent ATP-dependent RAF kinase inhibitors that block the MAPK signalling pathway in cultured cells.|PMC6094399|The same pigment was effective against neuroinflammation in mouse brain through the inhibition of mitogen-activated protein kinase (MAPK) and the activation of nuclear factor κB (NF-κB), as well as against bladder cancer through the inhibition of the signaling of phosphatidylinositol-4,5-bisphosphate 3-kinase/Akt or protein kinase B (PI3K/Akt).|PMC6943509|Moreover, the phosphorylation of ERK1/2, c-Jun, p38 MAPK and P90RSK were inhibited to varying degrees by both MTA and SAM.|PMC3543504","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"113975515":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The same study also found marked increases of Bcl-2, an apoptosis suppressor, and vascular endothelial growth factor (VEGF), an angiogenesis modulator linked to accelerated tumor progression and increased invasiveness, in malignant prostate tissues.|PMC3599181|Moreover, increased levels of hepatocyte growth factor (HGF) and VEGF were observed in the same group.|PMC5403966|Additionally, we revealed that the VEGF expression level in muscle on the operated side in the HMGB1-treated group was significantly higher compared with the non-operated side in the same group 4 days after EMS, while the expression level of VEGF in the cortex showed no difference on both sides between the two groups.|PMC6882763|In contrast, VEGF expression was upregulated after treatment with the same combination compared with treatment with β-GP and ascorbic acid only.|PMC2193567|Our study found that expression of CCN1 and VEGF was increased to the same level in ischemic retina of OIR, thus verifying that CCN1 and VEGF can participate in the pathological process of 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reduces the secretion of Alzheimer's beta-amyloid precursor protein containing beta-amyloid peptide in the rat without altering synaptic proteins|PMC5026886|Nicotine reduces the secretion of Alzheimer's beta-amyloid precursor protein containing beta-amyloid peptide in the rat without altering synaptic proteins|PMC3573893|Nicotine reduces the secretion of Alzheimer’s beta-amyloid precursor protein containing beta-amyloid peptide in the rat without altering synaptic proteins |PMC4098701|Nicotine reduces the secretion of Alzheimer’s beta-amyloid precursor protein containing beta-amyloid peptide in the rat without altering synaptic proteins |PMC2857410|Nicotine reduces the secretion of Alzheimer's beta-amyloid precursor protein containing beta-amyloid peptide in the rat without altering synaptic 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these cases, bevacizumab, a monoclonal antibody targeting vascular endothelial growth factor A (VEGF-A), is an off-label treatment option that can slow tumor growth.|PMC6621994|Strategies have been developed to inhibit the VEGF signaling pathway including anti-VEGF antibody therapy (e.g., bevacizumab), anti-VEGFR antibody therapy (e.g., ramucirumab), inhibitors of VEGFR-2 tyrosine kinases (e.g., apatinib), and inhibitors of angiogenic receptor tyrosine kinases (e.g., sunitinib, pazopanib, sorafenib, and regorafenib).|PMC6501144|The patient was restaged as T2N0M1 of lung adenocarcinoma, and chose 6 courses of systematic chemotherapy (pemetrexed combined with nedaplatin) plus bevacizumab, a monoclonal antibody targeting vascular endothelial growth factor at 3 weeks intervals.|PMC6710319|Based on successful phase III trials, antiangiogenic therapeutics, anti-VEGF agents in particular (e.g., sorafenib, bevacizumab, and sunitinib), have entered the clinical practice in the USA and 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mean cumulative number of anti-VEGF injections was significantly lower in PCV group (4.51 for AMD-CNV, 3.43 for PCV, p = 0.021).|PMC4076260|This theory is supported by previous findings that aqueous levels of VEGF are lower in PCV than in CNV-AMD.|PMC4470199|Intravitreal corticosteroids may therefore be useful in the treatment of PCV as they show a mild blocking of VEGF and a strong anti-inflammatory effect.|PMC5111116|Decreased levels of VEGF detected 1 week after PDT for PCV seems to reflect acute damage of vascular endothelial cells, one of the VEGF expression sites in PCV.|PMID:23664208|The rates of retreatment from 12 to 23 months were significantly higher in eyes with SRD at 6 and 12 months than in those without SRD (P = .004 and P < .001).In conclusion, during 24 months of antivascular endothelial growth factor (VEGF) therapy using ranibizumab for PCV, BCVA was maintained in those with good visual acuity at 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effect of betaine on pathologic retinal neovascularization via suppression of reactive oxygen species mediated vascular endothelial growth factor signaling.|PMID:27473515|Antiangiogenic effect of betaine on pathologic retinal neovascularization via suppression of reactive oxygen species mediated vascular endothelial growth factor signaling|PMC8124599|Our data suggest that betaine has an anti-angiogenic effect on pathologic retinal neovascularization via suppression of ROS mediated VEGF signaling.|PMID:27473515|In addition, betaine treatment alleviated diabetes-induced vascularization by suppressing VEGF and HIF-1α expression via downregulation of pAkt expression in the retina of the STZ-induced diabetic rats.|PMC4464397|A lower dose of betaine exerted a more potent inhibitory effect on the number VEGF-positive cells (Fig. 1, lower 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pathophysiology of marijuana-induced finger clubbing may be due to increase in the expression of vascular endothelial growth factor—alpha or of its receptors.|PMC5428643","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f73196103d4173b21fdbd78a3dbe5b74065d8d54cf4684cfdf2d1ba0490d9f34"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC5428643"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99935955","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"98712562":{"subject":"CHEMBL.COMPOUND:CHEMBL2052016","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9993298557142857","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0b59df65600a028391cf0e10da4a0c7b920f2b65716971cc2eeacf6a79629817","tmkp:48636ee77fd03a72170c3cd8016381345c98d8d985c1a1b003fd78e7f49f2560","tmkp:7d2ff98d04ffac9524bb854a81e597ce6d1e667c7e8cb33215504555fb3a0ba9","tmkp:41ae0bc375dad45e0299a818fd7ce02ecdb4ac993b21113bedaa805d37166058","tmkp:a73f67d0dc1c328e1b6ee93e07894991f1a9e9d5c542829a9281d6b7f0e1752e","tmkp:046b24a9ffa66883321504ef78bb6e933ce7cfea2a653ee16c0702826df82d66","tmkp:f65ec8457078690807fb7c2b3f89085e001760979a62cccf9ce5038986c29382","tmkp:ae4fc2d614976d00ea9a9f7c9b6d9cc11aaf0234e4a9a5dadfcf57d96bb71d08","tmkp:fa8f7bf452c49762918674bc58b975d4bec00a7d07cb4c964b538f80897720c3","tmkp:41e3a46ef5c80f8a293932ad914e91383f98e4081330f178474bde0b96ff7139"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC5701552","PMC2693977","PMID:31633245","PMC2693972","PMID:16987905","PMC4476543","PMC7791049","PMC6468149","PMID:19220205","PMID:23560774"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Laser treatment of CSC may also cause iatrogenic CNV while PDT with verteporfin has been proposed to upregulate VEGF secondary to choroidal ischemia, resulting in CNV in some patients.|PMC5701552|Visudyne eyeglass offers full protection against VEGF increases caused by verteporfin infusion but is only partially protective in eyes exposed to sensitizing light.|PMID:19220205|The presence of verteporfin at a concentration of 0.01 microg/ml did not affect the cell viability but significantly increased VEGF (p<0.001) and reduced PEDF (p = 0.03) expression.|PMID:16987905|In addition, it has been observed that PDT with verteporfin initiates an inflammatory response and up regulates VEGF and other growth factors that contribute to recurrence of CNV.|PMC2693977|In addition, anti-angiogenic agents might counteract up-regulation of angiogenic factors (including VEGF) that occur after PDT with verteporfin.|PMC2693972","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"113603565":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2898903","PMC5028300","PMC1382249","PMC4626203"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"At 30 minutes following injection, ERK1 and ERK2 phosphorylation was significantly higher in formalin-injected rats than in either normal control rats or saline-injected control rats (p < 0.05, p < 0.01; Fig 5a–5c).|PMC4626203|In the wild type mice, blots of tissue taken from the side of the spinal cord ipsilateral to the formalin injection showed significant stimulation of both ERK1 and ERK2 when compared to the contralateral side (Fig 5a and 5b), whereas ERK activation in the spinal cords from the DN MEK mice was not significantly different from their contralateral sides.|PMC1382249|Nonetheless, we reason that the sex differences observed here in ERK2 activation in the amygdala after formalin are primarily responsible for behavioral differences observed in mechanical hypersensitivity after restraint.|PMC5028300|We found that formalin injection increased phosphorylation of both ERK1 and ERK2 in the male CeA; acute restraint stress prevented formalin-induced phosphorylation of only ERK2.|PMC5028300|We found that formalin injection increased phosphorylation of both ERK1 and ERK2 in the male CeA; acute restraint stress prevented formalin-induced phosphorylation of only ERK2.|PMC5028300","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9991509854545455","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:be363fd863106f4f6d22994d4b74734d3108037b988cbe881b66bdee21330ec8","tmkp:a4548f9fb89bfc364cc71bd134a9d30ea2e7a2d4b2b111db0f9fc72612dd10d8","tmkp:cf7831274d5f7b2b54c850c3f10c8c7bedb9b12a7ca972555ce088e90a2534b1","tmkp:d0ae697a57a4ed7496a67a9003b9411014509d55c85864d4a612aab109c2b7d2","tmkp:499b3a66e865d86ff780598db703c1cd58dc6d0abe42de8d2076a4f57bafb6ea","tmkp:b292c93aec3343229a804c360779eabc08e350c81c6bde604e38ae44391c6d27","tmkp:2d3edf52050552d0b62ea54ed35a84814e8c7b563d69a221ed88ab47147869c0","tmkp:7cbf900e0af9dae5347af3fbb5e558560e94c9792580cae1a0b84f1e806ee21d","tmkp:fe44349610f77a9e692946a5d8f595988b1111e2053d47b6b4fb439ede82ff3b","tmkp:9dc163d5e50de0df384a3813196ba635fd638e98a7cc2f20fd1fd143c9ad0588"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"120292051":{"subject":"PUBCHEM.COMPOUND:4943","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99969588","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"We demonstrated that the expression of RAC1 was significantly decreased in HCC cells following incubation with TAMs from propofol–treated HCC tissue.|PMC4198740|61 Zhang et al 62 showed that propofol triggered the shutting of miR‐142‐3p from macrophages to HCC cells, which decreased the expression of Ras‐related C3 botulinum toxin substrate 1 (RAC1) and then inhibited the metastasis of HCC cells.|PMC7445405|61 Zhang et al 62 showed that propofol triggered the shutting of miR‐142‐3p from macrophages to HCC cells, which decreased the expression of Ras‐related C3 botulinum toxin substrate 1 (RAC1) and then inhibited the metastasis of HCC cells.|PMC7445405|Macrophage activation and shuttling of miR-142-3p containing MVs from TAMs to HCC cells stimulated by propofol might be the underlying mechanism, leading to down-regulation of RAC1 - a target gene of miR-142-3p- expression, and thereby inhibiting tumor cell growth, migration and invasion.|PMC5356911|The expression of RAC1, a known target of miR-142-3p, was significantly down-regulated in the HCC cells following incubation with TAMs from the propofol-treated HCC tissue (Figure 2C and 2D), suggesting that the level of functional miR-142-3p levels increased in the HCC cells.|PMC4198740","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:92f55d4c6006b11ec72e7e356c1c9a9821036b522e82a001fcbbe85ceaa8f92d","tmkp:500de0bc2bf4c3f0da0ec6a7bd21300be0a62a63fd9f4d59239fc6711d2cb313","tmkp:848731077d05289ffd3d39fece412ce05c6fba0b98a9a524b66af073619913f9","tmkp:64017d0bafd94e87e4ff4d6765b2dce02f3e4d9f5679c9557c62df44dd8002f5","tmkp:788fed81fc06c908f42664eb29f4c087cf7845952257e8d46e1be0e5f41c7d04"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC4198740","PMC7445405","PMC7445405","PMC5356911","PMC4198740"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"59625488":{"subject":"PUBCHEM.COMPOUND:5206","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:3aedf69c8bf1fd353e56ec7ee753ca815fc28e0cd6038e681e008cb757bf9ec1","tmkp:53291b097dd74331381b646c04d40cea008b1e44e129779fde4e26620d9dfde4","tmkp:1bb221c16ac834035de2971b0b9e2949cfcd3f7b14b4f6c77f9bf10bfbcf7806","tmkp:54e3e8151dae17af6d33792fd98539b308d5d4c19bae59a4919330c0f19becdb","tmkp:a703557606203536c91bfde8d7cb2e85dfb7b697993df06f7136f2f6880b89be","tmkp:05a56e5a14a3be7b74c83b00fe6f45a61a71d0246919dd6e5daebf215df804f9","tmkp:2e2691a5b4a59acea103e47d99235a8cffae27ebdf56566c627ac20e1f667f1a","tmkp:45ea0a4264c10a7eb9aa9a9f535d1d56c80ec57314d17959bc463668fdc3b305","tmkp:e394c4765c2e670c41b8cc13d5f46b8897b746a04f363e50f9892b5428d7eef2","tmkp:5497c52e3f445981c154e3b20cbc3f30774a27d896b57e97671b31e8c66eb042"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9947471437500001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Sevoflurane post-conditioning protects isolated rat hearts against myocardial I/R injury and inhibits cell oncosis and apoptosis via activation of the ERK1/2 pathway.|PMID:25345742|Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway.|PMID:25345742|Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway|PMC7288833|Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway|PMC7938236|Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway|PMC7197225","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7938236","PMID:25345742","PMC4318867","PMID:31103261","PMC4540577","PMC7197225","PMC7288833"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"100232216":{"subject":"PUBCHEM.COMPOUND:3715","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:36a7f961531994ea47958d1dcf9683a85bfa6645dd1d83acb3b902e17a8a1fa0","tmkp:bd651f9d47f288944a25bf0464aac632ef432d2dcab15ec9d9a3a675484f2cc3","tmkp:0e43e55e55ed1c47f32ba4324397d4ca0a2c8a97644b8f29f492871671026feb","tmkp:2ec44e42049a7eccb72305c333aedd46e1797003ed3e46fc68a767b869f5dae2","tmkp:ba133bf3d9412c7a3675c4199464f993edfd33b6d6525b1895a615b8153ea463","tmkp:08f2525c8a1e571e1b8102d89b82d3e637e16d316e84296246c3e922df8aa703","tmkp:94bb43e825040a0fe79c011b726c0162325f028c66f53a0737115a4db75bd2b0","tmkp:e50d07327c066c944f72bf7830b0faa44ff8fc80612bb0eae615664fb53fa1b8","tmkp:a182a7c9ed4721e4942f10aaa2c51c0080bb2938172ffb0268b867951939d717","tmkp:93cb8d85b906cbd5bfb66e58ac04d7e0aced2bf8eaf9475a4c82536071af8328"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4467441","PMC4085328","PMC3493357","PMID:17410434","PMC3232537","PMID:23542713","PMID:17440234","PMC3612487","PMID:11282914","PMC6461401"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"We observed significantly higher mRNA levels for VEGF (1.73-fold), FGF-2 (5.6-fold) and TGFbeta receptor III (2.93-fold), PDGF receptor alpha (2.93-fold) and receptor beta (2.91-fold) in rats receiving indomethacin compared to rats given placebo (p < 0.05).|PMID:17440234|Indomethacin, a nonsteroidal anti-inflammatory drug (NSAID) with PPARγ activity, up-regulated VEGF expression, but acetylsalicylic acid, a NSAID without PPARγ activity, did not.|PMID:23542713|Infusion of fetal lambs with indomethacin for 48 hours constricted the DA and increased the thickness of the avascular zone of the DA, which in turn induced the expression of vascular endothelial growth factor, endothelial nitric oxide synthase (due to ingrowth of vasa vasorum), neointima formation, and loss of smooth muscle cells; moderate degrees of DA constriction in utero increased NO production, which inhibited DA contractility.|PMID:11282914|In addition, to determine the possible mechanism of the effect of E-cadherin on the PC invasion and metastasis, we found that the protein levels of metastasis-related factors (MMP-2, MMP-9, VEGF), which were increased in PC cells after Si-E-cad and treatment with indometacin 100 mg/L for 48 h.|PMC4085328|Indomethacin also increases the thickness of the avascular zone by causing constriction of circumferential and longitudinal muscle, decreasing blood flow in the vasa vasorum, and causing vessel wall hypoxia with release of vascular endothelial cell growth factor (VEGF).|PMC3232537","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9913440175","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"109274658":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:355","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2212386","PMC2212386","PMC2212386"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Treatment with 5-fluorouracil, methotrexate, mitomycin, cisplatin, mitoxantrone, doxorubicin, etoposide, cyclophosphamide, and bleomycin led to upregulation of CD95 mRNA and of the CD95 receptor protein in HepG2 cells (wt p53), in AGS cells (wt p53), in HS746T cells (wt p53), and in MCF-7 cells (wt p53) (Table 1, and Figs. 1 and 2).|PMC2212386|Cisplatin, mitomycin, methotrexate, mitoxantrone, doxorubicin, and bleomycin at concentrations present in the sera of patients during therapy led to an upregulation of both CD95 receptor and CD95 ligand.|PMC2212386|Treatment with 5-fluorouracil, methotrexate, mitomycin, cisplatin, mitoxantrone, doxorubicin, etoposide, cyclophosphamide, and bleomycin led to upregulation of CD95 mRNA and of the CD95 receptor protein in HepG2 cells (wt p53), in AGS cells (wt p53), in HS746T cells (wt p53), and in MCF-7 cells (wt p53) (Table 1, and Figs. 1 and 2).|PMC2212386","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994470999999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0a9b46fd8a61d769e0c1e2efe0a292c53370e433cd0d1b8ec765f2fb80c3cee4","tmkp:62b4159b4eec90cb45c3c85dea98253d2a34f2856ba2d951ef11b21a75da605f","tmkp:85694feb73baa911b272ff2c110cf0aeef9419b33880fe5d2d8b4fb23dabbd10"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"16284333":{"subject":"NCBIGene:207","object":"PUBCHEM.COMPOUND:36314","predicate":"biolink:decreases_response_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:20361045"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"decreases 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survival.|PMID:25920465|Furthermore, ALA and DHLA upregulated the expression of survival-related proteins mTOR (mammalian target of rapamycin), Akt (protein kinase B), and Nrf2 (nuclear factor erythroid 2-related factor 2) in PC12 cells, which were previously downregulated by metal exposure.|PMC7926869|The phosphorylated Akt was significantly increased in ALA-treated mice, which indicated that ALA could activate PI3K/Akt pathway.|PMC4532939|We showed that an increase in activated Akt and mTORC1 only occurred in those groups of animals intravenously administered ALA500.|PMC6332275|Further study identified that hippocampal extracellular signal-related kinase (ERK) and Akt rather than calcium calmodulin kinase IV (CaMKIV) and protein kinase A (PKA), the upstream signalings of CREB, were also activated by ALA 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addition, the expression levels of some apoptosis and inflammatory markers, namely, caspase-3, Bax, Bcl-2, COX-2 and iNOS, were measured and were found to have decreased in dopamine-treated mice compared with control mice (Figure 7C).|PMC5687621|While the induction of D2R did not affect the slight but significant inhibitory effect exerted by dopamine (10 nM) on in vitro GH release by GH-oma cultured cells, in pituitary GH3 cell lines cis-9 RA enhanced the dopamine-induced inhibition of in vitro GH release (% inhibition: 16 +/- 2 versus 26 +/- 5, P < 0.05), cell proliferation (25 +/- 2% versus 44 +/- 5%, P < 0.05) and cell viability (16 +/- 0.8% versus 29 +/- 1%, P < 0.05), likely by activating caspase-3 (28 +/- 3% versus basal, P < 0.05).|PMID:18367633|Dopamine (100 microM) inhibited the decrease in mitochondrial transmembrane potential, cytochrome c release, activation of caspase-3, formation of reactive oxygen species, and depletion of glutathione (GSH) due to 500 microM SIN-1 in PC12 cells.|PMID:15202767|Ginsenosides (Rd, Rg1, or 20(R)-Rg3) attenuate mitochondria-mediated apoptosis in a middle cerebral artery occlusion (MCAO)-induced stroke model or glutamate/dopamine-induced primary cortical neurons/PC12 cells through the suppression of caspase-3 activation, mitochondrial release of cytochrome C, apoptosis-inducing factor, or oxidative stress.|PMC6026382|Dopamine melanin protected against norharman-induced upregulation of grp78, activation of caspase 3 and necrosis at low concentrations (5 and 50 microM).|PMID:17256107","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"89853651":{"subject":"PUBCHEM.COMPOUND:6322","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Treatment with arginine resulted in a significant increase in bcl-2 protein levels as well as a significant decrease in bax protein levels without changes in p-ERK and β-catenin levels compared to MTX rats.|PMC3355056|Expression of the anti-apoptotic gene bcl-2, which was stimulated within 1 h by PRL, was upregulated by L-arginine or DEA/NO alone at 2 h and 8 h, respectively.|PMID:10771518|It was shown that arginine induced expression of Bcl-2 and Bcl-xL, while rReg4 upregulated Bcl-2 and Bcl-xL expression by activating the EGFR/Akt pathway.|PMID:21193457|Thus, it may be concluded that L-arginine afforded significant protection from necrosis and apoptosis in I/R injury by upregulated Bcl-2 gene and nitric oxide production.|PMC2841413|Taken together, this study demonstrated that ARG is a potent inducer of apoptosis and this was accompanied by caspase-3 activation and upregulation of bax/bcl-2, which offers a potential mechanism for the apoptosis-inducing activity of 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inhibited the expression of Pik3ca and the phosphorylation of Akt in WT mice (Figures 1G and 2D) but not in KO mice.|PMC7378464|It is reported that sildenafil prevents cardiac mal-remodeling, suppressing Akt activity in mice exposed to PO, and P-Akt causes the inactivation of Foxos.|PMC7378464|Sildenafil attenuated the phosphorylation of Akt and AGO2 at Ser387 (S387) and the expression of cleaved caspase-3, a marker for apoptosis, in WT mice withTAC-induced PO but not in KO mice (Figure 1H).|PMC7378464|Another study indicates that sildenafil, an inhibitor of PDE5A, can suppress activations of PI3K/Akt and calcineurin/NFAT signaling through the cGMP/PKG pathway.|PMC3723916|Sildenafil suppressed the phosphorylation of Akt in WT mice but not in KO mice (Figure 1H).|PMC7378464","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"77343550":{"subject":"NCBIGene:5337","object":"PUBCHEM.COMPOUND:962","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"abundance"}],"attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:hmdb","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"}]},"6481085":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The PARP-1 and PAR (a product of PARP activity) expression and apoptotic cell death were also markedly increased in renal tubules after MTX administration.|PMID:22914891|Mitochondrial pathway of apoptosis was activated in the small intestines of MTX-treated rats as evidenced by intense immunostaining for cyt c, caspases 9 and 3, and PARP-1 and mitochondrial release of cyt c, activation of caspases, and PARP-1 cleavage by Western 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(Figure 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mice treated with bleomycin intratracheally and then exposed to CO or ambient air, the lungs from CO-treated animals displayed reduced lung hydroxyproline, collagen, and fibronectin levels relative to air-treated bleomycin-injured controls.|PMC3604600|In mice treated with bleomycin intratracheally and then exposed to CO or ambient air, the lungs from CO-treated animals displayed reduced lung hydroxyproline, collagen, and fibronectin levels relative to air-treated bleomycin-injured 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paclitaxel treatment resulted in a small but significant dose-dependent reduction in the ability for induced osteogenic differentiation in MSC1 (P < 0.05 for 50 nM) and MSC2 (P < 0.05 for 15 nM, P < 0.01 for 50 nM) stem cell preparations 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inhibitor, and in enteric neurons transfected with a dominant negative K44E mutant dynamin, which prevent clathrin-dependent, dynamin-mediated endocytosis.|PMC4193881","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9955263000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"67283016":{"subject":"UMLS:C4529301","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"In the examined nine patients, systemic bevacizumab therapy showed evidence for an effect on PED secondary to neovascular AMD in terms of a decrease in lesion height and diameter.|PMID:17050580|This study aimed to investigate the effect of bevacizumab on pigment epithelial detachment (PED) in occult choroidal neovascularization (CNV) in patients with age-related macular degeneration (AMD) and to determine predictive factors.|PMID:20532523|In clinical practice, patients with PED and no improvement on CDAV (bevacizumab 1.25 mg or ranibizumab 0.5 mg) are commonly encountered.|PMC4965601| Our results indicate that switching from intravitreal conbercept injections to bevacizumab or ranibizumab can lead to significant improvement of CMT, PED, and IRF and slight improvement of BCVA in a short period of time for persistent nAMD patients.|PMC7508218|The effect of the vascular endothelial growth factor (VEGF) inhibitors triamcinolone and bevacizumab (Avastin) on serous pigment epithelial detachment (PED) related to age-dependent macular degeneration (AMD) was analysed 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proinflammatory and proangiogenic factors, including G-CSF, stroma-derived factor (SDF), TGF-β, tumor necrosis factor (TNF)-α, VEGF, IL-1β, and IL-6 were found to be increased in sorafenib-treated mouse orthotopic liver tumors.|PMC6511249|Increases in serum VEGF have been noted in patients treated with sorafenib in phase II and III trials.|PMC6626665|In the sorafenib cohort, VEGF levels increased, whereas sVEGFR-2 and TIMP-1 levels decreased.|PMC3461173|During sorafenib treatment alone, there was a significant increase in plasma VEGF, PlGF, VEGF-D, sMET and TNF-α (at days 3 and 15), and sVEGFR1, CAIX and the fraction of CD8+ T cells (at day 15) and decrease in plasma sVEGFR2 and the fraction of CD56Dim NK cells (at day 3) and plasma sVEGFR2 and s-c-KIT (at day 15) compared to baseline (all p<0.05,|PMC6320284|In addition, sorafenib demonstrated significant activity against several receptor tyrosine kinases involved in neovascularization and tumor progression, including vascular-endothelial growth factor (VEGFR)-2, VEGFR-3, platelet-derived growth factor (PDGFR)-beta Flt-3, and c-KIT.|PMID:16474853","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"82537182":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9994468","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:58d82527581318762fdfd5ba577e1c44900d8d5069976b76112af8ffe70d78ae","tmkp:51bc4aa8057e958716f192b23edde90a02b5bed74e7f2e0187d05b8740c679ba","tmkp:3094b3a357cd67786eb6c04565d11527aeafbb90307bbb0d7076102901d1203b","tmkp:8c33c7abf2054f1268daaeaf961a213ecb6e4214dd77c9ba227be7155cec380e","tmkp:09d5337637b7d31a296a4eb2a19ed5a21f0da5756503d377f5cf3114096289b6","tmkp:67192072406fb9998de69d165216b22c5969dfe22c3956c1eb93e000efdd29a3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:25617811","PMC4436794","PMID:30536359"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"VEGF upregulation by pro-inflammatory stimuli, IFNγ, DNCB or formaldehyde is preceded by the production of IL-8, an acute inflammatory phase cytokine.|PMID:25617811|Lymphangiogenic VEGF-C gene transcription was significantly increased when NHKs were treated with formaldehyde, DNCB or urushiol, while transcription of VEGF-A and VEGF-B did not change.|PMID:25617811|There was significant upregulation of IL-1α,IL-1β, IL-5, IL-17A, leptin, NGF, VEGF, CXC and CC chemokines (*p < 0.05, unpaired t test) in formalin injected prostate, while expression of BDNF, IFNγ, G-CSF, IL-2, IL-4, IL-10, IL-12p70, IL-13, TNFα remained unchanged between the groups.|PMC4436794","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"88782167":{"subject":"PUBCHEM.COMPOUND:3958","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9930311","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:197e9f114d069d52164ad4b4f91fc94c54bd7b76f185884c97a44958f493d609"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC5470151"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Our data show that SE responsive to lorazepam in the PED was a negative predictor of mortality OR: 0.235 (95% CI: 0.090?0.618).|PMC5470151","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"76573537":{"subject":"PUBCHEM.COMPOUND:24759","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Sodium hyaluronate affected the fibrinolytic response of TNF-alpha-stimulated human peritoneal mesothelial cells, most notably by decreasing PAI-1 transcription and release.|PMID:11231848|Treatment with sodium hyaluronate statistically significantly decreased PAI-1 and uPA concentrations in medium of monocultures but decreased uPA concentration only in medium of co-cultures, compared with the case of controls.|PMID:16209995|Sodium hyaluronate significantly decreased PAI-1 concentration in the medium and reduced its gene expression 500-fold (P =.04), while PAI-1 concentration in cell lysates did not change.|PMID:11231848|Hyaluronic acid inhibits the expression of u-PA, PAI-1, and u-PAR in human synovial fibroblasts of osteoarthritis and rheumatoid arthritis.|PMID:10782829|Hyaluronic acid inhibits the expression of u-PA, PAI-1, and u-PAR in human synovial fibroblasts of osteoarthritis and rheumatoid 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with HG supplemented with 40 μg Aflibercept produced a decrease of both phospho-ERK1/2 and phospho-cPLA2.|PMC7589177|However, aflibercept was also able to inhibit PDGF-BB induced phosphorylation of ERK1/2 but not bFGF induced phosphorylation of ERK1/2 (S1D and S1E Fig).|PMC5201251|Furthermore, our findings indicate that increased phosphorylation of cPLA2 is linked to HG-induced VEGF-A upregulation; in fact, VEGF-A blockade with Aflibercept was able to prevent both HG-induced cell damage as well as phosphorylation of ERK1/2 and cPLA2.|PMC7589177","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.999653","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC7589177","PMC5201251","PMC7589177"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"26632786":{"subject":"PUBCHEM.COMPOUND:89594","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Previous literature has suggested that nicotine down-regulates the expression of growth factors like VEGF, PDGF, TGF-β1 and TGF-β2 but has a less significant effect on inflammatory markers like TNF, IL-6 and IL-12.|PMC6411046|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Theiss et al. demonstrated that the expression of collagen type I and II genes, bone morphogenetic protein (BMP), BMP-2, BMP-4, BMP-6, basal fibroblast growth factor (FGF), and the vascular endothelial growth factor (VEGF) was decreased by a systemic nicotine administration in rabbits through a posterolateral spine fusion with the autogenous bone graft.|PMC8038608|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Plasma vascular endothelial growth factor (VEGF) levels and lung VEGF mRNA expression decreased with advancing age, and nicotine exposure insignificantly decreased plasma VEGF levels and lung VEGF mRNA expression, compared with the control rats during the study 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on the TiO2 nanotube surface tended toward M2 polarization, particularly for the TNT60 group, with lower production of pro-inflammatory cytokines and higher expression levels of VEGF.|PMC6330985","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99943775","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6330985"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:23ee96a97a08385cd6fa90b01354f57a5103431a042d6346db9a8386383bf936"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"65604795":{"subject":"PUBCHEM.COMPOUND:2083","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99969413","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:11340331","PMID:17537664","PMC7731315","PMID:16083788","PMC3060863"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"(R)-Albuterol also significantly decreased airway goblet cell hyperplasia and mucus occlusion and levels of IL-4 in bronchoalveolar lavage fluid and OVA-specific IgE in plasma.|PMID:16083788|A comparative study of (R)- and (S)-albuterol in a murine model of asthma revealed that although both compounds were able to reduce leukocyte infiltration and mucus production in the lung of allergic mice, only (R)-albuterol was found to inhibit the production of IL-4.|PMC7731315","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:986c7f66724dae759a32c203aad2c1231def5372eeca3bbaa32b8820b22ac8f7","tmkp:a9a5441aea16e40325b775722ccd9548260249edf0891bd98e525f0698323b88","tmkp:69671992c66639b7ecff091de1672471bd9527ff03425346f2181c296306a227","tmkp:df9f0707acbbb07f638c6764e64b437d551e0c1a0395e81a4c5c66d7876367f9","tmkp:f67cda29016d4aac785c1f623c0e879f3b13edd3621b15d3fb297ac7f7c858d9","tmkp:cd24ec5fd85f3df1fafa70b19bbf076cc13b534ce164357b813c8390a6b8faa8","tmkp:dfbe63e6f85a76082b0619ba97d52f5a0214e88d3e3f1950c1d785fa96896bf7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"126455770":{"subject":"PUBCHEM.COMPOUND:5988","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a09c428ddae255a3a9ff616d4177600bfd01d63b2e5b8f16ec21ac5aea04ae5b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.99965966","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The inhibition of PARP1 N-terminus was performed using different stringency buffers as follows - Hypotonic buffer: 100 mM MES-NaOH, pH 6.4, 1 mM EDTA, 0.5 mM MgCl2, protease inhibitor, 30% sucrose in MiliQ.|PMC6923857","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6923857"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"120004602":{"subject":"PUBCHEM.COMPOUND:5206","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:9c0d7339435d0fe22dc70a0c276f4ad0cb3f6a6dfda4c0cb0f029b775d37c4bc","tmkp:0b9a3250674d1f2517a7f86aea2ebb5e9e9b04e188ea0c00368928f5e195deb0","tmkp:1ed7a3c80aafb98a82fedad8207b24e8c6d77e5b708ea4e59363baa5de82ab12","tmkp:2d920649925b1822618d2fac53daa6cb3a060a09ea7c13ebef7e8b1532a5481f","tmkp:222a9baf19b6ccda69bed1dc4222016240e7b57de52d2c1af8f5c0404b570fb7","tmkp:8dcb6aed4bffc8cc70b8f1683730c8cbc55e789c76252fa70385868b15c14889","tmkp:4149bc6f06ecd5000226df06fb49c57186d16095fe53b1c3561610812c8713bf","tmkp:fe23c46359db56e91882c845ab714f30a808d605e5ebb7379592c3e4bf53d55a","tmkp:614f6902d93cf1fccb8ffc00549fd098d030b631481528885844652924e39458","tmkp:befc5acee7148df5ff6592b4b27a1e07c4271bed520fa6810b9f31931ac2ce76"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6126114","PMC6966126","PMC6828596","PMID:24666314","PMC7825752","PMC6994546","PMID:25492570","PMC6905212","PMID:29464332"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In another study that was examined the effect of sevoflurane on glioma stem cells (GSCs) and the mechanisms of action in vitro, expression of VEGF and HIFs were up-regulated by sevoflurane.|PMC7825752|Notably, following the inhibition of the VEGFR pathway, there was significantly decreased cell proliferation in the cells treated with axitinib plus sevoflurane than with sevoflurane alone (Fig. 4C and D), implying that sevoflurane promotes the proliferation of HUVECs via activation of the VEGF/VEGFR pathway.|PMC6966126|Levels of CD133, VEGF, HIF-1α, HIF-2α, and p-Akt were up-regulated by sevoflurane in a time- and concentration-dependent manner.|PMID:25492570|As shown in Fig. 2a and Supplementary Fig. 3, we found that sevoflurane increased pro-inflammatory cytokines known to facilitate mammary tumor metastasis, such as IL-6, interleukin-12, vascular endothelial growth factor (VEGF), stromal cell-derived factor 1 (SDF-1 α), TARC (CCL17), chemokine ligand 1 (I-309/CCL1), and pro-matrix metallopeptidase 9 (Pro-MMP9) in comparison to reference .|PMC6994546|Sun et al demonstrated that preconditioning of MSCs with sevoflurane not only minimized cell apoptosis when exposed to hypoxic-serum deprived media but also enhanced MSC migration, suggesting that this improvement in the therapeutic potential of MSCs might be related to the upregulation of HIF-1α, HIF-2α, VEGF, and pAkt/Akt.|PMC6828596","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9976017880000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"86617606":{"subject":"PUBCHEM.COMPOUND:2244","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Thus, PAI-1 expression is increased in gastric epithelial cells in response to mucosal irritants such as aspirin and NSAIDs probably via an indirect mechanism, and PAI-1 acts as a local autoregulator to minimize mucosal damage.|PMID:23494120|Increased plasma plasminogen activator inhibitor-1 levels caused by additional aspirin treatment.|PMID:16676089|In Helicobacter pylori-negative patients with normal gastric histology taking aspirin or NSAIDs, we found elevated gastric PAI-1 mRNA abundance compared with controls; the increase in patients on aspirin was independent of whether they were also taking proton pump inhibitors.|PMID:23494120|Both the cyclooxygenase inhibitors acetylsalicylic acid and indomethacin enhanced PAI-1 induction.|PMID:1280469|The control group was characterized by higher PAI-1 following ASA treatment and sICAM-1 both at baseline and after ASA, but no differences in MDA and 6-keto-PGF-1 alpha and platelet aggregation were 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addition, CMP and cordycepin can significantly inhibit p-EGFR expression and its downstream signaling molecules p-Erk1/2, p-STAT3, and p-p70 S6K.|PMC5706830|3.4 cmp4 Reduces Cell Proliferation and MAPK Activation in KRasG13D Expressing Cancer Cells|PMC7925909|Taken together, these data identify a novel mechanism for the inhibition of Stat3 signaling by a resveratrol analog and suggest that the preferential growth inhibitory effects of Cmp1 occur in part by Erk1/2(MAPK)-dependent modulation of constitutively active 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inhibits TNF induced NF-λB activation and reduces expression of NF-λB dependent anti-apoptotic proteins, such as BCL2α.|PMC5342790|Doxycycline treatment of CTCL cell lines correlated with decreased levels of BCL2α in a dose dependent manner (Figure 6A).|PMC5342790|Doxycycline inhibits TNF induced NF-κB activation and reduces expression of NF-κB dependent anti-apoptotic proteins, such as BCL2α.|PMID:27732942|CEM-C7.H2 lymphoma cell stably transfected with a Neomycin selection vector (Neo) only (fluorescence displays 1–4), with the crmA cowpox protease inhibitor (graphs 5 and 6), or with a Bcl-2–expressing construct negatively regulated by doxycyclin (graphs 7–12).|PMC2198951|Reduction of Bcl-2 levels by doxycycline treatment induced caspase-3 and caspase-7 activation, which was followed by Bim 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expression of insulin growth factor II (IGF2) and its receptors IGF1R and IGF2R were all significantly up-regulated (P < 0.05) in betaine-treated group, together with a significant activation (P < 0.01) of the downstream extracellular signal-regulated kinase 1/2.|PMID:25410747|Interestingly, we found decreased ERK1/2 phosphorylation mainly in the 5-FU treatment and AS+5-FU, as well as an unexpected increase in the use of Trimethylglycine, which may indicate that administration of this adjuvant favors the ERK1/2 activity as reported in the primary cultures of human osteoblasts; this, however, contends with data reported in lipid metabolism in which the use of Trimethylglycine decreased ERK1/2 phosphorylation.|PMC7139326|However, at present, we cannot rule out that an increase in ERK1/2 phosphorylation by Trimethylglycine treatment could be a compensatory or alternative mechanism to escape cell death induced by adjuvant therapy with 5-FU.|PMC7139326|It has been reported that ethanol-induced abnormal hepatic methionine metabolism is specifically associated with the suppression of transmethylation reactions and with the inhibition of MEK/ERK1/2 activation, and that betaine supplementation, improving the AdoMet/AdoHcy ratio, is able to alleviate ERK1/2 activity 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this study, there were ten patients with multiple failed PKs and a sole AMT that resulted in PED with corneal ulceration.|PMC4369521|The multiple PK failures exhibited ocular surface stabilization failure with sole AMT, resulting in PED with corneal ulceration.|PMC4369521","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"96177654":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9971175048421053","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9a77be206f77b03fca6eca79ba5ba8e25bde5613ebfeb407359e115f05436e07","tmkp:20d99c7a2a5fb67d9573fcf4ec0a01a93947396c5f777ea0f4c0b68df08e6b55","tmkp:d6a7a40f872c89e5e384b20e4639ba92f74bed3f0cbbc8c40518d9dd262f4690","tmkp:7bfe01bdc4926518ad218d65925b22a109de74cbc712a4c26c1acbb6b0679f1a","tmkp:13a55647587a5a279e76b238eab0739714411b073b12d12c7232c5853aad104b","tmkp:aaa139960444a7293460230e66e6b1b6c59f6e83b499fe7bd4b783a6b6245904","tmkp:f3052965e6d07302432bc4c65255ce886ccdd444257755303172294c18a48b64","tmkp:3265ef600c9279eb869659badd94600bdfcc4883a374c78ebce36ef5510a175e","tmkp:58c850a425030cfc167850bea0ebcf072c2df65e3bbd94033458864f48e1375b","tmkp:738761f8ac2487b4ce305e0ba514783f99715d664dea621909e445970f0080c1"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:10207029","PMC2925144","PMC7318786","PMID:11093967","PMC3204341","PMC5471499","PMID:10974336"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Although no demonstrable effect of alcohol on tissue plasminogen activator activity was present from 1 hour after ingestion onward, tissue plasminogen activator antigen and tissue plasminogen activator inhibitor-1 antigen increased significantly 22 hours following alcohol ingestion.|PMID:10974336|Significant (7-fold) but transient increases in PAI-1 activity were found three hours after ethanol intake.|PMC7318786|Plasma levels of plasminogen activator inhibitor 1 activity (PAI-1) and serum triglycerides were increased by alcohol.|PMID:11093967|Although mRNA levels for PAI-1 and egr-1 decreased in chronic ethanol alone treated group, their levels were significantly increased in chronic ethanol – single binge group.|PMC3204341|Plasma levels of plasminogen activator inhibitor 1 activity (PAI-1) and serum triglycerides were increased by 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inhibitory effect of PAs on the expression of VEGF and hypoxia inducible factor 1 subunit alpha (HIF-1α) was also observed in cisplatin-resistant ovarian cancer 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glucose levels increased in both groups, but significantly more in men with low levels of visceral AT (p < 0.05), whereas plasma insulin concentrations increased significantly only in men with high amounts of visceral AT in response to adrenaline infusion (p < 0.01).|PMID:8817361|Epinephrine levels were also higher during insulin as compared to placebo infusion (249.8+/-17.4 vs. 212.8+/-21.1 pmol/l, p<0.001).|PMID:11149624|Compared with infusion of saline, epinephrine caused a small but significant rise in serum insulin of 10 +/- 26 pmol/L (p = 0.016), more than 70% increase in serum glucose (p < 0.0001) and a decrease in serum phosphate (p < 0.0001).|PMID:8777469|The insulin concentrations in serum were elevated in the adrenaline group and the triple-hormone group, but not in the cortisol group.|PMID:2605867|Insulin (1 and 10 U/kg) treatment caused similar reductions in blood glucose concentration (from 7.5-9 to 2-3 mmol/L); however, plasma adrenaline concentration was increased 20-30 fold in response to 10 U/kg insulin and only 14 fold following 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number of apoptotic cells increased and MR-1 mRNA and protein levels decreased with increasing doses of either paclitaxel or carboplatin, strongly indicating that these anti-cancer drugs exert their therapeutic effects by antagonizing the effects of MR-1.|PMC3132198|MR-1 expression decreased in a dose-dependent manner at both the mRNA and protein levels following treatment with paclitaxel or carboplatin.|PMC3132198","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.999645875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9b44e204e5e69cb083da4ab34afd8e8ac522eca5367279d1e16927cd1f0ee122","tmkp:0020645a4e91d43930269bc64efb84030ae5858a732a6a18c6d374669dc56b28"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"56256110":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:3172","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"decreased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"10090","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"dct:description","value":"decreases 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hepatocyte mRNA expression of Alb, Hnf4α, F7 and F9 on HB-EGF/heparin-IC surfaces was significantly higher than that on other surfaces with soluble HB-EGF (Fig. 8).|PMC6581876","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6581876"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.002257032","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"96783132":{"subject":"PUBCHEM.COMPOUND:3958","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:e77a54792ac98fa61dc94309acf6032c90a2e12a7eca836b1ef68d2fd8e0b79d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6166024"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9995047","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Our data showed that the levels of sFASL, HB-EGF, IL-8, TGF-α, uPA, and VEGF-A were significantly increased after the 6-week treatment of lorazepam.|PMC6166024","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"20146671":{"subject":"PUBCHEM.COMPOUND:3345","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Fentanyl (400 µg/kg) administered intraperitoneally to mice increased brain glucose transporter 1 (GLUT-1) and VEGF mRNA levels and concomitant use of naloxone (2.0 mg/kg) suppressed this induction within 12 h.|PMC8128984|We found that fentanyl increased the expression of key molecules (p-GSK-3β, β-catenin) and target genes (Cyclin D1, CD44, VEGF, and c-Jun) in Wnt/β-catenin signaling pathway (Figure 5A).|PMC5526971|Fentanyl augments NO concentration in wounds, which triggers VEGF synthesis in 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large increase in cell surface GLUT4 seen with sucrose treatment suggests that endocytosis of GLUT4 from the surface is also efficiently blocked by sucrose.|PMC2140164|With the disappearance of GSVs in the presence of sucrose or with incubation at 15°C, there is a concurrent increase of GLUT4 on the cell 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blot analysis revealed that the level of p-ERK decreased and that the level of p-p38MAPK increased after dexamethasone treatment compared with the control (Figures 5(a), 5(b), and 5(d)).|PMC4844876|Administration of the GR agonist dexamethasone rapidly increases the phosphorylation of cofilin, leads to the activation of extracellular signal-regulated kinase (ERK) ½, and accordingly stabilizes the actin cytoskeleton in dendritic spines.|PMC7378655|Summary of the fold increases in ERK1/2 MAPK activity induced by dexamethasone.|PMC6838933|As shown in Fig. 21, dexamethasone (1 nM) produced a biphasic activation of ERK1/2 MAPK.|PMC6838933|Similarly, in rat vascular smooth muscle cells, dexamethasone either alone or in combination with NE, rapidly (within 10 min) induces ERK1/2 and p38 MAPK 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at 5 μM and 10 μM significantly inhibited ET-1- induced activation of ERK1/2 by 65.1% and 87.1%, respectively (Figure 2D).|PMC2715373|Increase in bosentan concentration up to 10 microM further inhibited ET-1-induced activation of ERK1/2 and had a stronger inhibitory effect than BQ123 or the combined use of BQ123 and BQ788.|PMID:19575782|Our observation that Bosentan inhibits ERK1/2 MAPK activity and increases p27(Kip) expression may explain the observed reduction of vessel wall thickening, which has been documented in clinical studies.|PMC3756002|Our observation that Bosentan inhibits ERK1/2 MAPK activity and increases p27(Kip) expression may explain the observed reduction of vessel wall thickening, which has been documented in clinical studies.|PMC3756002|ET-1 activates and Bosentan prevents Erk1/2 MAPK 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has been reported in several systems, quercetin is a potent competitive inhibitor of GLUT1 whereas it was also reported to inhibit the uptake of glucose and of (nonmetabolized) deoxy-D-glucose in HepG2 cells, but over 12 h, increased mRNA expression of the main GLUTs GLUT1 and of GLUT9, presumably as a response to the acute inhibition.|PMC6207159","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"24447278":{"subject":"PUBCHEM.COMPOUND:5816","object":"NCBIGene:836","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:10728402"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"increases 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OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|However, OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|VEGF protein levels were unaffected in Caki-1 cells treated for 16h with dDAVP, but were significantly reduced by Tolvaptan and OPC31260 (Fig-5G).|PMC7007354","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"47836366":{"subject":"PUBCHEM.COMPOUND:6322","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Taken together, these data showed that l-arginine activated both ERK1/2 and its downstream effector, CREB.|PMC3961283|Activation of the ERK1/2 pathway was also confirmed by western blotting, which showed that phosphorylated ERK1/2 MAPK was elevated in poly-l-arginine-treated cells (Fig. 6B).|PMC2920803|These results suggest that l-arginine promotes the synthesis and secretion of GH and IGF-1 in vitro and induces the MAPK signaling cascade in cultured hepatocytes.|PMID:30263714|In the present study, we demonstrated that l-arginine treatment following a period of starvation resulted in the activation of ERK1/2 and CREB, suggesting the involvement of the entire ERK1/2 pathway in the response to l-arginine in human dermal fibroblasts.|PMC3961283|The expression of ERK-1 in brain was much higher in CHM group than in L-arg group (P < 0.05), the expression of MKP-1 was almost the same (P > 0.05); Both of them in liver were higher in CHM group than in L-arg group (P < 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in obese mice inhibited glucose sensitivity in OGTT, improved plasma leptin and insulin sensitivity, reversed hypothalamic pituitary adrenal (HPA) axis hyperactivity by reducing the corticosterone concentration, restored brain pro-oxidant/anti-oxidant balance by inhibiting MDA and elevating GSH concentrations and facilitated serotonergic neurotransmission.|PMID:26188166","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"81613686":{"subject":"UNII:15C2VL427D","object":"NCBIGene:7423","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"decreased"}],"attributes":[{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:drugcentral","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":11.717,"value_type_id":"EDAM:data_0006","original_attribute_name":"affinity"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Kd","value_type_id":"EDAM:data_0006","original_attribute_name":"affinityParameter"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"114906868":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Western blot analysis showed that after injection of AMD3100, minocycline, or both, the expressions of CXCR7, p-PI3K, and p-Akt were significantly increased in the spinal cords of SMIR rats (Fig. 6b, for CXCR7: F(3, 16) = 6.523,|PMC7362409|Characterization of MSC following treatment with IGF1 and AMD3100, which indicated elevated PI3k/Akt, suggests its effects on MSC proliferation.|PMC3339043|Thus, the level of threonine-phosphorylated Akt, pAkt(T308), was less than 10% of that in normal controls ( Fig. 2B and C ), suggesting that Akt was minimally activated in PBMC of the AMD patients.|PMC5460613|Active phosphorylated prosurvival kinase Akt is increased both in the beta-cells of RIP-SDF-1 mice and in INS-1 cells treated with SDF-1 and sensitive to AMD3100.|PMID:17878289|In line with this, we found that during the development of CPSP, an increase in A1 astrocytes was accompanied by reduced activation of the PI3K/Akt pathway, while the decrease in A1 astrocytes induced by AMD3100 and minocycline was accompanied by increased activation of the PI3K/Akt 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(LEV) increased the levels of vascular endothelial growth factor (VEGF), hypoxia-inducible factor-1α (HIF-1α), and heat shock protein 70 (HSP70) in the cerebral cortex of middle cerebral artery occlusion (MCAO) rats on day 14.|PMC8161206|Levetiracetam (LEV) increased the levels of vascular endothelial growth factor (VEGF), hypoxia-inducible factor-1α (HIF-1α), and heat shock protein 70 (HSP70) in the cerebral cortex of middle cerebral artery occlusion (MCAO) rats on day 14.|PMC8161206","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.999299925","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8161206","PMC8161206"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"46766863":{"subject":"PUBCHEM.COMPOUND:56603655","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"To review clinical data on the sequential use of the non-selective vascular endothelial growth factor (VEGF) inhibitors (ranibizumab and bevacizumab) and the selective VEGF inhibitor (pegaptanib) in the treatment of neovascular age related macular degeneration (n-AMD).|PMID:22283373|There are many other drugs that may play a role in DR therapy in coming few years such as somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|A number of drugs may play a role in DR therapy in the coming few years; eg, somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|Nowadays, VEGF-inhibitors like bevacizumab, ranibizumab, pegaptanib, are the first choice in therapies for the treatment of neovascular ocular diseases.|PMC6249906|In this way, the effect of VEGF inhibitors (pegaptanib, bevacizumab, ranibizumab) on primary cultures of human REC and CEC was evaluated by Stewart et al.. Significant differences between retinal and choroidal microvascular cells were observed, which highlights the need for specific treatment interventions in RNV or CNV.|PMC6321100","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.994459330137741","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a5b11a5824814a330d7833e39b2111e408efe21c2d57f91b17d0cb8a39fb2209","tmkp:a1045037a5b4997ec6e129ff26391d1dfc65332df0dec137ac13e0b2dd6db29e","tmkp:a818616ba635c55029c97fed42c1d6cf650b8244527a457eec9fa0b31b52132d","tmkp:71d30db22b5c44f1bae06728a8c1f643faceccff93cee35e6849757442abca0b","tmkp:df50b8010afb0e2bc8986df49f96e4c15e263513abceb552bf798ee605ee59ca"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:22283373","PMC2701130","PMC2701130","PMC6249906","PMC6321100"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"94234278":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7573922","PMC6977684","PMC7463778","PMC4035553","PMC6873690","PMID:12479367","PMID:19393235","PMC5372848","PMID:24184201","PMC6639401"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In these conditions, the combination DHA/Tamoxifen induced a significant increase of p-ERK1/2 and p-Akt expression compared to the control condition without either DHA or Tamoxifen.|PMC5372848|In addition, resistance to tamoxifen treatment was found to be not associated with alterations in expression of any AKT isoform, but resistance to tamoxifen is associated with a higher amount of pAKT1 and therefore AKT1 kinase activity in an ER-positive breast cancer cell line.|PMC6873690|Thus, injection of tamoxifen leads to the immediate activation of PKB/Akt, which in turn strongly activates mTORC1 (Fig. 8b).|PMC6639401|These studies show that endogenous Akt activity promotes breast cancer cell survival and therapeutic resistance, and that induction of Akt by chemotherapy, trastuzumab, or tamoxifen might be an early compensatory mechanism that could be exploited to increase the efficacy of these therapies.|PMID:12479367|In addition, cultured macrophages obtained from RagA-iKO mice 2 weeks after starting tamoxifen treatment showed reduced levels of RagA, reduced mTORC1 activation, and increased Akt activity (Supplementary Figure 4g).|PMC4035553","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9962409747945205","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:961fb188c0d77633be4f2b0dc69e894e452f92ad5d7b97dae2731188af6efddf","tmkp:a0d87ae8f40c29bbd633f17d0dd2a3c4015d7773f8c0eae6e4ef9193a02e901f","tmkp:a9aa28180abbdd8ece42e9505d4ec4f66ef1ff9a9315930ae6e1f24fa97daa5c","tmkp:8d9da54f8c379fd7b55dd0fdbbc96f5ace6cf97c2548f69d3db7712010c42279","tmkp:f7afbfcb06031e8bbf9f688cce2ad7b157c3cc9a40b1cc605104bc623eda7ac6","tmkp:1897a020752b6a5d16c033b408ead8f8b6fa2908ef3c237a76bfb3a916826594","tmkp:47d7e8ab6f7afb1369b548a526d6acb22898335f303359926d423c027df2ebbe","tmkp:2af6dbf582864402932fba8e53ac8080c742e2dd08d1cbb906770508baed3a4b","tmkp:5bcf097a6e4d2d63a34ca07d60e2184f7e82494ce78c5ca8acfb110f2795c041","tmkp:901ea096c09bdabda7e734722cae83d46dc6028a8ff822e9089b30d765fa1fd3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"22432869":{"subject":"PUBCHEM.COMPOUND:3121","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5503485","PMC3032892","PMC6213525","PMC2585842","PMC7461984","PMC3036563","PMC4624173","PMC2788821","PMC4549030","PMC6322559"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3d869db3080b37c012888cf65110a168101eb888e546b805ecd79f4013982c65","tmkp:15f3c1341b4236e2ae6e53b777eb079e2b7d9eab0d3595219261ff2698981fbc","tmkp:abb21da18d1f147a1f7810fa74d1531913c2d86c63658d4a8c97484329795327","tmkp:e6f46d0b89aa661bd6702659df7f94dd901faf6589b23cc4e20cc95f3d15895e","tmkp:7500c074dfcd7a3465c1880146de88230fd9791127b4664f1a013a23099ea8b7","tmkp:b43cb090a70e9cf90108845312fa1c1fad64319772fed0476d171aca2e9a4490","tmkp:675583cdfea43b1bd7143cb0553ab31c3525359cbe9c389be5ce5fe8990e1bca","tmkp:6a2fe357bbc3e1d18d42d4a3522f45571e583887e7de050f3ae401087bd91045","tmkp:27d4068f552742c7768df6bb78a1bd27fc7e79233573cf77c25a105884682d82","tmkp:05a7aa4a22bfd25db8325fcc4f60fdf1602be3abd0917a139bb408ef9712515d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Western blot analysis indicated that the phosphorylation of p38MAPK in LPS-activated microglia was significantly increased at 10 min after VPA addition compared with that in the control (Fig. 8A).|PMC6322559|Rats treated with clinically relevant doses of lithium or valproate demonstrate activation of the MAPK/ERK pathway and increased transcription of BDNF.|PMC5503485|These results suggest that VPA increases activated MAPK levels through inhibition of a cAMP/PKA dependent de-phosphorylation of pERK2 whilst the lithium-dependent effect occurs through GSKA/3-dependent signalling.|PMC3032892|VPA has been found to activate extracellular signal-regulated kinase, a protein kinase known to regulate AP-1 function, and mediate neurotrophic responses.|PMC2585842|Although VPA acutely affects gamma-aminobutyric acid (GABA) levels, recent studies have shown that chronic VPA robustly upregulates the ERK/MAPK cascade in neuronal cells; this raises the intriguing possibility that VPA, via its effects on the ERK/MAPK cascade, may be able to regulate Notch3/c-FLIP-mediated cytoprotection.|PMC2788821","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9960562072727273","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"68641549":{"subject":"PUBCHEM.COMPOUND:977","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In a rat model of bronchopulmonary dysplasia (BPD), exposure of neonatal lungs to high (95%) oxygen reduced the expression of Akt, while overexpression of Akt was protective against lung damage.|PMC7520643|↑, an increase in target protein; ↓, a decrease in target protein; PARP, poly ADP-ribose polymerase; ERK, extracellular regulated protein kinases; TGF-β1, transforming growth factor-β1; MMP, mitochondrial membrane potential; AQP1, aquaporin 1; VEGF, vascular endothelial growth factor; AMPK, AMP-activated protein kinase; EMT, epithelial-mesenchymal transition; PI3K, phosphoinositide-3-kinase; JNK, c-Jun N-terminal kinase; NF-κB, nuclear factor-κB; PCNA, proliferating cell nuclear antigen; COX-2, cyclooxygenase-2; HIF-1α, hypoxia-inducible factor-1; ROS, reactive oxygen species; STAT3, signal transducer and activator of transcription 3 Rac1, Rac family small GTPase 1; MAPK, mitogen-activated protein kinase; TNF-α, tumor necrosis factor α; PKC-α, protein kinase C system -α; LC3I, the protein expressions of light chain 3I; LC3II, the protein expressions of light chain 3II; Atg7, autophagy related 7; AKT, protein kinase B; GSK3β, glycogen synthase kinase 3β; P-gp, P-glycoprotein; MDR1, multidrug resistance protein 1; α-SMA, alpha-smooth muscle actin; LncRNA-ATB, long non-coding RNA activated by transforming growth factor-β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; HSP, heat shock protein; GRP78, glucose regulated protein 78; Bip, binding immunoglobulin protein; XIAP, X-linked inhibitor of apoptosis protein; MCL1, myeloid-cell-leukemia 1; cFLIP, cellular FLICE-like inhibitory protein; mTOR, mammalian target of rapamycin; B7-H3, GPI-linked CD59 and costimulatory molecule CD276; CTL, cytotoxic T lymphocytes; IDO-1, indolemaine-2,3-dioxygenase-1; CREB, cAMP-response element binding protein; GNF, gastric normal fibroblast; GCAF, gastric cancer-associated fibroblast; IFN-γ, interferon-gamma; MNNG, N-methyl-N′-nitro-N-nitrosoguanidine; TIGAR, TP53-induced glycolysis and apoptosis regulator; PLGC, precancerous lesions of gastric carcinoma; NOX, NADPH oxidase; iNOS, inducib|PMC7834967|↑, an increase in target protein; ↓, a decrease in target protein; PARP, poly ADP-ribose polymerase; ERK, extracellular regulated protein kinases; TGF-β1, transforming growth factor-β1; MMP, mitochondrial membrane potential; AQP1, aquaporin 1; VEGF, vascular endothelial growth factor; AMPK, AMP-activated protein kinase; EMT, epithelial-mesenchymal transition; PI3K, phosphoinositide-3-kinase; JNK, c-Jun N-terminal kinase; NF-κB, nuclear factor-κB; PCNA, proliferating cell nuclear antigen; COX-2, cyclooxygenase-2; HIF-1α, hypoxia-inducible factor-1; ROS, reactive oxygen species; STAT3, signal transducer and activator of transcription 3 Rac1, Rac family small GTPase 1; MAPK, mitogen-activated protein kinase; TNF-α, tumor necrosis factor α; PKC-α, protein kinase C system -α; LC3I, the protein expressions of light chain 3I; LC3II, the protein expressions of light chain 3II; Atg7, autophagy related 7; AKT, protein kinase B; GSK3β, glycogen synthase kinase 3β; P-gp, P-glycoprotein; MDR1, multidrug resistance protein 1; α-SMA, alpha-smooth muscle actin; LncRNA-ATB, long non-coding RNA activated by transforming growth factor-β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; HSP, heat shock protein; GRP78, glucose regulated protein 78; Bip, binding immunoglobulin protein; XIAP, X-linked inhibitor of apoptosis protein; MCL1, myeloid-cell-leukemia 1; cFLIP, cellular FLICE-like inhibitory protein; mTOR, mammalian target of rapamycin; B7-H3, GPI-linked CD59 and costimulatory molecule CD276; CTL, cytotoxic T lymphocytes; IDO-1, indolemaine-2,3-dioxygenase-1; CREB, cAMP-response element binding protein; GNF, gastric normal fibroblast; GCAF, gastric cancer-associated fibroblast; IFN-γ, interferon-gamma; MNNG, N-methyl-N′-nitro-N-nitrosoguanidine; TIGAR, TP53-induced glycolysis and apoptosis regulator; PLGC, precancerous lesions of gastric carcinoma; NOX, NADPH oxidase; iNOS, inducib|PMC7834967|↑, an increase in target protein; ↓, a decrease in target protein; PARP, poly ADP-ribose polymerase; ERK, extracellular regulated protein kinases; TGF-β1, transforming growth factor-β1; MMP, mitochondrial membrane potential; AQP1, aquaporin 1; VEGF, vascular endothelial growth factor; AMPK, AMP-activated protein kinase; EMT, epithelial-mesenchymal transition; PI3K, phosphoinositide-3-kinase; JNK, c-Jun N-terminal kinase; NF-κB, nuclear factor-κB; PCNA, proliferating cell nuclear antigen; COX-2, cyclooxygenase-2; HIF-1α, hypoxia-inducible factor-1; ROS, reactive oxygen species; STAT3, signal transducer and activator of transcription 3 Rac1, Rac family small GTPase 1; MAPK, mitogen-activated protein kinase; TNF-α, tumor necrosis factor α; PKC-α, protein kinase C system -α; LC3I, the protein expressions of light chain 3I; LC3II, the protein expressions of light chain 3II; Atg7, autophagy related 7; AKT, protein kinase B; GSK3β, glycogen synthase kinase 3β; P-gp, P-glycoprotein; MDR1, multidrug resistance protein 1; α-SMA, alpha-smooth muscle actin; LncRNA-ATB, long non-coding RNA activated by transforming growth factor-β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; HSP, heat shock protein; GRP78, glucose regulated protein 78; Bip, binding immunoglobulin protein; XIAP, X-linked inhibitor of apoptosis protein; MCL1, myeloid-cell-leukemia 1; cFLIP, cellular FLICE-like inhibitory protein; mTOR, mammalian target of rapamycin; B7-H3, GPI-linked CD59 and costimulatory molecule CD276; CTL, cytotoxic T lymphocytes; IDO-1, indolemaine-2,3-dioxygenase-1; CREB, cAMP-response element binding protein; GNF, gastric normal fibroblast; GCAF, gastric cancer-associated fibroblast; IFN-γ, interferon-gamma; MNNG, N-methyl-N′-nitro-N-nitrosoguanidine; TIGAR, TP53-induced glycolysis and apoptosis regulator; PLGC, precancerous lesions of gastric carcinoma; NOX, NADPH oxidase; iNOS, inducib|PMC7834967|↑, an increase in target protein; ↓, a decrease in target protein; PARP, poly ADP-ribose polymerase; ERK, extracellular regulated protein kinases; TGF-β1, transforming growth factor-β1; MMP, mitochondrial membrane potential; AQP1, aquaporin 1; VEGF, vascular endothelial growth factor; AMPK, AMP-activated protein kinase; EMT, epithelial-mesenchymal transition; PI3K, phosphoinositide-3-kinase; JNK, c-Jun N-terminal kinase; NF-κB, nuclear factor-κB; PCNA, proliferating cell nuclear antigen; COX-2, cyclooxygenase-2; HIF-1α, hypoxia-inducible factor-1; ROS, reactive oxygen species; STAT3, signal transducer and activator of transcription 3 Rac1, Rac family small GTPase 1; MAPK, mitogen-activated protein kinase; TNF-α, tumor necrosis factor α; PKC-α, protein kinase C system -α; LC3I, the protein expressions of light chain 3I; LC3II, the protein expressions of light chain 3II; Atg7, autophagy related 7; AKT, protein kinase B; GSK3β, glycogen synthase kinase 3β; P-gp, P-glycoprotein; MDR1, multidrug resistance protein 1; α-SMA, alpha-smooth muscle actin; LncRNA-ATB, long non-coding RNA activated by transforming growth factor-β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; HSP, heat shock protein; GRP78, glucose regulated protein 78; Bip, binding immunoglobulin protein; XIAP, X-linked inhibitor of apoptosis protein; MCL1, myeloid-cell-leukemia 1; cFLIP, cellular FLICE-like inhibitory protein; mTOR, mammalian target of rapamycin; B7-H3, GPI-linked CD59 and costimulatory molecule CD276; CTL, cytotoxic T lymphocytes; IDO-1, indolemaine-2,3-dioxygenase-1; CREB, cAMP-response element binding protein; GNF, gastric normal fibroblast; GCAF, gastric cancer-associated fibroblast; IFN-γ, interferon-gamma; MNNG, N-methyl-N′-nitro-N-nitrosoguanidine; TIGAR, TP53-induced glycolysis and apoptosis regulator; PLGC, precancerous lesions of gastric carcinoma; NOX, NADPH oxidase; iNOS, inducib|PMC7834967","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e9c9a328ad90ae6a7d7b01f873317dc52216bf2e1003574499f886938f161b38","tmkp:297cda5960634797db5cd4a0272381407dc71a562d4717aa693f2b1a774e3a6b","tmkp:c0d71e9dbe7eafb5a25dc4f159bfd4ee94c6708b0c0d286fd77a41b2f3b2b7e9","tmkp:cad5914cb0e64d8c2dfe4cc329fef6080916f1449294bdf8f5f37f4860bd97e7","tmkp:e1695280f71108c3da28599d4bc25b94c6e11e85bbd2201eaf728af067e562dd","tmkp:b8eec47195c95a1745605cdd34b330c5544a83210c83b52b8cca52103fa1b20a","tmkp:fff077fc49220c44fcb6b6119cc69e86a8573c580a03ed44a5b1cba836d3e1a9","tmkp:0ccf429235ff44ff9cbedd4e2476bf600ac0ab6f2c75aa1d71a9958f75a7743a","tmkp:1e6975dc15b0008543b0b8f94ea60dde715dea35fbb3a1c7b571833af6334aa0","tmkp:0edfb82ba70d2d38989fa4ab4643e0369ac85cc48c1fa8f5917e636ed403f35f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC7520643","PMC2817727","PMC6019737","PMID:17765386","PMID:19494322","PMC7834967","PMC4412352"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9949195535294119","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"17441050":{"subject":"NCBIGene:7423","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:ab2d107b8d73e42ed38e55e3995c42583ac8aec4fed3f74c1cdb053984c0bf01","tmkp:453915541096300c5fb42df5a7d4f7e394e03a693d920d9f9ed4d89e323a0389","tmkp:1fe00800ab0e7cd3be74c58347b8a031fdf3f560d5eae46abe65e616a629b512","tmkp:71877dfb4eacc3c7c90f963b88c24e9ac8ef79cdce85fc28e2537b114d34402b","tmkp:d06d482b80da5a46d10841107d51c91ebf41cd10669e871b2b3c0069e791ec37"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9924922993749999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Development of tears in the retinal pigment epithelium (RIP) has been described as a possible complication following anti-vascular endothelial growth factor (VEGF) antibody therapy with substances which have been available for years when treating pigment epithelium detachment (PED) in eyes affected by age-related macular degeneration (AMD).|PMID:24062151|Atrophy may complicate eyes with PED and nAMD after anti-VEGF therapy, especially in association with complete PED resolution.|PMID:29697591|Development of tears in the retinal pigment epithelium (RIP) has been described as a possible complication following anti-vascular endothelial growth factor (VEGF) antibody therapy with substances which have been available for years when treating pigment epithelium detachment (PED) in eyes affected by age-related macular degeneration (AMD).|PMID:24062151|RPE tears may develop during the course of anti-VEGF therapy for age-related macular degeneration-related PED.|PMID:17558312|Atrophy may complicate eyes with PED and nAMD after anti-VEGF therapy, especially in association with complete PED 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GLUT1 gene-related form of PED may respond to a ketogenic diet.|PMID:21626559|Mutations in SLC2A1, encoding the glucose transporter type 1 (Glut1), cause a wide range of neurological disorders: (1) classical Glut1 deficiency syndrome (Glut1-DS) with an early onset epileptic encephalopathy including a severe epilepsy, psychomotor delay, ataxia and microcephaly, (2) paroxysmal exercise-induced dyskinesia (PED) and (3) various forms of idiopathic/genetic generalized epilepsies such as different forms of absence epilepsies.|PMID:25022942|Mutations in SLC2A1, encoding the glucose transporter type 1 (Glut1), cause a wide range of neurological disorders: (1) classical Glut1 deficiency syndrome (Glut1-DS) with an early onset epileptic encephalopathy including a severe epilepsy, psychomotor delay, ataxia and microcephaly, (2) paroxysmal exercise-induced dyskinesia (PED) and (3) various forms of idiopathic/genetic generalized epilepsies such as different forms of absence epilepsies.|PMID:25022942|Mutations in SLC2A1, encoding the glucose transporter type 1 (Glut1), cause a wide range of neurological disorders: (1) classical Glut1 deficiency syndrome (Glut1-DS) with an early onset epileptic encephalopathy including a severe epilepsy, psychomotor delay, ataxia and microcephaly, (2) paroxysmal exercise-induced dyskinesia (PED) and (3) various forms of idiopathic/genetic generalized epilepsies such as different forms of absence epilepsies.|PMID:25022942|Mutations in SLC2A1, encoding the glucose transporter type 1 (Glut1), cause a wide range of neurological disorders: (1) classical Glut1 deficiency syndrome (Glut1-DS) with an early onset epileptic encephalopathy including a severe epilepsy, psychomotor delay, ataxia and microcephaly, (2) paroxysmal exercise-induced dyskinesia (PED) and (3) various forms of idiopathic/genetic generalized epilepsies such as different forms of absence epilepsies.|PMID:25022942","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:21626559","PMID:25022942","PMID:25022942","PMID:25022942","PMID:25022942"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"116719303":{"subject":"PUBCHEM.COMPOUND:5743","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7c8839baac1f359cf8bfc0e75539589da86416e4bfddb6a8adadaab4f6257994","tmkp:fc6bb16d230f0e9498c78249dd205a212505c1b800a937bb397a148febe36acf","tmkp:e27f24bbc24000974932511547f68748a34be027755a0a89a522cd512a3acc90","tmkp:12a50c86a5c1a4e8213a722e4ad7565752114b7cb43cc78eb8bd17c2727e696a","tmkp:61320d1be27cb4711033059e1d69aa9d452cc8bdfcc9bee6f241521351fb9cdd","tmkp:f5c9950e145e2fa126bbf318f55710ffba021ffa2b6bcc797a7ee6b0cd411c52","tmkp:477817c811fa491ff70a36fcff8f5ffeb6736867fb0c27b519e6f53d52050529","tmkp:b486635db97547407aafcf9affb659337e91e04e989384119f007f6fb3af9a8a","tmkp:26b90c653a5bf5b2864f7a5a7ab92363c4e1eb69a58d1a4b191c9c80fda40cd8","tmkp:5d8aba1d8b7df17037f574db4077ce93a202ad6715f4a619d08b2a76096c0a6d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:11246818","PMID:1738371","PMID:8452867","PMID:21079357","PMID:2536889","PMID:2469009","PMID:1375108","PMID:1704320","PMC6276259","PMID:2157975"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Incubation with 8-bromo-cAMP plus dexamethasone also results in an 80-90% decrease in PAI-1 mRNA, but causes a synergistic 10- to 20-fold increase in tPA mRNA and protein.|PMID:2157975|However, after 24 and 48 h, dexamethasone significantly reduced the IL-1beta induced increase in PAI-1 activity by 24-52% (p < 0.05), accordingly, PAI-1 mRNA expression was reduced 60%.|PMID:11246818|Dexamethasone and cA in combination cause a 150-fold increase in PA activity, the result of an 80% decrease in PAI-1 and a synergistic 15-fold increase in tPA mRNA.|PMID:1738371|After the follow-up period, gene expression of Pai-1 and Tgfβ was decreased both in vehicle and dexamethasone treated groups as compared to immediately after treatment (Fig. 3a and c).|PMC6276259|When resident or thioglycollate-activated macrophages were incubated with the anti-inflammatory agent dexamethasone, the drug depressed both the expressions of PA and PAI, in the lysate and conditioned medium of both cell types.|PMID:8452867","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9974900041666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"14830590":{"subject":"PUBCHEM.COMPOUND:36314","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2195578","PMC3189568","PMC6797991","PMC4652134","PMC4211477","PMC2914832","PMC3995800","PMC4317914","PMC7717644","PMID:20731895"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:25ef6044d6c4faf37040467610233b913616ca478c3c977e305e399f283bc0ab","tmkp:48e9d71064aacfd9a22f636b537bfbffdee7337c646f8a8c38b9973b662a26ed","tmkp:966f7721cdf2df4d150a63aab5ab3f9b6e062d8f204a87169fb81d296e49036d","tmkp:343da5f5e2b03e5f4198d42f8a6efb0bab0d0c928d2a36fb1407934c2fa0cab7","tmkp:c05e78e6b43339ca88fc493db7f9d555b7efecb37f435fdd6a79d45826bce01c","tmkp:76f45fb927794e2056924d4105552c3d290281d593effaf94f25a358f59b9a9e","tmkp:cb1dc5b445a8a5fc2eafde2c4f6d008f1b5171401edbd84557cc38c9e5f4769e","tmkp:6e07b37845af16c1720fd227822c4a6a960a14e586b4ead7eb42d6b4f1c0de4f","tmkp:4fb920d3bd4d9b955372ba06118a00eeae013730a7b7b073513a54ab74b225b1","tmkp:2217448e34f5acd12278f1f1dc1c1a58c758e9a4126111fb77a771338ae8109a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9938660186231885","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The tumor-inhibiting rate of paclitaxel plus LY294002 (92.47%) was significantly higher than the paclitaxel alone (65.59%)(P <0.05).The protein expression of bcl-2 in paclitaxel plus LY294002 group were significantly higher, while bax was significantly lower than that in the other two groups (P <0.05).|PMID:20731895|Furthermore, paclitaxel might also induce mitochondria-mediated apoptosis of malignant pleural mesothelioma cells, even though paclitaxel upregulated expression of the mRNA for the anti-apoptotic factor Bcl-2 in NCI-H2052 cells.|PMC4317914|Paclitaxel treatment following miR-17-5p transfection for 24 h resulted in the increase in Bax (pro-apoptotic)/Bcl-2 (anti-apoptoic) ratio in A549-T24 cells accompanied by an increase in p53 level and increase in the amount of a 19 kDa caspase-3 cleavage intermediate as well as cleaved poly (ADP-ribose) polymerase (PARP) (Fig. 8A and Fig. S5A–C).|PMC3995800|Activating TLR-4 with paclitaxel resulted in the recruitment of MyD88, induction of anti-apoptotic proteins X-linked inhibitor of apoptosis, Bcl-2, and Bcl-XL, and activation of pro-survival pathways, ultimately leading to increased cancer cell resistance to chemotherapy .|PMC4652134|In U87 cells treated with the combination of BPD and paclitaxel, BPD attenuated the paclitaxel-induced upregulation of YAP, TAZ, Bcl-2, and EGFR expressions by 56%−67% (Figure 4f–i).|PMC7717644","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"99466320":{"subject":"PUBCHEM.COMPOUND:3033","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Diclofenac increased the secretion of VEGF induced by LPS and 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of the ECM deposited by HDFs cultured under MMC revealed increased staining intensities for collagens I and IV, fibronectin and perlecan compared to cultures without MMC (Fig. 2A).|PMC6897920|Subsequent validation using ICC (Fig. 6) and complementary fluorescence intensity (Fig. S13) further confirmed the high deposition of collagenous proteins (I, III, IV, V, VI) and fibronectin under MMC conditions (0.5% HS, FC, 6 days in culture), whilst no difference was observed for unintended differentiation markers (α SMA) and phenotypic markers (CD34, keratocan; Fig. S14) for all time points (2, 4 and 6 days in culture).|PMC4348624","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"5693606":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:142","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:15905168","PMID:24124520"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"dct:description","value":"increases 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with ouabain (3 nM) followed by glycoside washout potentiated insulin induction at 2 mM, but not at 8 mM glucose, but this same pretreatment followed by incubation in Ca(2+)-free medium depressed insulin release under all conditions, and especially at high glucose; here, however, the preexposure to ouabain partially prevented the drop in insulin secretion at 8 mM glucose.|PMID:9440253|A twofold increase in insulin release that occurred in the 15 min period immediately following exposure to 1 mM ouabain was completely independent of [Ca](o).|PMID:327058|Furthermore, ouabain induces increased secretion of insulin and in vitro inhibits the metabolic effects of epinephrine.|PMC5358298|Our findings indicated an overall of 1.4-fold increase in insulin secretion by wild-type and ABCC8-deficient cells treated with ouabain (Fig. 1H).|PMC5466656|However, it remains unknown whether the insulin secretion increased by ouabain is dependent on KATP 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was observed that insulin signalling was elevated in livers from animals treated with clozapine indicating there was no insulin resistance in the early steps of insulin signalling.|PMID:24906220|However, we provide strong evidence that elevated insulin levels induced by clozapine are in fact the real cause of the drug's effects on Akt/PKB and GSK3 in the brain.|PMID:24800899|The clozapine 10-mg/kg group also had significant increases in plasma insulin concentrations compared with the vehicle group (12.70 [5.27] vs 7.62 [4.54] μIU/mL; P < 0.05) and IRI (3.01 [1.26] vs 1.51 [0.96]; P < 0.05).|PMID:24692793|Interestingly, this stimulatory effect on insulin release in vitro may be supported by recent clinical findings, showing elevated insulin levels in patients being treated with clozapine or olanzapine.|PMID:15013026|Clozapine treatment has been associated with elevated insulin levels when compared to patients taking typical antipsychotics, suggesting that clozapine induces insulin 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shown in Fig. 4B, CPZ reduced the growth of the WT strains and the mutants lacking Cig1 (and Cig1+Cfo1) or Vps45 on 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we hypothesized that p38 is phosphorylated and activates the p38-MAPK signaling pathway upon TNT treatment, so we evaluated p38 phosphorylation over time.|PMC6499805|Additionally, we identified enrichment of the p38-MAPK pathway in both TNT-treated ahRPE and patient-dissected PVR 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aflibercept was also able to inhibit PDGF-BB induced phosphorylation of ERK1/2 but not bFGF induced phosphorylation of ERK1/2 (S1D and S1E Fig).|PMC5201251|Furthermore, our findings indicate that increased phosphorylation of cPLA2 is linked to HG-induced VEGF-A upregulation; in fact, VEGF-A blockade with Aflibercept was able to prevent both HG-induced cell damage as well as phosphorylation of ERK1/2 and 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an in vitro study, Albano et al. found that only high molecular weight form of sodium hyaluronate efficiently inhibited the IL-17A-mediated activation of ERK1/2 and nuclear factor kappa B and production of reactive oxygen species in human nasal epithelial cells.|PMC6032683|In an in vitro study on human nasal epithelial cells, Albano et al. observed that only high-molecular-weight form of sodium hyaluronate efficiently inhibited the rhIL17Amediated activation of ERK1/2, IkBa phosphorylation and NF-kB signal pathway activation, ROS production, IL-8 and NOX-4 proteins, and mRNA levels, therefore exhibiting an anti-inflammatory/anti-oxidative effect.|PMC8186654|According to Yatabe, hyaluronic acid is effective in reducing ADAMTS-4 via a combined inhibition of NF-κB and ERK1/2 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carry out the western-blot analysis, proteins in the crude tissue extracts or in the cell membrane fractions were resolved by SDS-PAGE (10% Tris-Acrylamide-Bis) and electrotransferred from the gel to nitrocellulose membranes (Hybond-ECL, Amersham Pharmacia, Piscataway, NJ) as described by Towbin et al.. Nonspecific protein binding to the nitrocellulose membrane was reduced by preincubating the filter with blocking buffer (TNT, 7% BSA); then, membranes were incubated overnight with the primary antibodies Glut4 (sc-7938, diluted 1 : 2,500), Akt (sc-7126, diluted 1 : 2,000), and phosphorylated-Ser473-Akt (sc-101629, diluted 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reduced the proliferation and adhesion capacity of EPCs to fibronectin (FN), whereas it increased the adhesion capacity of EPCs to human umbilical vein endothelial cells (HUVECs).|PMC7453604","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"38034750":{"subject":"PUBCHEM.COMPOUND:65028","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5130050"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996635","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:bf493ad78bafe651766dcb522d607033853b20bb1f690055b85309919d88c8ea"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"To validate the Western blot analyses, Bio-Plex phospho-protein multiplex analyses showed that simultaneously examined phospho-protein end-points of Akt-Thr308, PDGFRα-Tyr754 and STAT1-Tyr701 were diminished in the tumor lysates from oseltamivir phosphate treated cohort compared to the untreated group.|PMC5130050","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"50437769":{"subject":"UNII:ZL1R02VT79","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"PED was associated with a higher number of ranibizumab injections only in the monotherapy group (+1.2).|PMID:25079064|(H) One month after the last injection of ranibizumab, a recurrent large PED can be seen.|PMC3935506|(I) Three months after the last injection of ranibizumab, a recurrence of the SRF and PED are observed.|PMC3935506|Intravitreal ranibizumab injection caused PED flattening with apparent contracture of the accumulated material within the PED.|PMID:19152869|Treatment with the loading dose ranibizumab failed in our patient, on the basis of the loss of vision and persistence of PED as observed on OCT imaging.|PMC5903101","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9879036878571429","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:25079064","PMC3935506","PMC3935506","PMID:19152869","PMC5903101"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:665a6783efe6ad9ec911aea6ba9102c5f4784632319c61b94c7936292fb17437","tmkp:633c5562369ef65cf4a9d2c1cf6a578a1489645fb13b67747934d2394def042c","tmkp:4b4108bbc75d9c261e1b0cddccb9702f70b5424feda8852e88b6b7f7effba9f3","tmkp:cc5226160052f647e57df73c6ec4c0fd5ba086e93ab0ca4c0ddfc2acde199bea","tmkp:3e589164649fbcc5e9c1de70e90f6a6f8d46f813b1d9a2fbfd8f1997e43c113e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"116976868":{"subject":"UNII:15C2VL427D","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4954942","PMC5454820","PMID:27314606","PMC4211604","PMC5207393","PMC7027529","PMID:25458604","PMC6893275"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b223e908e252cd06cffabf9394dd60c6b8ef514f44bb0478f6a4e2b5185ec4a5","tmkp:1eded4a4fd1b967bef00161ffbc406f7ad718b3a31e4d8b5604722b524d47a82","tmkp:985ece165b9806f9cc8744c30eb902d54607bc5986da79fa692be624fe796a08","tmkp:fcb354a6a3221d9570c64018abbd27bb6346bc4b8c78d7d372f8458fbda17429","tmkp:0d749d8409b734c15976335fe94252aa5d32c918b34c86578ea3a4632caf9c44","tmkp:ca7e092172520d43b2e9b1dc2ad12a6151caa0c765120b361633d567fea55da8","tmkp:353e10ba969e666ced413855e3ffecdcb15832f2ee9f4309a62ea7c8c0f6ad3f","tmkp:28611ba652c2928d5a7b56b7d188f57c94258c4550d4928b35bde4494be52cca","tmkp:af1cf829c0ae1be713eaead0cca1f2b09f39c10a555134d5a59766d758c26c40","tmkp:8b838a3a2115fa50989253af612d060ac75256de7857deb545dac57fdf7e9bc5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9980055585714285","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Real-time PCR analysis showed that treatment with 25 mg/kg BW aflibercept significantly upregulated the expression of fibroblast growth factor-2 (FGF-2), PlGF, VEGF, PDGF-BB, and transforming growth factor (TGF)–β mRNAs.|PMC4954942|Given the importance of the pro-angiogenic pathway downstream of VEGF, inhibiting the VEGF signaling axis has proven an effective therapy for patients with solid tumors and neovascular age-related macular degeneration; drugs such as bevacizumab and aflibercept which sequester circulating VEGF have shown efficacy in some of these clinical situations.|PMC5207393|In tumor tissues of Hepa1-6 cells, aflibercept significantly suppressed the phosphorylation of VEGFR-1 and -2 and upregulated the expression of HIF1-α, VEGF, and PlGF (Figure 4, A and B).|PMC4954942|Our results also showed that aflibercept upregulated HIF1-α expression in tumor tissues, in addition to the expression of VEGF, PlGF, FGF-2, PDGF-BB, and TGF-α.|PMC4954942|Thus, the proposed dose escalation of aflibercept was expected to achieve serum levels in excess of circulating VEGF levels reported in cancer patients as well as exceed the concentrations associated with preclinical studies.|PMC4211604","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"74634505":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:24","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7645167"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99645007","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"An 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the observed reduced tumor destructive effect of MTX/MNPs in comparison to MNPs is not fully explainable, protein analyses suggested a more unfavorable expression pattern (eg, elevated p-ERK1/2, BCL-2, VEGF, and MMP2) after MTX/MNP treatment, resulting in a progression of cell cycle as indicated, for example, by cyclin A.|PMC5388224|We found a slight upregulation of VEGF-R1 in the MTX/MNP group, indicating the insufficiency of this treatment to impair VEGF-R1 expression and inhibit tumor growth.|PMC5388224|LDE-MTX increased the expression of myocardial vascular endothelium growth factor (VEGF) associated with adenosine release; this correlated not only with an increase in angiogenesis, but also with other parameters improved by LDE-MTX, suggesting that VEGF increase played an important role in the beneficial effects of LDE-MTX.|PMID:28553113|Presence of ultrasound subclinical synovitis and increment of serum vascular endothelial growth factor in a patient with rheumatoid arthritis achieved in sustained clinical remission by treatment with adalimumab and methotrexate.|PMID:24533548|LDE-MTX increased the expression of myocardial vascular endothelium growth factor (VEGF) associated with adenosine release; this correlated not only with an increase in angiogenesis, but also with other parameters improved by LDE-MTX, suggesting that VEGF increase played an important role in the beneficial effects of LDE-MTX.|PMID:28553113","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"51700078":{"subject":"PUBCHEM.COMPOUND:104865","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9947031","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:27252842"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"However, 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tumor cells with Twist1 expression.|PMC4400392|The inhibition of MCF-7 cell growth by tamoxifen is also associated with reduction of CD36 and p-ERK1/2 (Fig. 4a–d).|PMC6302092|Additionally, TGF-β alone did not affect Akt/ERK signaling, while tamoxifen treatment abrogated Akt and ERK1/2 phosphorylation.|PMC3759878|Tamoxifen suppresses paclitaxel-, vincristine-, and bortezomib-induced neuropathy via inhibition of the protein kinase C/extracellular signal-regulated kinase pathway.|PMID:30360692|The strongest ERK1/2 inhibitory effect was observed after treatment with compound 2. A similar effect was observed after treatment with trastuzumab, tamoxifen, doxorubicin, paclitaxel and cisplatin plus echistatin, which also blocked the extracellular signal-regulated kinase (ERK1/ERK2) and 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of PDGF-AB and VEGF increased during the first days of low dose aspirin exposition; higher concentrations led to a depletion of cytokines after an initial liberation in the case of VEGF, mRNA of which was also dose-dependently increased by aspirin.|PMID:11376496|Paradoxically, this research group also reported an increase in VEGF expression in aspirin-treated female mice.|PMC6136175|Rats treated with ASA404 also produced elevated tumor tissue concentrations of cytokines and chemokines, including TNF, VEGF, IL-6 and IL-1α, MIP-1α (CCL3), KC (CXCL1) and IP-10 (CXCL10).|PMC3583340|In summary, ASA VI promotes angiogenesis of HUVECs in vitro via up-regulating the HIF-1α/VEGF pathway, and efficiently enhances the vascularization in regenerated tissue and facilitates wound healing in vivo.|PMID:29219948|The vascular endothelial growth factor level was significantly higher in the letrozole-treated group than aspirin-treated group (0.49 ± 0.26 vs 0.42 ± 0.22, P = 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and 2DG infused intravenously increased MMC period at lower dose range and in high doses induced fed-like pattern of motility.|PMID:2641423|Mitomycin C treatment of MNC from IDDM patients abolished insulin secretion inhibition in recipient mice.|PMID:7476331|Our previous study demonstrated that 10 µg/mL MMC concentration was optimal pretreatment dose, in which glucose stimulated insulin secretion and the percentage of viable islets was not decreased comparing nontreated islets which were cultured for 3 d, were implanted into the left renal subcapsular space of STZ-induced diabetic B6 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results show that the proportion of active Rho GTPases (namely RhoA-GTP, RAC1-GTP and CDC42-GTP) is increased in response to nicotine and RhoGDIA plays a crucial role in the process.|PMC5333142|Thus, further studies are required to understand the mechanisms underlying nicotine-induced changes in total RhoA, along with total RAC1 and total CDC42.|PMC5333142|As shown by qRT-PCR analysis, among the four main members of the Rho family of GTPases (RhoA, Rac1, Cdc42 and the regulatory factor RhoGDIA), RhoGDIA expression was seriously increased in response to nicotine treatment both in vitro (Fig. 3a and b) and in vivo (Fig. 3e and 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reduced airway inflammation by decreasing levels of the Th2 cytokines IL-4 and IL-13 as well as IFN-γ and CCL5 in a mouse model of asthma.|PMC6779894|Similarly, the IL-4 and IL-13 cytokine levels, evaluated by ELISA in liver homogenates, were significantly reduced in the clopidogrel-treated group (Fig 5B and 5C), likely reflecting an attenuated inflammatory cell migration to the hepatic tissue.|PMC4598158|(A) Liver collagen content, as assessed by hydroxyproline quantification, (B) IL-4 and (C) IL-13 were reduced in clopidogrel-treated mice compared to the untreated mice.|PMC4598158|Platelet inhibition resulted in significant lower infiltration of T cells and macrophages, and we also found significantly lower expression of IL-12, IL-4, IL-6, TNF-α, TGF-β, PDGFβ, MCP1, P-/E-selectin, ICAM1 and CD40L after treatment with clopidogrel.|PMID:23952051|In the murine model, treatment of S. mansoni-infected mice with the P2Y12 receptor antagonist clopidogrel reduced the size of liver granuloma, collagen deposition, the number of infiltrated eosinophils, IL-4 and IL-13 levels in liver homogenates compared with infected, untreated 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of PDGF-AB and VEGF increased during the first days of low dose aspirin exposition; higher concentrations led to a depletion of cytokines after an initial liberation in the case of VEGF, mRNA of which was also dose-dependently increased by aspirin.|PMID:11376496|Paradoxically, this research group also reported an increase in VEGF expression in aspirin-treated female mice.|PMC6136175|Rats treated with ASA404 also produced elevated tumor tissue concentrations of cytokines and chemokines, including TNF, VEGF, IL-6 and IL-1α, MIP-1α (CCL3), KC (CXCL1) and IP-10 (CXCL10).|PMC3583340|In summary, ASA VI promotes angiogenesis of HUVECs in vitro via up-regulating the HIF-1α/VEGF pathway, and efficiently enhances the vascularization in regenerated tissue and facilitates wound healing in vivo.|PMID:29219948|The vascular endothelial growth factor level was significantly higher in the letrozole-treated group than aspirin-treated group (0.49 ± 0.26 vs 0.42 ± 0.22, P = 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of PED (also known as PEA15) determines insulin resistance and impaired insulin secretion and may contribute to progression toward type 2 diabetes.|PMID:20396999|Overexpression of the PED/PEA-15 gene may contribute to insulin resistance in glucose uptake in type 2 diabetes.|PMID:9670003|Overproduction of phosphoprotein enriched in diabetes (PED, also known as phosphoprotein enriched in astrocytes-15 [PEA-15]) is a common feature of type 2 diabetes and impairs insulin action in cultured cells and in mice.|PMID:19789852|Overproduction of phosphoprotein enriched in diabetes (PED) induces mesangial expansion and upregulates protein kinase C-beta activity and TGF-beta1 expression.|PMID:19789852|The cellular abundance of the phosphoprotein enriched in diabetes (PED/PEA-15), a 15 kDa protein related to insulin resistance (IR), is increased in women with polycystic ovary syndrome 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variety of inflammatory mediators and signaling pathways are upregulated in response to paclitaxel administration such as IL-1β, IL-8, IL-6, and vascular endothelial growth factor (VEGF)-A.|PMC4061164|Moreover, significant increases in a few inflammatory mediators—such as TNF-α, VEGF, and IL-2—were observed in paclitaxel-treated mice, especially with P. gingivalis administration.|PMC6566430|Further, the expression of VEGF, the growth factor responsible for endothelial-cell proliferation and permeability, appears to be increased, following implantation of sirolimus-eluting stents, paclitaxel-eluting stents, and zotarolimus-eluting stents, as compared to the everolimus-eluting stents and bare-metal stents.|PMC6320818|A variety of inflammatory mediators and signaling pathways are upregulated in response to paclitaxel administration such as IL-1β, IL-8, IL-6, and vascular endothelial growth factor (VEGF)-A.|PMC4061164|As shown in Figure 2A-1 and A-2 and in Figure 2B-1 and B-2, RT-PCR and Western blots analysis showed that SKOV-3 and A2780 cells constitutively expressed the mRNA and and protein of VEGF and survivin, and that LPS and paclitaxel significantly (P < 0.05) increased the expression of VEGF and survivin by SKOV-3 cells in concentration-dependent manner but not by A2780 cells; Treatment with AO-1 alone significantly decreased the constitutive mRNA expression of VEGF but not survivin by SKOV3 cells (Figure 2A-1 and A-2), and also markedly (P < 0.05) counteracted the paclitaxel-induced increased mRNA and protein expression of VEGF and survivin by SKOV-3 cells but not by A2780 cells in a concentration-dependent manner.|PMC3899591","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"105776506":{"subject":"PUBCHEM.COMPOUND:4943","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9838244625","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Similarly, serum level of VEGF also increased in mice treated with sevoflurane compared to propofol with statistical significance obtained at one day after surgery (p = 0.03, two-way ANOVA + Dunnett’s post hoc tests).|PMC6994546|It was noteworthy that the ERK activator (phorbol 12-myristate 13-acetate [PMA]) treatment increased the MMP-9/VEGF levels after propofol treatment, and led to significant increase of proliferation, invasion and angiogenesis.|PMID:24089228|The expression of HIF‐1α and VEGF was increased by hypoxia and was alleviated by propofol.|PMC6515893|The expression of HIF-1α and VEGF was increased by hypoxia and was alleviated by propofol.|PMID:30680941","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6994546","PMID:30680941","PMC7417688","PMC7980239","PMC6515893","PMID:24089228","PMC8034479","PMC3980597","PMID:29805673"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:657698d6f9532e385b7cb18ab9560f5aa927195953abc497d3ec364d174f216c","tmkp:1dbd457c481a6390511e55b59c02555280fd6dd4338c52ef1dff49d72b38a166","tmkp:7812de6d8c9f0d300b264da53cd63f5bbf4b485c16369ebe1e01955c14e79fb3","tmkp:806ae1ceea439bb95d13d3c40b190a0d80af6a87f1df8c3ab2be942fdd07ecdd","tmkp:7a758d8fce5f42a480821b759074715d77b7a399a40169b51bbcb2e00fd22345","tmkp:021d2bb13d9d257f94daa2accfaff7eec78b544c0d694fb16d03a843678a2f4b","tmkp:77709570d8d5dc23375c1fd91139c5b01a8b29419c6e68477ecec8087d9176f9","tmkp:bfe75d6ca4fa7424e014de2789293a0896a2af95b9592ba2b6dc3785b8d97216","tmkp:cdf3569ac58fcb307b4661c2d75af85a174a36d3f4df0ede6abb23f0a0c04d9e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"43885073":{"subject":"PUBCHEM.COMPOUND:5755","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:25009118"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:663505f06016119d83cd33d40c0896d557da565a65692ef1d97d2fc1cadc89ce"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"This 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hit-to-lead optimization led to the identification of a group of new potent PARP-1 inhibitors, acyl-piperazinylamides of 3-(4-oxo-3,4-dihydro-quinazolin-2-yl)-propionic acid.|PMID:24388690","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9997192","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"125310457":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Human umbilical vein endothelial cells (HUVECs) treated with AS water extract activate VEGF gene expression and the p38 pathway, thereby increasing angiogenic effects of HUVECs both in vitro and in vivo .|PMC3170324|Peach seed water extract up-regulated VEGF and VEGF receptor 2 after ICH in a mouse model and inhibited glucose deprivation injury in PC12 cells.|PMC6288198|For example, hippocampal VEGF levels are increased with water maze training, and administration of VEGFR-2 inhibitors directly into the hippocampus following spatial training impairs long-term memory.|PMC3951730|A previous study using a chronic model of Pseudomonas infection of the lung in rats had shown that L-arginine given in drinking water resulted in lower IL-1β concentrations in BAL fluid in the L-arginine treated compared to the untreated group, whereas VEGF was increased.|PMC3940779|Treatment with doxycycline in drinking water will drive an increase in the expression of VEGF that results in severe vascular leakage and exudative retinal detachment within 4–5 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the phosphorylation of extracellular signal-regulated kinase (ERK) was increased by PFT-α, but not Akt phosphorylation.|PMID:21071999|Furthermore, PFT-α activated NF-κB, p38 and ERK1/2 pathways in HepG2 cells.|PMID:29258820|On the other hand, PFT-induced p53 inhibition enhanced mostly the ERK1/2 activation compared with p38 and JNK.|PMID:27012093|Concomitantly, PFT-alpha treatment prevented down regulation of ERK1/2 activation by either antibody or 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shown in Figure 4D, MAGEA6 protein remained low at 72 hr regardless of activation of KRAS/MAPK, as evidenced by the higher phosphorylation of ERK1/ERK2 Thr202 and Tyr204 under doxycycline treatment.|PMC7164953|In this cellular system, the expression of MAPK15, induced by doxycycline (Fig. 3C; Fig. S6A), also led to the increase of LC3B-II (Fig. 3C).|PMC3541284|Treatment with doxycycline/TPA or TPA alone increased phosphorylations of Elk-1(S383), PDK1(S241), Rb(S807/S811), PKCdelta(T505), p38MAPK(T180/Y182), MEK1/2(S217/S221) and ERK2(T185/T187).|PMID:19168130|Doxycycline-inducible cell lines for MAPK15 were generated by transfecting HeLa T-Rex cells with pcDNA4-Tet-On-MAPK15 plasmid.|PMC3541284|We found that the effects seen for JJN-3 cells with respect to tetR-mediated shRNA expression, as well as doxycyclin-mediated induction of ERK2 knockdown, were reproducible across the board (Fig 4D).|PMC6195277","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7164953","PMID:16202406","PMC6195277","PMID:19168130","PMC3541284","PMC8018966"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9920745666666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"47322228":{"subject":"PUBCHEM.COMPOUND:22833565","object":"NCBIGene:596","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"expression"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:11787776","PMID:15205081","PMID:15671997"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"dct:description","value":"increases 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same results have been obtained by inhibiting PED/PEA-15 interaction with PLD-1 in Ins-1EPED/PEA-15.|PMC4260953|The same results have been obtained by inhibiting PED/PEA-15 interaction with PLD-1 in Ins-1E(PED/PEA-15).|PMID:25489735|On the other hand, the first highly selective PLD2 inhibitor identified by the same group, VU0364739, has 75-fold selectivity for PLD2 versus 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enflurane has been recommended as the inhalation of choice due to its advantage of increasing blood glucose levels by inhibiting insulin release.|PMC4296367|A dose-related inhibitory effect of enflurane on glucose-stimulated insulin release was observed with almost complete inhibition being seen when the enflurane concentration in the gas phase was 3.21% (v/v), equivalent to 1.26 mM enflurane in the liquid phase.|PMID:6797325|Enflurane and halothane inhibit pancreatic insulin release, which results in hyperglycaemia.|PMC3371484|It is concluded that enflurane in the concentration range used clinically leads to a rapid, reversible inhibition of rat pancreatic islet insulin release, which is not attributable to interference with islet glucose metabolism or protein biosynthesis.|PMID:6797325|In animals, earlier studies revealed that inhalational anesthetics such as enflurane and halothane impaired glucose tolerance in dogs and that was related to inhibition of insulin secretion and 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staining of excised tumors revealed that IMD-0560 suppressed VEGF expression, tumor angiogenesis, and cancer cell proliferation.|PMID:26905334|In a xenograft model, the treatment of IMD-0354 significantly inhibited peritoneal dissemination with a marked reduction of intratumoral blood vessel formation followed by the inhibition of VEGF expression from cancer cells.|PMID:25637316|In our study, VEGF levels in lung homogenates and angiogenesis of mice exposed to Dp were decreased by IMD-4690 treatment.|PMC4364779|Systemic administration of IMD-0354 for 6 weeks to week-6 diabetic mice caused significant reduction in the loss of retinal ganglion cells and apoptotic signaling, with preservation of retinal vascular integrity and suppression of retinal VEGF expression.|PMID:25205865|In rat suture-induced CoNV, systemic IMD0354 significantly suppressed CoNV, decreased inflammatory cell infiltration, expression of inflammatory chemokines (CCL2, CXCL5, Cxcr2), and attenuated expression of angiogenic factors (VEGF) and inflammatory mediators 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aspirin treatment is associated with an increase in bcl-2 expression, which persists in the presence of the anticancer drugs.|PMC2375372|Although the mitochondrial Bcl-2 levels also decreased markedly, the p-Bcl-2 level and the ratio of mitochondrial p-Bcl-2 to Bcl-2 were increased in the ASA group, and largely decreased in the ASA + HS, which was beneficial for resisting HS (Fig. 3B).|PMC7169958|The present study also revealed that, although Bcl-2 levels were decreased, the p-Bcl-2 levels and the ratio of p-Bcl-2 to Bcl-2 in the ASA and ASA + HS groups were increased compared with those in the Con and HS groups, respectively.|PMC7169958|Moreover, after treatment with aspirin, Vitamin C, Vitamin E, or ozone, the expression levels of Bax were reduced when compared to the PM2.5 group, while levels of Bcl-2 were increased which resulted in a decrease in the ratio of Bax/Bcl-2.|PMC5463468|The histopathological analysis showed reductions in cystic fibrosis, atretic ovaries, increased 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When observed up to 18 months, PCP and DeltaCP levels in insulin + RSG group patients still stayed steady, while PCP and DeltaCP levels decreased more in the insulin alone group.|PMID:15386806|(2) PCP and DeltaCP levels in insulin + RSG group patients stayed steady during the 12 months' observation (P = 0.161 for both PCP and DeltaCP), while in the insulin alone group, both FCP (P = 0.021) and PCP (P = 0.028) levels decreased significantly.|PMID:15386806|Compared with the subjects without receiving insulin therapy, the subjects receiving insulin therapy had longer DD, higher SBP, WBCC, CRP, HbA1C, TC, LDL-C, FPG, 2h PPG, Fins, 2h Pins, and 24h UAE levels and had lower BMI, FCP, 2h PCP, TG, and SUA (all p < 0.05).|PMC7882504|(2) PCP and DeltaCP levels in insulin + RSG group patients stayed steady during the 12 months' observation (P = 0.161 for both PCP and DeltaCP), while in the insulin alone group, both FCP (P = 0.021) and PCP (P = 0.028) levels decreased 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[acetylsalicylic acid (ASA)] is an anti-inflammatory drug that protects against cellular injury by inhibiting cyclooxygenases (COX), inducible nitric oxide synthase (iNOS) and p44/42 mitogen-activated protein kinase (p44/42 MAPK), or by preventing translocation of nuclear factor kappaB (NF-kappaB).|PMID:12124433|These data imply that aspirin should be able to inhibit a LPS-induced increase in COX2 expression in BV-2 microglial cells, probably via inhibiting MAPK/JNK pathway, although the content of COX2 was not measured in this study.|PMC5187761|This study demonstrated that ASA distinctively attenuates MCT-induced PAH by inhibition of the ERK1/2 signaling pathway.|PMID:28055284|Aspirin reduces cardiac interstitial fibrosis by inhibiting Erk1/2-Serpine2 and P-Akt signalling pathways|PMC7138280|Aspirin Reduces Cardiac Interstitial Fibrosis by Inhibiting Erk1/2-Serpine2 and P-Akt Signalling 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administration of PCP reduced the production of serum total IgG1 and OVA-specific IgG1, as well as up-regulated the serum OVA-specific IgG2a and splenic Th1-related cytokine and down-regulated IL-4 and IgE levels in atopic dermatitis mice.|PMC4110622|Oral administration of PCP reduced the production of serum total IgG1 and OVA-specific IgG1 and upregulated the serum OVA-specific IgG2a and splenic Th1-related cytokine and downregulated IL-4 and IgE levels in atopic dermatitis mice.|PMC7049221|In addition, oral administration of PCP significantly reduced IL-4 and IgE expressions in a murine model of atopic dermatitis.|PMID:24625278|Exposure to TCDD alone or in conjunction with PCP suppressed many ovalbumin (OVA)-stimulated cytokines, including IL-2, IFN-γ, IL-4, IL-5, and IL-10.|PMID:24051191|Increases in SP-D content, gamma interferon, interleukin-4, interleukin-5, and tumor necrosis factor alpha in BAL fluid occurred but were attenuated in PCP-infected SP-A(-/-) mice compared to WT 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serum level of VEGF also increased in mice treated with sevoflurane compared to propofol with statistical significance obtained at one day after surgery (p = 0.03, two-way ANOVA + Dunnett’s post hoc tests).|PMC6994546|It was noteworthy that the ERK activator (phorbol 12-myristate 13-acetate [PMA]) treatment increased the MMP-9/VEGF levels after propofol treatment, and led to significant increase of proliferation, invasion and angiogenesis.|PMID:24089228|The expression of HIF‐1α and VEGF was increased by hypoxia and was alleviated by propofol.|PMC6515893|The expression of HIF-1α and VEGF was increased by hypoxia and was alleviated by propofol.|PMID:30680941","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6994546","PMID:30680941","PMC7417688","PMC7980239","PMC6515893","PMID:24089228","PMC8034479","PMC3980597","PMID:29805673"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"126728115":{"subject":"PUBCHEM.COMPOUND:10607","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6081811","PMC8021564"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c192ffee23190d86be8da2b86433a4f08c9e0b7859db2ce2bb3bfc773b3398aa","tmkp:1a3b0623d84c902a1c82a45d4d82d2ca1e2a9fd132c4380ceba92df91e726dcb","tmkp:e17c88b2c98cd78b3f1890875136a0cce9d03fd35b80d0e0b803ad6775fd84b4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999676","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The contents of IL-2, IL-4 and TIPE2 produced by splenic CD4+ T lymphocytes were decreased following trauma-hemorrhage, which were normalized by administrations of E2 or PPT, but not DPN or G1.|PMC8021564","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"23265691":{"subject":"PUBCHEM.COMPOUND:54729367","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:25268699","PMC3142953","PMC3943859","PMC4898774","PMC4529780","PMID:25128381","PMID:20042669","PMC3710317","PMC7689282","PMC4286153"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Doxycycline was administered continuously through the food for 90 days to one cohort of tumor-bearing mice from the time of weaning (~21 days of age) to suppress Akt expression.|PMC3142953|Addition of doxycycline caused a substantial decrease in P-Akt, and an increase in PDH phosphorylation (Fig. 3C).|PMC4529780|Furthermore, our results showed that doxycycline significantly attenuate histamine-induced systemic anaphylaxis-like reaction (HISA) with a significantly downregulation of PI3K/Akt/eNOS/VE-cadherin pathway.|PMID:25128381|Additionally, doxycycline treatment dramatically reduced the phosphorylation of NF-κBp65, Akt and eNOS in ILA and significantly inhibited matrix metalloproteinases (MMPs) activity in vitro and in ILA.|PMID:25268699|From a mechanistic standpoint, doxycycline downregulates PI3K/Akt and ERK1/2 pathway through SDF-1α/CXCR4 axis in SKOV3 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(400 µg/kg) administered intraperitoneally to mice increased brain glucose transporter 1 (GLUT-1) and VEGF mRNA levels and concomitant use of naloxone (2.0 mg/kg) suppressed this induction within 12 h.|PMC8128984|We found that fentanyl increased the expression of key molecules (p-GSK-3β, β-catenin) and target genes (Cyclin D1, CD44, VEGF, and c-Jun) in Wnt/β-catenin signaling pathway (Figure 5A).|PMC5526971|Fentanyl augments NO concentration in wounds, which triggers VEGF synthesis in 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only when U373 cells were treated by CuS@CaCO3-PEG in pH 6.5 + L group, the expressions of Bcl-2 protein were significantly down-regulated.|PMC7183209|It can be observed that PTX, ICG/PFP@HMOP‐PEG and ICG@HMOP‐PEG under laser irradiation significantly inhibit the expression of Bcl‐2 mRNA and promote the process of cancer cell apoptosis (Figure S14a, Supporting Information).|PMC6661946|Similarly, the MF‐Lip@PEG leaching liquor significantly reversed the CoCl2‐induced expression of Bax/Bcl‐2 (Figure 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Gene expression of IL-4 and IL-10 were significantly increased in PBMC from RA patients than in healthy controls after MTX exposure in vitro, while gene expression of IL-2 and IFNγ was significantly decreased.|PMC3400362|fish oil and/or genistein supplementation in MTX-treated rats reversed this trend to the extent that levels of plasma IL-4 were significantly greater in MTX+FO and MTX+FO+Gen groups than in the MTX alone group (P<0.05) ( Fig. 6C ).|PMC3741109|In contrast, production of IL-4 by TCR-primed CD45RA T cells was significantly increased upon MTX treatment.|PMID:10540171|Antiinflammatory and immunoregulatory action of methotrexate in the treatment of rheumatoid arthritis: evidence of increased interleukin-4 and interleukin-10 gene expression demonstrated in vitro by competitive reverse transcriptase-polymerase chain reaction.|PMID:9433869|Antiinflammatory and immunoregulatory action of methotrexate in the treatment of rheumatoid arthritis: evidence of increased interleukin-4 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the groups of rats treated with CPZ and with AMPH + CPZ, there was a slight elevation in serum insulin levels.|PMID:3275851|In the groups of rats treated with CPZ and with AMPH + CPZ, there was a slight elevation in serum insulin levels.|PMID:3275851|Chlorpromazine acted similarly, stimulating an increase in GFP and insulin mRNA of 2.33 ± 0.14–fold and 2.45 ± 0.19–fold, respectively (Fig. 5A).|PMC3374493|Ethopropazine and chlorpromazine increased endogenous insulin mRNA and eGFP mRNA relative to untreated cells.|PMC3374493","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"83557587":{"subject":"PUBCHEM.COMPOUND:3821","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Long-term ketamine administration also was shown to have detrimental proapoptotic effects on neurons, via an elevation of 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VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab ist seit Oktober 2019 in den USA und seit Februar 2020 in Europa zur Behandlung der neovaskulären altersabhängigen Makuladegeneration (nAMD) zugelassen.|PMC7935813|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|In den Phase-III-Zulassungsstudien HAWK und HARRIER zeigte der VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab (8- oder 12-wöchentliche Gabe) im Vergleich mit Aflibercept (8-wöchentliche Gabe2) nach 48 Wochen eine Nichtunterlegenheit in Bezug auf den Visus.|PMC7935813|Consistent with this focus, laser therapy, VEGF inhibitors like bevacizumab (off-label), ranibizumab, aflibercept, and brolucizumab, and corticosteroids such as dexamethasone intravitreal implant comprise the current therapies for DRD.|PMC8003049","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC7935813","PMC7263271","PMC7263271","PMC7935813","PMC8003049"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99211024375","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"37889323":{"subject":"PUBCHEM.COMPOUND:174","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5521188","PMID:28663087","PMC3795383","PMC6364594","PMID:26304505","PMC5691696","PMC4279188","PMC3121792"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:952f5ec75b4bf7989796a5b1ef3850db47550bde3c3c84c4fc2457d2c5dca254","tmkp:cdcee5cefbf49ed6f9ad88fa0ca0c9c9e6f524706e08aa953f4e1a09e7b6bdf2","tmkp:1451efdbc6e7409d21cb7a22336ef8fb9e9713ad78467b14ca1d3930fa8fc827","tmkp:499f169615b4e8bd84c88ee71fba70416b3f9bc6e47d9b276923e81ada475939","tmkp:da9dfbc50ff0f3937a9b5ce520007836a23b5e607df8bbde0ff911521ff852ac","tmkp:a68bb039c9856f4c2e5ea4d06e3de22c3c1d93a88c7390c16bd456f1bf5126a2","tmkp:a99c05faa21c48bd6bc2f35df8ef7f9c96b7c326ded3af3e442ed575fb3f89c1","tmkp:12f6364d1c2e902a1e32fc18532d17bd4c1d7f976d5e0ce56914a1654fc3fb70","tmkp:66a5f45732231bdf9d4110096c7748f15a4e2d4463755662c66765a7e6a2fe5a","tmkp:6bd8b33322674e259d9536c2b5cbbf0521573425715afd5dbf9a29b385e8696c","tmkp:cd8b1ad4ead72716affbe63adeff9652baa9b66c8396e927edb969a154ebd299","tmkp:b3187ce912a065919573d667b097b5dffd04b279f658f818c4785f663845fb13"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"PEG-LPrA2′s effects were accompanied by a significant decrease in VEGF/VEGFR-2, IL-1R tI, cyclin D1 and PCNA levels.|PMC3121792|Mechanistically, the NCs especially HA-NCs and PEG-NCs demonstrated precious anti-tumor effects in vivo revealed as reduction in the tumor volume and aromatase level, increased apoptosis, as well as inhibition of VEGF, NF-κB and TNF-α augmented by histopathological and immunohistochemical studies.|PMID:28663087|Mice treated with PEG-LPrA2 had diminished expression of VEGF/VEGFR2, OB-R, leptin, IL-1R tI, PCNA and cyclin D1 and showed reduced growth of 4T1, MCF7 and MDA-MB231 tumors.|PMC3795383|PEG-LPrA2 treatment decreased levels of human and mouse VEGF and leptin in MCF-7 ER+ breast cancer xenografts.|PMC3795383|The PEG-IFN-α2a treatment effectively suppressed the hepatic expression of OV6 and CD90, ameliorated the diminished hepatic expression of TGF-β receptor II (TGF-βRII) and β2-spectrin (β2SP), and significantly reduced the elevated hepatic expression of TGF-β1, interleukin6 (IL6), signal transducer and activator of transcription3 (STAT3), and vascular endothelial growth factor (VEGF).|PMID:26304505","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9938224684536082","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"7223384":{"subject":"PUBCHEM.COMPOUND:7814","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:6d66aef9e3e4dd7a236fa85a492dfbbea694af926e263601406b2725e410c5fc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"This study 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transfected cells were selected on solid minimal medium (EMM2) lacking leucine and supplemented with 2 μM thiamine to repress GFP-Er-MAPK1 constructs expression, and cultured in EMM2 without thiamine to induce GFP-Er-MAPK1 constructs expression.|PMC6811501","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"108373236":{"subject":"PUBCHEM.COMPOUND:3821","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Like barbiturates, ketamine, etomidate, and propofol inhibited GLUT-1 at concentrations near to those used 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mean cumulative number of anti-VEGF injections was significantly lower in PCV group (4.51 for AMD-CNV, 3.43 for PCV, p = 0.021).|PMC4076260|This theory is supported by previous findings that aqueous levels of VEGF are lower in PCV than in CNV-AMD.|PMC4470199|Intravitreal corticosteroids may therefore be useful in the treatment of PCV as they show a mild blocking of VEGF and a strong anti-inflammatory effect.|PMC5111116|Decreased levels of VEGF detected 1 week after PDT for PCV seems to reflect acute damage of vascular endothelial cells, one of the VEGF expression sites in PCV.|PMID:23664208|The rates of retreatment from 12 to 23 months were significantly higher in eyes with SRD at 6 and 12 months than in those without SRD (P = .004 and P < .001).In conclusion, during 24 months of antivascular endothelial growth factor (VEGF) therapy using ranibizumab for PCV, BCVA was maintained in those with good visual acuity at 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kaempferol and quercetin are also able to block angiogenesis, by inhibiting VEGF, another activity linked to antitumor properties.|PMC6237366|The most important finding in our study is the establishment of inhibitory effects on VEGF/Akt signaling by quercetin in AML cells.|PMC7758733|In experiments with the rhesus choroids-retina endothelial cell line RF/6A, quercetin has also been reported to inhibit VEGF-induced endothelial cell proliferation, migration, and tube formation, suggesting that it may efficiently inhibit choroidal or retinal neovascularization.|PMC6520779|Soo et al. founded that the anti-cancer efficacy of quercetin was determined by inhibiting vascular endothelial growth factor mediated angiogenesis in tamoxifen -resistant breast cancer cells.|PMC7602283|Silibinin and quercetin have been reported to inhibit the angiogenesis and proliferation of cancer cells in desmoplastic tumors through inhibiting VEGF 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(Akt inhibitor) level decreased to (0.42 ug/ul ± 0.04 ug/ul) at 2 mM PPA compared to (0.83 ug/ul ± 0.09 ug/ul) in control 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have been developed to inhibit the VEGF signaling pathway including anti-VEGF antibody therapy (e.g., bevacizumab), anti-VEGFR antibody therapy (e.g., ramucirumab), inhibitors of VEGFR-2 tyrosine kinases (e.g., apatinib), and inhibitors of angiogenic receptor tyrosine kinases (e.g., sunitinib, pazopanib, sorafenib, and regorafenib).|PMC6501144|The patient was restaged as T2N0M1 of lung adenocarcinoma, and chose 6 courses of systematic chemotherapy (pemetrexed combined with nedaplatin) plus bevacizumab, a monoclonal antibody targeting vascular endothelial growth factor at 3 weeks intervals.|PMC6710319|Based on successful phase III trials, antiangiogenic therapeutics, anti-VEGF agents in particular (e.g., sorafenib, bevacizumab, and sunitinib), have entered the clinical practice in the USA and 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VEGF signal was still detected higher in the prednisolone group compared with the sham group (Table 3).|PMC7968946|He presented with a high level of serum vascular endothelial growth factor (VEGF) and RS3PE syndrome-like pitting edema in the extremities, which improved following treatment with low-dose prednisolone.|PMID:24739614|Combination of PDGF-BB and prednisolone ameliorated changes in VEGF and VEGFR2, but decreased angiostatin, PDGFR-β, and Ezh2 (Fig 9C).|PMC6309783|He presented with a high level of serum vascular endothelial growth factor (VEGF) and RS3PE syndrome-like pitting edema in the extremities, which improved following treatment with low-dose prednisolone.|PMID:24739614","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"18151649":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:12fecb63980c01b4ac2012d18123cd6a3f00052f62d56c5b9b0e096365a19141","tmkp:d930a627147c44c441e83c846dfaa7f0ab81879de256338e596175f06a8c6725","tmkp:d90745cbd993d9df5beeb490afb011c189d6085a4a613438caa07b5ad1ab920c","tmkp:a9420e951f848d3b35f5340d9657232f3be11c43d086bd9ecf6602831d29f809","tmkp:6e1ace707c165d1579a13a932add03183831e6a08286818c6a3df811761a7cf1"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99936328","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Similar to what was observed in Jurkat cells, culturing PBMC with MTX resulted in concentration-dependent increases in total JNK1 protein and phosphorylated JNK1/2 [Figure 5B].|PMC3165146|MTX-treated platelets exhibited time dependent and concentration-dependent increase in phosphorylated form of JNK1/2.|PMC4471342|Culturing cells with MTX resulted in increased in total JNK1 protein levels and levels of phosphorylated JNK1/2 [Figure 5A].|PMC3165146|Culturing cells with MTX resulted in increased in total JNK1 protein levels and levels of phosphorylated JNK1/2 [Figure 5A].|PMC3165146|Similar to what was observed in Jurkat cells, culturing PBMC with MTX resulted in concentration-dependent increases in total JNK1 protein and phosphorylated JNK1/2 [Figure 5B].|PMC3165146","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC3165146","PMC4471342","PMC3165146","PMC3165146","PMC3165146"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"61902254":{"subject":"PUBCHEM.COMPOUND:24759","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC8077712","PMC6077506","PMID:16934786","PMID:21422731","PMC3590137","PMC3403533","PMC4685440","PMC3360616","PMC5287174","PMID:12145277"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9819915169aeda57febedca3476c3994cce8e1ff6d59f4892dae4080c4ada323","tmkp:f6468cb7cdbfcc37bae1fb68bb1e075590a335e79175bb83f8b4fd3b27f4721c","tmkp:e98dac07e7bb4412c8a658b29ef2c76d74e7748b326f3388922fb07d22d8e127","tmkp:02e69e63885f25ac5f456c0d014eb58f79de3cf7b0a9bc26fdd504d1b0ab3899","tmkp:051162ce22f60fdac453fe93b7ad7eb8c2e8c263ca19120a7efcc0e3baf0c7a1","tmkp:012167188a5c44e6661dc52518438223c494bea3b458eed3cb4214f666b4fe7c","tmkp:221ad0dcd778b41b918acc9eb7fdd49ab052b5785e10f299937e62392b8f1906","tmkp:5b751bde64f3ac172325202fac5f09659abac5a001860d27193fb58d36ea530d","tmkp:9442c340af55e693eb406a065e1e97eaadf7a6d5640c12693423af0f89f7dfc2","tmkp:da2ea62e3cb121e1f9c077f3b0a6c0ce3abbd4e7d86437410d9a8d4a7b5a9d94"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Hyaluronan induces vascular smooth muscle cell migration through RHAMM-mediated PI3K-dependent Rac activation.|PMC3590137|Hyaluronan induces vascular smooth muscle cell migration through RHAMM-mediated PI3K-dependent Rac activation.|PMID:16934786|Previous reports indicate that low molecular mass hyaluronan suppresses neutrophil apoptosis to trigger pulmonary inflammation via activating the PI3K/Akt pathway.|PMC8077712|Hyaluronan induces vascular smooth muscle cell migration through RHAMM-mediated PI3K-dependent Rac activation|PMC5287174|Hyaluronan induces vascular smooth muscle cell migration through RHAMM-mediated PI3K-dependent Rac activation |PMC6077506","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9982290903225807","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"122864630":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9983154454545455","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:16511354","PMC3156317","PMC7558230","PMID:29803913","PMC6834162","PMC4308769","PMID:23406595","PMC7037118"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Combination of 4-hydroperoxy cyclophosphamide and methotrexate inhibits IL-6/sIL-6R-induced RANKL expression in fibroblast-like synoviocytes via suppression of the JAK2/STAT3 and p38MAPK signaling pathway.|PMID:29803913|The anti-inflammatory drug methotrexate reduces MMP-1 through the MAPK pathway, and kynurenine was also shown to increase MMP-1 and -3 expressions to improve wound healing in vivo through the same pathway.|PMC7037118|The results showed that IL-6/sIL-6R-induced RANKL upregulation required phosphorylation-mediated activation of STAT3 and p38 signaling, and that 4-H-CTX and/or MTX inhibited RANKL expression in IL-6/sIL-6R-stimulated FLS by suppressing JAK2/STAT3 and p38MAPK signaling.|PMID:29803913|This study demonstrated for the first time the inhibitory effects of 4-H-CTX and MTX on RANKL expression in IL-6/sIL-6R-stimulated FLS via suppression of STAT3 and p38MAPK phosphorylation.|PMID:29803913|Moreover, MTX reduced LPS/TNF-α-dependent pro-inflammatory cytokine production, MAPK activation, IκBα degradation, and NF-κB activity via A20.|PMC7558230","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e5755daae699b867f89b50c4d3f5e67f9e282abe75bff030326abdaef42e7581","tmkp:f063b0078d24c51b727b2ff567690f079b7b806c80f322fe8bb74109987ac110","tmkp:d123ebd1cd4d5765b909a3cd4524ec01c5fe221a04b4ff75d35d6788c2ded67a","tmkp:991b6d37aad5aedd15b79a955f4dfb40ae6b80922828f4950eff173d81a05b76","tmkp:b5f5b47b32f286dd6d85a3fd708fe3248d10b8ed299778ca125900e7050707f2","tmkp:150dfc360ee2940e345205a496b467ce8cb0af5cca4449e9cd73e07abcd69e93","tmkp:657568decef9dbc5e0821b3f4c6885f0a64bf5df87493018d00c2968c81d8e66","tmkp:3510c2d6a2e1af5ea5b18232dfbabfa08b5d373b29c00f9bd1a38ad5645e85dc","tmkp:4f961eea2e3c9940b037404ed5cdd5ecd3632995a22e28bd04368500d0c67bdd","tmkp:04b2d4cd283dad35a78379b889115523d96d575414ed55b018a655d33dde39ae"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"90050089":{"subject":"UMLS:C0024808","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6466217","PMC7059731"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9968197999999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Alcohol and cannabis both modulate CB1 and CB2 receptors, resulting in activation of the MAPK signaling pathways, that further activates (i) nuclear factors CREB and NF-κB, (ii) histone modifications, and (iii) DNA methylation mediated by the epigenetic enzymes.|PMC6466217|It is known that marijuana activates CB1 receptors within the endothelium and there is a ROS-MAPK activation cascade.|PMC7059731","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:979a8a091f6cb94600135e844c5453c7069f0dc6ead9747012f6c9b44fb5251a","tmkp:b797c5466a5c64cbe71255b6b3cdf5ded09aa7fa2b0cd8f9d738f6199e660c4f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"46512961":{"subject":"PUBCHEM.COMPOUND:439501","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:28c60cbb0148e89ac02728c573a2903a572dd9ce669b0ec739a5d88033437d3f","tmkp:ee863866c5da0e25049c0f58593bed9422acf348c22a5ed06cf93665d78bc073","tmkp:61829a69b3e6578f49ff9c3be0f1b1a8df41ac0f6e3f33bbb40c5eb3cab2bc01","tmkp:867290a2e0fe5b8009e3ff60ae7236f062ef3bdc8a095dd193db123215b3915a","tmkp:9892fd930b67590272a8da13b55c01894e90215316c88c32215256d682ad9534","tmkp:ba6762b2f05df89ff1c1564dd7e014b7518fce3f0a27c3dba1d2c9c772ee4e8f","tmkp:c3c5c997470d8e2c0b2f7c41615e8fe42752411e927e6d5696daa790024f24ab","tmkp:4a36ef5943e3a6503f6cbd72173f028a9d753d7a46694474dde22dc007da5d48","tmkp:401dba343040d36f9a10eb32bfd96d0b06c048213cb647c29234cf201b94962a","tmkp:82eaf1735bad24555f11ea41877b6ae0d14ec82cc2f6d29f0b7269e7ddbb2aea"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Bcl-2 level increased in spiral ganglion neurons exposed to Neurobasal medium + 10 nmol/L ouabain at 6 h.|PMID:19441249|Consistently, whether Bax expression decreased with marinobufagin, Bcl-2 expression increased, similar to ouabain (Figure S4); the contrary was observed with telocinobufagin (Figure 4a,b, respectively).|PMC6163863|E. Western blotting indicated that although the anti-apoptotic gene Bcl-2 showed a trend of increasing at an early stage during ouabain exposure, the Bcl-2 level significantly decreased 24 hs after ouabain treatment.|PMC4190379|Low-dose ouabain protects against excitotoxic apoptosis and up-regulates nuclear Bcl-2 in vivo|PMC3955620|Low-dose ouabain protects against excitotoxic apoptosis and up-regulates nuclear Bcl-2 in vivo|PMC3818842","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9990809515789474","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:25959616","PMC4805603","PMC3955620","PMC4190379","PMC5688790","PMID:29277770","PMC3818842","PMC6154632","PMC6163863","PMID:19441249"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"1926640":{"subject":"NCBIGene:3630","object":"PUBCHEM.COMPOUND:702","predicate":"biolink:affects_response_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"10090","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:publications","value":["PMID:32171850"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"affects response to","value_type_id":"EDAM:data_0006","original_attribute_name":"description"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"91663808":{"subject":"PUBCHEM.COMPOUND:135398744","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In addition, it was previously reported that sildenafil exerts a protective effect on cardiomyocytes after ischaemia reperfusion through the activation of the ERK1/2 and p38 mitogen-activated protein kinase pathway.|PMC3548048|Sildenafil promoted ERK1/2 activation an effect that was paralleled by an increase in MnSOD expression that persisted 24 hr later.|PMID:21948520|We also show that ERK1/2 is activated following treatment with PDE5 inhibitors (except sildenafil), suggesting the involvement of this pathway in cell proliferation mediated by PDE5 inhibition.|PMC3914480|Pretreatment with 1 µmol/L sildenafil potentiated the phosphorylation of ERK1/ERK2, an increase in the percentage of cells in S phase and cell proliferation, compared with serotonin stimulation alone (P < 0.05).|PMID:22040433|Incubation of cells with sildenafil increased both extracellular signal regulated kinase 1/2 (ERK1/2) and p38 phosphorylation in a time-dependent manner.|PMID:17226792","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:26816265","PMC3548048","PMID:21220057","PMID:22040433","PMC6930755","PMC3914480","PMC4136836","PMID:17226792","PMID:21948520","PMID:23140764"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9894113330769231","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a656afa630c0639213b641dd833757f61504bcf5ce9009902ac5fd10103762e4","tmkp:5d8082de2ea972e1a3a974d483bcaebb09da5cf5b387304c493504f9e2663a35","tmkp:df6669fc5967274cd6e0542aa35f2b59a4b686d19a5b4f7bd9bcb09123cee617","tmkp:0af51233a36bd0bf2b7220a0a735a70eb453ea2b76ade25c102c91e19d4886a1","tmkp:b10a1d48cef0a251cb6f675211563d808da08cfffc1d816af886715d861afc6f","tmkp:7e3e11120ba748869bb8c9d71ac929ae287498447dcc71d1774fdbc4313c3725","tmkp:9bc7a636e2e7db50371bd8fafbb8e026ebaa09d22062d9002a3589d563f6812a","tmkp:0c6c868d1304758d1b60480200f69f21bb0e21b8a6a4b858d460d35b3ddb79d5","tmkp:e976c506a945ba192a6b46856de94cbc4e41dbf4534baa0a6159a29b737f6b24","tmkp:6aa9ec62c1733d1b125d125f25ec8d4505c7cd965bfb56d629fd581802ce5cbd"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"92394917":{"subject":"PUBCHEM.COMPOUND:247","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Activation of p38 MAPK pathway on A549 after betaine and/or phycocyanin treatment.|PMC5011231|Interestingly, we found decreased ERK1/2 phosphorylation mainly in the 5-FU treatment and AS+5-FU, as well as an unexpected increase in the use of Trimethylglycine, which may indicate that administration of this adjuvant favors the ERK1/2 activity as reported in the primary cultures of human osteoblasts; this, however, contends with data reported in lipid metabolism in which the use of Trimethylglycine decreased ERK1/2 phosphorylation.|PMC7139326|However, at present, we cannot rule out that an increase in ERK1/2 phosphorylation by Trimethylglycine treatment could be a compensatory or alternative mechanism to escape cell death induced by adjuvant therapy with 5-FU.|PMC7139326|It has been reported that ethanol-induced abnormal hepatic methionine metabolism is specifically associated with the suppression of transmethylation reactions and with the inhibition of MEK/ERK1/2 activation, and that betaine supplementation, improving the AdoMet/AdoHcy ratio, is able to alleviate ERK1/2 activity inhibition.|PMC4881448|While betaine alone and C-PC alone treatments show 1.5-fold increase, which is slight but insignificant, the combination of both gave an approximately 2.5-fold increase in the total p38 MAPK expression (Figure 3(b)—condition B + C-PC black 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the decrease of both RAC1B protein and transcript in ibuprofen-treated condition.|PMC7720772|As shown in Figure 4B, the transfection of GSK3βS9A into HT29 cells clearly countered the effect of ibuprofen on RAC1B levels, confirming that GSK3β inhibition by S9 phosphorylation was involved in the ibuprofen-mediated decrease of RAC1B.|PMC7720772|Accordingly, the presence of ibuprofen led to a reduction of HT29 cell survival in vitro and inhibited Rac1b-dependent tumor growth of HT29 xenografts.|PMID:23359345|Other possibilities include the natural products sanguinarine and the anti-inflammatory drugs ketorolac and ibuprofen, which also have been shown to inhibit Rac1b function, although the effects of these compounds as anticancer therapeutics in clinical settings remains to be evaluated.|PMC4701227|As mentioned briefly above, ibuprofen has been shown to inhibit RAC1B expression in HT29 cells and RAC1B-dependent tumor growth of HT29 xenografts.|PMC6356296","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9926710889473684","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"60100735":{"subject":"PUBCHEM.COMPOUND:2783","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3633781","PMC3633781","PMC3633781","PMC8217466","PMID:23207563"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99833719875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The phosphorylation of p38 mitogen-activated protein kinase (MAPK) increased after single-dose clenbuterol treatment and acute exercise in the soleus muscle but not in the TA muscle.|PMC3633781|The in vitro cell culture model suggests the possibility that β2-agonist clenbuterol-induced receptor phosphorylation through the activation of PKA may progress in slow-twitch soleus muscle, compared to fast-twitch TA muscle, which is responsible for the increase in the phosphorylation of p38 MAPK after clenbuterol treatment to a much greater extent in the soleus muscle than the TA muscle.|PMC3633781|These findings suggest that the activation of p38γ MAPK after clenbuterol treatment and exercise is involved in the anabolic and/or metabolic adaptation of slow-twitch muscles.|PMC3633781|In addition, clenbuterol—which increases ERK1/2 activation—also reduces caspase-3 expression, and AKT activation also reduces caspase-3 activation in cardiomyocytes exposed to I/R.|PMC8217466|Clenbuterol favorably 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Doxycyclin-induced heterologous expression of HNF4A, HNF6, and HNF1B in rat insulinoma (INS-1) cells (n = 2).|PMC5481429|Expression of HNF4α in HLE/tet-HNF4A cells was induced by the addition of 500 ng/mL of doxycycline (Sigma-Aldrich, Tokyo, Japan) into the medium for 24 h.|PMC7484291|We then stably transduced these cell lines with lentivirus enabling doxycycline (dox) induction of the HNF4α 8 isoform, a major product of the P2 promoter.|PMC7945295|MEFs without (OHT-) and with (OHT+) three days of tamoxifen treatment for depletion of Lsh, and without (Dox-) and with (Dox+) two days of doxycycline treatment for induction of the liver specific transcription factors Foxa2 and Hnf4a.|PMC6557562|DN-HNF1A and DN-HNF4A expression was induced in INS-1 cells by treatment with 500 ng/ml of doxycycline for 24 and 48 h as indicated.|PMC3707779","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9983152223529411","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5481429","PMC7484291","PMC7945295","PMC6557562","PMC3707779"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:71a2804eeb44a35c528509507ded8e2a050e489311d2e895921daba5d795403a","tmkp:b04f472d3c6ebef50d862a99f17db4d67d75c8c3850091ee785784a736a23b5f","tmkp:7af286510b1d505d952a897d4db2ff0b7a11fdafd05b4076b79fb41b7ce4c7b6","tmkp:e2f47fbdd1305bcb2af102d50754851175cd718b831e9e3ad0fc762109574509","tmkp:a0b672d368fe5e85db549d51188d7b3333d0af79ea0b7342822931fbb23b9dd8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"127371858":{"subject":"NCBIGene:6513","object":"MONDO:0012805","predicate":"biolink:genetic_association","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop","infores:pharos"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":0.64,"value_type_id":"EDAM:data_0006","original_attribute_name":"score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:disgenet","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"106305585":{"subject":"PUBCHEM.COMPOUND:5280343","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7430291","PMID:20510684","PMC6570913","PMC7669347","PMC5571156","PMC4629123","PMID:19243898"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:6a4dc5c55019294e2da3f0ef314d0c62ad6d826b2d8e73ab2609cc1266636a39","tmkp:f5cbec3fc1dab7921764e9e31c4311421347261b7cffb355228be99be2618377","tmkp:0bb8eb5e9120fb44d330daf72ffda94934969e18fc2a945b5e0c69dd939bd0fc","tmkp:61c028a489d19d7ba3e2c5c484ed5e489fbd8e71ec0fb62daff619da6dbf06fa","tmkp:f88d2964946d960055003b11074ba0af7cd7aed5f20ac0d2725f7a9cc186c1ea","tmkp:c86700066c8e9826c1dabe95401b3e246677cb796032a76905a0da3e7fe4a2bd","tmkp:d9196b82caa46c5f61517c8add49657db7ead98b3ab950fe06c24295acda5227"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Ansorge et al. demonstrated that propolis, CAPE, quercetin, hesperidin and some other propolis flavonoids can inhibit the cytokine production of Th1 and Th2 type T cells, while increasing TGF-beta 1, an important anti-inflammatory cytokine.|PMC7430291|Results indicate that quercetin increased TGF-beta-1 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the phosphorylation of Bcl-2 with caspase activation amplification including caspase-3, -8, and -9, and cleavage of poly [ADP-ribose] polymerase 1 (PARP-1), a caspase-3 substrate, was markedly increased when sildenafil was coadministered with vincristine; a similar feat previously demonstrated when sildenafil was combined with DOX on prostate cell lines incurring the coherence between the results reported between different studies.|PMC8234771|In this study, sildenafil induced the likely cell cycle arrest and the potentiation of PARP-1 cleavage in the presence of doxorubicin (Figure 1A).|PMC6344441|Further identification showed that sildenafil profoundly enhanced doxorubicin-induced activation of caspase −8, −9, and −3 by proteolytic cleavage as well as the increased cleavage of PARP-1, a caspase-3 substrate (Figure 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renoprotective effect of sildenafil against renal I/R might be due to the activation of antioxidant genes (Nrf2, HO-1 and NQO-1) and antiapoptotic gene (Bcl2) and attenuation of proinflammatory cytokines (TNF-a, IL-1β and ICAM-1).|PMID:26377490|Our findings suggest that the VEGF and Bcl-2 were up-regulated in response to sildenafil and functioned endogenously to promote myocardial angiogenesis.|PMC3828881|The protective effect of sildenafil also correlated with reduced cardiomyocyte apoptosis, as evidenced by reduced TUNEL-positive cells, increased anti-apoptotic Bcl-2/Bax ratio and inhibited caspase-3 activity in myocardium.|PMC4467614|Sildenafil also enhanced the Bcl-2/Bax ratio, phosphorylation of Akt, ERK1/2, and glycogen synthase kinase 3beta.|PMID:18723505|An early increase in Bcl-2 to Bax ratio with sildenafil treatment was also observed in myocytes after 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expression of VEGF has been demonstrated in most human tumors examined to date, including tumors of the lung, breast, thyroid, gastrointestinal tract, kidney, bladder, ovary, and cervix, as well as angiosarcomas and glioblastomas.|PMC2783916|Similar results of upregulation of VEGF mRNA expression have been reported for the vast majority of human tumors examined to date, including carcinoma of the lung, breast, gastrointestinal tract, kidney, bladder, and ovary.|PMC3383312|All wild-type HSV-1 strains tested to date have maintained the ability to up-regulate VEGF-A transcript and promoter reporter.|PMC3188529|After optimization of the gene switch architecture, an endogenous VEGF-A induction ratio of >100-fold can be achieved in HEK293 cells at 1 µM DHB, which is the highest endogenous induction reported to 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we demonstrate that VEGF mRNA levels are increased by anisomycin, a strong activator of stress-activated protein kinases.|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 3'-UTR).|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 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expression of p-mTOR, mTOR, HIF-1α, and VEGF were significantly reduced in 10.0 mg/kg C3C12PPD group compared with control (Figure 5B).|PMC6750213|Since mTOR is one of the targets of AKT, the p-mTOR and its downstream proteins HIF-1α, VEGF were also detected, and it was observed that they were downregulated by 100.0 µmol/L C3C12PPD (Figure 4B).|PMC6750213|Within the limitations of this study, it can be concluded that, rh-IGF-I+rh-VEGF treated sites resulted in greater improvement in PPD reduction, CAL gain as well as in osseous fill after 6 months when compared with rh-VEGF, rh-IGF-I and control sites.|PMID:27790578|Although PPD-type ginsenosides, Rb1 and Rk1, have been reported to inhibit vascular permeability induced by VEGF, lipopolysaccharide, thrombin, or histamine, it is not yet clear whether pro-angiogenic ginsenosides can induce vascular leakage similar to VEGF, or act as a leakage inhibitor, similar to ANG1, FGF and 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previously reported that sorafenib induces Th1 [interferon-γ (IFNγ)-positive interleukin 4 (IL4)-negative] dominance which prevents tumor cells from escaping the host immune system in patients with liver cirrhosis (LC) and advanced hepatocellular carcinoma (aHCC).|PMID:30952766|Sorafenib induces differentiation of BMCs into suppressive dendritic cells that inhibit autologous T-cell proliferation and stimulate CD4(+) T cells to express increased IL-1β, IL-2, IL-4, IL-10, IFN-γ and TNF-α, and reduced levels of IL-6 and CD25, which indicates that sorafenib-induced dendritic cells represent a distinct cellular subset with unique 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a significant activation of Rac1 was noted in U87 glioma cells stimulated with heparanase or the KKDC peptide (Fig. 6B, upper panel), activation that was abolished by the addition of heparin (Fig. 6B+heparin), while RhoA activation was not evident (not shown).|PMC2405934|We further showed that HCII could up-regulate cancer cell migration through the activation of PI3K, which acts upstream of Rac1 and Cdc42, and this effect could be blocked by 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and norepinephrine-induced ADRB2 activation lead to VEGF induction in prostate cancer cell lines through the cAMP-PKA-PI3K-AKT-HIF-1 alpha pathway.|PMC6498733|A variety of studies have confirmed that epinephrine promotes growth, invasion, and angiogenesis of malignant cells by upregulating the expression of vascular endothelial growth factor, matrix metalloproteinase (MMP)-2, and MMP-9, which are critical proteins related to carcinogenesis.|PMC6658366|In particular, in colon cancer cell line HT-29, adrenaline determined an increase in cell proliferation and production of proinflammatory and proangiogenic factors such as PGE2 and VEGF.|PMC4616528|Epinephrine and norepinephrine also upregulated the expression of IL-6, VEGF, MMP-2 and MMP-9 in oral cancer cell lines, mouse models, nasopharyngeal call lines and human melanoma cell lines.|PMC7825104|β-AR signaling activation via adrenaline and/or noradrenaline is implicated in the promotion of angiogenesis, through the upregulation of 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contrast to patients using sulfonylureas or metformin, diabetic patients using insulin had significantly larger mean LDL PPD (261 vs 254A, p < 0.006), lower triglycerides (115 vs 215 mg/dl,p < 0.0001), higher HDL-c (53 vs 40 mg/dl,p < 0.0001) and higher HDL2 levels (43 vs 29%, p < 0.0001).|PMID:12848306","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"66584763":{"subject":"PUBCHEM.COMPOUND:3121","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Trophic factors assessment, following treatment revealed the mRNA expression level of BDNF, GDNF and VEGF could be significantly up- regulated at various time points, mainly by 1 mM VPA.|PMID:30904572|VPA enhances postischemic angiogenesis via upregulation of HIF-1α and the downstream pro-angiogenic factors VEGF and MMP-2/9.|PMC6248271|In addition to enhancing HDAC inhibition, VPA potentiated MCAO-induced HIF-1α accumulation and upregulated VEGF protein levels and MMP-2/9 activities in the ipsilateral cortex on days 7 and 14 post-MCAO.|PMC3429729|The transcription factor hypoxia-inducible factor-1α and its downstream proangiogenic factors, vascular endothelial growth factor and matrix metalloproteinase-2/9, were upregulated after middle cerebral artery occlusion and significantly potentiated by VPA in the ipsilateral cortex.|PMID:22811460|As shown in Fig. 2a, the expression levels of 6 secreted proteins (GCSF, GM-CSF, M-CSF, PDGF Rα, PDGF Rβ, and PDGF-AA) were decreased and those of 4 secreted proteins (AR, EGFR, TGF-β2, and VEGF) were increased in VPA-treated cells, compared with the 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reduces S-nitrosation of cell death receptors and caspase-3, triggering a switch to caspase-3 from caspase-8.|PMID:29431086|Immunoblot analysis revealed that combined capsaicin and sorafenib at 75 μM and 2 μM respectively did markedly reduce the precursor form of caspase-9 and of caspase-3.|PMC5675664|Accordingly, we observed a reduction in caspase-3 positive cells after sorafenib co-treatment at 50 µM gentamicin concentration (Figure 11D, right panel).|PMC3711767|The overexpression of Trx1 increased caspase-8 activity (Fig. 4B) and cell proliferation (Fig. 4D) but decreased caspase-3 activity (Fig. 4C) in control and Sorafenib-treated cells.|PMC7210585|We found that sorafenib pretreatment significantly decreased the LPS-induced increase in caspase-3 levels in the cortex but had no significant effect in the hippocampus ( Figures 3B, C 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degradation of","value_type_id":"EDAM:data_0006","original_attribute_name":"description"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"97727247":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Interestingly, the selective estrogen receptor modulator (SERM) tamoxifen and the antiestrogen ICI 182,780 both promote GPR30-dependent transactivation of the EGF receptor and subsequent MAPK activation.|PMC2701913|Interestingly, the selective estrogen receptor modulator (SERM) tamoxifen and ER antagonist ICI 182,780 both promote GPR30-dependent transactivation of the EGF receptor and subsequent MAPK activation.|PMC5432040|Interestingly, the selective estrogen receptor modulator (SERM) tamoxifen and ER antagonist ICI 182,780 both promote GPR30-dependent transactivation of the EGF receptor and subsequent MAPK activation.|PMC3618441|Studies using the previously mentioned LTED cells as well as TAMR cells, a tamoxifen-resistant cell line generated by continuous growth of MCF7 cells in tamoxifen containing media for 4–6 months, show adaptive upregulation of EGFR and HER2 with resulting activation of the downstream effector, MAPK (Knowlden et al, 2003; Martin et al, 2003).|PMC2360507|In a tamoxifen-resistant cell line obtained by selection after prolonged exposure to tamoxifen, MAPK activity was found to be elevated and S118-P was 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methods revealed a statistically significant decrease in Bcl-2 expression and an increase in Bax in IHs tissues after propranolol treatment.|PMID:28279700|Treatment of these tumours at TT with propranolol did not further alter the expression of these proteins; however, blockade of β1-, and β2-adrenergic receptor signalling at ST with propranolol resulted in significant decreases in the expression of BCL-2 and BCL-XL, (Fig. 10a,c) and diminished phosphorylation of BadS112 (Fig. 10b).|PMC4471870|There were increases in expression levels of BCL10, TRAF family members, interleukins, TLR1-4, TNFRSF10B, NF-κB, and the inhibitors of NF-κB genes, and significant decreases in expression levels of Bcl-2 in response to propranolol treatment were observed.|PMID:23080133|Western blot assay have demonstrated that propranolol activated pro-apoptotic protein Bax and up regulated the expression of cleaved-PARP, caspase-3, -8, and -9 as well as down regulated Bcl-2 expression.|PMC7477428|Western blots showed 100μM propranolol significantly reduced the expression of Bcl-2 while increasing the expressions of Bax, cytochrome c, cleaved capase-9 and cleaved caspase-3, and down-regulated the levels of p-AKT, p-BRAF, p-MEK1/2 and p-ERK1/2 in melanoma cells, after a 24h incubation.|PMC5356557","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:236f0d2cd7a25a0deb17529c91c377b8e38e3dd08bee86e63e07f9c71ab1f951","tmkp:4e0138aa05091499c00306a90c8e3205f94a2dde94d5b6a35ac936b8e329d257","tmkp:881ed5981be29f8b67923610091f03ae5f28d5572a8f5683d27db3a21cf59d2f","tmkp:b4c4757129809942902fba5f75acf723c23d0677772d60e32bb2820b06708319","tmkp:2b5f2f36311d456e0225bc5978c730d91e5026e647b36a7514b572cb46dc5846","tmkp:4441503486d173e73d580dd7636e634f2874ca0120893d23850998547bd036d8","tmkp:1cae07a0d2be58c469687e7c7b6cec2919ae14da5e169d96b0c01ede3a1af6f2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"60016589":{"subject":"PUBCHEM.COMPOUND:2802","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"PED can effectively be treated with clonazepam.|PMID:25099510|Five milligrams per day of clonazepam allowed for excellent control of PED.|PMID:25099510|Later, Mahajan et al. have described PED in an 8-year-old boy with ECHS1 gene mutation and they also showed clinical improvement with mitochondrial cocktail and clonazepam.|PMC7900734","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:25099510","PMID:25099510","PMC7900734"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9993797333333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:233cc06dd3196c744f193901a051bdb1629bc7d6a941cb360f1b75b6a44c8550","tmkp:c7f694427e7853feb1da2e06b12bca0fad7e7d2734d097be0be54c47c127d226","tmkp:2d0a5231c9105712d95e3b9ae536c4294c46d6ad96f5edf7b258e7c5695198ba"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"14959717":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:687d7bb223d7a7d8168af939c29662bb4584aaebd6515cedc6d86b864aebfc3e","tmkp:c336a0afc18d103f87bb542dab02ae887fb2ee5584aaecb4c6f126dc622da83f","tmkp:3e2ca2d7f8c02fbd01c05bb180222abb737c4cc9ed3f0cad4c7a278bbaeac3c5","tmkp:dd589d1fa0e62e14d0e605a95768fd85255b6a20609285d5f52a1622698facf9","tmkp:b14734209057c916c0b54502fd8fb5387d3535cefde8d7ce4388b7c6f98528e4","tmkp:2d296b4b03c35fc2c6336c621a77a00b3b7bcc7deca44a0c256c045a5cb5c719","tmkp:88a31bf1b8d8f0abf7c40bc0d463eaf9385f969ab4676b4411acf2aa581ba85f","tmkp:9368634da1f90ec9c1379ffa87e68f76a3a49db7f9f1175f620007688fc24b9c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9993589333333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The results showed that following supplementation with EPS, interleukin (IL) 6, IL1β and tumor necrosis factor (TNF) α mRNA expression in VAT were significantly reduced, while Glut4, pAMPK and SirT1 protein expression were markedly increased when compared with KKAy mice gavaged with water.|PMID:24337047|Another study suggested that a cinnamon extract affects a tyrosine phosphatase that would otherwise inactivate the insulin receptor and Cao and coworkers reported that a water extract of cinnamon increased insulin-dependent glucose transporter 4 (GLUT4).|PMC5067830|It has been reported that several herbal extracts, such as cinnamon water‐soluble extract, could increase the expression of GLUT4 in C2C12 cells 23.|PMC6487711","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5324216","PMID:24337047","PMID:30263314","PMC5067830","PMC6010401","PMC7339438","PMC6487711","PMC6196785"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"96157214":{"subject":"PUBCHEM.COMPOUND:60606","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Clopidogrel reduced PAI-1 (ng/ml) in volunteers, -5.30 (2.20) (p < 0.05), and patients, -3.61 (2.75) (non-significant trend).|PMID:16421011|In line with this, clinical data suggest that long-term antiplatelet therapy, for example, with aspirin and/or clopidogrel, is basically effective to reduce plasma PAI-1 levels.|PMC3712849|The expression levels of Fbg and PAI-1 were reduced in all GXNT groups and the positive group (12.5 mg/kg clopidogrel), compared with those in the model group (P < 0.01, P < 0.05; P < 0.01).|PMC7237702|Clopidogrel pretreatment completely abolishes the increase of PAI-1 active antigen after coronary stent implantation.|PMID:18558425|Clopidogrel pretreatment abolishes increase of PAI-1 after coronary stent implantation.|PMID:18558425","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:16421011","PMC3712849","PMC7237702","PMID:18558425","PMID:18558425"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995525814285714","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:863e3065225b8a9798b959997a12751dff53b4341cf9e0fc679b4a8f4c3cf1fb","tmkp:3dea5d3873ff496fe210eb4c60c5e47f6f436ec83890847e58eaf88e92540667","tmkp:7f42c04608ba1b6eb8a1b01bd8f2adf9c2390a5caac5461884d2442fda5a1686","tmkp:2943a92610a6069e3473f8c446726fa5da592d03833febb8bfd628ec570547f5","tmkp:985223fffaca1defde99f54e121498e8b8e49e9e1adf70951d5b7da37f1f8960"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"104697047":{"subject":"PUBCHEM.COMPOUND:1032","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9997155","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"IMD-4482, 3-[3-(4-tert-butylphenoxy)-4′- (trifluoromethoxy) biphenyl-4-yl] propanoic acid, a synthetic PAI-1 inhibitor, was supplied by IMMD Inc. (Tokyo, Japan) and used for the functional inhibition of PAI-1 in the subsequent experiments (Figure 2C).|PMC5685717","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4c4465090eea6fc3f78a9cac3008982ba00572459f9e21b997c69e194eb75e87"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5685717"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"65574738":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:cc5be444bff440f508d1db11f4d066e3016fb9ff160cdd4acb638e4cf57347a3","tmkp:2a79921ef60bd8fa332eb8af6426777ab39ab8e3944b5e853402ca9f2446a118","tmkp:9fd88d88121fef735ed8aed24a51182a9a17b9bfb7a18506cb898048b0b2456a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5386356","PMC4079329"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9921451","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"This study shows that the PARP-1-mediated necrotic pathway is distinct from that of the canonical parthanatos, serving as a novel mechanism of RPE loss in the pathogenesis of dry AMD: (1) PARP-1 is activated, leading to the death of ARPE-19 cells through mitochondrial dysfunction and cellular energy collapse in response to H2O2; (2) AIF, a typical downstream effector of PARP-1, does not participate in the execution of cell death in H2O2-induced ARPE-19 cells; (3) the essentiality of PARP-1 was validated in mouse and rabbit dry AMD models.|PMC5386356","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"125591558":{"subject":"PUBCHEM.COMPOUND:9871419","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:36c3aafdde626a1e4b4879d1997d824743455f122d42dab73d29b2e32038a22c","tmkp:33ee2b16bb963c4c817cb32180e7d0b5af9906ac6571dce115f3ed18d988e0ef","tmkp:fa172801988a89756bd1fd1ca5f9ef6388362cf7222729d03b4d595f38e44418","tmkp:a5b667f9cd7eca97e6a71478f16f4db17eb585fa0312ba8abe031d8369b32607","tmkp:fff91df4e665dc4cf71fbf3a7f132d30f25987932713f6acda17e015858028cc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9996805514285715","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8052144","PMC8052144","PMID:29042978","PMC8052144","PMID:29042978"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, ticagrelor treatment also significantly increased the IL-10 protein level and decreased VEGF protein level in ischemic tissues.|PMC8052144|Furthermore, ticagrelor treatment significantly increased the IL-10 protein expression and inhibited the VEGF protein expression in ischemic tissues of IL-10+/+ mice.|PMC8052144|Furthermore, the possible mechanisms underlying the effect of ticagrelor were associated with its functions of attenuating the expression levels of VEGF and EGF, as well as suppressing the phosphorylation activation of ERK1/2, P38 and nuclear factor-κB P65.|PMID:29042978|The major results of the study showed that IL-10 negatively adjusts angiogenesis induced by ischemia, and ticagrelor inhibits the angiogenesis and blood reperfusion recovery, significantly increases IL-10 level, and reduces the VEGF expression in the IL-10+/+ mouse ischemic hindlimb, which were abolished in IL-10−/− mice.|PMC8052144|In addition, ticagrelor significantly decreased the ulcer-stimulated expression levels of EGF, VEGF, phosphorylated extracellular signal-regulated kinase (ERK), phosphorylated P38 mitogen-activated protein kinase and nuclear factor-κB P65 at the ulcer margin (P<0.05).|PMID:29042978","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"5946228":{"subject":"UMLS:C4529301","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:de978fe596432347758c4b75d064cf733ee2f553ef624ad7514c1a17ab774ec0","tmkp:40b820e67efd71d0ad684c9dff5468b0d1acce13e0fe3b86e3aa4f2441fbca98"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"IL-4 secretion was significantly reduced in the 92.1 and OCM-1 cell lines after bevacizumab treatment (223.00 ± 35.44 pg/mL versus 124.33 ± 16.74 pg/mL; 213.50 ± 31.93 pg/mL versus 114.25 ± 19.03 pg/mL, respectively; Student’s t-test; P< 0.05, for both).|PMC3729237","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC3729237"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999726","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"84399086":{"subject":"NCBIGene:3630","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Overexpression of the gene encoding phosphoprotein enriched in astrocytes 15 (PEA15), also known as phosphoprotein enriched in diabetes (PED), causes insulin resistance and diabetes in transgenic mice and has been observed in type 2 diabetic individuals.|PMID:17021921|Overexpression of PED (also known as PEA15) determines insulin resistance and impaired insulin secretion and may contribute to progression toward type 2 diabetes.|PMID:20396999|Transfection of PED/PEA-15 in differentiating L6 skeletal muscle cells increases the content of Glut1 transporters on the plasma membrane and inhibits insulin-stimulated glucose transport and cell-surface recruitment of Glut4, the major insulin-sensitive glucose transporter.|PMID:9670003|Transfection of PED/PEA-15 in differentiating L6 skeletal muscle cells increases the content of Glut1 transporters on the plasma membrane and inhibits insulin-stimulated glucose transport and cell-surface recruitment of Glut4, the major insulin-sensitive glucose transporter.|PMID:9670003|Overproduction of phosphoprotein enriched in diabetes (PED, also known as phosphoprotein enriched in astrocytes-15 [PEA-15]) is a common feature of type 2 diabetes and impairs insulin action in cultured cells and in 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with the argument for an important role of VEGF in osteoarthritis, Gallelli et al. showed that ibuprofen, diclofenac and celecoxib decrease VEGF levels in the synovial fluid of the osteoarthritic joint, with a concomitant improvement in joint pain as well as joint function in osteoarthritis patients.|PMC4391471|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off at the end of week 10, delayed the development of dyskinesia, and decreased striatal cyclooxygenase-2 (COX-2) and vascular endothelial growth factor (VEGF) levels.|PMC8150526|For instance, Gallelli et al. found that diclofenac, ibuprofen, and celecoxib can decrease tumor necrosis factor-alpha (TNF-α), interleukin-6 (IL-6), and vascular endothelial growth factor in the synovial fluid of the osteoarthritic joint with a parallel improvement in joint pain and function of patients.|PMC6335784|Treatment with ibuprofen or piroxicam in 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shown in Figure 2, both basal and insulin-stimulated de novo lipogenesis were inhibited by propionic acid and butyric acid, significant inhibition was seen at the lowest concentration (1 mM).|PMC4496978|In addition, we show that propionic acid and butyric acid inhibit basal and insulin-stimulated de novo lipogenesis, which is associated with increased phosphorylation and thus inhibition of acetyl CoA carboxylase, a rate-limiting enzyme in fatty acid synthesis.|PMC4496978|Propionic acid and butyric acid inhibited isoprenaline- and adenosine deaminase-stimulated lipolysis in the presence of phosphodiesterase (PDE3) inhibitors as well as propionic acid and butyric acid inhibited basal and insulin-stimulated de novo lipogenesis, which was associated with increased phosphorylation, thereby inhibiting the activity of HMG-CoA, the rate-limiting enzyme for fatty acid 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the contrary, binding of Met variant of proBDNF or of the BDNF pro-peptide results in dendritic spine loss via the inhibition of Rac1 and the activation of caspase-3.|PMC7529616|In Fig. 3A-E, we showed that compared with the control animals, the aortic endothelial protein expression levels of NOX-1, p22, Rac-1 and p47 were significantly increased in the 1% methionine group, whereas they were significantly decreased in the 1% methionine plus exercise group compared with the 1% methionine group.|PMC5596261|For the high level of μ, the expression of Rac1 and RhoA is strongly inhibited, thus the plasticity of cell migration driven by Grb2 and Gab1 is limited only to {LL} and {LH} phases, indicating that only EMT/MET could occur (the 1st-2nd panels to the left, Fig. 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and fluphenazine inhibited GLUT4-mediated glucose transport in the rat muscle L6 cell line.|PMC6659786|Clozapine also significantly inhibited the mRNA expressions of lipogenic genes ACC, SCD1, GLUT4, aP2, and CD36 as well as adipokines such as resistin, leptin, and adiponectin.|PMC3465748|When the transcriptions of typical lipogenic genes were examined at 8 days after the adipogenic induction of brown preadipocytes, clozapine was shown to significantly decrease the transcription of all genes except for FAS, and the inhibitory potency was particularly higher in GLUT4, aP2 and CD36 (P < 0.05) (Figure 4A).|PMC3465748","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6659786","PMC3465748","PMC3465748"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9997021333333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:aa7b7a7aaa9425a697ddbf58a592a17d8f852e9f7ebd7daf8f7d62bd88ef10f4","tmkp:fb3068ddaf33de5c84c464ddca686c0e14c98882c2ac572897443f29c194258e","tmkp:08a36ffbcc71cd47b6dac53a97b3ee1b601b8526687d6a91daab91d4c63a031d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"30874923":{"subject":"PUBCHEM.COMPOUND:22833565","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:9e64faf97fa62a25bc44aadd37c54a7b5edfe4eb7855dfa78f560f746099f0d0","tmkp:95095ce8b2f7d4f0e5ac1a724f39fe9d04a8e66949ee7db178bcd59060914776"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Again, heparin and 8-Br-cGMP decreased PMA-stimulated ERK2 activation (Figure 4).|PMC4149598|In the presence of FGF-2, FGFR-1 kinase and subsequent mitogen-activated protein kinase Erk2 activities were augmented in a dose-dependent manner, whereas high concentrations of heparin resulted in decreased activity.|PMID:10816596","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4149598","PMID:10816596"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.98899977","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"85777547":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Importantly, several cytokines and chemokines (e.g., MIP-2, MIP-1, IL-4, IL-6 and osteopontin) involved in neutrophil infiltration were upregulated in hepatic NKT cells isolated from chronic-plus-binge ethanol-fed mice compared to pair-fed mice.|PMID:25661730|These data indicate that IL-4 and IL-13 signaling is increased by ethanol in neuronal-microglial co-culture, suggesting a role for these cytokines in neuronal-glial ethanol-induced signaling.|PMC6770440|In our study, we confirmed that SH-SY5Y IL-4 and IL-13 signaling is enhanced following ethanol treatment in BV2/SH-SY5Y microglial co-cultures, with an increased induction of IL-4R and IL-13R by ethanol in co-cultured SH-SY5Y.|PMC6770440|Ethanol caused the elevation of mucosal interleukin-4 level (compared to the control, P < .05).|PMID:21244242|IL-4 and IL-13 is increased by ethanol in co-cultured BV2 microglia.|PMC6770440","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9964932882692307","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:25661730","PMID:16085180","PMC3887500","PMID:21244242","PMC6770440","PMC5391607","PMID:20116195"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b13c1006b4ce1e319e41a0147c07c5683d25fad45561cdd6704da3d12e8e9e19","tmkp:ef6373b078b3155dda00ef21e2e50b6efd9cc4c5a0f643e1a341d0122a7860e4","tmkp:10cebc3cf3ae80c2fa4f8bca81c3052a7fbf5d2679561fb90259999b23333097","tmkp:7442596db0ac7f8fd614290d5c7eeb953421fcc242f36f88e5f49612e3ea929b","tmkp:b7ae908a82946a8a3280958d412c33ecfd5e4641e87266e51e05f7364b732b50","tmkp:5b2b8f2e8c9d51d5a00424339bb078559ca229c71609328331bc9e395e8986d1","tmkp:544a655cc6ad5e079c6b97729f2fabd5d20f0a8dcc09792c88dba2b689228a9e","tmkp:22425ae0bd67c970af7093a4797d9194f7fff5e2a49c35648fe5b3992c773e12","tmkp:bd9b5b18085bf29f831070235183640737d2edbff6a9dd6d3650514d3c2c0acc","tmkp:f2ff4b5356ce72b532b6432aa47e000390461ab4f9caeae4a61c7c610ef69e82"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"107972271":{"subject":"PUBCHEM.COMPOUND:5073","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"As RT-PCR and Western blot revealed that the treatment effects of risperidone and haloperidol seemed to be mediated through activation of VEGF and MMP2.|PMID:19579000|The findings indicate a promoting effect of risperidone and haloperidol on survival of young neurons in the hippocampus by enhancing the expression of the anti-apoptotic protein BCL-2 and by activation of VEGF/MMP2, whereby an interference with ketamine and thus a priority role of the NMDA system was not evident.|PMID:19579000|Moreover, in a previous study we showed that administration of risperidone was able to increase VEGF expression and angiogenesis in the hippocampus of 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flavonoids, diazepam inhibited the release of vascular endothelial growth factor (VEGF) and granulocyte-macrophage-colony stimulating factor (GM-CSF) into supernatants of cultured in the SNU-C4 and MDA-MB-231 cells.|PMID:18239283|Like flavonoids, diazepam inhibited the release of vascular endothelial growth factor (VEGF) and granulocyte-macrophage-colony stimulating factor (GM-CSF) into supernatants of cultured in the SNU-C4 and MDA-MB-231 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polyubiquitinated proteins in intact Jurkat T cells; (iii) inducing activation of caspase-3/-7 and cleavage of poly(ADP-ribose) polymerase in intact Jurkat T cells; and (iv) inducing the appearance of spherical cells preferentially in prostate cancer PC-3 over the normal NIH 3T3 cell 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rats.|PMC6437962","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9987097666666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"8090692":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:142","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:30368987","PMID:27984176","PMID:21410490"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"10090","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"increases 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induces muscle atrophy by suppression of the insulin-like growth factor 1 (IGF-1)/Akt/PI3K signalling pathway.|PMC8153455|NAC and dexamethasone suppressed the phosphorylation of Akt in lungs.|PMC7487305|Dexamethasone impairs cell-cell communication in osteocytes by autophagy through inhibiting Akt-mTORC1 signaling pathway, contributing to the deleterious bone effect.|PMC6064191|In light of this potential Akt-PDE interaction and the opposing actions of dexamethasone on CREB and Akt, we hypothesized that dexamethasone might be activating CREB by inhibiting Akt and PDEs.|PMC6173943|Combination of erythromycin and dexamethasone improves corticosteroid sensitivity induced by CSE through inhibiting PI3K-delta/Akt pathway and increasing GR expression|PMC7123456","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"82667165":{"subject":"PUBCHEM.COMPOUND:6137","object":"NCBIGene:3172","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In AGS cell, BBR and MET significantly decreased the protein level of HNF4α (Figures 5A,B).|PMC6202939|As we expected, MET and AICAR also decreased the protein expression of HNF4α in SGC7901 cells (Figure 5C).|PMC6202939|As shown in Figures 8E–H, the BBR (100 mg/kg) and MET (250 mg/kg) decreased the HNF4α, WNT5A and cytoplasmic β-catenin expression comparing with the normal control group (P < 0.0001).|PMC6202939|BBR (30 μM), MET (30 mM), and AICAR reduced the mRNA expression of HNF4α (Figure 5D).|PMC6202939|Notably, HNF4α-mediated repression in EMT/MET dynamics is associated with chromatin topological remodeling of HOTAIR regulatory sequences.|PMC6461983","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC5548255","PMC6202939","PMC6461983","PMC8080681","PMC3852538","PMID:24992599"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ca552602bd1045244d6c9c711db5558a4b93c2d4ca375a9cf9ce6e6f6f45acb2","tmkp:77888a9519f4e2a207f2dae063ec86a883b01fb2f16a04fc38414744986df59f","tmkp:e729461480ad91c10bf4991bb5a1836915257b59b41281f7de9fb3bba38a1ce0","tmkp:1aec4b9278e3ee77c75117b1be7647f6f86a1fa585ac3046c83b782b5948785e","tmkp:8ddcaf92422b6ff3f4e6fbe3e5d5294321f8e0c5c1717c1a374013e1e09a9489","tmkp:8142adcb5f09aa18375632c777a33ecf782e6395ad7ab2c6a2ab19b9899d780b","tmkp:2fa2b4a3942e967732f1575e94dcbd82ead353883589d5deb936102c4307a5df","tmkp:4080fe3a087e6515993f9e2fc45afb58d55956ce398055aee67271d0e3fb1162","tmkp:6a9f478e097ab46f05f12cf5aab830d29a44e0ed1ca4122a6afc091e0c716b51","tmkp:0548560f7cff2b9dc5e726b8f07f58f1308ef45830ad244b4e3a17ff919c8a79"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994277966666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"2504185":{"subject":"PUBCHEM.COMPOUND:4943","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"We found that propofol significantly decreased inflammatory cell counts and interleukin-4 and inflammation score in vivo.|PMID:27884341|The results showed that propofol significantly decreased the number of eosinophils and the levels of IL-4, IL-5, IL-6, IL-13, and TNF-α in BALF.|PMID:29532264|Compared to propofol, sodium thiopental reduced the concentration of IFN-γ and IL-4 without affecting the concentration of IL-2.|PMC7539048|Compared to dexmedetomidine, propofol had elevated mRNA or serum levels of IL-2 and TNF-α, plus significantly lower IL-4 or IL-10 expression (p<0.05).|PMID:28387890|The secreted cytokines such as IL-2, IL-3, IL-4, IL-5, and IL-6 were downregulated by propofol by 67.1%, 78.2%, 65.1%, 75.6%, and 71.9% 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(PED).|PMID:31027714","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:caa203ae1d2d61f36de9d80d8ebf39205bcca9483ac782c3e60e23c70d912ac1","tmkp:bf27ebcc1253e8e414f05469d9f45a04de3eadf4d4fbead327bb6a552e98974f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"11562727":{"subject":"UMLS:C2740652","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Contents and microenvironment of a large PED with an Onion 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cellular abundance of Ped/Pea-15, an Akt substrate and inducer of insulin resistance, was also increased following clozapine exposure, both in the absence and in the presence of cyclohexymide, a protein synthesis inhibitor.|PMC3306790|Thus, in these experimental models, clozapine deranged Akt function and up-regulated Ped/Pea-15, thereby inhibiting insulin stimulation of PKC-ζ and of glucose uptake.|PMC3306790|Similar as in cellular models, in the caudate–putamen and in the tibialis muscle of clozapine-treated C57/BL/KsJ mice, Akt phosphorylation and Ped/Pea-15 protein levels were increased and PKC-ζ phosphorylation was decreased.|PMC3306790|Similar as in cellular models, in the caudate-putamen and in the tibialis muscle of clozapine-treated C57/BL/KsJ mice, Akt phosphorylation and Ped/Pea-15 protein levels were increased and PKC-ζ phosphorylation was decreased.|PMID:21618539|Similar as in cellular models, in the caudate–putamen and in the tibialis muscle of clozapine-treated C57/BL/KsJ mice, Akt phosphorylation and Ped/Pea-15 protein levels were increased and PKC-ζ phosphorylation was decreased.|PMC3306790","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"95073261":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7400689","PMC6764771","PMC6764771","PMC6764771","PMC6764771"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:492468a9f611007446f851815a0394372461b254bdfb1fcf6c8e4dc02d0ff0c5","tmkp:52680a5858407462639cd4f738bd278a071bb2018f0ee4260b13779a7e7f6060","tmkp:f5fb1610be7b7483c88ba5d48c91d7efbfbc42b40da310cd1d6c354fb3ec23b1","tmkp:c6eafd098120a8c0bbc4798cb789883e495c20c0ac59e39ff1cb22a1f7953b75","tmkp:cde479a96575572acf57c0484eb7290abf3b62556b4199b63b4b3cdde07fa675"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9925673868421052","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In a small study of HLA-DQ8 + patients with recent-onset T1D, methyldopa was shown to specifically block insulin peptide binding to HLA-DQ8 and to decrease inflammatory T-cell responses to insulin .|PMC7400689|We also evaluated the ability of methyldopa to decrease primary insulin-specific T cell responses in treated patients, as opposed to the effects on antigen presenting cells described above.|PMC6764771|Functional testing of T cells showed that methyldopa blocked both insulin (T1D) and gliadin (Celiac disease) reactive T cells restricted to DQ8, but those T cells restricted to peptides presented by other MHC class II molecules (e.g.|PMC6764771|Furthermore, we showed that methyldopa blocks insulin-specific T cell responses restricted to DQ8 but not those of tetanus toxin, a common vaccination.|PMC6764771|This indicates that methyldopa treatment reduced inflammatory insulin-specific T cell responses while leaving responses to a commonly received vaccine intact.|PMC6764771","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"53145451":{"subject":"PUBCHEM.COMPOUND:2783","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4267238"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99947435","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Stimulation with clenbuterol resulted in prolonged activation of Rac1 in response to the CCR7 ligand CCL21 and CXCR4 ligand CXCL12 in both B and T cells, whereas the effect of β2AR stimulation was unremarkable in response to the CXCR5 ligand CXCL13 in B cells (Fig. 4 A).|PMC4267238","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f38db294a7f433a2286d250bd8d98d5ced4a1735cff2fc01c5c0064f24abf5a0"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"88450955":{"subject":"PUBCHEM.COMPOUND:2726","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In this case, VEGF induced a transient reaching 1.2030 ± 0.0005 (p < 0.01; n = 6 Figure 2C), which was larger than the ratio induced by VEGF in the presence of CPZ (p < 0.05; n = 6; Figures 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we found that when we combined ZA and nab-paclitaxel the prevention of Rac1 activation was 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HGF, VEGF and G-CSF levels were increased after heparin administration.|PMID:31738878|In addition, heparin significantly increases expression of a series of growth factors, including FGF14, FGF20, BDNF, IL6 and VEGF, but not FGF2 (Fig. 3C and data not shown) as well as the expression of a number of cell surface proteins, including ITGA6 (integrin α6) and NGFR, but not ITGA5 or ITGB3 (Fig. 3C and data not shown).|PMC5330685|The protein levels of VEGF were markedly increased only in the VEGF189-transfectants cultured in the presence of heparin.|PMID:12429975|VEGF mRNA expression was significantly inhibited by N-desulfated heparin and was higher in normal saline group than in N-desulfated heparin group (Ct value 19.51 +/- 1.01 vs 22.55 +/- 1.36, P < 0.05).|PMID:17230619|In the retina, VEGF paracrine signaling has been correlated with upregulation of the Heparin Binding EGF ligand (HB-EGF) after injury, which acts through 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promotes ERK1/2 activation via phosphorylation, and correspondingly activates the MAPK signaling pathway for the prevention of ER stress-induced cell death.|PMC7212460|LPS signals through CD14 via the TLR4-MD-2 pathway whereas PPD triggers the MAPK (ERK1/2/P38) pathway mostly via TLR2 signalling.|PMC4425930|On the other hand, PD98059 attenuated PPD-elicited phosphorylation of ERK1/2 and p70S6K without affecting Akt and mTOR (Figure 3c and d).|PMC5668468|It was found that 20(S)-25-OCH3-PPD inhibited the up-regulation of TM-induced SelS expression, implying that 20(S)-25-OCH3-PPD promoted the phosphorylation of ERK1/2 and thereby protecting cells from ER stress-induced cell death.|PMC7212460","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:19957370","PMC5708136","PMC2799537","PMID:30735802","PMC7212460","PMC5668468","PMC4425930"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.997283225","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"14676003":{"subject":"PUBCHEM.COMPOUND:5073","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"We found a reduced level of Bcl-2, Mcl-1 (antiapoptotic protein) and an elevated level of Bax (proapoptotic protein) after olanzapine (40 μM), risperidone, amisulpride and aripiprazole treatment compared with the control 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expression analysis revealed elevated levels of angiogenic vascular endothelial growth factor in the clopidogrel group.|PMID:30801550|In addition, NXT protected HUVECs against clopidogrel-induced cell death by inhibiting expression of tumor necrosis factor-like cytokine 1A and activating expression of vascular endothelial growth factor α. Taken together, our study indicates the potential application of NXT in antithrombosis by multiple antithrombotic 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vivo induction of AP by either supramaximal caerulein or L-arginine leads to increase in caspase-3 activation.|PMC5037034|Increased caspase-3 activation was observed also in acini prepared from animals treated with either supramaximal caerulein or L-arginine (Figure-3D).|PMC5037034|Taken together, this study demonstrated that ARG is a potent inducer of apoptosis and this was accompanied by caspase-3 activation and upregulation of bax/bcl-2, which offers a potential mechanism for the apoptosis-inducing activity of ARG.|PMID:18717345|Next, the role of apoptosis in the mechanism of cytotoxicity induced by Arg8-ELPBC-cBH3 was investigated by the activation of the effector enzyme caspase-3.|PMC3985949|Activation of caspase-3 activity and apoptosis in MDA-MB-468 cells by N(omega)-hydroxy-L-arginine, an inhibitor of arginase, is not solely dependent on reduction in intracellular polyamines.|PMID:11698350","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"42863123":{"subject":"PUBCHEM.COMPOUND:5280934","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999410112","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:372e0a28e2caa201b7f94593bf186df34d235039d5c928a8837888aef8bf83a9","tmkp:dea94c9f9137bd96438ed0155a92f712e1665a93b7090921de48d6004f3a017d","tmkp:67daebeab7cba657f9a18352131552bc33f71abdd327967b80b586b96dccf72c","tmkp:135a42dc6cf9c493a2e623e848dc613a460b7c6ad055813370a3ee0b836aa728","tmkp:24f2e4cc8716b71b5b2cd8ee41894abadc55d7000aac58e259e469f513cdfda9"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In addition, ALA ameliorates proteinuria by down-regulating the expression of TGF-β1 and fibronectin proteins, and these favorable effects are related to the inhibition of phosphorylating activation of the p38 MAPK pathway in the renal cortex of OLETF rats.|PMC5691398|These results suggest that ALA ameliorates proteinuria by attenuating expressions of TGFbeta1 and fibronectin proteins, and these favorable effects are related to inhibition of phosphorylating activation of p38 MAPK pathway in renal cortex of OLETF rats.|PMID:19375583|Rudhorfer et al. observed a dramatic downregulation of the fibronectin gene after ALA-PDT of the squamous cell carcinoma line A-431.|PMC3780570|After ALA treatment for 5 weeks in OLETF rats at 30 weeks of age, plasma malondialdehyde, urinary protein excretion, renal cortical TGFbeta1, and fibronectin protein levels were decreased; and urinary protein excretion was positively correlated with renal cortical TGFbeta1 and fibronectin protein levels.|PMID:19375583|Both ALA and DHLA downmodulated the surface expression of the alpha4beta1 integrin (very late activation-4 antigen; VLA-4), which binds fibronectin and its endothelial cell ligand vascular cell adhesion molecule-1 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results indicate that this combination of VPA with HCCA not only enhances the protein levels of Bax, cytosolic cytochrome c, caspase-3 and PARP-1 but also reduces the protein expressions of Bcl-2, cyclin D1 and NF-κB as well as inhibits the phosphorylation and expressions of Akt, EGFR, VEGFR2 and c-Met in the cancer cells.|PMID:23161221|Cell death with DNA breaks in the nucleus was greater using combined regimens of PAM and HDAC inhibitors such as trichostatin A (TSA) and valproic acid (VPA) than a single PAM treatment and was accompanied by the activation of poly (ADP-ribose) polymerase-1 (PARP-1), depletion of ATP, and elevations in intracellular calcium levels.|PMID:27470189|Co-treatment of VPA with DOX led to synergistic suppression of cell viability with an increase in caspase-3 activity and CDKN1A, CCNE1, PARP1, and PARP3 proteins expression in ovarian cancer cell lines.|PMC5454960|Cell death with DNA breaks in the nucleus was greater using combined regimens of PAM and HDAC 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(filled bars in Figure 2D).|PMC2292137|In contrast, subcutaneous abdominal fat of the same patients showed increases in PTP-1b, VEGFa, IFNγ, PAI-1, and NOS-2 not observed in omental fat.|PMID:22323564|At the same time, the expression of plasminogen activator-inhibitor (PAI-1) expression is increased, inhibiting the fibrinolytic system.|PMC3285293|FaDu cells showed the same tendency with significantly enhanced PAI-1 expression levels after 4 h, and maximal PAI-1 expression levels after 20 h of hypoxia (Fig. 3B).|PMC1973081|Fasting concentrations of markers of inflammation; monocyte chemoattractant protein-1, plasminogen activator inhibitor-1, and E-selectin; as well as retinol binding protein-4 and the liver enzyme, gamma glutamyl transferase, were also increased in these same subjects consuming 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obtained to date suggest that reduced Akt phosphorylation and PPAR beta/delta expression in the liver, reduced JNK1 phosphorylation and increased PGC1alpha expression in the muscle, and increased expression of IGF1 and insulin receptor in the heart are either related to mechanisms of CR action on longevity or represent potential biomarkers of delayed 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resulted in greater G0/G1 arrest and suppression of the cell survival protein bcl-2 than are observed with just tamoxifen, promoting the novel concept in breast cancer that combined signal transduction inhibitor/endocrine therapy may be considerably more effective that endocrine therapy alone.|PMC1064090|Tamoxifen has multiple influence on the rate of growth of cancer cells: depends on estrogen receptor (ER), conducts reduction of proliferation rate; depends on ER and other mechanisms conducts to suppressions of Bcl-2 protein expression and induction of cell death through apoptotic pathway.|PMID:10870682|Tamoxifen could decrease spleen mass and Bcl-2 protein expression, increase the Bax protein expression as well as exert uterotrophic effects by increasing uterus index and inducing the gene expressions in the uterus.|PMC3943014|Among the cell cycle and survival genes, BIRC5 (gene for survivin), BCL2, CCNA2 (gene for Cyclin A2), and MKI67 (gene for Ki-67) were downregulated by study treatments, though these effects were most profound in the BMS-754807 + tamoxifen treatment group, particularly for MKI67.|PMC4004036|Decreased bcl-2 expression was observed in several cancer cell types treated with tamoxifen and daidzein and in equol-induced apoptosis in mammary 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similar 6-fold decrease in mouse VEGF was observed in animals treated with Verteporfin-PDT followed by anti-mouse VEGF, but bevacizumab had no effect on mouse VEGF levels (Figure 2B).|PMC4476543|Therefore, verteporfin can inhibit VEGF-induced YAP pathway activation by inhibiting YAP activity.|PMID:31633245|The present review is divided into two major sections: the period prior to the use of anti-VEGF agents (triamcinolone acetonide, verteporfin photodynamic therapy) and the period following their introduction (pegaptanib sodium, bevacizumab, ranibizumab, aflibercept).|PMID:23560774|Also, administration of verteporfin significantly reduced VEGF-induced blood vessel formation in Matrigel plugs using mouse endothelial cells, suggesting an important role of YAP/TAZ in VEGF-induced angiogenesis in vivo.|PMC6468149|Verteporfin was also able to inhibit the HIF-1α activity upregulated by paclitaxel and CA4 (Fig. 4B), and the VEGF gene expression upregulated by paclitaxel in TNBC MDA-MB-231 cells (Fig. 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demonstrates that there is clinical overlap with other PxD subtypes [i.e., paroxysmal non-kinesigenic dyskinesia (PNKD) and paroxysmal exercise-induced dyskinesia (PED)], reinforcing the suggestion that the clinical description of PxD should not be solely tailored on the type of trigger, but should include duration of the attacks and response to AED, especially carbamazepine (CBZ).|PMC7969989|This demonstrates that there is clinical overlap with other PxD subtypes [i.e., paroxysmal non-kinesigenic dyskinesia (PNKD) and paroxysmal exercise-induced dyskinesia (PED)], reinforcing the suggestion that the clinical description of PxD should not be solely tailored on the type of trigger, but should include duration of the attacks and response to AED, especially carbamazepine 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the 4T1 breast tumor bearing model, mannan-hyaluronic acid-manganese dioxide nanoparticles were found to reduce the expression levels of HIFs and VEGF and to shift TAMs toward M1 type, as evidenced by elevated levels of interleukin-12 and inducible nitric oxide synthase.|PMC7032173|Significant (P < 0.01) decreases of caspase-3, PARP, TNF-α, COX-2, and iNOS were detected while VEGF and IL-1β-immunoreactive cells decreased non-significantly in 0.1% sodium hyaluronate treated rats compared with CAI control rats.|PMC4911203|Topical application of hyaluronic Acid-RGD Peptide-Coated Gelatin/Epigallocatechin-3 Gallate (EGCG) nanoparticles inhibits corneal neovascularization via inhibition of VEGF production|PMC7408368|LPH (liposome-polycation-hyaluronic acid) nanoparticles, modified with single-chain antibody fragment (scFv), for targeted systemic delivery of siRNA and miRNA into murine B16F10 melanoma, could also effectively downregulate target genes (c-Myc/MDM2/VEGF) in lung 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and norepinephrine-induced ADRB2 activation lead to VEGF induction in prostate cancer cell lines through the cAMP-PKA-PI3K-AKT-HIF-1 alpha pathway.|PMC6498733|A variety of studies have confirmed that epinephrine promotes growth, invasion, and angiogenesis of malignant cells by upregulating the expression of vascular endothelial growth factor, matrix metalloproteinase (MMP)-2, and MMP-9, which are critical proteins related to carcinogenesis.|PMC6658366|In particular, in colon cancer cell line HT-29, adrenaline determined an increase in cell proliferation and production of proinflammatory and proangiogenic factors such as PGE2 and VEGF.|PMC4616528|Epinephrine and norepinephrine also upregulated the expression of IL-6, VEGF, MMP-2 and MMP-9 in oral cancer cell lines, mouse models, nasopharyngeal call lines and human melanoma cell lines.|PMC7825104|β-AR signaling activation via adrenaline and/or noradrenaline is implicated in the promotion of angiogenesis, through the upregulation of 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the observed reduced tumor destructive effect of MTX/MNPs in comparison to MNPs is not fully explainable, protein analyses suggested a more unfavorable expression pattern (eg, elevated p-ERK1/2, BCL-2, VEGF, and MMP2) after MTX/MNP treatment, resulting in a progression of cell cycle as indicated, for example, by cyclin A.|PMC5388224|We found a slight upregulation of VEGF-R1 in the MTX/MNP group, indicating the insufficiency of this treatment to impair VEGF-R1 expression and inhibit tumor growth.|PMC5388224|LDE-MTX increased the expression of myocardial vascular endothelium growth factor (VEGF) associated with adenosine release; this correlated not only with an increase in angiogenesis, but also with other parameters improved by LDE-MTX, suggesting that VEGF increase played an important role in the beneficial effects of LDE-MTX.|PMID:28553113|Presence of ultrasound subclinical synovitis and increment of serum vascular endothelial growth factor in a patient with rheumatoid arthritis 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expression of cleaved-caspase 3 and cleaved-PARP-1 by the sorted-SCC and MSC/SCC fused cells, compared to naïve SCC-25 by western blotting in a time dependent manner with paclitaxel treatment.|PMC7732973|We recently described a significant reduction in PARP1 protein levels in vitro and in vivo in patients treated with standard carboplatinum-paclitaxel chemotherapy, raising the question whether the sequence of treatment used today with chemotherapy followed by PARPi is optimal.|PMC6327434|The rationale of this study was triggered based on our previous findings that reported a dramatic reduction of the target of PARPi, the intratumoral PARP1 protein levels in HGSOC tumors obtained in patients after exposure to chemotherapy with platinum and paclitaxel.|PMC6327434|Recently, a study defined the resistance mechanism of paclitaxel and olaparib (inhibitor of PARP1) in resistant ovarian cancer cells that was reversible with the MDR1 inhibitors, verapamil and elacridar.|PMC8208690|The 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ALA/SFC induces autophagy via activation of MAPK/Nrf-2/HO-1 signaling pathway to protect cardiomyocytes from hypoxia-induced apoptosis.|PMID:27693692|Our present study also demonstrates H-ALA or ALA mediated PDT in H460 cells are closely related to the activation of p38 MAPK and JNK signalling pathway.|PMID:21864799|Furthermore, ALA-PDT can activate the MAPK pathway, and promote the expression of p38, JNK, and ERK.|PMID:29131243|Our present study also demonstrates H-ALA or ALA mediated PDT in H460 cells are closely related to the activation of p38 MAPK and JNK signalling 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(target)"],"value_type_id":"EDAM:data_0006","original_attribute_name":"hetio_source"}]},"92694617":{"subject":"PUBCHEM.COMPOUND:56603655","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"To review clinical data on the sequential use of the non-selective vascular endothelial growth factor (VEGF) inhibitors (ranibizumab and bevacizumab) and the selective VEGF inhibitor (pegaptanib) in the treatment of neovascular age related macular degeneration (n-AMD).|PMID:22283373|There are many other drugs that may play a role in DR therapy in coming few years such as somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|A number of drugs may play a role in DR therapy in the coming few years; eg, somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|Nowadays, VEGF-inhibitors like bevacizumab, ranibizumab, pegaptanib, are the first choice in therapies for the treatment of neovascular ocular diseases.|PMC6249906|In this way, the effect of VEGF inhibitors (pegaptanib, bevacizumab, ranibizumab) on primary cultures of human REC and CEC was evaluated by Stewart et al.. Significant differences between retinal and choroidal microvascular cells were observed, which highlights the need for specific treatment interventions in RNV or 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celecoxib has a greater inhibitory capacity than the rest of CL sample, the rhizome extract from MR-1 present only 36% less inhibition than celecoxib at the same concentration (3 µg/mL).|PMC7785433|In the same cells, the steady-state level of Mmr1, Vac17 and Inp2 was reduced.|PMC6506691","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"77549217":{"subject":"UMLS:C4529301","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Bevacizumab in combination with 5-FU resulted in a greater antifibrotic effect compared with monotherapy with 5-FU or bevacizumab alone, as evidenced by the attenuation in fibronectin and mature collagen I expression and deposition (P < 0.05).|PMID:19797222|In the bevacizumab (BVZ), 5-fluorouracil (5-Fu) + BVZ, and mitomycin C (MMC) + BVZ groups, the mRNA expression 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increased the mRNA of genes involved in the acute phase response (hemeoxygenase-1 and metallothionein-1), ER stress (C/Ebp-homologous protein and Growth arrest and DNA-damage-inducible protein), inflammatory cytokine (interleukin 1 beta), chemokines (macrophage inflammatory protein 2 and mouse keratinocyte-derived chemokine), as well as apoptosis (early growth response factor and BCL2-associated X protein) in livers of Nrf2-null and wild-type mice, but these genes increased less in mice with more 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cells into Th1-like cell lines and clones, but also the development of their cytolytic potential.|PMID:1401925|After treatment, the control group showed the lowest serum IL-12 and IL-4 levels compared with the MMR- and PPD-treated groups with statistically significant difference in between.|PMID:25847793|In vitro restimulation of splenocytes from MTB infected mice with PPD led to increase in IFN-γ levels and decrease in IL-4 levels resulting into higher IFNγ/IL-4 ratio which indicates the presence of Th1 polarized cells in G1-4A treated splenocytes.|PMC4858241|The depressive effect of IL-4 on the development of PPD-specific T cell lines with both Th1 cytokine profile and cytolytic potential was dependent on early addition of IL-4 in bulk 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with sildenafil demonstrated increased VEGF and Ang-1 mRNA after early reperfusion.|PMC3828881|In this regard, we have recently reported that exposure to sildenafil significantly accelerates tuborogenesis in HCAEC on matrigel along with the activation of VEGF/Ang-1 system.|PMC3828881|The cells exposed to sildenafil (1-20 microM) demonstrated significantly accelerated tubular morphogenesis with the induction of thioredoxin-1 (Trx-1), hemeoxygenase-1 (HO-1) and VEGF.|PMID:16716755|The sildenafil-treated group exhibited 10- and 2.6-fold increase in VEGF expression as compared to their corresponding controls, following 2 and 4 days of reperfusion respectively (Fig. 6C).|PMC3828881|Increased expression of VEGF (1.9-, 2- and 4-fold) and Ang-1 (5-, 11- and 23-fold) mRNA was observed ontreatment with sildenafil 8, 12 and 24 hrs after reperfusion as compared to the control (Fig. 4A and 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same study also found marked increases of Bcl-2, an apoptosis suppressor, and vascular endothelial growth factor (VEGF), an angiogenesis modulator linked to accelerated tumor progression and increased invasiveness, in malignant prostate tissues.|PMC3599181|Moreover, increased levels of hepatocyte growth factor (HGF) and VEGF were observed in the same group.|PMC5403966|Additionally, we revealed that the VEGF expression level in muscle on the operated side in the HMGB1-treated group was significantly higher compared with the non-operated side in the same group 4 days after EMS, while the expression level of VEGF in the cortex showed no difference on both sides between the two groups.|PMC6882763|VEGF-A expression was also significantly increased in the same set of tumors versus adjacent uninvolved pancreatic tissues from the same individuals.|PMC5340089|In contrast, VEGF expression was upregulated after treatment with the same combination compared with treatment with β-GP and ascorbic 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acid induces dendritic spine loss by MAPK/ERK signaling and dysregulation of autophagic flux|PMC7579125|Propionic acid induces dendritic spine loss by MAPK/ERK signaling and dysregulation of autophagic flux 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of MAPK phosphorylation, which reflects activation of intracellular signaling pathways downstream of the VEGF receptors, showed that all three agents completely blocked MAPK phosphorylation when the VEGF inhibitors were pre-incubated with VEGF-A overnight, before addition to the cells, while VEGF Trap was more potent than either ranibizumab or bevacizumab when preincubated with VEGF-A for shorter time periods (5 and 30 min).|PMC3338918","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.964473","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"97139078":{"subject":"PUBCHEM.COMPOUND:7814","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"As shown in Fig. 3C, the protein levels are consistent with the results of quantitative real-time PCR; the bcl-2 expression level was significantly higher in the PPD-MPT64 group than that in the PPD group.|PMC4085073|As shown in Fig. 3C, the protein levels are consistent with the results of quantitative real-time PCR; the bcl-2 expression level was significantly higher in the PPD-MPT64 group than that in the PPD group.|PMC4085073|PPD-B-stimulated LTA and IL-8 could potentially differentiate M. bovis-infected cattle from HC, and PPD-B-stimulated BCL2 and CHI3L1 have the potential power in differentiating bTB PCR-P cattle from bTB PCR-N cattle.|PMC7266948|The mRNA-expression level of BCL2 induced by PPD-B was significantly higher in bTB PCR-P cattle than in bTB PCR-N and HC cattle (Figure 4C), with an AUC value of 0.9100 (Figure 4G).|PMC7266948|These data suggest that PPD can downregulate ERα expression and upregulate PRα expression, and further induce a high level of autophagy and high ratio of pro-apoptosis molecules (Bax/Bak) to anti-apoptosis molecules (Bcl-2/Bcl-XL) in eESCs in 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H2-blocker, ebrotidine, also known for its gastroprotective effects, reduced the indomethacin-induced lesions by 90.2%, epithelial cell apoptosis decreased by 61% and ET-1 showed a 58.2% decline, while IL-4 increased by 30.6% and that of cNOS showed a 3.1-fold 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literature has suggested that nicotine down-regulates the expression of growth factors like VEGF, PDGF, TGF-β1 and TGF-β2 but has a less significant effect on inflammatory markers like TNF, IL-6 and IL-12.|PMC6411046|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Theiss et al. demonstrated that the expression of collagen type I and II genes, bone morphogenetic protein (BMP), BMP-2, BMP-4, BMP-6, basal fibroblast growth factor (FGF), and the vascular endothelial growth factor (VEGF) was decreased by a systemic nicotine administration in rabbits through a posterolateral spine fusion with the autogenous bone graft.|PMC8038608|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Plasma vascular endothelial growth factor (VEGF) levels and lung VEGF mRNA expression decreased with advancing age, and nicotine exposure insignificantly decreased plasma VEGF levels and lung VEGF mRNA expression, compared with the control rats during the study period.|PMID:22245234","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3563266","PMID:18472096","PMC6411046","PMID:11839560","PMC8038608","PMC5466671","PMC3432052","PMID:17369603","PMID:22245234"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9955639083333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"24349273":{"subject":"NCBIGene:5595","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:20648624"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In 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in mind the healing properties of AM we investigated the efficacy of AMT in persistent epithelial defect (PED) on the corneal graft.|PMID:21305721|We would like to appreciate the authors on comparing and evaluating the clinical outcomes of tarsorrhaphy and amniotic membrane transplant (AMT) in the healing of persistent epithelial defects (PED) and subsequent corneal vascularization, if any, thereby providing symptomatic relief.|PMC7574137|To review the uses and previously proposed mechanisms of action of amniotic membrane transplantation (AMT) and to suggest a new mechanism of action for the effectiveness of AMT in resolving a persistent epithelial defect (PED).|PMID:11973378|Three of them needed AMT for PED treatment.|PMC7158933|After treatment for persistent corneal epithelial defect (PED) by amniotic membrane transplantation (AMT) or tarsorrhaphy, the conventional treatment was 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promoted apoptosis, inhibited cell proliferation concomitant with upregulation of p27, and reduction in the expression of FGFR2-4, p-FRS-2, p-ERK1/2, p-p70S6K/4EBP1, Cdc25C, survivin, p-Cdc2, and p-Rb.|PMC7764786|In addition, we showed that bevacizumab inhibits the differentiation of retinoblastoma cells by blockade of extracellular signal-regulated kinase (ERK) 1/2 activation.|PMC3310877|Herein, we demonstrated that bevacizumab as an anti-VEGF antibody could inhibit differentiation of retinoblastoma cells without affection to cellular viability, which would be mediated via blockade of extracellular signal-regulated kinase (ERK) 1/2 activation.|PMC3310877|Interestingly, phosphorylated Erk was only significantly reduced upon bevacizumab treatment.|PMID:19859900|Bevacizumab blocks the binding site for VEGF-A on the cell surface, thereby inhibiting the tyrosineprotein kinase CSK and its downstream effectors, including Raf-1 and MAP kinase-1 that mediate proliferation, migration, invasion 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of enhanced Glut-1 expression on the cell surface and of decreased mitochondrial membrane potential by Met treatment might support the change of metabolic profile from oxidative phosphorylation to glycolysis.|PMC5704053|In the present study, the abundance levels of SLC2A1 (GLUT1), SLC2A4 (GLUT4) and SLC2A3 (GLUT3) in the placenta were higher in the 25% Met-Met group than those in the 35% Met group, suggesting a higher glucose supply for fetal development in the 25% Met-Met group.|PMC6165284|We speculate that MET could increase 18F-FDG accumulation by upregulating GLUT1 expression but not PKM2 expression.|PMC5709992|In the present study, the abundance levels of SLC2A1 (GLUT1), SLC2A4 (GLUT4) and SLC2A3 (GLUT3) in the placenta were higher in the 25% Met-Met group than those in the 35% Met group, suggesting a higher glucose supply for fetal development in the 25% Met-Met group.|PMC6165284|In the present study, the abundance levels of SLC2A1 (GLUT1), SLC2A4 (GLUT4) and SLC2A3 (GLUT3) in the placenta were higher in the 25% Met-Met group than those in the 35% Met group, suggesting a higher glucose supply for fetal development in the 25% Met-Met 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addition, ticagrelor significantly decreased the ulcer-stimulated expression levels of EGF, VEGF, phosphorylated extracellular signal-regulated kinase (ERK), phosphorylated P38 mitogen-activated protein kinase and nuclear factor-κB P65 at the ulcer margin (P<0.05).|PMID:29042978|Furthermore, the possible mechanisms underlying the effect of ticagrelor were associated with its functions of attenuating the expression levels of VEGF and EGF, as well as suppressing the phosphorylation activation of ERK1/2, P38 and nuclear factor-κB P65.|PMID:29042978|Ticagrelor blocked the activation of phosphatidylinositol 3-kinase (PI3K) and extracellular signal-regulated kinase 1/2 (ERK1/2) in ADPβS-treated DCs.|PMID:29958560|Ticagrelor blocked the activation of phosphatidylinositol 3-kinase (PI3K) and extracellular signal-regulated kinase 1/2 (ERK1/2) in ADPβS-treated DCs.|PMID:29958560","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:15ed1b8e9af4b8ad2c06d625238d268767e7808572215c7eabbe4a0bd3339a48","tmkp:46bb22c0fe46736f429719ed33a42ed84921136aa606f92a86a4142da8ead040","tmkp:ca0d99c6f31ebb1a2e09de9f5e20dc681c3aa331bc65261f231919f959450759","tmkp:545426d0d646e8b83720da31d1ef718e176cdba270bd6c24be7d16a7e4e6f52c","tmkp:115aa7d2ede7519f73f1cd5a2ee0a07bdd731ee4985933c8323fbf1aa8617749","tmkp:f1596384053958ee800657e30376ad89f30c9709efcbeb29f934b918e9c9ceef","tmkp:b861ca633030b0cba90c65b690e5e281292bfbfbe70e70e72052d21d7481e97d","tmkp:4f7dfa17fb127af92966782acf6a859a6a4f38c5bf2a8da87b5689f4b9e7f222","tmkp:f460da0b7d41a43c7bdcdc5adbaec218f83a9ea3f859b9e4b6feb77c61896e67"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"47371299":{"subject":"PUBCHEM.COMPOUND:3440","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7662760","PMC7662760","PMC7662760"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9997027333333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Furthermore, our previous study already demonstrated that furosemide, which prevents the ADSHE onset of S284L-TG, inhibits MAPK/Erk signaling.|PMC7662760|Our previous study, using S284L-TG, demonstrated that, before ADSHE onset, chronic administration of furosemide prevents ADSHE onset via the upregulation of the K+/2Cl- cotransporter (KCC); however, another line of vitro studies also demonstrated that furosemide inhibits mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (Erk) signaling.|PMC7662760|Our previous study, using S284L-TG, demonstrated that, before ADSHE onset, chronic administration of furosemide prevents ADSHE onset via the upregulation of the K+/2Cl- cotransporter (KCC); however, another line of vitro studies also demonstrated that furosemide inhibits mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (Erk) 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number of apoptotic cells increased and MR-1 mRNA and protein levels decreased with increasing doses of either paclitaxel or carboplatin, strongly indicating that these anti-cancer drugs exert their therapeutic effects by antagonizing the effects of MR-1.|PMC3132198|MR-1 expression decreased in a dose-dependent manner at both the mRNA and protein levels following treatment with paclitaxel or 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vivo microdialysis revealed that microinjection of either tPA or plasmin into the nucleus accumbens (NAc) significantly potentiated whereas plasminogen activator inhibitor-1 reduced the nicotine-induced dopamine release in the NAc in a dose-dependent manner.|PMID:17122062|In vivo microdialysis revealed that microinjection of either tPA or plasmin into the NAc significantly potentiated whereas plasminogen activator inhibitor-1 reduced the nicotine-induced dopamine release in the NAc in a dose-dependent manner.|PMID:18646640|Microinjection of PAI-1 into the NAc dose-dependently reduced morphine-induced dopamine release and hyperlocomotion.|PMID:15948318","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"107374022":{"subject":"PUBCHEM.COMPOUND:5284371","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Codeine-induced gonado-spermotoxicity was associated with a reduction of circulatory testosterone, suppression of testicular HER2, Ki67, and Bcl-2 expression, down-regulation of oestrogen signaling, and upregulation of testicular caspase 3 activities and p53 signaling 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we determined the PED phenotype of both Tap 1 knockout mouse embryos and control mouse embryos.|PMID:10708239","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"124162259":{"subject":"PUBCHEM.COMPOUND:10297","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Prolonged administration of AMG100 mg/kg and AMG200 mg/kg resulted in a significant decrease in caspase-3 levels [one-way ANOVA: F(5,25) = 0.936; p = 0.474] and Bax [one-way ANOVA: F(5,25) = 0.611; p = 0.692] levels and increased Bcl-2 levels [one-way ANOVA: F(5,25) = 0.833; p = 0.538] 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in particular, has been shown to have anti-inflammatory effects through the inhibition of MAPK signaling factors (ERK1/2, JNK and p38MAPK) and, consequently, to inhibit the secretion of inflammatory cytokines IL-1β and IL-6, MCP-1 and TNF-α in 3T3-L1 adipocytes and macrophages.|PMC8158719|Quercetin induces apoptosis by inhibiting different signaling pathways including the MAPK/Erk, PI3K/Akt, and NF-κB signaling pathways; it also inhibits the migration and invasion of CRC cells via regulating the toll-like receptor 4/NF-κB signaling pathway.|PMC7431655|In addition, the treatment of LPS- stimulated RAW 264.7 macrophages with quercetin has been shown to inhibit the activation of phosphorylated ERK MAP kinase and p38 MAP kinase but not JNK MAP kinase.|PMC2768691|As the ability of quercetin to inhibit several serine-threonine kinases including phosphatidylinositol 3-kinase and mitogen-activated protein kinase ERK kinase-1, we can postulate that the molecule could participate in Mcl-1 mRNA 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contrast, in Ins-1EPED/PEA-15 PLD-1 inhibition by propranolol reduced the anti-apoptotic action of PED/PEA-15 in presence of hydrogen peroxide (Fig. 6a, 6b).|PMC4260953|Pretreatment of Ins-1E with propranolol, a well known inhibitor of PLD-1 pathway, abolishes PED/PEA-15 ability to block hydrogen peroxide-induced 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addition, the expression levels of the EMT-related proteins fibronectin and vimentin were also decreased after sorafenib therapy (Figure 1).|PMC5122390|Sorafenib upregulated the epithelial marker E-cadherin and downregulated the mesenchymal markers vimentin and fibronectin (Figure 5F).|PMC4621898|Our results indicated that sorafenib treatment significantly reduced the expression of OPA1 as well as Mfn1 and Mfn2 in xenograft HCC tumors (Figure 7c).|PMC3860369|Compared to those in the control group, the levels of mitochondrial fusion-related proteins, such as Mfn1 and Opa1, were marginally downregulated in the sorafenib-treated group (Fig. 5a–f), and this effect was exaggerated by IL-2.|PMC6234789|Congruent with microarray results, fibronectin protein levels were decreased in HSC, after a 24-hour treatment with sorafenib (Figure 4A).|PMC3145033","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996444126666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:39a19373162fa389b92f04b3d875f3637b5c6e79f1e084566dbfee097a30cea2","tmkp:211804a97868f7f0ffe135c00c06c7bc815f9e125a4e933b2c60c163591a0819","tmkp:0bdb3c04b3230f0fbc317cd65364bd8bbd0de1be565ae32ded846d436d8b3232","tmkp:2ad74afe4103dda1cda31da703cc07a70f2345b999943d13dae2376200d70555","tmkp:7c974ea7fc38947cfed7a57cfe54b5440bdc4458c0fe4e6d83749ef0f2cd20ca"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"6708777":{"subject":"UMLS:C4529301","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:26066903","PMC6320227","PMC7973261","PMC4402130","PMC3151740","PMC7963216","PMC4189677","PMC4200479","PMC3058319","PMC4573901"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e046804080aa45f486df0cb026a5c3c40292a94f5a353df6475829ac62ae1653","tmkp:f603e04966a785c91d0269d05341c35bf8b101ebaf09465cc19ee3efd9df1871","tmkp:93db8af41e08c949a19bb67d0891f0eb4e174794481d50c95b489ae0ccede7a8","tmkp:168c6cb2374c4491b23c02f39e9611b8e97cae044bf8ef488ffbfa93b8691995","tmkp:0ba0177d860d822a5fa9e26b219a94bb190ddcb6008631197b1a0ce7bfd45d55","tmkp:26107cc3cca51f67bf8175d45c81ac33944035a78999f42c5aa130d0bae382c9","tmkp:4b47d6c2a9a21eaf0cbe461a8c122bccaf05b14586cd19a045a50a4be1c8ddc1","tmkp:755f70c942f697e6aaa80d9065f2d957109b684baf33742f8c3e1ed8e835d8bc","tmkp:4c786df6752a9e0948512cf815119bb5aef87fdf5ee086dececec10d67420be2","tmkp:f1012c339e175a806ccb0e3356e0c67b838aff63745eafa7c7b8a62bcfc65374"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9942675758563535","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In this experiment, intermittent treatment with bevacizumab induced less OA progression, as shown by both histological and gene expression assays, through increases in the gene expression of ChM-1 and VEGF in the articular cartilage and decreases in the gene expression of MMP 13 and ADAMTS5 in the synovium.|PMC4189677|Unexpectedly, this clinical trial definitively disproved our hypothesis that continued VEGF suppression would occur with the sequential combination of these two agents, as VEGF levels continued to rise with subsequent and continued treatment with sunitinib and bevacizumab.|PMC4200479|Similar increases in plasma VEGF concentration have been observed following treatment with bevacizumab.|PMC4402130|Plasma levels of VEGF, P1GF, and sVEGFR2 significantly and persistently increased after bevacizumab and chemotherapy treatment (at days 15 and 43; VEGF and P1GF also were increased at day 71 and end of study), although plasma bFGF was transiently increased only at day 15; plasma sVEGFRl, IL-lb, IL-6, IL-8, TNF-α, and urinary MMP activity did not significantly change at any of these time points (Table 3 and Supplementary Tables S3 and S4).|PMC3151740|Gordon et al. reported that the intravenous injection of bevacizumab led to an increase in serum total VEGF in clinical trials while free VEGF concentration was reduced.|PMC3058319","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"124062256":{"subject":"PUBCHEM.COMPOUND:2157","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Some of the reported P-gp inducers comprise (listed alphabetically):Abacavir, Actinomycin D, Aflatoxin B1, Aldosterone, Ambrisentan, Amiodarone, amprenavir, m-amsacrine, apigenin, artemisinin, asiatic acid, atazanavir, atorvastatin, avermectin, beclomethasone, benzo(a)pyrene, benzo(e)pyrene, berberine, betamethasone, bilirubin, bosentan, bromocriptine, budesonide, caffeine, cadmium chloride, capsaicin, carbamazepine, catechin, celiprolol, cembratriene, R-cetirizine, CITCO, chlorambucil, cholate, chrysin, ciclesonide, cisplatin, clotrimazole, colchicine, corticosterone, curcuma extracts (extracts of Curcuma longa, Curcuma zedoaria and Curcuma aromatica), curcumin, cyanidin, cyclophosphamide, cyclosporine A, cytarabine, daidzein daunorubicin, daurunavir, depsipeptide (FR901228, FK228, NSC630176), desvenlafaxine, dexamethasone, diclofenac, digoxin, dihydroxylated xanthones (e.g., 1,2-dihydroxy-9H-xanthen-9-one (X2)), 1α,25-dihydroxyvitamin D3, diltiazem, dimethylformamide, 6,16α-dimethylpregnenolone, dimethylsulfoxide, docetaxel, doxorubicin, doxycycline, efavirenz, emetined, epigallocatechin-3-gallate, epirubicin, eriodictyol, erythromycin, β-estradiol, ethinylestradiol, etoposide, fenbufen, flavone, 5-fluorouracil, flutamide, fluticasone, genistein, ginkgolides a and b, hydroxyurea, hyperforin, hypericin, Hypericum perforatum extracts (Saint John’s wort), idarubicin, ifosfamide, indinavir, indomethacin, insulin, isosafrole, isoxanthohumol, ivermectin, lopinavir, LY191401, mangiferin, meloxicam, mepirizole, methotrexate, methylprednisolone, midazolam, mifepristone, mitoxantrone, morphine, mx2, myricetin, naringenin, nefazodone, nelfinavir, nevirapine, nicardipine, nifedipine, nimesulide, norathyriol, oleocanthal, ouabain, oxycodone, paclitaxel, parthenolide, pentylenetetrazole, phenobarbital, phenothiazine, phenytoin, phorbol 12-myristate 13-acetate, piperine, platelet-|PMC6153761","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6153761","PMID:21512308","PMID:28962527"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9265469","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d654c3c498aa013d38059714959ab7f32cbe2532db91e95b208e4b4f14f3e288","tmkp:b8b93596353e45fe94feabe5c263be3ce8da5fefd46eda4af9472b431653beb4","tmkp:228df05229577773321b3874ea9c1cb6165704787af83410fbb79c23e52d0c07","tmkp:4520c772f73d57d1fbba8cfe6f583e7c216652e9f145d63f1b00c83e00ce5393"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"113720698":{"subject":"PUBCHEM.COMPOUND:5280343","object":"NCBIGene:207","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"decreased"}],"attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop","infores:drugcentral"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:chembl","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"IC50","value_type_id":"EDAM:data_0006","original_attribute_name":"affinityParameter"},{"attribute_type_id":"biolink:Attribute","value":5.27,"value_type_id":"EDAM:data_0006","original_attribute_name":"affinity"}]},"28215645":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6240058"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"MMC attenuates these effects after debridement injury by increasing serpine1 gene and protein expression preserving L1CAM on axon surfaces of reinnervating sensory nerves.|PMC6240058","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:89026373955d65fb340d00d78698102a6470155982d3244754c6543095ac822e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9991491","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"50142848":{"subject":"PUBCHEM.COMPOUND:5280343","object":"NCBIGene:355","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Additionally, quercetin treatment also increased the expression of Fas ligand (FasL, a pro-apoptotic factor that activates Fas receptor-mediated apoptosis) 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the 131I-His-IN group the vascular endothelial growth factor (VEGF) decreased gradually compared to other groups.|PMC3627608|Histidine improved the transfection efficiency of PEGylated PLL/siRNA nanocomplexes for silencing endogenous vascular endothelial growth factor (VEGF) expression.|PMC7435460|In the 131I-His-IN group the vascular endothelial growth factor (VEGF) decreased gradually compared to other groups.|PMC3627608|His serum level of VEGF decreased to 68 pg/mL when the planned primary treatment was completed.|PMID:31748497|Histidine improved the transfection efficiency of PEGylated PLL/siRNA nanocomplexes for silencing endogenous vascular endothelial growth factor (VEGF) expression.|PMC7435460","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"55546583":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"One study showed significant decreases in IL-2, IL-4 and IFN-γ production from anti-CD3 activated human T-cells at lower dopamine levels (5–25 nM).|PMC3488577|Dopamine or the D2-like receptor agonist, bromocriptine, inhibits lymphocyte proliferation, decreases the antigen-induced macrophage activation and the secretion of IL-2, IL-4, and IFNγ.|PMC6342207|Another study by Ghosh et al. showed that 3-5 ng/mL of dopamine added to human pan T-lymphocytes, activated with anti-CD3 antibody, showed significantly reduced proliferation and secretion of IL-2, IFN-γ, and IL-4.|PMC6679768|Dopamine inhibits the release of interleukin-2 (IL-2), interferon (IFN)γ and IL-4, and the lipopolysaccharide-stimulated production of IL-12 p40, but stimulates the production of the anti-inflammatory IL-10 in immune cells.|PMC6342207|Dopamine inhibited proliferation and the expression of IL-2, IFN-γ and IL-4 in T cells treated with anti-CD3, a method of Treg activation in vitro.|PMC4303241","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6679768","PMC6261559","PMC3488577","PMC6342207","PMC4303241"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9978518099999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f6522d2abb982555615e47c5cfcba31e638a19c688a0d920f4ec723ab298f12d","tmkp:e1b3346a51482a8562a32826cbc59a3fd8f3d692792534c8412edfa030c38634","tmkp:4ac2d75207da84d5d4a8e2c102a82850d33f63d51752541f303a12b4d86debb6","tmkp:d10c61accf4a8cf7acb454b87621d53ac01d451aedb992f71277e048a3b8a59c","tmkp:d9843f7a27adc7827d4931f10b3675a2b2ddb55f66dd475cfec54965b4fefc68","tmkp:b7b5ecdc2461a10c8a3eae035a254437f0d4e44e878fde86bc1d1ac1414e7751","tmkp:03a3539e48080af308618f0b90d0107d831551afd539dc9829e137dc8a883564"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"59607996":{"subject":"PUBCHEM.COMPOUND:5280934","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:26952131","PMC7178006","PMID:29663489","PMC4125699","PMC6271012","PMC4438966","PMC7923095","PMID:22739213","PMID:18096126","PMC6274312"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9983111521739131","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4deb89be0ea80d6982fc25bf5deead03bd2704ddf8cea2351c642b591c4f1570","tmkp:21bbc7701a02c728299b6c06e3edbf784abb262c4f21c89d749e41aa12e1e6a4","tmkp:d7ee5f83a0161fbb092257dbe67d2ce446fa18a120513a862e0c345fb0045493","tmkp:45635912709c23af47a21149b3caf913c2f422d2f1c5530a2a10262f190c3c63","tmkp:9d3afdc6025dce81854fa9bd59af2111601581a44db27ce4e8cfbe6ac7554909","tmkp:897e06adcf61e32003f39f9eb1c5f9aee6db460be4b401fa383a5b922051d418","tmkp:d645046f124d5ccece40d1cfd021d798b5663d530fe3b4bf1161b347430f9da8","tmkp:7d38ee7c7308d09e98f13b60ca21374d2d3f9a3459ebd87bee692f8796c4fea7","tmkp:dd83296a956eaa2314ffbda78d6e073566d8c92b76709833063e35aecb7725e0","tmkp:3438ebd489300f1a4fc099cccb9ba57fe4d8eddd828c6bd7886d5dcfe543001c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Rats that received ALA demonstrated significantly enhanced Sca-1 mRNA expression compared with the irradiated group (Figure 6A,C).|PMC7178006|This study has reported that caspase-3 and -9, HIF-1alpha, Bcl2, Cox2 and the phosphorylated AKT were enhanced upon PDT with ALA.|PMC4125699|Immunohistochemical staining and western blotting demonstrated upregulation of Bax, cytochrome c and caspase-3, and downregulation of Bcl-2 for both in vivo and in vitro cases after ALA-LIU treatment.|PMID:22739213|Induction of apoptosis in K562/ADM cells by γ-linolenic acid involves lipid peroxidation and activation of caspase-3 |PMC6274312|(b) Western blot analysis of the knock down of ABCG2 and FECH by RNAi in HeLa cells, (c) fluorescence microscope analysis of mitochondria, and (d) ALA-mediated PpIX accumulation with photoirradiation leading to the activation of caspase-3 and caspase-9 like activity, which induces apoptosis.|PMC7923095","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"121451318":{"subject":"CHEMBL.COMPOUND:CHEMBL292268","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:2ac5f64586414328d6ba721d7e54563cf00e98fe03db49b76ce94a820fe01706","tmkp:39b1ddbe9402abd7e2d97f78f4d2f89721d19694984555e43015d03f9246d7ca","tmkp:0b6dbd324dbb289f8728653c14e73f7576b5e3436167f825f5a495b63128e7b4","tmkp:36d1cfeacbac63ef532edb908deac5d7861897344d89557c15beac047f88fa5e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, low-dose MDA treatment for 48 h on ARPE-19 cells was demonstrated to induce VEGF expression and modifications in autophagic activity, whereas the MDA-induced VEGF increase was reduced by 3-methyladenine and ammonium chloride, an autophagy and a lysosomal inhibitor, respectively; therefore, the authors speculated that MDA might act on VEGF secretion through the autophagy–lysosomal pathway.|PMC8145578|The finding that the hypoxia-mediated secretion of soluble factors like VEGF, FGF2, IGF-1, and HGF is sensitive to PI3K inhibitor 3-methyladenine (3-MA) in mBMSCs, apparently, supports the concept that a hypoxia-responsive AKT/PKB-mTOR-EIF4EBP1 pathway participates in the translation of cytokines/growth factors.|PMC6800910","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC8145578","PMC5730625","PMC6800910","PMID:27138352"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.989232075","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"45073927":{"subject":"NCBIGene:1891","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Further, we present the first case of ECH1-associated PED with initial symptomatic improvement with a mitochondrial cocktail.|PMID:28039521","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.98727393","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:28039521"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:6a53b2042e9f7c058fc1371efd4a03a33e7a9477a1224202f9e1322573fee9aa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"38673271":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:5594","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"increases 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while bevacizumab treatment reduced the expression of Cyclin D1, GLUT-1 and MCT-1, TH reverted such effects, thus showing that VEGF-A is not the only TH-target gene in tumor promotion, and that VEGF-A is part of pro-tumorigenic cascade in the TH-dependent tumorigenic action.|PMC8199095|Expression of HK2, VEGF, PDK1, CA9, and GLUT1 are expressed as fold-change mRNA expression relative to levels observed after bevacizumab alone for each patient |PMC7670584","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3472924","PMC6918655","PMID:24700751","PMC8199095","PMC7670584"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"12272064":{"subject":"PUBCHEM.COMPOUND:2157","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7502042","PMC7072462","PMC4626804"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In accordance with declining ER stress, we found decreased caspase-3/-7 activation in amiodarone-treated hepatocytes.|PMC7502042|Indeed, autophagy was induced in HepG2 cells and most strongly pronounced at 8 h of amiodarone treatment, paralleled by decreased ER-stress and caspase-3 activation.|PMC7502042|However, both Caspase-3 cleavage and Caspase-8 cleavage were slightly lower in amiodarone-treated PHx mice compared with 0 h-treated PHx mice (Fig. 5C).|PMC4626804","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99965209","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:6ee89f252e8c0e609b800a2878ed57df103090859be4209101b0110c5e4bfc44","tmkp:15a81e923b619240955b6516517d026a41de3e0d291b126eb5886ac443cb82df","tmkp:dddd438d54548447ae989cf29b9fa447fad9d729aee09ad0936eb91519515c8e","tmkp:fe40c167660ab2e00c4ade8b43123bbc11806bc392060b379a4c9d9fcf9da8c5","tmkp:048924da22bdf777aa6f0555792b150818135b01a62683b30ac954cc40a91d2e","tmkp:327bd3b9a3438b9afa80559a76dca5ede3d16551a1c411f29083bde8ec8101d7","tmkp:f14edb55a8c6c9375ed62f782477d734061eba406fcbcfff1defb13adaf7ed58","tmkp:f46813a7020be9299f4480c1e9b3c74cb4b0fb6d7bcb16a9321c5d1d278cf77a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"92321303":{"subject":"PUBCHEM.COMPOUND:443894","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Upregulation of NAD(P)H oxidase p22(phox), p47(phox), and gp91(phox), EMT markers such as transforming growth factor-β1, vimentin, and fibronectin expression, and Rho-kinase and ERK1/2 phosphorylation in DS rats were significantly suppressed by tolvaptan.|PMID:23676370","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:813c8b24c3b370b1741dd68839091da7554d39730721359a19490d00afcd5217"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9982054","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:23676370"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"125143565":{"subject":"PUBCHEM.COMPOUND:5282412","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9470459","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The patient had polypoidal vessels in the vicinity of the site superior to the fovea, and PED was observed using fluorescein (Fig.?2a) and using indocyanine green (Fig.?2b).|PMC3777170","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8a755b81a554f6122d7518b818868b1b8cdea8e417ffd5e6cf0df87177bf3a68"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC3777170"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"48099127":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"AMD3100 administration resulted in a significantly reduced hyaline cartilage volume (day 14), callus volume (day 42) and mineralized bone volume (day 42) and reduced expression of genes associated with endochondral ossification including collagen Type 1 alpha 1, collagen Type 2 alpha 1, vascular endothelial growth factor, Annexin A5, nitric oxide synthase 2, and mechanistic target of rapamycin.|PMC3704138|Furthermore, immunohistochemistry results revealed that expression levels of vascular endothelial growth factor, CXC chemokine ligand 12, CD68, CD3, and tumor necrosis factor α in the lesion area were significantly lower in treated (topotecan or AMD3100) brains versus control brains, while ionized calcium-binding adapter molecule 1 (Iba1) and HIF-1α expression was similar, though somewhat reduced.|PMID:29485043|In the AMD group, mean +/- standard deviation(SD) aqueous VEGF levels decreased from 68.0 +/- 32.1 pg/ml at baseline to 26.3 +/- 19.0 pg/ml after the first injection (p = 0.028) and to 25.2 +/- 12.8 pg/ml after the second injection (p = 0.005).|PMID:19997926|At the protein level, generally the flavonoids and methyldopa decreased the level of VEGF, and the administration of methyldopa with quercetin also showed a strong inhibitory effect in relation to the action of methyldopa alone.|PMC7956652|Until now, the main focus of drug target development for AMD was the inhibition of VEGF, due to its key role in 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and high dose adrenaline infusions yielding plasma adrenaline levels of 0.9 +/- 0.1 and 3.4 +/- 0.4 nmol/l, respectively, dose-dependently increased t-PA levels with a concomitant decrease in PAI-1 levels.|PMID:2119530|Our investigation revealed that exposure of cardiomyocytes to epinephrine in an in vitro environment can up-regulate the expression of angiopoietin-2 gene (+2.1 times), and down-regulate the gene expression of neuregulin 1 (−3.7 times), plasminogen activator inhibitor-1 (−2.4 times) and SPARC-related modular calcium-binding protein-2 (−4.5 times).|PMC5044710|Importantly, epinephrine dose dependently inhibited PAI-1 parameters, an effect that was reproduced by isoproterenol.|PMID:10566656|It has been reported that an epinephrine or an isoproterenol infusion, but not an NE infusion, increases plasma tPA levels and activity in a dose-dependent manner and decreases plasma PAI-1 activity without changing its plasma concentration.|PMC4933351|Metoprolol treatment did not influence the resting levels of the fibrinolytic variables studied, but tended to enhance the t-PA response to CWT and further reduce PAI-1 during adrenaline infusion.|PMID:2119530","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"30819231":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"• VEGFR-2 mRNA and protein concentrations and urinary VEGF concentrations were increased in bladders of rats instilled with MMC.|PMID:20735383|It is nteresting to note that expression of angiogenic genes HGF, bFGF, and VEGF was induced at 24 h after Mitomycin C treatment.|PMC6150649|We have previously shown that VEGF111b expression is induced in SKOV3 cells after 100 μg/ml mitomycin C treatment, and VEGF111b protein was detected by our homemade VEGF111b polyclonal antibody.|PMC4480579|Our data showed that the number of fibroblast, capillary density and fibrotic tissue in the 0.5 and 0.7mg/ml MMC groups was significantly lower than the control, 0.1 and 0.3mg/ml MMC groups; while the expression of VEGF in control and 0.1mg/ml MMC groups was notably higher than 0.3, 0.5 and 0.7mg/ml MMC groups.|PMID:22056834|After culturing for 24 h, the VEGF levels in RPE cells in the BVZ and BVZ + 5-Fu groups were significantly lower than that in the control group, while the VEGF levels in the 5-Fu and MMC groups significantly increased (Figure 2).|PMC6151201","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9974846736363637","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6925728","PMC6863018","PMC6151201","PMC6885197","PMID:20735383","PMC5444031","PMID:22056834","PMC7474357","PMC4480579","PMC6150649"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c881d1831337bebb7fea7890930252d583ba003991dbcb04f5d3a1fbfb60cde0","tmkp:189c49045749fc01a9adc2019bc155cc07656a737f2554c32d1f856827001ee9","tmkp:af30270eeeccc5598e3a50da47f5d892be4ced85e785c9fa8d7c44accd8e70f7","tmkp:061de446371cf21fd72a361147c873d56d4aae31adb9243d5824ce3ccf15700e","tmkp:a624f7f6f081eeae1467afc53eb94408b815f6df552f65d38d83af4f4050b2fa","tmkp:8b0f861d7380626b49ff3cea2faa69e1d681ea20f19804432d2abaab4ad44f2d","tmkp:def9e313a2a503e2356d0e58187a37353c45eaaf7a6cbb1bfcb8154ec08609ce","tmkp:384501099be90a3e8ab1e3bb1dc55a752010ff022a7061d92abac00fde9fd87b","tmkp:030ec7217bfbd18b4c09d3231b2c48d5709fbcee121943c60a5ea19270fa8e4c","tmkp:badb5c5f4e8d94dc6ab99ef761c64b470803e0f69379d18e4ebfdd3745a63635"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"25878881":{"subject":"PUBCHEM.COMPOUND:5988","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:833145754b7d9a6771bc99915f06ea0e855e230fed8152924d6fac6a1c76c8a4","tmkp:f745df54e1a33effec25f8e3e8aba6a33fd446213441bb8313270efb4c63a343","tmkp:db99762468ef9c5ad2b27ca46fd1e5f44ee6751ca371990a05dad2851a3f37aa","tmkp:98be247e28b4d203a6b50db19f854f06f0c66af9adb3cf19a7fd07cf88666019","tmkp:43952d33536498bb4daf8df997700d3a7c4fde6e622395a812fc79887ade0330","tmkp:14869a191521e12c5dc6e448b1672cdfe3b008e73cae47b7df1dfe6c9658f54b","tmkp:4b48bcb285e7a6e2dcf543fb9203e1c8415e59dfd9afa07b0d5a453d6f327cc8","tmkp:b7891e3a3568a2e2d3363ec89491cbc5f6d2a8d9b469749b7912f2f116efd4e7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6461046","PMID:15993383","PMID:30340815","PMC4390809","PMC7594708","PMC5355302","PMC2933813"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Increases in VEGF expression and secretion were also observed after the addition of 100 mM sucrose to the medium (Figure 1C,D).|PMC4390809|The high NaCl- and sucrose-induced VEGF gene expression showed different time dependencies (Figure 1A,C), suggesting that both hyperosmolarity and alteration of the transmembrane NaCl gradient induce VEGF gene transcription.|PMC4390809|SD rats fed a high fat/sucrose diet showed increases in serum insulin and VEGF (both p < 0.01).|PMID:15993383|RLYE significantly attenuated VEGF-induced sucrose permeability in endothelial cell monolayers (Figure 8A).|PMC5355302|Consumption of a high sucrose diet has been reported to increase left ventricle weight and expression of markers of cardiac function (VEGF, BNP and TGF-β1) in the left ventricle .|PMC6461046","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.998844242","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"16270244":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Human umbilical vein endothelial cells (HUVECs) treated with AS water extract activate VEGF gene expression and the p38 pathway, thereby increasing angiogenic effects of HUVECs both in vitro and in vivo .|PMC3170324|Peach seed water extract up-regulated VEGF and VEGF receptor 2 after ICH in a mouse model and inhibited glucose deprivation injury in PC12 cells.|PMC6288198|For example, hippocampal VEGF levels are increased with water maze training, and administration of VEGFR-2 inhibitors directly into the hippocampus following spatial training impairs long-term memory.|PMC3951730|A previous study using a chronic model of Pseudomonas infection of the lung in rats had shown that L-arginine given in drinking water resulted in lower IL-1β concentrations in BAL fluid in the L-arginine treated compared to the untreated group, whereas VEGF was increased.|PMC3940779|Treatment with doxycycline in drinking water will drive an increase in the expression of VEGF that results in severe vascular leakage and exudative retinal detachment within 4–5 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PC-12 cells, U0126, Clozapine, and N-desmethylclozapine all attenuated the phosphorylation of ERK1 (p44), and Clozapine attenuated the phosphorylation of ERK2 (p42).|PMC2881214|This activation of both ERK1 (p44) and ERK2 (p42) was attenuated by pre-treatment with DETC and both concentrations of Clozapine.|PMC2881214|In cultured cortical neurons, the neuregulin-stimulated phosphorylation of Erk1, Erk2, and Akt was similarly inhibited by clozapine [F(4, 10) = 8.909, P = 0.002 for Erk1; F(4, 10) = 8.47, P = 0.003 for Erk2; F(4, 10) = 318.8,|PMC6675791","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9995089300000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3735488","PMC2759290","PMC6675791","PMC3936900","PMC2881214","PMID:19277491","PMC4153869"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"80510527":{"subject":"PUBCHEM.COMPOUND:3345","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:46617604249ab8db9fe36ab2f10474ebca8996b6137778c620bdf1dd84785a05","tmkp:fd22af311389df3ddf5c1209ae741ba08fb731028d3a896014baf67be9470e01"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:8542487","PMID:8542487"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"To evaluate the safety and to describe the use of combination IV diazepam and fentanyl in the pediatric emergency department (PED) as outpatient conscious sedation (CS) for orthopedic procedures.|PMID:8542487|At the doses given in the study, the use of combination diazepam and fentanyl for outpatient CS of PED patients during orthopedic procedures was not associated with serious 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flavonoids, diazepam inhibited the release of vascular endothelial growth factor (VEGF) and granulocyte-macrophage-colony stimulating factor (GM-CSF) into supernatants of cultured in the SNU-C4 and MDA-MB-231 cells.|PMID:18239283|Like flavonoids, diazepam inhibited the release of vascular endothelial growth factor (VEGF) and granulocyte-macrophage-colony stimulating factor (GM-CSF) into supernatants of cultured in the SNU-C4 and MDA-MB-231 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the observed reduced tumor destructive effect of MTX/MNPs in comparison to MNPs is not fully explainable, protein analyses suggested a more unfavorable expression pattern (eg, elevated p-ERK1/2, BCL-2, VEGF, and MMP2) after MTX/MNP treatment, resulting in a progression of cell cycle as indicated, for example, by cyclin A.|PMC5388224|We found a slight upregulation of VEGF-R1 in the MTX/MNP group, indicating the insufficiency of this treatment to impair VEGF-R1 expression and inhibit tumor growth.|PMC5388224|LDE-MTX increased the expression of myocardial vascular endothelium growth factor (VEGF) associated with adenosine release; this correlated not only with an increase in angiogenesis, but also with other parameters improved by LDE-MTX, suggesting that VEGF increase played an important role in the beneficial effects of LDE-MTX.|PMID:28553113|Presence of ultrasound subclinical synovitis and increment of serum vascular endothelial growth factor in a patient with rheumatoid arthritis achieved in sustained clinical remission by treatment with adalimumab and methotrexate.|PMID:24533548|LDE-MTX increased the expression of myocardial vascular endothelium growth factor (VEGF) associated with adenosine release; this correlated not only with an increase in angiogenesis, but also with other parameters improved by LDE-MTX, suggesting that VEGF increase played an important role in the beneficial effects of 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another study that was examined the effect of sevoflurane on glioma stem cells (GSCs) and the mechanisms of action in vitro, expression of VEGF and HIFs were up-regulated by sevoflurane.|PMC7825752|Notably, following the inhibition of the VEGFR pathway, there was significantly decreased cell proliferation in the cells treated with axitinib plus sevoflurane than with sevoflurane alone (Fig. 4C and D), implying that sevoflurane promotes the proliferation of HUVECs via activation of the VEGF/VEGFR pathway.|PMC6966126|Levels of CD133, VEGF, HIF-1α, HIF-2α, and p-Akt were up-regulated by sevoflurane in a time- and concentration-dependent manner.|PMID:25492570|Medan values of serum VEGF-C is significantly increased from 806 pg/mL to 1385 pg/mL (P = 0.01) in sevoflurane group while postoperative levels of serum VEGF-C remain same in patients who received propofol and paravertebral block.|PMC8092146|As shown in Fig. 2a and Supplementary Fig. 3, we found that sevoflurane increased pro-inflammatory cytokines known to facilitate mammary tumor metastasis, such as IL-6, interleukin-12, vascular endothelial growth factor (VEGF), stromal cell-derived factor 1 (SDF-1 α), TARC (CCL17), chemokine ligand 1 (I-309/CCL1), and pro-matrix metallopeptidase 9 (Pro-MMP9) in comparison to reference 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expression of Bcl-2 was upregulated when treated with 20 mM ethanol and this effect was diminished with the treatment of SL0101 or Cariporide.|PMC5106393|In the current study, there was a decline in autophagy as reflected by decreased LC3 flux and decreased Beclin and Atg 7 levels coupled to increased expression of P62 and Bcl-2 (Fig 5A,5B) after acute alcohol administration.|PMC3432162|In contrary to our expectation, the expression of BCL2, as an anti-apoptotic marker, was also higher in the alcohol group.|PMC8196229|Some studies found that ethanol has an influence on renal damage, such as apoptosis and epithelial mesenchymal transdifferentiation. Nesreen and Sayed discovered that alcohol consumption significantly increased renal caspase3, caspase8, and caspase9 activity, and ethanol toxicity can increase the ratios of Bax and Bcl-2 in kidney tissues compared to a control group.|PMC6767945|Rats undergoing MCAO-induced transient ischemia followed by reperfusion, had significantly decreased pro-apoptotic protein levels such as Bax, caspase 3, and apoptosis inducing factor (AIF) after administration of 1.5 g/kg ethanol, and the ethanol treatment enhanced anti-apoptotic Bcl-xL and Bcl-2 protein 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antiproliferative effects of NPT, bevacizumab, and sunitinib correlate with increased phospho-stathmin and cleaved PARP-1 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with cigarette smoke-exposed asthma group, the number of airway inflammation cells decreased in the BALF, and the expressions of ET-2, JNK1/2, MDA and GSH decreased in the lung tissues of the dexamethasone treated group, bosentan treated group, and dexamethasone-bosentan treated group.|PMID:28871941|Compared with cigarette smoke-exposed asthma group, the number of airway inflammation cells decreased in the BALF, and the expressions of ET-2, JNK1/2, MDA and GSH decreased in the lung tissues of the dexamethasone treated group, bosentan treated group, and dexamethasone-bosentan treated group.|PMID:28871941|After treatment with dexamethasone/bosentan, the expression of IL-17, JNK1/2, MDA, and GSH decreased compared to the smoking group; airway inflammation and the staining intensity in the lung tissue were also reduced.|PMID:31629215","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"12625436":{"subject":"PUBCHEM.COMPOUND:34755","object":"MONDO:0011724","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"A later study by the same group followed up patients with GLUT1 deficiency syndrome between 18 and 41 years old.|PMC8173065","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9989479","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d44e8b48ed1cd780d6144eb1c6b08a0ff6311d1e2a347de33ae2cef3ca5bf078"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8173065"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"96641258":{"subject":"PUBCHEM.COMPOUND:3821","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Seven days (on P14) after injection of NMDA, the length of fibronectin associated with blood vessels was shorter, but that in the retinal parenchyma was longer compared with the vehicle-treated eyes (Figure 5F).|PMC6801463","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995437","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:edb9182269f930aef80878e7d7c620db5f93b66a00615cb5da8169f8b2467c4d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6801463"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"109446111":{"subject":"PUBCHEM.COMPOUND:3821","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5356012","PMC6612444","PMC6008657","PMC2633690","PMC4908499","PMC2527681","PMID:7556603","PMC5306336","PMID:26688567"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Ketamine sedation was shown to reduce glucose clearance, insulin secretion and counter regulatory hormonal production in a NHP model (Lehmann et al.,) and 2% isoflurane altered glucose uptake in the brain in a rodent model (Nasrallah et al.,).|PMC5306336|1994); (2) the ketamine/xylazine combination (Ket/Xyl) increases BG and inhibits insulin secretion (Goldfine and Arieff 1979; Pomplun et al.|PMC4908499|The results showed that high glucose together with NMDA induced a more obvious reduction in both GSIS and insulin gene expression compared to β-cells treated with NMDA or glucose alone (Fig. 4a,b).|PMC5356012|In addition, NMDA reduced glucose-stimulated insulin secretion (GSIS).|PMID:26688567|Moreover, in the STZ-induced animals, treatment of hippocampal slices with insulin resulted in a significant decrease in the number of NMDA receptors that consequently affected LTP and decreased postsynaptic densities (van der Heide et 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this experiment, intermittent treatment with bevacizumab induced less OA progression, as shown by both histological and gene expression assays, through increases in the gene expression of ChM-1 and VEGF in the articular cartilage and decreases in the gene expression of MMP 13 and ADAMTS5 in the synovium.|PMC4189677|Unexpectedly, this clinical trial definitively disproved our hypothesis that continued VEGF suppression would occur with the sequential combination of these two agents, as VEGF levels continued to rise with subsequent and continued treatment with sunitinib and bevacizumab.|PMC4200479|Similar increases in plasma VEGF concentration have been observed following treatment with bevacizumab.|PMC4402130|Plasma levels of VEGF, P1GF, and sVEGFR2 significantly and persistently increased after bevacizumab and chemotherapy treatment (at days 15 and 43; VEGF and P1GF also were increased at day 71 and end of study), although plasma bFGF was transiently increased only at day 15; plasma sVEGFRl, IL-lb, IL-6, IL-8, TNF-α, and urinary MMP activity did not significantly change at any of these time points (Table 3 and Supplementary Tables S3 and S4).|PMC3151740|Gordon et al. reported that the intravenous injection of bevacizumab led to an increase in serum total VEGF in clinical trials while free VEGF concentration was reduced.|PMC3058319","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"70817843":{"subject":"PUBCHEM.COMPOUND:174","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Similar to our studies using PEG in primary cultures of neonatal rat cardiac myocytes exposed to hypoxia and reoxygenation, PEG treatment again led to the upregulation of myocardial prosurvival signaling as measured by the phosphorylation of Akt, ERK1/2, GSK-3β, and eNOS indicative of increased activity of these signaling pathways.|PMC4459731|Cell survival signaling was upregulated after H-R with PEG, as demonstrated by increased phosphorylation of Akt, GSK-3β, and ERK1/2.|PMID:21335476|VEM delivered in star-PEG-PPS hydrogel led to increased phosphorylation of extracellular signal-regulated kinase (p-Erk) and cell proliferation (ki-67 positive) compared to VEM delivered in DMSO and controls (Figure 4d, e, and Supplementary Figure S6).|PMC6082662|We confirm Aldo-PEG activates phosphorylation of ERK1/2 in rat cardiomyocyte H9c2 cells similar to Aldo and G protein-coupled receptor 30 (GPR30 or GPER) agonist G1.|PMID:26121234|Cumulatively, these data indicate: 1) that both PEG-Scl2-2 and PEG-Scl2-3 hydrogels supported increased osteogenesis relative to PEG-Scl2-1, perhaps due to the increased JNK and ERK1/2 signaling associated with both Scl2-2 and Scl2-3, and 2) that PEG-Scl2-2 constructs supported increased osteogenic lineage progression relative to PEG-Scl2-3 gels.|PMC7147932","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:26121234","PMC7654221","PMC4459731","PMID:23768781","PMC6082662","PMID:21335476","PMC5472176","PMC7147932"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0b620163c1f55a9e1e68e699ed88f7e1594424d0452b73f2baa19bfc6db2c430","tmkp:af3e667161ed6e6708de4c6fe2890add4702aa7e590bdc0bc356705afef65e34","tmkp:8bd7f20cab3fee00be9691a6b5fc39c0f14decfc7caf0b8f5854eea47a843148","tmkp:77385d598f3a3ab05446fbd2cbd3fe7ec6eec9ae904a02fd0df14c0769b90724","tmkp:480f77d9160fa2420968b6eb2b1e53996736e835c19ab2e354601d080e6ddc75","tmkp:5aa981643a9c6567f300febd993672c4f1e902b9d25f9a0ad897f2445aa5351d","tmkp:c5186f50657372ee7b652aac213bf81755c7939bdc4a185fe21cd64ead00794c","tmkp:0639d2d690b1fbba26193866a92622e98dcc893f856724e0b70f1a3937179466","tmkp:2770afaeb1c516bf47f5a3beaa49bbd114202fff3606a21db2faa9e8d30f0e57"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9967445039999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"119833229":{"subject":"PUBCHEM.COMPOUND:5280934","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9976424659493671","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:54a19a6db0070f7de427a512c2b7bd72c5946bc8f514df10ac76363482a88f45","tmkp:2f9e836c834c847544507c8c9a5f0e45a4c23a1445cb66a700f48f3ac9007614","tmkp:ea77c5c969edd6fc09babecbb16dd5463e0f9ef40b2f2a1f6ba850978ba1d01a","tmkp:ef966e54a3700e667786363e7b9d94e37f21153dfabfb43c26908fff14442a8c","tmkp:b5b2282ed36477862d3a8909f319e1e3d9b23444020992fb9baf222506d1f67b","tmkp:2e079dedd4a1f11baad5c7a7091ea28a4b4a5baf0bf187c15e8d1f822589de90","tmkp:5ca591913e6b72d13a80cbdb473eb3250c6c44622de15ad6c33fff8598b9e595","tmkp:5cd28383a5135ecfcf18f7d221cbfd2246d9f1eaf61b6b4a4e3d60ce5a8529ad","tmkp:af240676fe1158421f5320c196d687302283714096369004427c04754bf10a78","tmkp:cce543899743734cf88109571e49f6bb9abca444161386e8dd85555b408188d4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC7646523","PMC6471297","PMC4951144","PMID:28965129","PMC7564314","PMC3238166","PMID:23343676","PMID:8690147","PMC4358912","PMID:11334419"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"These adaptive responses after chronic ALA administration were also associated with significantly lower (15-17%) plasma levels of insulin and free fatty acids.|PMID:8690147|In contrast, in the X/Ala group, there was a decrease of both second-phase insulin secretion (533 +/- 58 to 427 +/- 48 pmol/min, P = 0.02 vs. Pro/Pro) and in the response to arginine (from 7,518 +/- 1,306 to 6,458 +/- 1,040 pmol/min, P = 0.014 vs. Pro/Pro).|PMID:11334419|In contrast, within eWAT, ALA supplementation attenuated insulin signalling, decreased mitochondrial respiration and increased the fraction of electron leak to reactive oxygen species (ROS).|PMID:28965129|As shown in Table 1, dietary ALA significantly decreased serum insulin and leptin concentration of WT mice, while increased serum adiponectin concentration.|PMC4358912|Meanwhile, ALA significantly reduced the fasting glucose (FG) (Fig. 1I) and fasting insulin (INS) (Fig. 1J) levels, resulting in improved insulin resistance (IR), as suggested by the lower homeostasis model assessment of insulin resistance (HOMA-IR) index (Fig. 1K).|PMC7646523","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"53776119":{"subject":"UMLS:C2740799","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The development of PB inhibitors represents a major advance in the field given that most of clinical grade RAF inhibitors to date elicit ERK1/2 hyperactivation in vitro and the formation of cuSCC/KA in 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data from compound 2 are more complex, it appears that his compound acts both on the tumor and cells of the vasculature to decrease RTK and MAPK signaling.|PMC2825747|L-Histidine and sodium azide had an inhibitory effect on UVA activation of p38 MAPK, pointing to a role of singlet oxygen in transduction of the UVA effect.|PMID:12945585|Morin and his colleagues discovered that, in a monocrotaline-induced pulmonary hypertension model, pulmonary artery remodeling might be improved via downregulation of the activity of p38 MAPK and the expression of MMP-9.|PMC5023842|Chiu and his group further observed that RITA mediates Stat3 and Erk suppression, which can be activated in apoptosis caused by 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of DDR by inhibiting ATM or ATR in MMC-treated macrophages dampened substantially the increase in CD9, ALIX and RAB10, RAC2 and RAC1 protein levels (Fig. 5i and Supplementary Fig. 5C).|PMC6940362|In line with Er1F/- sera or the EV fraction of Er1F/− macrophage media (Fig. 5f–h, Supplementary Fig. 5A), we find a substantial enrichment for EV-associated protein markers CD9 and Alix and an accumulation of Ras GTPases RAB10, RAC2 and RAC1 in the EV fraction isolated from the media of MMC-treated cells compared to those of untreated cells 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PED and nAMD after anti-VEGF therapy, especially in association with complete PED 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Prevents Cell Apoptosis by Inhibiting MMP-9 Expression and c-Jun N-Terminal Kinase (JNK) Phosphorylation|PMC5343851|Similarly, RNA-sequencing and proteomics analysis were performed in prenatally VPA-exposed male juvenile rats, and showed reduced expression of genes such as CDK1 and MAPK8 , which are related to pathways such as neural development and cellular growth.|PMC6221834|It was found a decreased on JNK1 in the hippocampus of rats submitted to the d-AMPH and treated with Li or VPA (Fig. 3A).|PMC6525279|We observed that the expression of jnk1, creb1 and c-jun was inhibited by 73, 87, and 77% in dn-wnt2bb fish at 7 dpa, whereas this expression was enhanced by 51, 43, and 24%, respectively, in wnt2bb-overexpressing hearts (Figures 4A–C,E–G,I–K,M).|PMC7261892|It can also be observed that VPA also reduced JNK1/2 phosphorylation in the hippocampus of rats pretreated with 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3 weeks of oral prednisone therapy, an area of RPE elevation is apparent with discontinuity at the temporal edge, adjacent to the highest area of pigment epithelial detachment (PED), as well as overlying subretinal fluid.|PMC6071675","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"16134333":{"subject":"PUBCHEM.COMPOUND:3121","object":"NCBIGene:22803","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3757384"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"It has also been reported that histone deacetylase inhibitor (HDACi)-treated tumor cells, including trichostatin A (TSA) and valproic acid, are capable of presenting antigens via the MHC class II pathway and also of enhancing the expression of molecules (TAP1, TAP2, LMP2, LMP7, Tapasin and MHC class I) involved in antigen processing and presentation via the MHC class I in melanoma 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NOB-PEG-PCL repressed the RANKL-induced MAPK signaling pathway to finally inhibit the OC differentiation of BMMs.|PMC6769031|Furthermore, CBSA-PEG-TIIA-NPs significantly decreased the mRNA expressions of iNOS and p38MAPK, upregulated PPARγ expression, and inhibited the protein levels of iNOS, GFAP and p38MAPK phosphorylation.|PMID:23111336|PEG 35 reduces p38-MAPK activation whereas it has no effect on JNK and ERK phosphorylation.|PMC4620277|Cells cultured on the heparin functionalized PEG hydrogels exhibited a decrease in mitogen-activated protein kinase (MAPK) activation, a critical protein activated in the bFGF signaling pathway, as compared to cells cultured on PEG hydrogels crosslinked in the absence of photo-crosslinkable heparin.|PMC3307527|Cells cultured on heparin-modified PEG hydrogels showed decreased activation of mitogen-activated protein kinase (MAPK), a protein that is part of the FGF-2 signaling cascade, when compared to cells cultured on PEG hydrogels lacking 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groups.|PMID:25539628","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:28962331","PMID:25539628","PMC6981094"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9992945","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"76223186":{"subject":"PUBCHEM.COMPOUND:6274","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Similar findings reported by Fouad and his colleagues in 2017 showing a marked increase in caspase-3 protein levels and Bax/Bcl-2 ratio in rat testis treated with 10 mg/kg cisplatin, in addition, our research team reported before marked expressions of caspase-3 and Bax in rat kidney treated with 6 mg/kg cisplatin.|PMC6052634|Similar increases in T cell numbers were also observed in HIS mice that received the hIL-7 lentivector, and this correlated with higher expression of 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our recent study, the VPA-mediated neuroprotection after ONC was accompanied by decreased caspase-3 activity, cyclic adenosine monophosphate (cAMP) response element binding protein (CREB) induction, and phosphorylated extracellular signal-regulated kinase (pERK) 1/2 activation but not by altered histone acetylation, as shown in western blots.|PMC3036563|VPA decreased EGFr (total and activated), ERK1, ERK2, pERK and pP70S6k.|PMC4549030|However, in the hippocampus, the groups Sal + VPA, d-AMPH + Sal and d-AMPH + VPA showed a decrease in the content of ERK1 phosphorylation.|PMC6525279|VPA-treatment decreases the activation of Akt and ERK1/2 in both HeLa and SiHa cells in a time-dependent manner.|PMID:26942921|The present result indicated that the expressions of reelin and its down-stream molecules, PI3K, p-Akt, and p-ERK1/2, were decreased in the VPA-treated group compared to the control group 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of catecholamine synthesis via activation of p44/42 MAPK in cultured bovine adrenal medullary cells by milnacipran.|PMID:17211600|Furthermore, incubation of cells with milnacipran (30-100 ng/ml) for 5 min activated p44/42 MAPK, whereas paroxetine and fluvoxamine did 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Ranibizumab was injected at 3 and 7 days after OGI (P3d = 0.0268, P7d < 0.0001) (Figure 5(d)), and PAI-1 level was significantly decreased when Ranibizumab was injected at 0.5 hours and 3 days after OGI (P0.5h = 0.0089, P3d = 0.0025) (Figure 5(e)).|PMC8064804|Both Ranibizumab and Conbercept showed better effect on reducing PAI-1 levels at 3 days treatment time point (PAI-1RBZ = 6.57|PMC8064804|In contrast to Ranibizumab, Conbercept significantly decreased VEGF level only when injected at 7 days after OGI (P = 0.0107) (Figure 5(b)) and decreased the levels of PDGF, TGF-β, and PAI-1 in vitreous significantly when injected at 3 days (PPDGF = 0.0015, PTGF-β = 0.0266, and PPAI-1 = 0.0011) and 7 days after OGI (PPDGF < 0.0001, PTGF-β < 0.0001, and PPAI-1 = 0.0298) (Figures 5(c)–5(e)).|PMC8064804","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9996730899999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0055170b460b5fcb2768deefc06746db9eea110de46bb081bca7a6a25d7ee413","tmkp:e15c85e764a640a99044da7da01f12574cece8d90dc65cf1af97997c71531a96","tmkp:779f9a9f1ff986764da4d2be9526db398d1b6158b122a487d9343c9910c9c7aa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"86735361":{"subject":"NCBIGene:6513","object":"MONDO:0000188","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:16581179","PMID:24847886","PMC7072975","PMID:25022942"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d973889a06da6f347c51b3f6a57022f73270df0f55cde44a1037322d33b99782","tmkp:ba50dce0b5625b5860479d72568138eb079a6455cf662b17eeb381c254a7da5f","tmkp:ec757ae10753af664a40ae5880e62994aefbde5b1ca4ec7aa10ca15784789724","tmkp:0698fe441752e08d898eda4b572e1b2278e7515325fb4a75853e4a793d1bda2e","tmkp:131745803b44438375eeacaffe1e3994c3021bad834d1455759847997866506a","tmkp:6b1c6fdc55a37e51a339ef7afad3d41a8f9d81a4f4769df7f583630777bffda2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9830961","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Thus, loss of GLUT-1 in endothelial cells of the brain is directly linked to brain damage and related to several diseases, including GLUT-1 deficiency syndrome and Alzheimer’s disease.|PMC7072975","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"31405606":{"subject":"PUBCHEM.COMPOUND:1775","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"We also observed a significant inhibition of ERK1/2 phosphorylation by phenytoin and TTX treatment (Fig. 5) consistent with an involvement in VGSC-mediated invasion of pII cells.|PMC4734602|Blocking the Na+ current by phenytoin results in the downregulation of EGF expression and EGF-induced ERK1/2 phosphorylation, reducing the activity of MMP7, cathepsin E, and kallikrein-10, among which phenytoin showed the greatest inhibitory effect on cathepsin E. It has been proven that higher cathepsin E levels in the serum are positively correlated with poorer clinical prognosis in breast cancer patients, thus, phenytoin might serve as an effective drug for improving therapeutic efficiency and survival of patients.|PMC7393602|Phenytoin-induced suppression of MMPs/TIMPs gene expression and reduced α2β1 integrin-mediated collagen endocytosis in gingival fibroblasts through MAPK (ERK1/2) and NF-κB signaling pathways finally leads to accumulation of extracellular 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same treatment also decreased the expression of the glucose transporter (Glut1), which is under HIF control and usually upregulated in cells exhibiting high glycolysis.|PMC5737722|On the other hand, while some members of the flavonoid family were reported to stimulate the expression of Slc2A4 gene and glucose transport, other phytochemicals of the same family were identified as inhibitors of glucose transport mediated by GLUT1 and/or GLUT4.|PMC8073144|The expression of GLUT-1 mRNA was also decreased in the same X-ray dose between before and after X-ray radiation.|PMC3753417|Extending the kifunensine treatment of HK2/ES-FUCCI cells to a full two weeks showed little change in cell cycle distribution (Figure 5D), suggesting that cells had reached cell cycle homeostasis within the same 72-hour window required to stably decrease GLUT1 levels.|PMC7282979|Substantial reductions were also seen in Glut 1 protein and mRNA per fat cell in the same rats (62% and 76%, respectively; P less than 0.05).|PMID:1855475","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8215783","PMC3753417","PMID:25227787","PMC8073144","PMC4977274","PMC5511613","PMC5737722","PMC7282979","PMID:1855475","PMID:8749801"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"7113385":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9916397811333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:da9d109cf29c70d838c6731cb18f42b44ce9ec8088aaf13beb23936337366a08","tmkp:3cc07438b3a10606f743fbc25d8aebe7abb42c9501d65562792d6ed901d3b145","tmkp:46d2334ceec766a2ce3d530f7d484053dec50ec61775c5956862f4cbfe635db8","tmkp:32c02cfc0509baddc2f3df5896e34377c4a8cfa380c7828901bbd6d23c224450","tmkp:224054cd30e30af6aa744b400c9703a16ab7e9c635c9c003f4d60a628d974813","tmkp:4c91c0842690889496e9f5aa80dbe137d823239ba4e961d05b34c654fda4c5e5","tmkp:edb91b81078870052d6918d9c962690128f4a8333bb4653aa91392aa9356257f","tmkp:da7a50ea62b40ee710e85fe9e6457cb67d2206178c8a0eb5d4c115889f7fb41f","tmkp:ddbca16f4d1f08157a7452b4090afde6381d0cc1e8995d9331db9b5ba2ac77a1","tmkp:4e824d95385e9651814403c978265643b4a88a99c5c05a3747cd9e18cd182bc6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC8004757","PMC4102640","PMC8062590","PMC3543504","PMC5512002","PMC4414159","PMC5891198","PMID:27581120","PMC3130102","PMC7114495"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, the ratio of phospho-ERK1 and phospho-JNK of IPEC-J2 cells significantly increased at the same time post-infection.|PMC7114495|An increase in phosphorylated Erk (pErk) was observed at the same UVB dosages associated with decreased differentiation markers.|PMC4102640|We have shown here that the same samples caused a notable increase in the expression of p-ERK1/2 with once again a distinct variation from sample to sample.|PMC8004757|At the same time, expression of CD44s and p‐ERK1/2 also was up‐regulated in TGF‐β‐treated cells (Figure 8A).|PMC5891198|Whereas the same treatment showed increasement of Erk phosphorylation (p-Erk1/2-T202/Y204) through western blot analysis.|PMC4414159","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"32180836":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99965525","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7927a5878c6664a94ce77af3ae8628c06d8b3c60380a1962cc49f408b0a0ef7e","tmkp:f4bebecde95a59cf3eece96b9cc206c511d15b7eda18ab2d79183f135dd1ee98","tmkp:6d2dd80e81ee9626c6f5cc5190ef65fec7b1c8209be1929a005be340189bc200","tmkp:a93307a6ea5be52c00e6d1e98cd3edeafa4b975d08070ead480d552e3b7d310e","tmkp:aa3a48f4f522095cab89ae25361a82b1b35fac3ce672020c7c71ffeb0cc58ee3","tmkp:753cd3621f7db067348b202d02669d3efc507ec3b364dd82f1c56173326f218a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC4449530","PMC2935680","PMID:21926424","PMC2860679"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Intra-plantar 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same study also found marked increases of Bcl-2, an apoptosis suppressor, and vascular endothelial growth factor (VEGF), an angiogenesis modulator linked to accelerated tumor progression and increased invasiveness, in malignant prostate tissues.|PMC3599181|Moreover, increased levels of hepatocyte growth factor (HGF) and VEGF were observed in the same group.|PMC5403966|Additionally, we revealed that the VEGF expression level in muscle on the operated side in the HMGB1-treated group was significantly higher compared with the non-operated side in the same group 4 days after EMS, while the expression level of VEGF in the cortex showed no difference on both sides between the two groups.|PMC6882763|In contrast, VEGF expression was upregulated after treatment with the same combination compared with treatment with β-GP and ascorbic acid only.|PMC2193567|Our study found that expression of CCN1 and VEGF was increased to the same level in ischemic retina of OIR, thus verifying that CCN1 and VEGF can participate in the pathological process of ROP.|PMC4425238","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3599181","PMC6479528","PMC7810204","PMC4025968","PMC2193389","PMC2193567","PMC4425238","PMC5403966","PMC6882763","PMC2978798"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9913872485964913","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"81283468":{"subject":"PUBCHEM.COMPOUND:6047","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9969592933333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"whereas resistance exercise or levodopa treatment reduced cleaved caspase-3 expression in PD rats.|PMC8103184|However, when levodopa/carbidopa (50/12.5 mg/kg) was combined with cabergoline (0.25 mg/kg), the effect reduced levodopa's enhancement of caspase-3, -8, and -9 activities in the 6-OHDA-lesioned mouse brain.|PMID:15596235|However, cleaved caspase-3, a death-related protein, increased in nPC12 cells treated with 200 μM L-DOPA but decreased significantly in cells treated with 200 μM L-DOPA and 5 μM EPO.|PMID:21683736","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:37a7f02ac168be6114ea7f3060e843af385c8dc25a3292e6d15a996e88e1c1c7","tmkp:c5541a30bd10a9903ec4c8697e211307b1827c72a64cd8ad83e7011f57b22dfb","tmkp:af2e86f12e75de2b8397aa9a72e25af67b2d0cffaefa6f253769bead9f52b5fe","tmkp:9f8fdda51b70365bef8cb28e0ed8c8a1d76b95af947f4f912f9ffffa47a42317","tmkp:e81b0a58be5df0c66ec988a8250887d25c1ef19a33f3caae7433398852d8ef88","tmkp:9ba3fba8b40ba4307d59decbf8cb170120ba82d2a79817e4b9b1887eec8a0164","tmkp:80dd62ace8ab60bf2107578936b39d4b19ed7a75c9dab05d692c0dfc4909b1e4","tmkp:96f3ff1f97c9019d84ecca6ba5ca9acfc2c8fe5f8d2a17bd093fbaec785408c5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8103184","PMID:21683736","PMC4143606","PMID:15033810","PMID:18387727","PMC3509089","PMID:15596235"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"96126155":{"subject":"PUBCHEM.COMPOUND:5073","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9944566266666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5616375","PMC8236946","PMC3410627"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ceab466839940d1f3e479eefff59cf34d49a024eb4fc657b56f727411922dca1","tmkp:4a8c97f3353c346d54fcfb0fffdb73ad3e0d45545f2e766e71f073003754d640","tmkp:ee5f2bee975d49ebe4bff336d61ad69febcb17ef132db5fcc083998d2352b70d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Phosphorylations of ERK1/2, MEK1/2, and p90RSK after the injection of risperidone 2mg/kg were increased in some sample according to time-course.|PMC5616375|Moreover, treatment of WT mice with neuroleptics (haloperidol, clozapine, and risperidone), used to treat SZ, increased the PKA-mediated Ser221 phosphorylation of STEP via DARPP-32/PP1 pathway, along with increased phosphorylation of GluN2B, Pyk2, and ERK1/2, and surface expression of GluN2B.|PMC8236946|The atypical antipsychotics, clozapine and risperidone, similarly increased STEP61 phosphorylation (P<0.05 and P<0.005, respectively; Figure 4c), as well as the tyrosine phosphorylation of Pyk2 and ERK1/2 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study has further displayed clopidogrel improved adenylyl cyclase-mediated signaling including increased Akt- and eNOS-phosphorylation contributing to improved NO-mediated vasorelaxation and EPC mobilization.|PMC3479044","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7666529","PMC3479044"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"14226034":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"A new water soluble MAPK activator exerts antitumor activity in melanoma cells resistant to the BRAF inhibitor vemurafenib.|PMID:25795251|A new water soluble MAPK activator exerts antitumor activity in melanoma cells resistant to the BRAF inhibitor vemurafenib|PMC6204874|A new water soluble MAPK activator exerts antitumor activity in melanoma cells resistant to the BRAF inhibitor vemurafenib|PMC5133127|A new water soluble MAPK activator exerts antitumor activity in melanoma cells resistant to the BRAF inhibitor vemurafenib|PMC5362503|A new water soluble MAPK activator exerts antitumor activity in melanoma cells resistant to the BRAF inhibitor 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presented in Fig. 3, the protein and mRNA expression levels of fibronectin and type IV collagen were significantly increased in MMCs treated with HG compared with the control cells; betaine treatment decreased the levels of fibronectin and type IV collagen in MMCs in a dose-dependent 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intracellular signaling.|PMC3091851|When NGF was withdrawn, treatment of SCG neurons with 10µM Nicotine with and without nAChR antagonists resulted in significant differences in ERK1 and ERK2 expressions [F (3, 12) =9.6227 (*p<0.002)]|PMC6312731","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9006f79f05ef640905f6a49836f2ede2ed9f8badf51d12468333bf0d56aebd39","tmkp:b544909e1655e3a502e0528018b095d076b9baf5f0dd8c080a73ff8c319cbdba","tmkp:0934e302c756c2a79e184796784e7f33903dced7f11ad9cb06d0653638adbc1b","tmkp:f2c9b1418da9c8b7edca4adffc426d2c116e5fd17f57711dd04fafe890ca25ee","tmkp:f9fb0fcba3d0cafcbc5d0cc2330f473b94f35edbf84f50d041c897e083879ece","tmkp:d3a9afe1a4819cb85c7343d87f6648839a2103bd628c9e78ea76cb72f9052000","tmkp:646d081a2ccce1a67d9fe2c66a39dae59f275b0cbb2e68a67f4f60264df7d41b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:12421819","PMC3091851","PMC6312731","PMC3915512","PMC4769750","PMC4054617"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"69826821":{"subject":"PUBCHEM.COMPOUND:4943","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9993926","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:26921778","PMC6141459"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ca7ca246768c0551e7849c3854c64282b7ef0466a20b4c8df78e505d35f64237","tmkp:fc793e7a81abcbf4a77ae3fbca9c1e630d1b77a40bee39ef7087011449e48a74","tmkp:4d040a076a291750cb6a000ac85105b84b1c14c6123a381a1b375c81e565eaad","tmkp:3b54b1b3e855b7eaa39ef43e40368666aae3d6496d28dfb3b5333da04156c1f0"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Taken together, it appears that propofol protected MNNG or OGD/reoxygenation-induced cell death, which is associated with parthanatos, involving PARP-1 activation, PAR formation, and AIF translocation to nuclei.|PMC6141459","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"67774348":{"subject":"PUBCHEM.COMPOUND:4649","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999697366","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b3ac625c3cd14506b169865f5c0ca6eac1a047109bd99c23f84c490422509c88","tmkp:1160c95330ddf678772ccf9bd7a842a1518ad231a4b739e77053bac417b64d12","tmkp:5c94f0308d6f7aec0388613c5e62681221291b3ceed2004b22f2e3b283cbd3c2","tmkp:c05a14f120a4f2193c8c9facd9e43e20b1bc55e73acb3ee053addff233a479f5","tmkp:d46a07a466de26847f6612b52db96e21bc4a92691a42b7cbbae1fd59fa849385","tmkp:842ff71e2a3670bc24b737433b4094116e79d03b44854220b14fafe1df417dbb","tmkp:d831aa1d37b55503b164f4ee90d0d17b7fa7bbf2c886171b199b476adc2cbad0","tmkp:b4f65533664b68e854b5f602a90fdbb1dae7fb98e32b5c1de0bbf75639a69246","tmkp:08cbaacc28b1728a1c0ef87aec53ec114ce866df2328e769ef37ea24534c8f8b","tmkp:42ebe9dbf80aadf0d0566080b5680f77265bf47e586e7df3181e8f7d7b3c7b60"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Insulin was significantly lower either in OCT, PAS or OCT/PAS group compared with CONT.|PMC5436842|Insulin was significantly lower either in OCT, PAS or OCT/PAS group compared with CONT.|PMC5436842|In our present study, since both insulin and glucagon were significantly lower either in OCT alone or OCT/PAS group compared with CONT or PAS alone, it is suggested that the dosage of OCT was sufficient to reduce PAS-induced glucagon level.|PMC5436842|This data indicated that PEGV was not able to compensate the hyperglycemia induced by PAS, probably due to the mechanism of action of the drugs: PEGV improves insulin sensitivity by antagonizing GH action, while the hyperglycemic effect of PAS is related to inhibition of insulin production by β-pancreatic cells, in addition to suppression of incretins, regardless of insulin resistance.|PMC7774757|Either insulin, salicylate, or pyridoxamine treatment attenuated the deposition of the PAS-positive materials in the glomeruli (Figure 3).|PMC5155113","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4258142","PMC7366918","PMC5155113","PMC5436842","PMC7774757","PMC2789346","PMC7162833"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"98148028":{"subject":"UMLS:C4529301","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4326070","PMID:18566238","PMID:22539090","PMID:17699714","PMC7377050","PMID:25113866","PMID:20490863"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Furthermore, both tumors showed an early bevacizumab-induced increase in downstream activators from these receptors, like insulin-like growth factor binding protein 2 (IGFBP2), 3-phosphoinositide-dependent protein kinase 1 (PDK1), Akt and glycogen synthase kinase-3 (GSK3) (Supplementary table 1).|PMC4326070|The downregulation of phospho-Akt is of particular interest, as Akt was found continuously activated after bevacizumab and doxorubicin combination therapy.|PMC4326070|Silencing receptor protein tyrosine phosphatase mu expression (small interfering RNA) in human EC inhibited both synergy between MNTX and bevacizumab or 5-FU and increased VEGF-induced tyrosine phosphorylation of Src and p190 RhoGAP with enhanced activation of Akt and the actin cytoskeletal regulatory protein, RhoA, whereas silencing Src, Akt, or RhoA blocked VEGF-induced angiogenic events.|PMID:18566238|In addition, we show that bevacizumab itself acts on glioblastoma cells by activating the Akt and Erks survival signaling pathways.|PMID:25113866|In conclusion, the present study suggests biological mechanisms underlying growth inhibiting effects or acquired resistance to bevacizumab treatment, where activation of the Raf/MEK/ERK and the PI3K/Akt/mTOR pathway seems to be of particular importance.|PMC4326070","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9953401249999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:158d2e1b1f8b88b002e53bcb4b75bf79ce3204046d2afe2b074112be8de32ce3","tmkp:d0fc87d8a3b49e784dd3f84437dd273ef8a1b1f670ebb8e305def5262bc4b5e4","tmkp:fdb09cd139662466cae60f08d486529835c1fa0905913a58297649bc4a777920","tmkp:dcb00c3fe9b94fda989ac6ccf79abd11226a7beeccc4dffd7c5011db158ebc8a","tmkp:347011213680ab3289aa6aba9885ce45ef723a69881f3b2de1de836ce4a77970","tmkp:491c604e5b6956f998ba374b33cdcbbc858b958231ef6cdd2f08d01050a01be7","tmkp:76d037116e2232ddff7fbf655d2df0f6143db4c6f1830f5eb30895616265a160","tmkp:08a26233d68c9c8729c069021cf2d67c54be1d019cea4ad0296b9626f9b02e88","tmkp:27206982903cb9196a183e0b581a9a747bff3c1a78e2bf18030dcc35dc5506c9","tmkp:0eff4cfe3c40955c247f7bea648c8836c234c09ce3988ec056c4f3bf40a3d46e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"32521816":{"subject":"PUBCHEM.COMPOUND:5988","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:396b263f98e73022eb90f31e7b4dc550ec7ab48159c0e690a85fa9de0cf7dcf5","tmkp:7afa328e966d47b5a56aca3dce0506679383c9c541d08a55385e2c235090163c","tmkp:e96c7e5145f1b9f51ad35a5c781e11c978333e30ef41128a3ecb510d55ed32cb","tmkp:b6779932e4eefad774b583378742ef6f174f0174f82536892eb164f344d4b419","tmkp:2b2dd9c74959a441691a9a28fa9a579d9d3e3d8c8a2f50676bbc74c865b7ad97","tmkp:aee1625bbf4b4f29daf4def1f7b0dd19de384a0ed300d99efc3f4aeb3e8c9194","tmkp:a06c99e9dcd9891f9a0e479e5e3d831b99066b89f5800c1b85d4f67544b79f1a","tmkp:0311d06909c7a3d8065cf1c438bcb25f583a828169d674725a58b230a04ca758"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6461046","PMID:15993383","PMID:30340815","PMC4390809","PMC7594708","PMC5355302","PMC2933813"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Increases in VEGF expression and secretion were also observed after the addition of 100 mM sucrose to the medium (Figure 1C,D).|PMC4390809|The high NaCl- and sucrose-induced VEGF gene expression showed different time dependencies (Figure 1A,C), suggesting that both hyperosmolarity and alteration of the transmembrane NaCl gradient induce VEGF gene transcription.|PMC4390809|SD rats fed a high fat/sucrose diet showed increases in serum insulin and VEGF (both p < 0.01).|PMID:15993383|RLYE significantly attenuated VEGF-induced sucrose permeability in endothelial cell monolayers (Figure 8A).|PMC5355302|Consumption of a high sucrose diet has been reported to increase left ventricle weight and expression of markers of cardiac function (VEGF, BNP and TGF-β1) in the left ventricle .|PMC6461046","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.998844242","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"19130067":{"subject":"UMLS:C5242471","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:239e76c9052427c21753259c86a1639bc064211041a057593327e9abc9d4fce5","tmkp:103ec453e6a80b46b90e41536afefdec7159b2d0a9c860f9cc7ba68fd9fb0812","tmkp:6f69c8a6c9a337be9df46e7763179029b2ff41760001fee795c530a10a056822","tmkp:acc3e1ec5d856b389180c49d745aa277e3001b75c32b78be63049d395b5323f2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Using this strategy, Raychaudhuri and colleagues reported that Slc2a4 promoter methylation was lower in rats that received breast milk compared to the high-carbohydrate formula group.|PMC5336253|Membranes were incubated overnight at 4°C with the following primary antibodies diluted in blocking solution (5% milk/PBST): Catalase, Mfn-2, MnSOD, Nrf-1, UCP-2, UCP-3, VDAC-1/Porin (Abcam); Bcl-2 (BD Transduction Laboratories); Phospho-AMPKα (Thr172), AMPKα, Cytochrome C, Phospho-p38 (Thr180/Tyr182), p38, SIRT3 (Cell Signaling); Fis1 (Enzo Life Sciences); tFAM (GenWay Biotech); ATP Synthase (Invitrogen); SIRT1 (Millipore); PGC-1α (Millipore and Novus Biologicals); Nrf-2 (R&D Systems); GAPDH, GLUT4, Mfn-1 (Santa Cruz).|PMC3706566|Membranes were blocked with 5% milk in Tris Buffered Saline with Tween 20 (TBS-T) and subsequently incubated with primary antibody in TBS-T supplemented with 5% blocking milk in 1: 1000 dilution of rabbit anti-mTOR (#2972S, Cell Signaling, USA) and anti-p-mTOR (Ser2448) (#2971P, Cell Signaling, USA), anti-IRS-1(59G8) (#2390, Cell Signaling, USA) and anti-p-IRS-1 (Ser302) (#2384, Cell Signaling, USA), anti-PI3Kp85 (#4292, Cell Signaling, USA) and anti-p-PI3K p85 (Tyr458) (#4228, Cell Signaling, USA), anti-AKT (4685S, Cell Signaling, USA) and anti-p-AKT(Thr308) (#2965P, Cell Signaling, USA), and anti-GluT4 (#2213S, Cell Signaling, USA) and anti-β-actin (sc-47778, Santa Cruz, USA).|PMC4288420|The evaluation of adenosine receptors A1, A2A, and A2B, UCP1, GLUT4, GLUT2, insulin receptor, insulin receptor phosphorylated at Tyr1361, Akt, and Akt phosphorylated at Ser473 was performed according to Sacramento et al. and Matafome et al.. Briefly, after blocking for 1 h at room temperature with 5% non-fat milk in Tris-buffered saline (TBS), pH 7.4 containing 0.1% Tween 20 (TTBS) (BioRad, Spain), the membranes were incubated overnight at 4°C with the primary antibodies against A1 (1:200), A2A (1:200), A2B (1:200), GLUT4 (1:200), GLUT2 (1:200), insulin receptor (1:200) (Sta Cruz Biotechnology, USA), insulin receptor phosphorylated (phospho-Tyr1361, 1:500; Abcam, UK), Akt (1:1,000, Cell Signaling, USA), Akt phophorylated (phospho-Ser473, 1:1,000, Cell Signaling, USA), and UCP1 (1:1,000, Abcam, USA).|PMC7198774","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9848729875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5336253","PMC3706566","PMC4288420","PMC7198774"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"121777825":{"subject":"PUBCHEM.COMPOUND:2803","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:ee94380b36a80b6aabd37e5bcee7e58ee3e78bc4b1a23745bf1541927e8dda12","tmkp:7dc981ad05feeadf362d062c632e8ff74e192a1690c6b732892e60e10b457953","tmkp:768909b3a552f6141a50c9b0d361c288027cb7f7c931e71095a274206cbf9f1b","tmkp:6043812131f3c58c4464b41bf235bf96601fdd2fe6c88a1e001c2413cea58c29","tmkp:725a35a874e3cee084eba90d04257f864267d3e3e254c4f5affe5817b1c72246","tmkp:cec6388c1f1ef5b74e20b2d9c3c6c272bcab8fc89446a99ee7ec17da43695203","tmkp:5bebefe0a45dde2a8b5b3116a6c11e0a8cc9a9ca32a9bf856f5433ab5a3f6a1b","tmkp:4a0847bcf5cf3b6e1200293c5066515c032901d316396e7918543e0e833513f3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Finally, Loftus et al. used a complex trauma model including haemorrhage, lung contusion, and stress over 7 days to explore the effects of clonidine (10 μg/kg) on lung injury, finding high doses of clonidine increased vascular endothelial growth factor (VEGF) and its receptor expression in the lungs.|PMC6907244|Finally, Loftus et al. used a complex trauma model including haemorrhage, lung contusion, and stress over 7 days to explore the effects of clonidine (10 μg/kg) on lung injury, finding high doses of clonidine increased vascular endothelial growth factor (VEGF) and its receptor expression in the lungs.|PMC6907244|Clonidine restores vascular endothelial growth factor expression and improves tissue repair following severe trauma.|PMC7978382|Clonidine restores vascular endothelial growth factor expression and improves tissue repair following severe trauma|PMC6907244|Clonidine restores vascular endothelial growth factor expression and improves tissue repair following severe 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a week after the exposure to nicotine or nicotine plus NNK, Bcl-2 expression was augmented, accompanied with the increased resistance to cisplatin-induced apoptosis.|PMC3683296|Consequently, our data showed a significant elevation in the expression of Bcl2 in macrophages after nicotine stimulation while MAP infection alone did not alter the expression of Bcl2 (Figure 2).|PMC8158352|Levels of phosphorylated Akt, an effector of PI3K, and Bcl-2 were increased by nicotine.|PMID:11278378|The protein level of bcl-2 (see brown sites, arrows) is elevated in nicotine-received animals compared to control-sham group, Scale bars: 40 µm.|PMC5339662|Interestingly, a week after the exposure to nicotine or nicotine plus NNK, Bcl-2 expression was augmented, accompanied with the increased resistance to cisplatin-induced 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Immunoblotting showed upregulated protein expression of activated Caspase 3 after verteporfin administration.|PMC7815513|The results demonstrated that verteporfin enhanced the inhibitory effects of artesunate on C918 cells, further inhibiting cell viability (Fig. 4A), elevating caspase-3 and caspase-9 activity levels (Fig. 4B), and increasing intracellular ROS and LDH release (Fig. 4C and D) compared with those in the cells treated with artesunate alone.|PMC8228376|We observed that combined treatment of trastuzumab with verteporfin significantly reduced pH3 expression (p = 1.2 × 10−4, Figure S9B) and increased c-casp3 expression (p = 7.2 × 10−5, Figure S9C) in vivo, compared to single treatment with trastuzumab, which correlated with a significant decrease in tumor proliferation and enhancement of apoptosis rates, respectively.|PMC7281325|In this study, we show for the first time that photodynamic therapy (PDT), using benzoporphyrin derivative monoacid ring A (BPD-MA, verteporfin) as the photosensitizer, induces the complete cleavage and subsequent activation of caspase-3 (CPP32/Yama/Apopain) but not caspase-1 (ICE) in human promyelocytic leukemia HL-60 cells.|PMID:14555976|Verteporfin (VP), a YAP inhibitor, could induce phosphorylation of YAP and cleavage of caspase-3 and PARP; the combination of VP with Dox (VP+Dox) further increased the levels of phospho-YAP, cleaved caspase-3, and cleaved PARP in HCMs (Figure 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the activation of p38 and the increase in insulin sensitivity induced by anisomycin were completely prevented by pretreatment of muscles with the p38 inhibitor SB-202190.|PMID:15585585|Three hours after anisomycin treatment, by which time the acute effect on glucose transport had partially worn off, sensitivity of muscle glucose transport to 60 microU/ml insulin was markedly increased.|PMID:15585585|F: mRNA expression of Atf4, Chop, Hsp60, Hsp10, ClpP, and Lonp1 after 16 h of insulin stimulation of vehicle treated or 1 μM anisomycin treated CLU183 cells.|PMC6407370|Addition of anisomycin reduced ER stress and ER calcium leak from translocon, leading to restored insulin secretion.|PMC4749224|Metabolic stress modeled by anisomycin, thapsigargin, or tunicamycin increased many of the same Ser(P)/Thr(P) residues as insulin, some of which (Ser(P)-302(Irs1), Ser(P)-307(Irs1), and four others) correlated significantly with impaired insulin-stimulated 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Glucose transporter type 1 deficiency syndrome patients treated with MCT experienced improvement of their symptoms and a 10% increase of their brain Pi/PCr ratio during visual stimulation as measured by 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the aid of the literature, it is known that triamcinolone acetonide regulates VEGF in a concentration-dependent manner, such that triamcinolone acetonide exerts a biphasic effect on retinal pigment epithelial cell proliferation, stimulating cell growth at lower concentration (lower than 1 μM, ie, 0.44 μg/mL) but inhibiting cell growth at higher concentration (higher than 100 μM, ie, 44 μg/mL).|PMC3428247","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"84644914":{"subject":"PUBCHEM.COMPOUND:3821","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Collectively, these findings demonstrated that ketamine attenuated the expression of VEGF and cell migration ability in colorectal cancer cells, probably via blockage of NMDA receptor.|PMID:30817910|In chronic ketamine abusers, peripheral blood serum vascular endothelial growth factor (VEGF) protein is reduced.|PMC8228861|compared with NMDA-induced rats (228 ± 18% of control), and VEGF was decreased (133 ± 14%, 133 ± 16%, and 127 ± 20% of control, resp.)|PMC5660823|In accordance, Figure 5(e) presented that the IVB (0.25, 2.5, and 25 mg/ml) treatment decreased the expression of VEGF in the retinas of rats treated with NMDA (168 ± 11%, 137 ± 11%, and 140 ± 18% of control, resp.)|PMC5660823|In chronic ketamine abusers, peripheral blood serum vascular endothelial growth factor (VEGF) protein is 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release.|PMID:22818390","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999683175","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"41953093":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9990427066666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Combining the two set of data together, PARP1 was identified to be significantly up-regulated both in embryonic stem cells and the residual tumors after Sorafenib treatment (Fig. 1a, Additional file 1: Fig. S1C).|PMC7824946|PARP1 is activated in embryonic stem cells and the residual tumors after Sorafenib treatment and significantly potentiated Sorafenib both in vitro and in vivo.|PMC7824946|Reactivation of PARP1 expression was also detected in HCC residual tumors after sorafenib treatment in xenograft mouse model, indicating the potential important roles of PARP1 in stem cell pluripotency and HCC sorafenib treatment resistance.|PMC7824946|PARP1 is activated in embryonic stem cells and the residual tumors after Sorafenib treatment|PMC7824946|In addition, western blot analysis confirmed significant increase in PARP-1, caspase-9 and caspase-3 cleavage protein in sorafenib-treated miR-216a-3p OE groups, whereas, sorafenib-treated miR-216a-3p KD significantly decreased in Huh-7 and HepG2 cells compared to the corresponding controls (Figure 3D and 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extract of asafoetida gum has been shown to enhance insulin secretion and to reduce fasting sugar levels in Wistar rats, and it functions as a hypoglycemic and hypolipidemic agent.|PMC7310983","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:16310255","PMC4016206","PMID:25903395","PMC4550293","PMID:8243430","PMC3609812","PMC4452420","PMC7310983","PMC3741492","PMC4550301","PMC4710862"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"36793839":{"subject":"PUBCHEM.COMPOUND:6322","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:20071141","PMID:18331270","PMC4468226","PMC6479373","PMID:16631200","PMC4036672","PMID:18085359","PMID:28078001","PMC3940779"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Local arginine supplementation results in sustained wound nitric oxide production and reductions in vascular endothelial growth factor expression and granulation tissue formation.|PMID:16631200|Local arginine supplementation results in sustained wound nitric oxide production and reductions in vascular endothelial growth factor expression and granulation tissue formation|PMC4468226|In a published report, the culture of SKOV-3 and MDAH2774 ovarian cancer cells with L-NAME (an L-arginine analog) significantly reduced the ability of cells to produce vascular endothelial growth factor (VEGF) and completely blocked their capacity for angiogenesis, in the in vitro angiogenesis assay.|PMC6479373|L-Arginine further significantly increased MDA and NO, and decreased VEGF (P < 0.05 vs aortic IR).|PMID:18085359|C-terminal arginine-like compounds have established efficacy for inhibition of VEGF/Nrp binding.|PMC4036672","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9983327200000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a73bf96ba18006d92c64ae29f5a80f00fb5e27874ff90bed0de1df16a25cb9e3","tmkp:555b1713261e38f86ad805e313005488c0b8af5da1b0859d4cf8b0f954f7e378","tmkp:59870f84da0ce0e5705893d007f2e77040db4615ba52b8bdee4c0e2d9d359b13","tmkp:b1fc8f574420fc5e7f701a10b1b5d0ae30ff85ad972973063d96f8ac42115787","tmkp:7ae73ee8074bdf6fef00df38b43e206643165498634e11356e29b17761a0d84e","tmkp:71a0e445cbd61d5fa5099e6780f889a83c936e109f5482b2327f61312f788e3f","tmkp:afddff32a994258790b476872877fdf1001582c0ccca8378ee071381f2721fdd","tmkp:fa63e308398ab916d617c9654b13c2259f68389ad9e714c4db47a081a702b4cb","tmkp:cea347cca49a02bf5ccd1850ffcdc5de41e696c2c78126038cb7bc6bfb44dc5d","tmkp:62efdad29b31aa0d933bc418417965aff5a0bb8bbae9be885528592a71418bc8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"5704803":{"subject":"UMLS:C4529301","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9934519972682927","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:26066903","PMC6320227","PMC7973261","PMC4402130","PMC3151740","PMC7119170","PMC4189677","PMC4200479","PMC3058319","PMC4573901"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In this experiment, intermittent treatment with bevacizumab induced less OA progression, as shown by both histological and gene expression assays, through increases in the gene expression of ChM-1 and VEGF in the articular cartilage and decreases in the gene expression of MMP 13 and ADAMTS5 in the synovium.|PMC4189677|Unexpectedly, this clinical trial definitively disproved our hypothesis that continued VEGF suppression would occur with the sequential combination of these two agents, as VEGF levels continued to rise with subsequent and continued treatment with sunitinib and bevacizumab.|PMC4200479|Similar increases in plasma VEGF concentration have been observed following treatment with bevacizumab.|PMC4402130|Plasma levels of VEGF, P1GF, and sVEGFR2 significantly and persistently increased after bevacizumab and chemotherapy treatment (at days 15 and 43; VEGF and P1GF also were increased at day 71 and end of study), although plasma bFGF was transiently increased only at day 15; plasma sVEGFRl, IL-lb, IL-6, IL-8, TNF-α, and urinary MMP activity did not significantly change at any of these time points (Table 3 and Supplementary Tables S3 and S4).|PMC3151740|Gordon et al. reported that the intravenous injection of bevacizumab led to an increase in serum total VEGF in clinical trials while free VEGF concentration was reduced.|PMC3058319","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2b2663970e63ae547d5caecff1d76811a174621ce5aeb14a7b31a0b920cbefa3","tmkp:ea7564927b25ea81845e0fe145f4199a7cd0439198e5ba5fca09ea0b30e67481","tmkp:29d71f6eba0e58c6845b2e89281a51800fc614dc3b12bab80ac60c99fe51a416","tmkp:ecbe51ae03b82e03d2b76e602ae7f1af15a6e5a51c6da69a9f928af3c0156247","tmkp:f9d6ad01fbd0219e73df3869e078bd7c4be7dbb011c425b346e6e592ca070b45","tmkp:f30947589513f3c0c33c4156e1b9283dde381732fa067589f11ca3f95ca3a770","tmkp:0fcbad2edb6aa58466f1aa45970171c1da228edcf9de45c38982c18a2e5f323b","tmkp:1d3bb92f00142b35452c2505b93229dd3e9d0ee8f4f502e406d6262c30963922","tmkp:f150654f28c3277252254a0774ded0b7b5a9b834067d459efcb00ae13f69fbc5","tmkp:6233699c0fc77a58450a03df7c7bf3e3c95c475120090ac121ef425e17f2e9d8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"77545707":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9980806957142858","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6112212","PMC3702466","PMID:26728267","PMC3161880","PMID:31823256"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Arici et al. treated rabbits with formaldehyde and observed a decrease in Bcl-2 expression while an increase in caspase-3 and Bax proteins.|PMC6112212|The expression of P53, caspase 3 and caspase 9 mRNA increased sharply by 261.5%, 248.2% and 90.5%, respectively, in the formaldehyde-treated group.|PMC3702466|Furthermore, formaldehyde caused a concentration-dependent increase in nuclear fragmentation and in the activities of the apoptosis-initiator caspase-9 and apoptosis-effector caspase-3/-7, indicating apoptosis progression.|PMID:26728267|Formalin injections led to a significant rise in the levels of cleaved caspase-3 compared to saline group (1.48 ± 0.13 vs. 0.97 ± 0.17 folds; p < 0.05), whereas rhEPO co-treatment strongly prevented caspase-3 activation (0.84 ± 0.16 vs. 1.48 ± 0.13 folds; p < 0.05) (Figure 3F).|PMC3161880|Meanwhile, mRNA expression levels of Tnf-α, NFĸB, and caspase-3 significantly increased but the Bcl-XL level did not show significant alteration by formaldehyde treatment.|PMID:31823256","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:aefdf8232b6fc3070b121f2213a3ff8400144ae8a91becfb47f42d7835dbb97e","tmkp:8e74f560427770632cff9d1513d841e752cd509486a996794c90cb384969d331","tmkp:7aa137def9bdb1ac2b19e65509519a2ccfaaa96587252d9893513976d6d68ab0","tmkp:f90ddf0dcdeb1dbcca040d48de5802e5768e43f7f38125de069ab81dcda3b294","tmkp:b4379e610f29382adec37f6993266f262738ec79a9c2f2ab7db7ef07d8eb22fc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"112526169":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9953621492592594","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC4838126","PMID:24495518","PMC5883600","PMC5537710","PMC4067478","PMC4898593","PMC3531874","PMC7696252"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Our previous study indicated that S-adenosylmethionine (SAM) reduces the expression of Rac1, Smad3 and Smad4 in activated HSCs; however, the association between Rac1 and Smads in activated HSCs has yet to be revealed.|PMC4838126|A markedly increased methylation status was shown in the SAM-treated cells compared with the untreated ones, which indicated that the Rac1 promoter could be methylated by SAM in LX-2 cells, explaining the inhibitory effect of SAM on Rac1 expression.|PMC4838126|Furthermore, following our previous study, the mechanism underlying the inhibitory effects of SAM on Rac1 expression was explored.|PMC4838126|This suggested that inhibition of sirtuin activity with the same doses and duration that induced TIAM1 acetylation and decreased Rac1 activation also decreased the GEF activity of TIAM1.|PMC4067478|SAM inhibits the proliferation, adhesion, migration and invasion of LX-2 cells in vitro probably via attenuating the expression and activation of Rac1 and up-regulating MMP-2 and MMP-9 expression, which possibly provide a molecular basis for potential application of SAM in the therapy of liver fibrosis.|PMID:24495518","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:697e20611fb9a634d9100470a89b4320d260f1520bcd6507c1c2e19ec7bec9f1","tmkp:5f55f22baecce20ab2ae968d1dcf4f63695a10634fe2bba7e1d4df88216f23e8","tmkp:cdf0390e7a6065079001e6065bbf51443437c2f8c352589dfaf57b0405dcfac7","tmkp:eb8dd99563f802cea291c5273135519d44c7f68d4143fcfad427764bd2aa9bf0","tmkp:0442f1bbfad07f1948e870b472b434052ef1151797978df388423ee47ff63ff3","tmkp:08367214a31a14000df3a990c644b8bb2c2b25f659f588ae60dfe1e1d1bd83ed","tmkp:52d8e4c958f2d751585b97f04d8e1926276a4666dac772fa8c39ae2472e41cee","tmkp:0036f6d24fd650204c5df51c1efac939e0d076e75581e61af1f9de06961e1e94","tmkp:aaa4aa6782ca4afe49af1eeecf849cedb565b59d2a0aafc05a579a26ee88d866","tmkp:1c3693b40762c7f19bad42834b0e01a6f58cc620759c83b4d5ae863f0bbf4dfc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"18734474":{"subject":"NCBIGene:3140","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"PKD has been linked to the pericentromeric region of chromosome 16, PNKD is associated with mutations in the myofibrillogenesis regulator 1 (MR-1) gene on the long arm of chromosome 2 (2q32-36 locus), and PED is associated with mutations in the glucose transporter gene, GLUT1, responsible for glucose transport across the blood-brain barrier.|PMID:19364451","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:bdf8015c53574c510a1c9667353968a4947b1af0d2d24ba8827d7d5f9e1646df"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9979329","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:19364451"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"125473419":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:4e01d41f15f20fde9cdf6712097137332d34c1747495a6fb45a5f51595622660","tmkp:112fb746bdb24817b6a3e4e74c838adc7bfeb6aa16e7482da24b6831bac69508","tmkp:c6ce0dec2b9727f12d00372080006488ba97b6263ba885bc838dede375a61e8e","tmkp:af913aa459bdc311f8bb3232767e56d5f389bc52a1af536dee3c767f5fefba8c","tmkp:77812d4578811a85b0c1204fbf2a32b65b41c8daa1ab2b95dff4bcc6fab14fee","tmkp:02aa0f9aec648814339b4838b49b33afd2af64778eef58d2889d93dfa65dcfc3","tmkp:d8c882438d1cefb4f337f3d10d144bf90f5d539f3f5944d36f65671eecee041b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9880321","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Expression of glucose transporter-1 (Glut1), a HIF-dependent gene, was also elevated in the hearts of tamoxifen treated Vhlfloxed-UBC-Cre-ERT2 mice (Figure 4D).|PMC3141062|GLUT1 and GLUT3 expression, particularly that of GLUT1, was markedly enhanced in VHL-KO (VHLf/fCreER™ with tamoxifen) livers, whereas that of GLUT2 was not (Figure 7).|PMC3706433","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7311173","PMC3706433","PMC7066233","PMC3141062","PMC7386868","PMC7464784"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"42273390":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:5595","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:30236600","PMID:16352387","PMID:23219522","PMID:22138297"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"increases activity of","value_type_id":"EDAM:data_0006","original_attribute_name":"description"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"59713085":{"subject":"PUBCHEM.COMPOUND:5988","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"The use of pacifier with sucrose as procedural analgesia for venipuncture in the PED is effective in reduction of pain in infants 0?3 months old, as shown by decrease in crying times.|PMC1950500|Pusa Early Dwarf; PED) was the treatment of 1 mg L?1 Zeatin, 0.2 mg L?1 IAA, and 2% 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these data indicate that levetiracetam regulates the striatal expression of molecules involved in the mechanisms of dyskinesias, that is, ΔFosB, p-DARPP-32, and p-ERK1/2.|PMC4322303|Levetiracetam-induced expression changes of the ΔFosB and phosphorylation of ERK1/2 in the dorsolateral portion of the 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addition, ASA significantly inhibited CF apoptosis, and decreased the levels of apoptosis markers (cleaved caspase 3 and Parp1), which might serve as a side effect of anti-fibrotic effect of ASA.|PMID:28216620|Caspase-3, as the main terminal cleaving enzyme in the process of apoptosis, also declined after using aspirin (Fig. 3g, h).|PMC6993447|Combination of aspirin and ginkgolide injection could better reduce brain water content, reduce apoptosis rate of cortical cells P < 0.05, reduce expression levels of caspase-3, Bax and p-REK1/2 proteins in ischemic brain tissue P < 0.05, and increase expression level of Bcl-2 protein than aspirin and ginkgolide injection alone P < 0.05).|PMC8176056|These results also suggest that PM2.5-induced apoptosis was dependent on caspase-3 activation, and aspirin, Vitamin C, Vitamin E, or ozone can decrease PM2.5-induced apoptosis of ovarian cells by reducing the activity of caspase-3.|PMC5463468|And interestingly, we have also observed that the expression of caspase-3 in PM2.5 + aspirin, PM2.5 + Vitamin C, PM2.5 + Vitamin E, or PM2.5 + ozone group was significantly decreased compared to the PM2.5 group, which indicates that aspirin, Vitamin C, Vitamin E, or ozone might have protective effects on PM2.5-induced apoptosis in ovarian cells.|PMC5463468","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:17ccc6556a1f23d492a2e46c0e06991b4911e14da045fce8422b069e5f69450a","tmkp:a433033f46de5066be31ec7ec07d8a3c2cb99cfe39caf89c638eb28617df5354","tmkp:6fff8e5d51154f1b5e1d6f2502bc83f15164c5409cad95edd787684509f1a97c","tmkp:191350517fcf8f6d72c147c5c342949cec699429ce7f6df8dce8633c1a481634","tmkp:52b664100dcd421f177f88d9012fb2d663aa1db4b833ec68939e9e562bb296f1","tmkp:8b7aaf612a6b34ff7ecd9bbbdf6ff9e5f7c8bb880fdd8cfccfe7a8220e33d5e4","tmkp:487e75e026668a6f386f1c343f5a658f362e8e40a8fcbc0dc5c658828537ce43","tmkp:2dbc387c3a0bb4bcd6c2e330322f0ca6dc328867cb56af6f99e7e456dc7ead52","tmkp:af751a0aeae7080805f1121ac7e926320ed36fc219a2ee21ceb4342960fcd14f","tmkp:8ab992c5613bd63a732ef0d0325402e32d73ebf32bf88a852bdaafcf4b1f1c62"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9970541075","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:28216620","PMC6849393","PMID:21343676","PMC3854680","PMC5227127","PMC8176056","PMC5463468","PMC4134270","PMC6993447"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"80532848":{"subject":"PUBCHEM.COMPOUND:6137","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5405996","PMC6479528","PMC6781303","PMC6669428","PMC3140528","PMC7040518","PMC7212392"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In contrast, in MET-treated animals, the serum levels of both IFN-γ and IL-4 cytokines were significantly increased compared with those in vehicle-treated animals.|PMC5405996|In contrast, the level of IL-4 increased significantly in the MET (288.50 pg/ml) and combination of MET and CUR (255.5 pg/ml) treated animals compared to the control (113 pg/ml), and it was insignificantly reduced in the CUR treated group (94 pg/ml).|PMC5405996|In contrast, the level of IL-4 increased significantly in the MET (288.50 pg/ml) and combination of MET and CUR (255.5 pg/ml) treated animals compared to the control (113 pg/ml), and it was insignificantly reduced in the CUR treated group (94 pg/ml).|PMC5405996|Met showed similar effects on reducing the levels of IL-1β and IL-2 and enhancing the levels of IL-4, IL-10, MMP-9, and G-CSF in the serum of db/db mice (P < 0.05) (Table 2).|PMC7212392|The phenotypic plasticity of T helper cells may explain the rise in both IFN-γ and IL-4 levels following MET administration in our study.|PMC5405996","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:6566ab8cda354375f7e62fbde69e49281634a6f37767dfc6b7f1edd4e370d169","tmkp:3a2f9cc3920b07be5fd058fa427b91e41a42b438232f329d601ade20c096fa81","tmkp:a59cad13e321dd68d7c1cd06ace3f21990387e8c0f9371143b5e411321cfb540","tmkp:5ad79d9819530a24baf6020bcd572f961f10df2f9a081e955acfafc923ae7ea9","tmkp:cb18278fdb9a390fe2bffc0150d7a99f4a82ce9ba76f4564fdb9316c352eb321","tmkp:02c104afd8cef3a38d14fd329b8cb4de188ee577e84dbd9b06978637979fce2c","tmkp:3a01a7c1cbfb66086f52a719a41053e1fc657916eeec821c298a80933565c23d","tmkp:48180cc06416f0b1d7beaa616dcf3204fc2a68bab699d92ebc36924198d18e83","tmkp:73d68747fe15cfc196d60259857e8aee4e52dbc4e12fbdbe18f018894f835adc","tmkp:13afa0d87c6552558a7b1e388915f26083d4e63ce92b2415ba697b965c1aa884"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.99906661875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"42193279":{"subject":"PUBCHEM.COMPOUND:4943","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:db11da8bcbf312288c22a8094a16e72b4d3f33c09793bb6a2c7f99522c486be3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"At anesthetic doses that produced loss of righting reflex, isoflurane, propofol, and ketamine all reduced phosphorylation of the activating residue T183 of ERK2 (but not of ERK1); S897 of the NR1 NMDA receptor subunit; and S831 (but not S845) of the GluR1 AMPA receptor subunit in cerebral 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and molecular modeling of novel P38α MAPK inhibitors targeting breast cancer, synthesized from oxygen heterocyclic natural compounds |PMC7717492|Design and molecular modeling of novel P38α MAPK inhibitors targeting breast cancer, synthesized from oxygen heterocyclic natural compounds.|PMID:30792101|Therefore, it is very likely that the activation of SMG-1 by low oxygen restrains the hypoxia-induced malignant responses in tumor cells partially through inhibition of the MAPK pathway and the consequent HIF-1α activation.|PMC2719310|Liu et al. demonstrated that 1, 4-naphthoquinone induces apoptosis in lung cancer cells by activating oxygen-dependent down-regulation of the proteins related to the MAPK cascade.|PMC6627947|Hyperbaric oxygen treatment suppresses MAPK signaling and mitochondrial apoptotic pathway in degenerated human intervertebral disc 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inhibited phosphorylation of ERK1/2 (pERK1/2) and increased ERK1/2-dependent PUMA expression.|PMID:30024623|Taken together, these results demonstrate that propofol attenuates CFA-induced neuroinflammation (TNF-α, IL-6, and IL-1β expression) through a mechanism that involves activation of ERK1/2/NF-κB signaling pathway.|PMID:30536812|Propofol induced AKT and ERK1/2 activation.|PMID:21447487|Consistently, propofol elevated the expression of apoptosis‐related proteins such as Caspase‐3, Bax and phosphorylated ERK1/2 in cardia cancer cells.|PMC7445405|Propofol partly inhibited inflammatory cytokine production, including IL-1β and IL-6, and the anti-inflammatory effect may result from inhibition of JNK-MAPK, and enhanced NF-κB and extracellular signal-regulated kinase-MAPK signaling at clinical concentrations.|PMID:29904429","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:cf3c2082f2c1402b3626a9551de7e8a7b9c1040d451fa73edb27fef8e284e473","tmkp:6c02cfebce514d3958408f4542d1f8eda2fcd9e981cb7179a7e66b4c8d64b392","tmkp:e768cf24bcbafe6c7b075799afbf55ee4905b7d69d74392f491b760124ed35a1","tmkp:b536036824cc399738359d3ac5961ba1d4be67fc6e49d305dc3be4c45acdabdb","tmkp:23fccebbef8daa51e0838389e37fbf8154f0c5b8829b493db154caacc952b780","tmkp:72701652cfc06f71f9440f7075578405a4b8c848278f7213b1e15826c579d169","tmkp:d6ca8ccc95a68f7d7feaf9586f607dd9ba5c50fef78fa6a4b26228b5dbcd696a","tmkp:dba28958bab32c911791db8bf50cc4a4aaeaf07cd3626325e5e7de2db11007e6","tmkp:88c30bac3fbce3a31afccd9c215bbafc47a700e0bd877a203dfd0397f5e41f54","tmkp:c03a28100aeaca00663fda64b8c9f8f5e3d24a8f7c49d635a84d0367bad14af2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.985776761","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:29904429","PMID:23670191","PMID:30536812","PMC8240101","PMID:21447487","PMC7445405","PMID:17592535","PMID:30024623"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"58153403":{"subject":"PUBCHEM.COMPOUND:2083","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:7000415","PMID:6760909","PMC4403074","PMID:9088585","PMID:3525429","PMID:602717","PMID:1438670"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"This in-vitro study provides the first evidence that salbutamol and beclomethasone can significantly inhibit the contractile response of insulin on guinea pig airways and salbutamol is more efficacious than beclomethasone in this regard.|PMC4403074|3. Measurement of concentrations of blood glucose, lactate, pyruvate, glycerol, ketone bodies, non-esterified fatty acids, insulin, plasma cyclic AMP and cyclic GMP were made after each increment of salbutamol and all showed an increase apart from cyclic GMP. 4. After chronic inhalation of salbutamol there was a decrease in the airway, metabolic and insulin response to intravenous salbutamol.|PMID:7000415|This insulin induced tracheal smooth muscle contraction was significantly reduced in salbutamol and beclomethasone treated groups from 35 ± 1.13 mm (control) to 14.55 ± 0.62 mm and 22 ± 1.154 mm respectively (Table 1).|PMC4403074|Our data showed that maximum constrictor response of insulin in the presence of salbutamol and beclomethasone was reduced by 41.57 and 62.86 percent respectively as compared with control group (Table 1).|PMC4403074|Although salbutamol and beclomethasone both had a profound inhibitory effect on insulin induced airway hyper-reactivity, yet salbutamol is more efficacious than 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can disrupt VEGF and NO signaling pathways via down regulation of eNOS.|PMC6008318|In postnatal phase 1 of ROP, increased oxygen exposure suppresses hypoxia-inducible factor 1 alpha (Hif1α) and vascular endothelial growth factor (VEGF), contributing to vascular attenuation.|PMC7568562|Compared to the intrauterine environment, the immature retina is exposed to a relatively hyperoxic environment after birth under oxygen supplementation, which leads to the down regulation of VEGF and IGF-1.|PMC7352796|In postnatal phase 1 of ROP, increased oxygen exposure suppresses hypoxia-inducible factor 1 alpha (Hif1α) and vascular endothelial growth factor (VEGF), contributing to vascular attenuation.|PMC7568562|Animals exposed to 100% oxygen for an average of 9 days had an 80% decrease in lung VEGF mRNA abundance, decreased alveolar epithelial cell VEGF expression, and decreased VEGF 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elevated expression of two key receptor molecules GPR43/41 for microbial SCFAs as well as their well-known downstream targets (ERK2, P38 and JNK1/2) showed in mice after supplementation with betaine or betaine-altered gut microbiota (Supplementary Figure 6D).|PMC7889173","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"107867629":{"subject":"PUBCHEM.COMPOUND:1130","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"It 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glomerular tuft area, glomerular volume, MVD, VEGF protein expression in glomeruli and VEGF mRNA expression in the renal cortex tissue were significantly increased in diabetic rats and finasteride-treated rats when compared with controls (P < 0.01, P < 0.05).|PMID:25789687|The glomerular tuft area, glomerular volume, MVD, VEGF protein expression in glomeruli and VEGF mRNA expression in the renal cortex tissue were significantly increased in diabetic rats and finasteride-treated rats when compared with controls (P < 0.01, P < 0.05).|PMID:25789687|MVD, VEGF, and HIF-1alpha values were significantly lower statistically (P <0.001) in group 1 compared with group 2. In the finasteride group (group 1), the positive correlation of the immunoreactivity of CD34 and HIF-1alpha, VEGF and HIF-1alpha, and VEGF and CD34 was statistically significant (P <0.001).|PMID:16904480|MVD, VEGF, and HIF-1alpha values were significantly lower statistically (P <0.001) in group 1 compared with group 2. In the finasteride group (group 1), the positive correlation of the immunoreactivity of CD34 and HIF-1alpha, VEGF and HIF-1alpha, and VEGF and CD34 was statistically significant (P <0.001).|PMID:16904480","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"113551914":{"subject":"PUBCHEM.COMPOUND:3440","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Compared to the I/R group, furosemide significantly (p < 0.01) upregulated the phosphorylation of 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treatment increased the expression of B-72, interleukin (IL)-1β, IL-4, IL-6, IL-10, matrix metalloproteinase-8, Fas ligand, tumor necrosis factor (TNF)-α and metalloproteinase inhibitor 1 levels in the lacrimal gland of the dry eye model.|PMC7308241","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"103329004":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9934119257142857","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"To analyze the activation ERK1/2 in cardiac fibroblasts and the involvement of CXCR4 receptors in UB signaling, cells were pretreated with AMD or PD (a selective inhibitor of ERK1/2 pathway) for 30 min followed by treatment with UB for 15 min.|PMC6173983|As shown in Figure S2, AMD3100 inhibited SDF-1-induced phosphorylation of Erk in Mz-Cha-1 cells.|PMC6134930|However, AMD3100-pretreated BMSCs showed significantly lower expression of p-ERK1/2, which suggests that SDF-1 activates the intracellular ERK phosphorylation in osteogenic differentiation of MSCs (Figures 2(e) and 2(f)).|PMC8179778|We confirmed p-ERK1/2 was upregulated in the ACLT group by immunofluorescent staining, and the level of p-ERK1/2 was decreased in the AMD group (Figures 3(e) and 3(f)).|PMC8179778|Interestingly, AMD3100 specifically inhibited SDF4-induced ERK1/2 and p38 but not AKT1 activation (Fig. 5E), implying the existence of other SDF4 receptors on 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classes of 3-substituted indolin-2-ones containing propionic acid functionality attached to the pyrrole ring at the C-3 position of the core have been identified as catalytic inhibitors of the vascular endothelial growth factor (VEGF), fibroblast growth factor (FGF), and platelet-derived growth factor (PDGF) RTKs.|PMID:10602697|Three classes of 3-substituted indolin-2-ones containing propionic acid functionality attached to the pyrrole ring at the C-3 position of the core have been identified as catalytic inhibitors of the vascular endothelial growth factor (VEGF), fibroblast growth factor (FGF), and platelet-derived growth factor (PDGF) RTKs.|PMID:10602697","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"47800483":{"subject":"UMLS:C4529301","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"I read with interest the case report on the closure of a macular hole over a serous retinal pigment epithelial detachment (PED) with intravitreal bevacizumab.|PMC5778566|H. 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injections.|PMID:25390416","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9896201471428572","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5778566","PMC3853783","PMC3560685","PMC2969161","PMID:25390416"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e329fe043040b5765376ffd8b78dbdbab3c65e6e76d5a2db582326b3c3bff38f","tmkp:4ee85d9e5e4d3f6568c5ace6f3e7e169f0a0afe69ad3f7d8c268c4bd5e6e41fb","tmkp:eda429e956ce7fcdc52bc252ea2b463824a1dd8030eca40e3bbaa2b33751e5e5","tmkp:bf3d61d6ac02675a04811c035689637a8ea47259da0338c97338719903403cc1","tmkp:f7c3f5eae6bb652e43fe225e875ccc19cc4cbb37a7e2804840d0073b792e353b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"77437106":{"subject":"PUBCHEM.COMPOUND:174","object":"NCBIGene:2643","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In experiments involving GCH1 inhibition, DAHP (150 mg/kg in 50% PEG/PBS) or vehicle was injected intraperitoneally 30 minutes prior to Cp48/80 or HCQ, and scratching time was measured as described above.|PMC6349351","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b72a16e78f7de5ef3671c9bc2b33af0292608bed140d4becdcf2435886b69522"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6349351"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99452895","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"5314914":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:225689","predicate":"biolink:directly_physically_interacts_with","attributes":[{"attribute_type_id":"biolink:Attribute","value":["ChEMBL","PubChem"],"value_type_id":"EDAM:data_0006","original_attribute_name":"hetio_source"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:hetionet","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"}]},"42289752":{"subject":"PUBCHEM.COMPOUND:174","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:16555285","PMC4267064","PMID:1367488","PMC4231942","PMID:11214754","PMC4120760","PMC8240898"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9978007499999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Matrix production by vascular smooth muscle cells grown on adhesive ligand-modified glass surfaces and in PEG hydrogels containing covalently bound adhesive ligands was increased in the presence of 0.04 pmol/ml (1 ng/ml) TGF-beta1.|PMID:11214754|At concentrations of 3 and 30 g/l, PEG increased the rate of recovery of active protein in the absence of 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serum vascular endothelial growth factor (VEGF) C concentration was significantly higher in the GA group than in the PPA group.|PMC5209272|Lastly, serum vascular endothelial growth factor (VEGF) C concentration was significantly higher in the GA group than in the PPA group.|PMC5209272","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"86010625":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"As demonstrated in Fig. 1A, the VEGF immunoreactivity in the mammary tumor tissues of mice exposed to alcohol was higher than that of the control mice.|PMC4081417|We conclude that moderate levels of ethanol can induce VEGF expression and stimulate angiogenesis in chick CAM.|PMID:11404314|Regarding the mechanism of the growth, although moderate levels of ethanol was shown to induce expression of vascular endothelial growth factor and stimulate angiogenesis, chronic ingestion of ethanol in rats was reported to increase the ventricular expression of p53, which is known to inhibit angiogenesis.|PMC3213039|We observed an increase in the expression levels of VEGF protein when TG1-1 cells were treated with a combination of ethanol at 0.2% and 0.5% and estrogen, in a dose dependent manner, compared with estrogen treatment alone.|PMC6218769|Furthermore, it appeared that alcohol induced VEGF expression in breast cancer cells in vitro and in 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studies have shown that VEGF expression levels decrease after exposure to nitrous oxide during urological surgery.|PMC5513670|according to Pre-operative 0th min VEGF levels decreased (28%) more in the group who were given nitrous oxide than the group (11%) who were not given nitrous oxide suggests that the decrease occurred due to nitrous oxide.|PMC3955540|according to Pre-operative 0th min VEGF levels decreased (28%) more in the group who were given nitrous oxide than the group (11%) who were not given nitrous oxide suggests that the decrease occurred due to nitrous oxide.|PMC3955540|Compared with preop levels, VEGF levels were found to be low at postop 4 and 24 hours in the 30 patients who had mastectomy operation under general anasthesia using nitrous oxide but no statistically significant difference was 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of cells with the histone deacetylase inhibitors (HDACi's) trichostatin A and valproic acid upregulated PGC-1alpha and glucose transporter 4 (GLUT4).|PMID:19118529|Treatment of cells with the histone deacetylase inhibitors (HDACi’s) trichostatin A and valproic acid upregulated PGC-1α and glucose transporter 4 (GLUT4).|PMC2656381|Accordingly, we found that MEF2 and PGC-1α are present in the same neuronal populations in rat brain, and preliminary experiments have shown that valproic acid can increase PGC-1α and GLUT4 expression in mature primary hippocampal and cortical neurons (not shown, RMC).|PMC2656381","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:389e8d54e7909a59dc2f2cfe27316691795fe50270d5bd782d59bad1930e387a","tmkp:50a3685b8ac41c97db37bec583299d5d620a4837ce127c66ac8aae810072ea93","tmkp:3373e2b20dd477f79c8d56cc4f6fa6c886def27bb32973d0a4471412c6a0f76c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9983792833333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:19118529","PMC2656381","PMC2656381"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"37070499":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:2643","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4485422"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:fe53193c6f22628bae11a960960c083e97a5615d81ea497e41d59cd48e246beb"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99947673","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Tamoxifen administration (1 mg per mouse i.p. for 5 days) induced GCH1-HA in all sensory neurons observed 1 week after the end of treatment (Figure 2Q), and the mice developed hypersensitivity to contact heat (Figure 2R) but not to von Frey filaments (Figure S2H).|PMC4485422","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"125576644":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:994","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2874720"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99967384","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Western blot analysis showed that overexpression of the full-length FOXM1 prevented the down-regulation of FOXM1 targets such as CDC25b and PLK in response to tamoxifen treatment.|PMC2874720","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:21275ce6801c30b0ec109ffe2fe5c01b711938fa8e1ec959e2128967d1cd2573"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"68458207":{"subject":"PUBCHEM.COMPOUND:6274","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9980124225","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"His elevated serum interleukin-4 (IL-4), IL-6, IL-12 p70, interferon-γ, and tumor necrosis factor-α returned to undetectable levels four days after surgery.|PMID:21606720|While the His10-Ag group produced significantly more IFN-γ, IL-10, IL-17a, IL-2, and IL-4 compared to the PBS group (Fig. 6a,b).|PMC5288705|C) Both CFP-10:Fcγ2a- and CFP-10:His immunized groups showed increased level of IL-4 production, as a marker of Th2, compare to BCG and PBS control groups (P<0.05).|PMC5339651|His elevated serum interleukin-4 (IL-4), IL-6, IL-12 p70, interferon-γ, and tumor necrosis factor-α returned to undetectable levels four days after surgery.|PMID:21606720","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c91fd16b61fe588c51df2e681a6dc87660017f58b6833a203c78a7d6f97550a2","tmkp:6a72d5621de7f9500f0eaca4e130089d1193e8a22ba5a6e8ae86e1056f5a37b5","tmkp:79281e2079e4b45d151d1ddc03efee36ecc3afa82b6b563b60032a706eb6f587","tmkp:a98d75308440023b9e7933ab2c7b4cb678f4401014f07096bc774c3bcd28c65c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:21606720","PMC5288705","PMC5339651","PMID:21606720"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"28907807":{"subject":"NCBIGene:596","object":"PUBCHEM.COMPOUND:5743","predicate":"biolink:increases_response_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:10200551"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"increases 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treated cells showed increased levels of p-MEK, p-ERK1/2, p-p38, p-Elk-1, p-JNK and p-c-Jun.|PMID:27032574|ALA increased heme oxygenase-1 (HO-1) to protect vascular smooth muscle cells, ameliorated glucose/glucose oxidase- (G/GO-) induced injury of rat cardiomyoblast, inhibited adipocyte differentiation, protected cortical neurons from 4-hydroxy-2-nonenal- (HNE-) mediated oxidative damage and neurotoxicity, and promoted neurite outgrowth via activation of Erk.|PMC6446120|However, Erk signaling activated by ALA has been reported to protect cardiovascular system and nervous system.|PMC6446120|ERK1/2, p38, and SAPK/JNK pathways were activated by ALA/SFC and their specific inhibitors significantly reduced ALA/SFC-mediated HO-1 upregulation.|PMID:27693692|In our studies, a series of n-3 (ALA, DHA, and EPA) and the agonist TUG-891 had similar ability in activation of ERK1/2.|PMC4449883","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"31606870":{"subject":"PUBCHEM.COMPOUND:89594","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Previous literature has suggested that nicotine down-regulates the expression of growth factors like VEGF, PDGF, TGF-β1 and TGF-β2 but has a less significant effect on inflammatory markers like TNF, IL-6 and IL-12.|PMC6411046|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Theiss et al. demonstrated that the expression of collagen type I and II genes, bone morphogenetic protein (BMP), BMP-2, BMP-4, BMP-6, basal fibroblast growth factor (FGF), and the vascular endothelial growth factor (VEGF) was decreased by a systemic nicotine administration in rabbits through a posterolateral spine fusion with the autogenous bone graft.|PMC8038608|Similarly, VEGF expression was also significantly decreased in the 2 μM nicotine, 1 μM and 2 μM cotinine as well as 1 μM and 2 μM nicotine-cotinine mixtures (326.24 ± 25.77, 216.83 ± 31.58, 156.45 ± 20.87, 188.39 ± 18.28, 150.18 ± 18.06 pg/ml, respectively) in a dose-dependent manner, when compared to the vehicle control (367.96|PMC5466671|Plasma vascular endothelial growth factor (VEGF) levels and lung VEGF mRNA expression decreased with advancing age, and nicotine exposure insignificantly decreased plasma VEGF levels and lung VEGF mRNA expression, compared with the control rats during the study period.|PMID:22245234","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3563266","PMID:18472096","PMC6411046","PMID:11839560","PMC8038608","PMC5466671","PMC3432052","PMID:17369603","PMID:22245234"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9714ef705b45dc5d950a0455829306048d06e86c91b6d79868826aa066f5d6cc","tmkp:974dcc188aee7fa939fd8e0b42a9fe7292b4ee9bb904fcfac5b9bb2bc4c7eab5","tmkp:8dfd2441ff7a6a4ea9ba4023965f9af84e8920866fbac26de0905354a59be8ff","tmkp:4ef57ab73ba5a38be8684ecac897b01054749bccdaccdf9dff4ba13d802718bd","tmkp:6ab274edeb4a70ffb9be93324c5079e815560cefb9f4a172a7c8135126a96cb3","tmkp:4647598222efba747d62819062d1adf2471b9ff54e2aca8e5754f3b7021927ea","tmkp:3ae9dff27c82ba3ab2da0813af502c9ec7378e68d2999127170ed1cb0d8cb2ce","tmkp:c980b648cd6023b175e672417561ff25accc15813bd378f532a21c335e259ddc","tmkp:db48b7ec7a9dd3339e2320d802be750baec4b5456389450321f6a92d4b80f58f","tmkp:715cb7e792bcb71e10809fba0961f243fd0ce308c80166e4ebc2a13d0f1abfe3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9955639083333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"23987955":{"subject":"PUBCHEM.COMPOUND:5988","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:53d6869d4700935a7b15025858d85c7d69d1704714ddc159050ed5b23d7437dd","tmkp:43bb7948549ae1d3d76f46d73fb9235cfef56c02637cc4eae1ce49b13dd5f659","tmkp:03c50f728e32a59a5f0a963452280daf3e9945798b050900d0fd74d25fac932d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC7462922","PMID:16555472","PMID:9566602"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99163928","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Increased mRNA levels of GLUT1 (1.6- and 2.6-fold, respectively) and GFAT1 (about 1.7-fold) in gastrocnemius, and of ACC1 (about 1.5-fold) in soleus, were found in both the sucrose and fat groups.|PMID:16555472|Cerebral microvessels from rats treated with DEX/sucrose demonstrated increased GLUT1 and brain glucose extraction compared to controls.|PMID:9566602","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"66942529":{"subject":"PUBCHEM.COMPOUND:253602","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3754951","PMC8056003","PMID:11323415","PMC3610382","PMC7001243","PMC4227232","PMID:23261849","PMC3158843"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a9a7050ec7f867ab90384bd0c0cb912667431c18937e92cb88feb564061e5465","tmkp:ecf6213a2011388553b47f05f68a31c6b42b7e9b85f567e55cd355510a17561a","tmkp:dad5382530ec75a94d4079c6589c6546b398f29aaf2e2597bfb240e55a919b61","tmkp:b3912b6ab9b013750b9317e1f5de48cbacb93d166d93bf32cee443f17d4df763","tmkp:af473cbe9449b69335964a9672e870ee39ddcf79281d90e80d4c14e2f4f8adcc","tmkp:dcfef4c755544920fbd65f0cd4a11bb42633789088d3571483582af344952823","tmkp:42e7191f4c5b5330ea916ad53f754668fd6120c3e55619819eed88023a841669","tmkp:46f664f31879f7c91ff6ee4c76dce29645857300003f51d36b5007f0125b006c","tmkp:4e5be828dbe24c6f4f14714bbc2fe02bd72fbf2d04810755f1ecbfe17fd3a256","tmkp:aa5c83b24c2ad181dff41a872c8e7d8ce34843463426ab657222b1d51dc976aa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9877208266666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Anisomycin treatment led to the down-regulation of Bcl-2 expression at the transcriptional level, and the over-expression of Bcl-2 inhibited the apoptosis induced by the combination treatment of anisomycin and TRAIL.|PMID:23261849|Results indicate that anisomycin, a potent activator of the stress kinase JNK/SAPK, can induce Bcl2 phosphorylation at Ser(70) and that JNK1 can be latently activated following IL-3 withdrawal to mediate Bcl2 phosphorylation.|PMID:11323415|HO-1-UCMSCs and anisomycin activate the JNK/Bcl-2 signaling pathway, and the changes above can be reversed.|PMC7001243|To confirm that Bcl-2 phosphorylation was in fact JNK-mediated, we silenced JNK expression using siRNAs, and again, anisomycin-induced Bcl-2 phosphorylation on Ser70 was detectable at 60 minutes in mock transfected cells (Figure 2D).|PMC3158843|Anisomycin-induced increases in Bcl-2 Ser70 phosphorylation were not impacted by pretreatment with 10µM Tat-Scramble (Figure 3E).|PMC3158843","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"86457996":{"subject":"UMLS:C2702371","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99378708","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:1170877","PMID:6368152","PMID:6198228","PMC3792009","PMID:1936626","PMID:2677227"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:90af6f7dd430537e072350051510348f2f0a1230c7729bbfa255916437d59974","tmkp:11dee5389163bd0910695ec995ba46dc79e480a1f621b3c9577c3128035a4064","tmkp:e7ab962c25a2e12b226a8a3bd8b469e06502dd86d357916de5a04b6367950d49","tmkp:eaaee3edd5b5bf697d4152c141d7704d05ff7ffb9105266e76eaa75cd4eb3e41","tmkp:124c3a1a29a9157cb6b046194b4305558957fe9f197b4b733c9d923a212e37c4","tmkp:3554e6aabc059107683c5594b5b57bea3507b99efc6e02a921ec1afed5496ea8","tmkp:26cb5cb2ee58a4ad9bef598d6562b2f80151190a22b29de3c71281f89e8fecfc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"As 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results further demonstrate that NGO-PEG-PEI/Cer has the capacity to reduce levels of multidrug resistance-related proteins and Akt, phospho-Akt, c-Jun, phospho-c-Jun (Figure 4C).|PMC6376252|Our results further demonstrate that NGO-PEG-PEI/Cer has the capacity to reduce levels of multidrug resistance-related proteins and Akt, phospho-Akt, c-Jun, phospho-c-Jun (Figure 4C).|PMC6376252|Ola-PEG inhibited the BM-MSC-dependent up-regulation of p-ERK, p-Akt and p-Src in MM cells, and also similarly affected Akt-downstream targeted proteins (Figure 6D).|PMC4194173|Further work revealed that NGO-PEG-PEI/Cer may play a role in subverting multidrug resistance (MDR) in HCC cells by inactivating MDR and Akt signaling.|PMC6376252|Notably, ola-PEG treatment exerted a stronger effect when used in combination with bortezomib: in particular, ola-PEG was able to overcome the bortezomib-dependent activation of p-AKT, together with a more pronounced inhibition of Akt-downstream targeted proteins (p-S6R; 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ticagrelor treatment also significantly increased the IL-10 protein level and decreased VEGF protein level in ischemic tissues.|PMC8052144|Furthermore, ticagrelor treatment significantly increased the IL-10 protein expression and inhibited the VEGF protein expression in ischemic tissues of IL-10+/+ mice.|PMC8052144|Furthermore, the possible mechanisms underlying the effect of ticagrelor were associated with its functions of attenuating the expression levels of VEGF and EGF, as well as suppressing the phosphorylation activation of ERK1/2, P38 and nuclear factor-κB P65.|PMID:29042978|The major results of the study showed that IL-10 negatively adjusts angiogenesis induced by ischemia, and ticagrelor inhibits the angiogenesis and blood reperfusion recovery, significantly increases IL-10 level, and reduces the VEGF expression in the IL-10+/+ mouse ischemic hindlimb, which were abolished in IL-10−/− mice.|PMC8052144|In addition, ticagrelor significantly decreased the ulcer-stimulated 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and the increase in AM and ICAM in the lumbar spinal cord of pSNL-injured mice.|PMC4132096|The present study found that, among MAPK pathways, intrathecal AMD3100 downregulated spinal phosphorylation level of JNK1 and p38, but did not affect ERK1, ERK2 or JNK2.|PMC4132096|Western blotting revealed that intrathecal AMD3100 decreased the phosphorylation level of the JNK1 (C), p38 (E) and p65 (H) pathway, but did not affect the phosphorylation levels of the ERK1 (A), ERK2 (B), JNK2 (D), AKT (F) or STAT3 (G) at hour 8 after the injection.|PMC4132096|Moreover, intrathecal AMD3100 downregulated the activation of JNK1 and p38 pathways and the protein expression of p65 as assessed by western 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activation of HER1 is required for the insulin-induced increase in expression of the HER1 ligands heparin-binding epidermal growth factor-like growth factor, amphiregulin and epiregulin.|PMID:17116246|The chronic oral heparin use alleviated the course of severe alloxan diabetes in rats, by contributing to the reduction of hyperglycemic levels, to the elevation of blood insulin concentrations, thus promoting their higher survival.|PMID:8657446|Plasma insulin responses where higher (P <0.05) in the Liposyn/heparin+EAA group than the saline+EAA group both before (14 +/- 4 vs. 6 +/- 1 microIU .|PMID:19454587|Several therapeutic trials revealed that (1) intravenous regular insulin improved her metabolic control; (2) continuous subcutaneous infusion (CSII) treatment with regular insulin or insulin lispro caused hyperglycemic period with hypoinsulinemia and hypoglycemic period with hyperinsulinemia alternately; (3) adding heparin to insulin lispro in CSII resulted in dramatic increase of serum insulin level and improvement of glycemic control; and (4) regular insulin plus heparin in CSII could not increase serum insulin level and thus the glycemic values was not improved.|PMID:11689276|Liposyn/heparin infusion resulted in a 9.4-fold increase in plasma FFA concentration (from 132 to 1,237 mumol/l), a 46% increase in insulin secretion rates (from 241 to 352 pmol/min, P < 0.05) (determined by deconvolution of plasma C-peptide concentration), and a 30% decrease, during the initial 24 h, in the rate of glucose infusion needed to maintain hyperglycemia (from 55.5 to 39.1 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and PPVII activate p38MAPK, thereby increasing Cyt-c expression; as a result, caspase-9 also becomes activated.|PMC7956893|20(S)-25-OCH3-PPD promotes ERK1/2 activation via phosphorylation, and correspondingly activates the MAPK signaling pathway for the prevention of ER stress-induced cell death.|PMC7212460|LPS signals through CD14 via the TLR4-MD-2 pathway whereas PPD triggers the MAPK (ERK1/2/P38) pathway mostly via TLR2 signalling.|PMC4425930|20(S)-25-OCH3-PPD promotes ERK1/2 activation via phosphorylation, and correspondingly activates the MAPK signaling pathway for the prevention of ER stress-induced cell death.|PMC7212460|These studies highlighted that 20(S)-25-OCH3-PPD could activate the ERK/MAPK pathway and reduce the effect of ER stress on liver and kidney 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subsequent study utilizing the same animal model found that chronic levodopa treatment induced expression of vascular endothelial growth factor (VEGF) in the basal ganglia in a dose dependent fashion.|PMC4314428|Using a validated rat model of l-dopa-induced dyskinesia, this study demonstrates that chronic treatment with l-dopa dose dependently induces the expression of vascular endothelial growth factor in the basal ganglia nuclei.|PMID:21771855|The use of l-DOPA, a small molecule drug shown to up-regulate VEGF in the Parkinsonian brain, can potentially resolve these issues by substituting for VEGF.|PMID:27261334|Animal models have also evidenced that chronic l-dopa treatment induced expression of vascular endothelial growth factor (VEGF) in the basal ganglia in a dose-dependent manner.|PMC8001922|Animal models have also evidenced that chronic l-dopa treatment induced expression of vascular endothelial growth factor (VEGF) in the basal ganglia in a dose-dependent 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RT-PCR and Western blot revealed that the treatment effects of risperidone and haloperidol seemed to be mediated through activation of VEGF and MMP2.|PMID:19579000|The findings indicate a promoting effect of risperidone and haloperidol on survival of young neurons in the hippocampus by enhancing the expression of the anti-apoptotic protein BCL-2 and by activation of VEGF/MMP2, whereby an interference with ketamine and thus a priority role of the NMDA system was not evident.|PMID:19579000|Moreover, in a previous study we showed that administration of risperidone was able to increase VEGF expression and angiogenesis in the hippocampus of 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K analogs, NSC 663284, naphthofurandione 3-benzoyl-naphtho[1,2-b]furan-4,5-dione (5169131), adociaquinone B, IRC-083864, and BN82685 are the most potent CDC25B inhibitors reported to date; however, none of these compounds have entered clinical trials for ovarian cancer 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the other hand, collagen IV and fibronectin levels are comparably increased in both sexes by tamoxifen treatment.|PMC6768287|Moreover, Cortes and his colleagues demonstrated that tamoxifen treatment reduces the hypoxic response of PSC, leading not only to a reduction of fibronectin alignment and thickness, which are associated with lower cellular invasion, but also to an increase of fibronectin protein expression in in vitro experiments.|PMC7072496|Similarly, Yuan et al found that β1 integrin and fibronectin were markedly increased in tamoxifen resistant as opposed to tamoxifen sensitive MCF7 breast cancer cells.|PMC5370511|Comparative gene expression analysis of RNA samples isolated from organoid culture of Lgr5-EGFP-CreERT2; Ppp2r1aflox/flox mice 50 days after DMBA and tamoxifen administration revealed marked upregulation of stem cell genes, such as Lgr5, CD44, Ephb3, Egr2, Notch1, and Sox4; as well as EMT markers, such as Snail1, Snail2, Twist1, fibronectin, and vimentin; and a 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agreement with these observations, our data revealed that treatment with propranolol initiated the intrinsic apoptotic pathway in IHECs, as shown by the increased release of cytochrome c and AIF into the cytoplasm and the enhanced cleavage of caspase-3 and 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SK-N-SH.|PMID:12820377|It was demonstrated that dexamethasone and montelukast significantly induced apoptosis of lymphocytes and eosinophils which were assocreased with increased expression of Fas antigen and caspase-3.|PMID:14633444|In this study, we report hormonal induction of FAS mRNA in human fetal lung explants (16-23 week gestation) cultured up to 7 days in Waymouth's medium (no serum) supplemented with dexamethasone (Dex, 10 nM) or agents that increase cAMP (8-Br-cAMP, 0.1 mM; isobutylmethylxanthine, 0.1 mM; forskolin, 0.01 mM; PGE1, 0.01 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glomerular tuft area, glomerular volume, MVD, VEGF protein expression in glomeruli and VEGF mRNA expression in the renal cortex tissue were significantly increased in diabetic rats and finasteride-treated rats when compared with controls (P < 0.01, P < 0.05).|PMID:25789687|The glomerular tuft area, glomerular volume, MVD, VEGF protein expression in glomeruli and VEGF mRNA expression in the renal cortex tissue were significantly increased in diabetic rats and finasteride-treated rats when compared with controls (P < 0.01, P < 0.05).|PMID:25789687|MVD, VEGF, and HIF-1alpha values were significantly lower statistically (P <0.001) in group 1 compared with group 2. In the finasteride group (group 1), the positive correlation of the immunoreactivity of CD34 and HIF-1alpha, VEGF and HIF-1alpha, and VEGF and CD34 was statistically significant (P <0.001).|PMID:16904480|MVD, VEGF, and HIF-1alpha values were significantly lower statistically (P <0.001) in group 1 compared with group 2. In the finasteride group (group 1), the positive correlation of the immunoreactivity of CD34 and HIF-1alpha, VEGF and HIF-1alpha, and VEGF and CD34 was statistically significant (P 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oxygen and nitrogen species cause damage to DNA, which activates PARP-1.|PMC4348018|Reactive oxygen species, responsible for the most plausible and currently acceptable global mechanism to explain the aging process, strongly activate the enzymatic activity of PARP1 and the formation of poly(ADP-ribose) (PAR) from NAD(+).|PMID:20157531|Reactive oxygen species, responsible for the most plausible and currently acceptable global mechanism to explain the aging process, strongly activate the enzymatic activity of PARP1 and the formation of poly(ADP-ribose) (PAR) from NAD+.|PMC2806023|In the inflammatory processes, the oxygen and nitrogen free radicals that are released result in DNA damage that leads to the constant activation of PARP-1 and consequently to the depletion of the cellular levels of NAD+ and ATP.|PMC4539103|Levin et al. studied 5 gliomas and reported that low oxygen elevates the levels of HIF1, PARP1-cleaved Src, p-AKT-273, and p-AKT-308.|PMC3777891","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"129090258":{"subject":"PUBCHEM.COMPOUND:6468","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:19766705","PMC2760688","PMC7519454","PMC2643957"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:25869fb7fbcbd7a975efeaefbed6e922802268d08c4e19b8dfbb17e8204ef677","tmkp:dc979e7bde9b8999ac8a9f685f9cca2651e2d5895475192f87430bfaa71772a7","tmkp:9d09410e5ac9f43c6d5ba9ef5cc7bbc5f34a0229f647c43191a6d0ae4c649ecf","tmkp:1eb4d41122e6403eb4ea524d1b0c75fd0813b83ff4b2b68d62f604425c437487","tmkp:277086dde6c9551192771526a926b5ed156db5c5f6acff8e9bdb9e2c49f58b14","tmkp:de42e9dd20780e8e87dc8ff2224fa956a8ec2b2b1c602d13584f8a10dd478e5b","tmkp:68b17305e0581bae76897a242258abcdee22b8b7b29e550d0c0ff3db2baa3cc4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9996951000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In conclusion, the treatment of alcohol liver with PCP mainly inhibited the activity of CYP2E1 enzyme, PI3K/Akt promoted Bcl2, and Bax-related apoptosis regulator, and inhibited the expression of caspase 3 protein to play an antiapoptotic role.|PMC7519454|Moreover, fluorimetric assay of the caspase-3 activity revealed that 2,4,5-TCP, chlorocatechols and TeCG in the range of the concentrations of 1-50 ppm increased the caspase-3 expression, whereas PCP in its highest concentration of 50 ppm decreased the activity of this enzyme.|PMID:19766705","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"8587316":{"subject":"NCBIGene:5599","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:b16faada3bcef77f5d701f36aea2d2de112dc2b97059181296abd9684397c411"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:11790785"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9840438","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In 293(PED) cells, decreased apoptosis induced by anisomycin and H(2)O(2) was also accompanied by block of JNK1/2 and p38 phosphorylations, 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authors describe bilateral and sequential pigment epithelial detachment (PED) formation in a 16-year-old girl with ABCA4-associated Stargardt's disease (STGD1).|PMID:23883535|Optical coherence tomography-guided morphological analysis of lesion development in ABCA4 disease with documentation of PED formation may suggest a plausible role for disruption at the level of Bruch's membrane in the pathophysiology of 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the asthma model, the percentages of IL-4 expressing cells and the serum levels of OVA-specific-IgE in the La1-treated and water-treated group were significantly increased compared with those in the control group.|PMID:21810385|Both IL-4 and IL-17A AUC values were significantly increased after an SFA high-fat meal intake, accompanied by water, but not by orange juice.|PMID:29068453|IL-4 level significantly increased after exercise in warm water (p = 0.003), while there was no significant change after exercise in temperate and cold water.|PMID:30256758|Similarly, in mouse models of AD, application of metallic soaps and water led to increased levels of IgE and proinflammatory cytokines, including IL-4, IL-5, IL-13, TSLP, and TGF-β.|PMC7355223|Results indicated a strong trend toward increased serum IL-4 in the EtOH-fed septic relative to water-fed septic animals (p = 0.05, Fig 11B), and a statistically significant increase in both IL-6 and IL-10 in the sera of EtOH-fed septic relative to water-fed septic animals (Fig 11E and 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the down-regulation of genes ACC1, TSC13, FAS1 in KM exposed in ethanol (Groups ⑥ and ⑦), is accordant with the previous report, which may account for K. marxianus’ weak ethanol tolerance before adaptive evolution.|PMC6429784|Moreover, alcohol consumption resulted in significantly lower percentages of effector memory (CD95+CD28-) CD8 lymphocytes as well as activated Ki67+CD8 cells in the intestines.|PMID:16652027|However, chronic ethanol intake resulted in remarkable decline of the protein levels of ACC, phospho-ACCser79, and FAS, which was significantly suppressed by CMZ co-treatment.|PMC4043914|CMZ co-treatment significantly suppressed ethanol-induced decrease of ACC and FAS protein levels and further increased DGAT2 protein levels, which indicated that CMZ co-treatment might suppress the decrease of de novo fatty acid synthesis and further enhance the TG synthesis.|PMC4043914|The ethanol extract of C. indium showed a dose-dependent suppression of PPAR-γ, CEBP-α, and FAS expression 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contrast, light chain 3 II and beclin-1 levels were significantly less and those of cleaved caspase-3 significantly greater in the 3-methyladenine group.|PMID:28624177|However, pretreatment with 3-methyladenine (3MA) a specific inhibitor for autophagy, remarkably strengthened FPN toxicity and further induced activation of caspase-3 in these cells.|PMID:24008047|Moreover, cardiomyocytes pretreated with 3-methyladenine conferred resistance to the cytoprotective effect of miR-19a and displayed notably increased TUNEL staining and caspase-3 activity.|PMID:27220268|Exposure to autophagy inhibitor, 3-methyladenine, led to a reduced expression of these markers with a concomitant increase in the expression of pro-apoptotic caspase-3.|PMID:29603067|When heat shock was combined with 3-methyladenine (3-MA), an inhibitor of autophagy, the mitochondrial loss and the reduction of total cytochrome c were both inhibited, and then caspase-3 activation and cell apoptosis were 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Analysis of TSLP mRNA in ears of mice treated with ethanol or MC-903 for 1, 3, 4 and 5 days and a comparison of induction TSLP and CYP243A1, a known Vitamin D-dependent gene, after 4 days of application of ethanol or MC-903 to the ear.|PMC4297686|(A) Acute alcohol (EtOH) increases c-fos signals in the A1–A2/C1–C3 cell region, identified by DBH.|PMC3176674","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9631459","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"86076893":{"subject":"PUBCHEM.COMPOUND:9871419","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Meanwhile, exosomes from CPC precondition with ticagrelor show improved antiapoptotic activity through the activation of the ERK1/2 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Italian pedigree in which three members in the same generation were affected by rolandic epilepsy, paroxysmal exercise-induced dystonia (PED), and writer's cramp was subsequently reported.|PMID:11520321|along with dry pellets from the same lot for 7 days and observed for clinical signs of PED.|PMC6714588|An Italian pedigree in which three members in the same generation were affected by rolandic epilepsy, paroxysmal exercise-induced dystonia (PED), and writer's cramp was subsequently reported.|PMID:11520321|We describe a pedigree in which 3 members in the same generation are affected by Rolandic epilepsy (RE), paroxysmal exercise-induced dystonia (PED), and writer's cramp (WC).|PMID:10072049","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9491056","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"6637629":{"subject":"UMLS:C5242471","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9993131","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:66813a28340014ba7561c0f59b364abe45dc0992df736052088b9fffff7119b9","tmkp:f9678b451e856cde2ac9c8628db59f7f22dc2c4cd370c59a5d2a93df90771896","tmkp:7d775870b84c40693f9a0e622ef42381f185b0797aeefc9c3090ba9786323cfa","tmkp:4adde0c1eb6bb3d1d379be3629ed9b455eef53e342d928855a2f80393478a584","tmkp:df625b4eba00a0b27f14652cea721da956a11662d7198903bfd380b45cdbb882"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:18641189","PMC4637187","PMC3145778","PMID:9276788"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The 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TGF-beta1 and I procollagen in human normal dermal and hypertrophic scar fibroblasts cultured in vitro.|PMID:16463783|In pulse-chase experiments, adrenaline was shown to inhibit the maturation of HL from the 53 kDa, Endo H-sensitive precursor to the Endo H-resistant, catalytically active protein of 58 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neonicotinoids on promoter-specific CYP19 expression were due to an action on the PLC and/or MEK/MAPK 1/3 pathways, we determined the promoter-specific expression of CYP19 in Hs578t cells treated with either thiacloprid or imidacloprid () in the presence of a selective inhibitor of either the PLC (U73122, ) or MEK/MAPK 1/3 (PD98059, ) 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blood glucose was not affected, serum insulin was increased (P = 0.047) by PEG feeding.|PMID:15644506|Patients co-treated with pegvisomant (SSA+PEG, N=4) had a numerically increased secretion of insulin and glucagon compared to patients on SSA (N=11) during OGTT (insulin AUC mean (SEM), SSA+PEG 49 nmol/l*min (8.3) vs SSA 25 (3.4),|PMC7207322|Mice treated by PEG-SMLA had higher insulin levels at the both 0 and 30 minutes compared to non-treated mice (Figure 4C).|PMC3965386|Moreover, insulinoma cells encapsulated with polyethylene glycol added with collagen IV and laminin induced a significant increase in insulin secretion when compared with cells inserted in standard capsules.|PMC3680884|PEG-MLA also reduced systemic and mucosal inflammatory cytokine expression, increased insulin levels and enhanced systemic and mucosal Tregs in mice with chronic 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MQA inhibited NMDA-induced phosphorylation of ERK1/2, p38, and JNK1/2.|PMID:26096046|Ca2+-mediated activation of c-Jun N-terminal kinase and nuclear factor kappa B by NMDA in cortical cell cultures|PMC3003258|Ca2+-mediated activation of c-Jun N-terminal kinase and nuclear factor kappa B by NMDA in cortical cell cultures|PMC2518916|Ca2+-mediated activation of c-Jun N-terminal kinase and nuclear factor kappa B by NMDA in cortical cell cultures|PMC3146341|Ca2+-mediated activation of c-Jun N-terminal kinase and nuclear factor kappa B by NMDA in cortical cell 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found that 6-month L-arginine supplementation resulted in significant decrease of PAI 1. Significant increase of NO, TAS, and insulin sensitivity level were noticed.|PMID:22732180|In contrast, L-arginine+ramipril reduced morning plasminogen activator inhibitor-1 antigen (10.8+/-9.5 ng/mL) and the molar ratio of plasminogen activator inhibitor-1:t-PA (2.3+/-1.6)|PMID:16432054|In contrast, L-arginine+ramipril reduced morning plasminogen activator inhibitor-1 antigen (10.8+/-9.5 ng/mL) and the molar ratio of plasminogen activator inhibitor-1:t-PA (2.3+/-1.6)|PMID:16432054|After the 1st and the 7th infusion of L-ARG the spontaneous (PAR) as well as the ADP- and collagen-induced platelet aggregation were suppressed, the euglobulin clot lysis time (ECLT) shortened, plasma levels of platelet activator inhibitor (PAI) decreased, and cGMP levels increased.|PMID:8867484|All disease measures except proteinuria and including matrix accumulation, TGF-beta, fibronectin and PAI-1 production and mRNA expression for TGF-beta, fibronectin and PAI-1 were significantly and similarly reduced by about 50% in groups treated with L-arginine or with low protein 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with doxycycline in drinking water will drive an increase in the expression of VEGF that results in severe vascular leakage and exudative retinal detachment within 4–5 days.|PMC6939309|The mRNA expression levels of CRT, VEGF, and GAP43 were confirmed by real-time PCR and were increased after doxycycline treatment.|PMC5593816|VEGF levels were higher after the injection of TGF-beta(2) than after administration of talc or doxycycline.|PMID:11779736|Upregulation of FGF-2 synthesis by addition of doxycycline resulted in a dramatic increase in VEGF expression.|PMC2132998|Liver peliosis-like phenotype and thymus degeneration are associated with the doxycycline-induced overall VEGF-A-164 expression in adult pCAGGS-CreTg/+, ROSA26-rtTA-IRES-EGFPTg/+, tet-O-VEGF-A-164Tg/+ mice.|PMC1069131","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"120070259":{"subject":"PUBCHEM.COMPOUND:5280343","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999318912","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:27477310","PMID:15735102","PMC2820992","PMC6213637","PMC3338068","PMID:21787598","PMC4148366","PMC5000709","PMID:30203888","PMC6129317"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In addition, quercetin selectively activated the c-Jun N-terminal kinase (JNK) pathway in KRAS-mutant cells, while inhibition of phospho-JNK by SP600125 blocked quercetin-induced apoptosis.|PMID:30203888|Additionally, quercetin activated c-Jun N-terminal kinase (JNK) in a dose-dependent manner, which in turn induced the proteasomal degradation of cFLIP, and JNK activation also sensitized pancreatic cancer cells to TRAIL-induced apoptosis.|PMID:27477310|Furthermore, quercetin may activate the MAPK pathway (ERK 2, JNK1, and p38) leading to expression of survival and defensive genes (i.e., glutathione-S-transferase, etc.) resulting in survival and protective mechanisms (homeostasis response; Kong et al.,).|PMC3338068|But low concentrations of quercetin could also promote cellular survival by activation of the MAPK pathway (ERK2, JNK1, and p38), leading to expression of downstream survival genes (c-Fos, c-Jun) and defensive genes (phase II detoxifying enzymes; GSH S-transferase, quinone reductase).|PMC2820992|In summary, quercetin and ellagic acid combined increase the activation of p53 and p21(cip1/waf1) and the MAP kinases, JNK1,2 and p38, in a more than additive manner, suggesting a mechanism by which quercetin and ellagic acid synergistically induce apoptosis in cancer 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in a chronic de novo treatment with non-human primates, we observed increases in both striatal pERK1/ERK1 and pERK2/ERK2 ratios of l-DOPA-treated MPTP monkeys whereas MPEP prevented this increase.|PMC4122180|L-DOPA-activation of ERK2 in the dopamine depleted striatum is not significantly reduced in DARPP-32 knockout 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expression analysis revealed elevated levels of angiogenic vascular endothelial growth factor in the clopidogrel group.|PMID:30801550|In addition, NXT protected HUVECs against clopidogrel-induced cell death by inhibiting expression of tumor necrosis factor-like cytokine 1A and activating expression of vascular endothelial growth factor α. Taken together, our study indicates the potential application of NXT in antithrombosis by multiple antithrombotic 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serum VEGF and TGF-β concentration in PPA group was significantly lower than that in SGA group (P < 0.05).|PMC6882595|The serum VEGF and TGF-β concentration in PPA group was significantly lower than that in SGA group (P < 0.05).Thoracic paravertebral nerve block-propofol intravenous general anesthesia can reduce the dosage of opioids, improve the effect of postoperative analgesia, and reduce the serum concentration of tumor angiogenesis-related factors in patients undergoing radical resection of lung cancer.|PMID:31764844|The expression levels of VEGF and TGF-β in PPA group were significantly lower than those in SGA group 24 h after operation (P < 0.05).|PMC6882595|The expression level of VEGF in PPA group was significantly lower than that in SGA group 24 h after operation (P < 0.05), and the level of TGF-β in PPA group was also significantly lower than that in SGA group (P < 0.05).|PMC6882595|There was no significant difference in serum levels of VEGF and TGF-β between before and after operation in PPA 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insulin secretion was induced by doxycycline in a dose dependent manner.|PMID:12126552|Immune reactive insulin (IRI) level in cell medium was found increased at 24 hours of doxycycline incubation, and still increased at the 5th day.|PMID:15669184|(H-J) Akita-INS cells were transduced with shCtrl or shPDIA6 (clone 1) lentiviruses and Akita insulin expression was induced with 2μg/mL doxycycline (Dox).|PMC3977204|Where indicated pro-insulin expression was induced by doxycycline (DOX 20 ng/ml) and the cells were exposed to 0.3 mM BSO (18 h).|PMC5368998|The cells secreted insulin at the rate of 9.7 U/24 h/1.0 x10(6) cells without doxycy cline treatment, and the amount of secreted insulin increased to 241.0 U/24 h/1.0 x 10(6) cells (25-fold) in the presence of doxycycline(1 000 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VEGF secretion from cardiac microvascular endothelial cells induced by AngII.|PMC4876321|When evaluated at 7 days after stroke, inhibition of VEGF was partly abrogated followed by improvements in infarct volume and behavioral functions in PFT-α 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reduces p38 activation in thymocytes after the stimulation of concanavalin A, decreases p53 synthesis by inhibiting Src or MAPK activation, or decreases the phosphorylation of p38 and NF-κB in macrophages.|PMC6053945|Interestingly, ouabain suppressed the phosphorylation of ERK1/2 in the presence of CoCl2 (Figures 7E,F).|PMC7544989|Nevertheless, ouabain not only inhibited EGF-induced Erk1/2 and Akt signaling, but also reduced EGF-induced cell motility, and prevented the morphological changes in the actin cytoskeleton that were induced by EGF.|PMC4302666|Indeed, ouabain inhibited EGF-induced Erk1/2 and Akt activation and, moreover, prevented EGF-induced formation of actin stress fibers and cell motility, probably by activating a stress signaling response.|PMC4302666|However, in medulloblastoma cells, ouabain did not transactivate EGFR as has been reported in other cell lines, and ouabain inhibited EGF-induced Erk1/2 and Akt activation (Wolle et 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this experiment, intermittent treatment with bevacizumab induced less OA progression, as shown by both histological and gene expression assays, through increases in the gene expression of ChM-1 and VEGF in the articular cartilage and decreases in the gene expression of MMP 13 and ADAMTS5 in the synovium.|PMC4189677|Unexpectedly, this clinical trial definitively disproved our hypothesis that continued VEGF suppression would occur with the sequential combination of these two agents, as VEGF levels continued to rise with subsequent and continued treatment with sunitinib and bevacizumab.|PMC4200479|Similar increases in plasma VEGF concentration have been observed following treatment with bevacizumab.|PMC4402130|Plasma levels of VEGF, P1GF, and sVEGFR2 significantly and persistently increased after bevacizumab and chemotherapy treatment (at days 15 and 43; VEGF and P1GF also were increased at day 71 and end of study), although plasma bFGF was transiently increased only at day 15; plasma sVEGFRl, IL-lb, IL-6, IL-8, TNF-α, and urinary MMP activity did not significantly change at any of these time points (Table 3 and Supplementary Tables S3 and S4).|PMC3151740|Gordon et al. reported that the intravenous injection of bevacizumab led to an increase in serum total VEGF in clinical trials while free VEGF concentration was 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confocal images showed that NMDA-PC increased MDM2 levels expression after OGD and prevented OGD-induced activation of caspase-3 (Fig. 4c).|PMC5785500|In contrast, NMDA treatment decreased mRNA and protein levels of caspase-3 in these neurons.|PMID:15093730|In contrast, NMDA substantially inhibited staurosporine-induced caspase-3 activity on 7 DIV in neocortical and hippocampal cultures.|PMID:16153713|Densitometric analysis of the immunoblots showed a significant reduction in the caspase-3 mediated SBDP120 levels in NMDA+3-MA co-treated cultures as compared to NMDA-treated cells (Fig 9B).|PMC2836363|Here, we show that NMDA-PC prevents ischemia-induced apoptosis and caspase-3 activation in Pro72-p53 neurons, but fails to protect Arg72-p53 cortical neurons against 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the observed reduced tumor destructive effect of MTX/MNPs in comparison to MNPs is not fully explainable, protein analyses suggested a more unfavorable expression pattern (eg, elevated p-ERK1/2, BCL-2, VEGF, and MMP2) after MTX/MNP treatment, resulting in a progression of cell cycle as indicated, for example, by cyclin A.|PMC5388224|We found a slight upregulation of VEGF-R1 in the MTX/MNP group, indicating the insufficiency of this treatment to impair VEGF-R1 expression and inhibit tumor growth.|PMC5388224|LDE-MTX increased the expression of myocardial vascular endothelium growth factor (VEGF) associated with adenosine release; this correlated not only with an increase in angiogenesis, but also with other parameters improved by LDE-MTX, suggesting that VEGF increase played an important role in the beneficial effects of LDE-MTX.|PMID:28553113|Presence of ultrasound subclinical synovitis and increment of serum vascular endothelial growth factor in a patient with rheumatoid arthritis achieved in sustained clinical remission by treatment with adalimumab and methotrexate.|PMID:24533548|LDE-MTX increased the expression of myocardial vascular endothelium growth factor (VEGF) associated with adenosine release; this correlated not only with an increase in angiogenesis, but also with other parameters improved by LDE-MTX, suggesting that VEGF increase played an important role in the beneficial effects of LDE-MTX.|PMID:28553113","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"117975664":{"subject":"PUBCHEM.COMPOUND:10297","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Poly(phosphoramidate-dipropylamine) (PPA) and Lipid-Protamine-DNA (LPD) nanoparticles consistently showed the highest level of human insulin mRNA expression and luciferase protein expression in these 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with ibuprofen or piroxicam in combination with l-dopa preserved the effect of l-dopa at the end of week 10, delayed the development of dyskinesia and decreased striatal COX-2 and VEGF levels.|PMID:27016022|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off at the end of week 10, delayed the development of dyskinesia, and decreased striatal cyclooxygenase-2 (COX-2) and vascular endothelial growth factor (VEGF) levels.|PMC8150526|When co-administered with l-dopa, a small molecule inhibitor of vascular endothelial growth factor signalling significantly attenuated the development of dyskinesia and completely blocked the angiogenic response and associated increase in blood-brain barrier permeability induced by the treatment.|PMID:21771855|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off at the end of week 10, delayed the development of dyskinesia, and decreased striatal cyclooxygenase-2 (COX-2) and vascular endothelial growth factor (VEGF) levels.|PMC8150526|Furthermore, animals treated with candesartan along with l-dopa were characterized by lower levels of VEGF, IL-1β, and less severe dyskinesia compared to animals receiving only l-dopa.|PMC8001922","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996017671428571","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"99163138":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:d734a1733deab60624cef04f024cdb7fd3c101d1099c3547dc7704df182a651a","tmkp:82e2a374634f5a49a5e1b575be34ec17c9dbd007df65584607cba3c5a4d33452","tmkp:c093c5d3700e11ce2c34110ff24095153ac0e35375b3c5a7f2ec1c1ad7b6fbfc","tmkp:edc07fec92ad20e41a3f18b6a0580a5f50323a839b03387cd81734fe31d7a40f","tmkp:d5e6289d12940d65374380967cad98636fbb2b755100f2d82d9d2b84abce8212","tmkp:6d372ae4a647e7d29fc271896ccbe55c74257c1e78d85deca76749d6ddd8878e","tmkp:5ebc043d61b9409e512d6ca251435fa275cbe4b634eac1339bf2d8792e2ce313","tmkp:bf0fb60870bd8b54022a8ceff227ae5e577852cb63e0be9e4b0f5f554252f5b8","tmkp:7650c4124e6bff0bc7e0a1fb8b22d9f8c5dc55767e1c4aa5e224274615734523","tmkp:d7d2e7d5d365a5c64a9d16229b77711410ccc7cb932a4ecb1ceb26f5401311be"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Indeed, in resistant HCC patients ERK1/2 activity was highly increased after 21 days of treatment with sorafenib.|PMC3858550|Sorafenib treatment also caused up-regulation of p-c-Raf Ser338 and p-extracellular signal-regulated kinase (ERK) Thr202/Tyr204 in gastric cancer xenografts.|PMID:19723882|Morphometric analysis and statistics, shown in the bar graphs, revealed that treatment with sorafenib significantly increase Ki67 and ERK1/2.|PMC3460040|However, sorafenib elicited the upregulation of phosphorylated Erk1/2 and STAT3-pY727 in CRPC.|PMC4438623|Expression of IGF-1Rbeta and phosphorylation of c-Raf Ser338, MEK1/2 Ser217/221 and ERK1/2 Thr202/Tyr204 were increased by sorafenib 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relative expression of Vascular Endothelial Growth Factor (VEGF) in the propranolol group was significantly higher than that in the control group on the 2nd day (p<0.05),|PMID:31173327|The largest increase in expression was evident after 48 hours of treatment with 100 μM of propranolol (approximately 3.5-fold increase in HIF1α, approximately 15-fold increase in VEGF expression, and approximately 15-fold increase in GLUT1 expression; p < 0.0001).|PMC7265978|Propranolol leads to a discordant increase in VEGF mRNA expression while also reducing intracellular VEGF protein expression due to interference with VEGF mRNA translation.|PMC7265978|Propranolol Induces HIF, VEGF, and GLUT-1 mRNA Expression in VHL-HB Cells|PMC7265978|Some researchers indicated that isoproterenol (a β-adrenoceptors agonist) could not decrease aortic microvessel sprouting, while propranolol caused increase in VEGF-mediated microvessel 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high-fat diet-fed mice, vascular inflammation and insulin resistance were completely prevented by sildenafil administration at a dose that had no effect in mice fed the low-fat diet.|PMID:20093624|Sildenafil treatment, with or without l-arginine, resulted in lower fasting insulin and glucose levels and enhanced rates of glucose infusion, disappearance, and muscle glucose uptake during a hyperinsulinemic (4 mU x kg(-1) x min(-1))-euglycemic clamp in conscious mice.|PMID:17229936|Although the effect of HF-feeding to raise fasting plasma glucose and insulin levels was attenuated by daily sildenafil treatment (Figure 3B and C), this intervention did not significantly alter body weight (Figure 3A).|PMC3342311|Our laboratory and others have shown that, in mice, sildenafil increases endothelial NO signaling (by inhibiting degradation of cGMP), reduces several markers of insulin resistance while restoring hepatic insulin signaling, prevents Kupffer cell M1 activation during HFD feeding, and 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previous study using a chronic model of Pseudomonas infection of the lung in rats had shown that L-arginine given in drinking water resulted in lower IL-1β concentrations in BAL fluid in the L-arginine treated compared to the untreated group, whereas VEGF was increased.|PMC3940779|A previous study using a chronic model of Pseudomonas infection of the lung in rats had shown that L-arginine given in drinking water resulted in lower IL-1β concentrations in BAL fluid in the L-arginine treated compared to the untreated group, whereas VEGF was increased.|PMC3940779|Following the L-ARG treatment, the expression of the pro-angiogenic factors (VEGF and FGF-2) was higher and the expression of anti-angiogenic factors (endostatin) was lower than the vehicle-treated animals.|PMID:28078001|The productions of vascular endothelial growth factor, basic fibroblast growth factor, prostaglandin E(2), and matrix metalloproteinase-2 were higher with Arg 100 and 1000 micromol/L than with Arg 0 and 50 micromol/L Arg, and this was consistent with the expression of CD51/CD61 by ECs.|PMID:20071141|VEGF and cGMP levels in the L-arg-treated group were also significantly greater than those in the control 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tumours by inhibiting the expression of vascular endothelial growth factor (VEGF).|PMC7694406|(A) Schematic of possible ways by which VEGF can block MET activation.|PMC4068350|Met-F-AEA has been shown to decrease levels of VEGF and VEGFR-1 in K-ras-transformed thyroid cells and in experimental tumors of xenografted nude mice.|PMC3366283|Finally, MET appears to have a paradox effect on angiogenesis as it promotes or inhibits expression of the pro-angiogenic vascular endothelial growth factor (VEGF) depending on breast cancer subtype.|PMC5405996|In conclusion, we found a reduced expression of VEGF and HIF-1α in the MET NVB + Endo group and a higher expression of VEGF and HIF-1α in the MTD NVB + Endo 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a separate study, we have observed significant reduction in ERK2 phosphorylation of endothelial progenitor cells (EPCs) in HCC patients after sorafenib therapy (unpublished work).|PMC4986927|MAPK1 (ERK2) and MAPK3 (ERK1) are downstream of HER2 signaling as critical components of the oncogenic RAF/RAS/MAPK pathway and can be inhibited with the FDA-approved drug sorafenib.|PMC4193948|A previous study has shown the downregulation of ERK2 phosphorylation in the PBMC of HCC patients treated with sorafenib alone or in combination with octreotide long-acting release (LAR).|PMC4986927|Interestingly, sorafenib treatment under low glucose condition reduced Erk2 protein levels by a currently unknown mechanism (Fig. 3D).|PMC2651576","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC2651576","PMC4986927","PMC4732463","PMC4193948"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99969671","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:bb7f888430afed02c58c52969810e05b3246b46f02966339b0834f71f3dbe7ea","tmkp:fced083292092dc7c42f0ec7947a4134605a4c92b8dd792b459d1142e105f9f2","tmkp:e5cafdc5083699a1f821cb214b2311e08c1970df5785c8b5f69928c060a39cad","tmkp:5496a08c756587d3a29c9b405aa7fcd1c3f1f5d7d590d3e9c5e6b6a18f2295e1","tmkp:38d20d0d20d0247e4c4c358e6e7aef085ad1e1e64c0b0a94b60aa87505de9f51","tmkp:7ab0fbc7a59d345b7076022de6479620819aff7a0845dcd345924dcec5e97d2b","tmkp:da3d8c77e540118ff1d82e51a14f862ce3d0a7899f72629a8ded7182a8000295","tmkp:eed4b920bbeda191568378b2f4060a7636fcf3e2250b26287fa143af58f53dad","tmkp:2471b6aa4761b47c375ce49238babd83010040263577915e2c44580eca47b515"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"93746717":{"subject":"PUBCHEM.COMPOUND:3033","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:30406888","PMC3832653","PMID:25644785"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8f78f3482cd0b736147f604edfbfaa385ed6ae333849ad27a7dfee291423efc2","tmkp:eb942f444922a247bf7da97d3dde28a8d7a202a9bb2a50d24301ccda9c10cc0d","tmkp:c546e3398a621b86f3a2eed532fefc59529222c47b23480d609afbdba14f41d2","tmkp:c2257f4ffcd29a1d0eab1ad29ef21889562bb1b78342ab52b5a14c337dc98808","tmkp:93edee4b2c87d132bfa624bcc2402baa69d1876c221f3194eecb419e6b2efdf8","tmkp:34683d4d626404df9c783650f54ac998b6458d68e20b968ef171bd79a3730e95"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9991959","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Diclofenac 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administration leads to increased VEGF-induced phosphorylation of SHP-2 and this increased phosphorylation parallels the increased phosphatase activity of SHP-2.|PMID:19706677|Activation of the dopamine (Dp)/dopamine receptor 2 (Dp-r2) pathway was involved in the VEGF/VEGFR-2 signaling process and can reduce neoangiogenesis.|PMC6191968|Dopamine stimulation slightly decreased the surface expression of vascular endothelial growth factor receptor-2 (VEGF-R2) but induced the phosphorylation of VEGF-R2 through Src in 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the use of ALA in combination with other anti-oxidants agents accelerated the skin wound healing with increased expression of vascular endothelial growth factor (VEGF) in the wound area.|PMC4124142|VEGF and IL-10 serum levels, both before and after ALA-treatment, were higher in this group than in T2DM and CAD patients, while circulating bFGF was higher and MCP-1 serum level lower in patients with T2DM and CAD and DSPN only in the post-ALA-treatment, compared to the T2DM and CAD group.|PMID:25511715|Compared to the control group, red light group, and ALA group, the levels of TGFβ-1 and VEGF in the ALA-PDT group were higher than those in the control group on the 3rd, 7th, and 14th days after treatment (P < 0.05) (Figure 5).|PMC7746815|Moreover, the use of ALA in combination with other anti-oxidants agents accelerated the skin wound healing with increased expression of vascular endothelial growth factor (VEGF) in the wound area.|PMC4124142|Furthermore, in comparison with the control group, the number of blood vessels and VEGF-positive cells in treated groups with GLN and Ala-GLN were significantly 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tolvaptan and OPC-31260 inhibitmitogen-activated protein kinase (MAPK) signaling which may mediate the proliferative response to cAMP in the kidney.|PMC3313734|Upregulation of NAD(P)H oxidase p22(phox), p47(phox), and gp91(phox), EMT markers such as transforming growth factor-β1, vimentin, and fibronectin expression, and Rho-kinase and ERK1/2 phosphorylation in DS rats were significantly suppressed by 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treatment, and VEGF111b protein was detected by our homemade VEGF111b polyclonal antibody.|PMC4480579|Our data showed that the number of fibroblast, capillary density and fibrotic tissue in the 0.5 and 0.7mg/ml MMC groups was significantly lower than the control, 0.1 and 0.3mg/ml MMC groups; while the expression of VEGF in control and 0.1mg/ml MMC groups was notably higher than 0.3, 0.5 and 0.7mg/ml MMC groups.|PMID:22056834|After culturing for 24 h, the VEGF levels in RPE cells in the BVZ and BVZ + 5-Fu groups were significantly lower than that in the control group, while the VEGF levels in the 5-Fu and MMC groups significantly increased (Figure 2).|PMC6151201","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:676e3d3ca37b22cf7fa7e9ff4f9cb6bd5c8253eb1eee98179bd70056fc50e644","tmkp:9422c199b2f8a89f6d59b099759ca6340cb4d043ecf3dedee1b7a06e33f1f6c3","tmkp:6aed46112e6e5c341e0aba805e33380088a17a60300304f8ceb4a21d9884eb36","tmkp:b2011ac9baebd32f8a1de24c0eadbd415c8c759f0b72fc21468b84b3e3944249","tmkp:c84a7376ecaf15aca876a0f853346fd6fe22dede7a41c3e6a45340368a76d9ae","tmkp:a2cdc7f4769a465c2556e1790f253dd09f0f8a69fd62087a15cbbef2909ecafd","tmkp:67230106c172c1560a2ff9e47493c873671ecd11b178db971b0e7df0b71e1fb3","tmkp:e581614d9a6cb731d6816f324dfbcfcb7c46dc2419848e41155f14702ee4a4f5","tmkp:f314ac3074969b2d9daf67cdf5d2f3f64a9f20ecc71ed51f6e497f8ae96d0c05","tmkp:248ee7323ee8f910b14d6d95d7272c5cd1285d1e0be46983ee9462c674d8cdff"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6925728","PMC6863018","PMC6151201","PMC6885197","PMID:20735383","PMC5444031","PMID:22056834","PMC7474357","PMC4480579","PMC6150649"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.6509727265810398","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"36407440":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:d15e41f6dfeaa8545a68b179d1724c5a62dd93fd4ede43440afe4bdb46f5f4f3","tmkp:6143ab9973d4d2eb3f6339a016165382632f106646f89521a6dbc4a51e569043","tmkp:bab68693e52e7c92c5f4a1f163caf0db0292a5c731791cafa7843e95974a8508","tmkp:8c67716b5972941350ddb0d0e159d9fb095ddc7d94615e6d92674c2953c8082d","tmkp:7672d13ec1350b2cd4c02460162f489faa6a9f6c59bcf7a231d27d87b7cc31b0","tmkp:f83f67c8e57353c4a3afcde4433bbac99edc46b23f5695d68772aa2621239ddf","tmkp:a7915fdffe13b5b08fb853398efa65983f19667c857e57d2e72c4181ef36a8c0","tmkp:f60f1e992be2a8c6a87051d7d08850109242382a0cafd78f56009e6dd8304e23","tmkp:f18904aac15b78c5528651c07e74c6c3c68943da5663f1ca92d6f55509c17937","tmkp:f0d6a47e001f3eaf9c4d20b72855f4f6996c26d3847b34eae2bc098091013e72"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC8230691","PMC5520887","PMC3860369","PMC2908017","PMC4745697","PMC3574194","PMID:22025881","PMC4575108","PMC4252022"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"More importantly, we observed that p-c-Raf and p473-Akt were increased in sorafenib-treated cells in a concentration-dependent manner, even though apoptosis occurred as mentioned in Figure 1 (Figures 2c and d).|PMC3860369|The phosphatidylinositol 3-kinase (PI3K)/Akt pathway cross-talks with the Raf/MAPK/ERK pathway, and represents a key signaling pathway activated in hepatocarcinogenesis. Sorafenib activates Akt and its downstream factors such as ribosomal protein S6 kinase (S6K) and eukaryotic translation initiation factor 4E-binding protein 1 (4EBP1) in HCC cells.|PMC4745697|In a previous report, we showed that sustained sorafenib treatment could activate Akt in both human HCC patients and mouse HCC models.|PMC4575108|Sorafenib induces reciprocal upregulation of Akt phosphorylation; and simultaneous inhibition of downstream mTOR with rapamycin leads to synergistic effects.|PMC2908017|We found that treatment with sorafenib induced upregulation of p-c-Raf and p473-Akt in a time-dependent manner.|PMC3860369","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9958831556521739","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"36274391":{"subject":"PUBCHEM.COMPOUND:977","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:f0feda0506d11a63860f80ebc4f73dceca0a0f0ec79f4f3287befaef7b614a5c","tmkp:5264571691eaf2be1834034545881e72854c6894208f3efd6fd2c3ab36f0663a","tmkp:49eb31ce2a3f39c003bfc0e51a6355bf586ee366609c7e9c34fb2819e4755a70","tmkp:a09c80514ea56fdf69aaa2be29015d59c2c02d97d0ef261ce1ac0ab234752da0","tmkp:98919f3bb2efbc2a17e29f22aaf3ece2a9d496f7f80cc48b3528484396e22f04","tmkp:75a1402f2b8a8462c83d2215b0ccc701745cc5fc24a560152b57a741a0285373"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Compared with HTK-flushed kidneys, organs preserved using oxygen-precharged HTK-perfluorohexyloctane emulsion had increased elevated adenosine triphosphate content and a significantly lower gene expression of hypoxia inducible factor-1α, vascular endothelial growth factor, interleukin-1α, tumor necrosis factor-α, interferon-α, JNK-1, p38, cytochrome-c, Bax, caspase-8, and caspase-3 at all time points assessed.|PMID:22795349","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9997004","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6375284","PMC3906848","PMID:22795349","PMC6004101","PMID:21324895"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"25396876":{"subject":"PUBCHEM.COMPOUND:24759","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Therefore, a combined treatment with polynucleotides and hyaluronic acid was able to restore Bcl-2 positivity in basal colonic-restored crypts of the DNBS + Poly + HA group (Figure 7D).|PMC7589719","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9989818","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9746f97d3993eec80bf7ba3fecd27323dd9a26f9d132b4c562e22d7e139ae4d2","tmkp:7e42b156e1e3d03946404e04fcc38507bc259c6e072a7c5d13d41b57b36f936a","tmkp:41777cee7081dac082ffa75aa3adaa2508a6363a28841b3c3347b8307f681995","tmkp:66556ead145d97799a994645258b6ca44ba96d7ccccb91e05ffb3beaba33d148","tmkp:d6262448a9f5116d98d9023c2d1a9eca7f69c2e955331c518800572b733cd1a5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6953059","PMC7332498","PMC8036762","PMC7589719"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"29112079":{"subject":"PUBCHEM.COMPOUND:253602","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"These observations show that stretch, IL-1beta and anisomycin activate the same components of the MAPK cascade, but differentially activate LAP and liver inhibitory protein (LIP) perhaps accounting for the increase in OTR by stretch and anisomycin but not IL-1beta observed in this study.|PMID:17348037","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c4eab7d3107794e14c44032b932183f4944baf7e0a7d01cdd48990c6c92c934c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:17348037"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99757546","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"87458398":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"During MMC treatment, targeting of CCN2 improved cytotoxicity of MMC and promoted MMC-induced apoptosis, probably by inhibiting activation of proliferation-related Erk1/2 and survival-related Akt pathways.|PMC5630414|Effect of specific inhibitors of Wnt, Hedgehog, PI3k, NF-κB, JNK, ERK, MAPK, and Notch on Bcl-2 expression that was decreased by the combination treatment of curcumin and MMC. a MCF-7 BCSCs were treated with specific inhibitors of Wnt, Hedgehog, PI3k, NF-κB, JNK, ERK, MAPK, and Notch for 12 h.|PMC5615796|A decrease in thymidine phosphorylase, ERCC1 and RAD51 can also be observed with this combination and with mitomycin C and curcumin, which is due to the inhibition of ERK1/2 activity and an increase in their ubiquitin-mediated 26S proteasome degradation.|PMC7710985|When treated with mitomycin C (MMC), CCN2-scilencing UBC cells showed lower survival and higher apoptotic rates and these effects were probably mediated via inactivation of Akt and Erk pathways.|PMC5630414|In conclusion, the current study provided evidence that MMC and curcumin combination treatment reduced MMC side effects by inhibiting GRP58-mediated DNA cross-linking through the ERK/p38 MAPK pathway.|PMID:19703194","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:edf289c375ede1d2dbd896ad66bab7619ae991d548d1e0f9c98f3ed9d62caa07","tmkp:adfa5d88d6fc8cacce52e94c21fe2e2ef5eefba00e43de169bbe17967c1f9d02","tmkp:370af0d4fccc07accd30e887a08035503f056574793ed42af96a61265c0c565f","tmkp:a424bfb736e28c2c86d894090795cc31f96601b7a3d5f5deb7b8b6c2b296f49b","tmkp:203d9010238855dbee1eb11f39cd0d5421d64884b48b3edce79261e141f397da","tmkp:d574eb2c5c4e6850ad2a3aa69394ad461c663e1410e207f75d22558d504a3f7f","tmkp:90ac4d404ce51e29f4ee82a813fc8fdadda0564bf93fcbdc5f67c4ebde7692ce","tmkp:39b0c3659a6cae6673675740267e72c77b876b8736e5ce6b32fcbd818b4e4c96","tmkp:fc50c9b70ac0e79ac9850e386319251fdf2c7684937fd80a99e77065f2e735e1","tmkp:21d4d9b0665c9f01d2ee07e49d15acddd82bfa4d4162114660c5d3aea00bee1a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9851977133333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5630414","PMID:18544565","PMC3330700","PMID:25938833","PMC7710985","PMC5615796","PMID:19703194","PMID:20130020"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"112742918":{"subject":"PUBCHEM.COMPOUND:5755","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9994605","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Increased production of TGF-beta1 was seen in skin lesions after 6 months of prednisolone treatment.|PMID:15908402","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:15908402","PMID:11728950"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a3a19c8fe35c531cf361f421665f13672577d038a946547b2927a9cb8fd46418","tmkp:6d92173b3875ce605a5d5660de415834aa4e23975152730eeab80951a17d4d76"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"59315081":{"subject":"PUBCHEM.COMPOUND:22833565","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:31738878","PMC3669540","PMID:22082677","PMID:19893601","PMC4287728","PMC7695853","PMC5330685","PMID:10023691","PMC2958111"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"An increased VEGF-A level in the ocular fluid (11.3-fold increase) in the heparin-injected eyes with reduced NV (reduction by 80.8%) was observed in OIR models, which was attributable in part to the resistance of heparin-bound VEGF-A to proteolysis, but not increased transcription of mVegf.|PMC2958111|NO, HGF, VEGF and G-CSF levels were increased after heparin administration.|PMID:31738878|The heparin-dependent induction of angiogenesis by HMGB1 was accompanied by increases in the expression of tumor necrosis factor-alpha (TNF-alpha) and vascular endothelial growth factor-A120 (VEGF-A120).|PMID:19893601|This indicated that increased VEGF-A in the ocular fluid of heparin-treated eyes occurred by post-transcriptional mechanisms.|PMC2958111|In addition, heparin significantly increases expression of a series of growth factors, including FGF14, FGF20, BDNF, IL6 and VEGF, but not FGF2 (Fig. 3C and data not shown) as well as the expression of a number of cell surface proteins, including ITGA6 (integrin α6) and NGFR, but not ITGA5 or ITGB3 (Fig. 3C and data not 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with ibuprofen or piroxicam in combination with l-dopa preserved the effect of l-dopa at the end of week 10, delayed the development of dyskinesia and decreased striatal COX-2 and VEGF levels.|PMID:27016022|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off at the end of week 10, delayed the development of dyskinesia, and decreased striatal cyclooxygenase-2 (COX-2) and vascular endothelial growth factor (VEGF) levels.|PMC8150526|When co-administered with l-dopa, a small molecule inhibitor of vascular endothelial growth factor signalling significantly attenuated the development of dyskinesia and completely blocked the angiogenic response and associated increase in blood-brain barrier permeability induced by the treatment.|PMID:21771855|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off 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later study by the same group followed up patients with GLUT1 deficiency syndrome between 18 and 41 years 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clonidine reduced ipsilateral neuritis-induced hypersensitivity in a delayed manner (3 days after treatment), along with a reduction at this time in lymphocyte number and an increase in caspase-3 and TGF-beta1 expressing cells and macrophages co-expressing TGF-beta1 in the sciatic nerve.|PMID:17079113|One day after injection clonidine treatment was associated with a reduction in lymphocytes and pro-inflammatory Th-1 cells as well as increased numbers of caspase-3 and TGF-beta1 expressing cells and macrophages co-expressing TGF-beta1 in sciatic nerve.|PMID:17079113|One day after injection clonidine treatment was associated with a reduction in lymphocytes and pro-inflammatory Th-1 cells as well as increased numbers of caspase-3 and TGF-beta1 expressing cells and macrophages co-expressing TGF-beta1 in sciatic nerve.|PMID:17079113|Peri-neural clonidine reduced the increase in tissue content of the proinflammatory cytokines IL-1beta and particularly TNFalpha in sciatic nerve, DRG and spinal cord while increasing concentrations of the anti-inflammatory cytokine TGF-beta1.|PMID:14499442|Perineural clonidine reduced ipsilateral neuritis-induced hypersensitivity in a delayed manner (3 days after treatment), along with a reduction at this time in lymphocyte number and an increase in caspase-3 and TGF-beta1 expressing cells and macrophages co-expressing TGF-beta1 in the sciatic 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vitro, TGF-beta1 protects neurons against excitotoxicity by inhibiting the t-PA-potentiated NMDA-induced neuronal death through a mechanism involving the up-regulation of the type-1 plasminogen activator inhibitor (PAI-1) in astrocytes 4. In addition, TGF-beta1 has been recently characterized as an antiapoptotic factor in a model of staurosporine-induced neuronal death through a mechanism involving activation of the extracellular signal-regulated kinase 1/2 (Erk1/2) and a concomitant increase phosphorylation of the antiapoptotic protein Bad. 5. Altogether, these observations suggest that either TGF-beta signaling or TGF-beta1-modulated genes could be good targets for the development of new therapeutic strategies for stroke in man.|PMID:14514014|In vitro, TGF-beta 1 protects neurons against excitotoxicity by inhibiting the t-PA-potentiated NMDA-induced neuronal death through a mechanism involving the up-regulation of the type-1 plasminogen activator inhibitor (PAI-1) in astrocytes.|PMID:12910629|(R)-ketamine, but not (S)-ketamine, ameliorated the reduced expressions of Tgfb1 and its receptors (Tgfbr1 and Tgfbr2) in the PFC and hippocampus of CSDS susceptible 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ethanol exposure also resulted in significant increases in mRNA expression of NOX regulatory subunits, including p22phox, p67phox, NOX activator 1 (NOXA1), NOX organizer 1 (NOXO1) and a Rho-family small GTPase RAC1 (Fig. 2).|PMC2822117|Here, we report that ethanol increased the surface area of growth cones in a dose-dependent manner, which is consistent with activation of Rac1 and Cdc42 that has been shown in other studies to correlate with protrusion of F-actin-rich lamellipodia and filopodia in the growth cone.|PMC3117431|These findings are consistent with an effect of ethanol that reorganizes the growth cone cytoskeleton, and implies that Rac1 and Cdc42 could be activated.|PMC3117431|In addition, the ethanol treatment significantly increased mRNA expression of the NOX regulatory components, p22phox, p67phox, NOXO1, NOXA1 and RAC1.|PMC2822117|For example, exposure of 7-day-old rat pups to ethanol for 3 hours moderately increases BAC (approximately 40 mM) and inhibits neurite 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data indicate that the CRISPR/Cas9-mediated depletion of VEGFR2 expression is alternative to that of either aflibercept or ranibizumab in blocking VEGF-induced activation of Akt in HRECs.|PMC5338630|Another study demonstrated that application of Ranibizumab protected rabbits from developing PVR via suppressing PDGFR/PI3K/Akt signaling.|PMC8064804|Furthermore, as expected, both aflibercept and ranibizumab blocked VEGF-induced activation of Akt, but this blocking was less effective than that with K12-sgRNA/SpCas9–mediated depression of Akt activation (Fig. 3C).|PMC5338630|We next compared the efficiency of editing the genomic VEGFR2 locus using CRISPR/Cas9 with aflibercept (800 μg/mL) or ranibizumab (200 μg/mL) in blocking VEGF-induced activation of Akt and its downstream effectors (e.g., p-BAD and Caspase 9).|PMC5338630|In addition, there were lower levels of Akt phosphorylation in HRECs with VEGFR2-sgRNA/SpCas9 than those with LacZ-sgRNA/SpCas9, and there was less VEGF-stimulated Akt activation, proliferation, migration, or tube formation in the VEGFR2-depleted HRECs than those treated with aflibercept or 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results suggested that prednisone is able to protect podocytes from apoptosis, and reduce urinary protein levels by inhibiting the FAK/RANKL/MAPK signaling pathway in kidney tissue samples.|PMID:26459042","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9997365","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"66221477":{"subject":"UMLS:C2740652","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:1ba0991a64bb840c935d31e9b46a38a98b62356b3e4bc67ddf67d92de298c01b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"In STZ-induced male Sprague Dawley rats, eight days of treatment with onion peel extract (1%) significantly (p = 0.0148) improved glucose tolerance, liver and skeletal muscle glycogen content (p < 0.0001 and p = 0.0089, resp.), and insulin receptor (p = 0.0408) and GLUT4 (p = 0.0346) expression in muscle tissues.|PMC5046019","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5046019"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999166","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"130215192":{"subject":"CHEMBL.COMPOUND:CHEMBL2052016","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:d14c4957698d9a88e60a4405d1506fd9c3d989d3b6f8f1bbd8bace8bcfc27f0c","tmkp:60977f95e5b8c48d31eb8c794d071166dda538abf6ba9839bd7433132cdee961","tmkp:a604c7b86f802a95a6cee676b3432f492f4de5d83ac0c14dc656380fd54dc773","tmkp:8c4943634c4f004bfeffe05533f1dde71b831151b7fd40b5477a69cb734c5744","tmkp:4518f9237421090a9f2b5477c545f1a2397969d56fa754b13212f0ffb01b6dab","tmkp:0084bcd0a7b81fc9816a49ddc069943ff890841ca01a1979ce54c72c81e9b15c","tmkp:d87b653bf81cb712cead1ad5507e8e86d6944d91b20d93578e82f4a699a314e6","tmkp:b95c56e773143457ea02379786f7fccd86ea6ef68c68bda817b00f5185d40d74","tmkp:8894049fe90617310c5ec37827d2bb1dec3f12b297fefea19360f79932fa952e","tmkp:ef8ddfb20eabf1961cf8dbd30817e12ad8184f4a8ec71b43cc302df95aec2625"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"A similar 6-fold decrease in mouse VEGF was observed in animals treated with Verteporfin-PDT followed by anti-mouse VEGF, but bevacizumab had no effect on mouse VEGF levels (Figure 2B).|PMC4476543|To understand the mechanism underlying the antiangiogenic effect of the combination therapy, we analyzed angiogenesis-associated genes in zebrafish embryos and found a significant reduction in vascular endothelial growth factor A (VEGFA) and the VEGF receptor after treatment with verteporfin and CA4.|PMC7791049|VERTEPORFIN DOWN-REGULATES YAP-TEAD CONTROLLED CELL MIGRATION AND ANGIOGENESIS FACTORS CYR61,CTGF AND VEGF-A|PMC4135181|Therefore, verteporfin can inhibit VEGF-induced YAP pathway activation by inhibiting YAP activity.|PMID:31633245|The present review is divided into two major sections: the period prior to the use of anti-VEGF agents (triamcinolone acetonide, verteporfin photodynamic therapy) and the period following their introduction (pegaptanib sodium, bevacizumab, ranibizumab, aflibercept).|PMID:23560774","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC5701552","PMC2693977","PMID:31633245","PMC2693972","PMID:16987905","PMC4476543","PMC7791049","PMID:19220205","PMC4135181","PMID:23560774"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9994671009999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"74985165":{"subject":"PUBCHEM.COMPOUND:2244","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7352791","PMC3223940","PMC6202076","PMID:28216620"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In addition, ASA significantly inhibited CF apoptosis, and decreased the levels of apoptosis markers (cleaved caspase 3 and Parp1), which might serve as a side effect of anti-fibrotic effect of ASA.|PMID:28216620|Changes in Bcl-2, BAX, PARP1, Cyclin D1 and P21 protein expression in RA-FLS treated with aspirin are shown: Bcl-2, PARP1, Cyclin D1 and P21 were decreased while BAX was increased, each with increasing aspirin concentration.|PMC6202076|Intracellular PARP1 content also decreased with increasing aspirin concentration (Fig. 5A).|PMC6202076|The study proposed by Professor Dion could include a combination of aspirin with a poly (ADP-ribose) polymerase 1 (PARP1) inhibitor (PARP1 is involved in cell proliferation and differentiation and DNA repair).|PMC3223940","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a21a5ae8fd511f125c506904820f2156de78c331ef6b7995c6433bc5bb1c1388","tmkp:5b2fffb51cb4a93341a5a7da5fea5aff7a6cf0392d2e9098c1d938d19d98b3af","tmkp:334b215cd1695699ee9eb14ff021ce81ff43c2f4d5050503ec60801ce06d041f","tmkp:780c96090db9620b10a8d3a866434959f1120b216f922b68896408838ddc6010","tmkp:40ecb41ceb255f6fd409f5b77af3ad20ae9a4ef6713f503b20b8338610c55254","tmkp:12b185c51f3f6f79072b6099a61cd4951b21a7400d22dcf6115321386179ac7d","tmkp:1e950ba4b0faa9e7bd0fffe5e85d1404a5e7c6a31a2dba4ee0b9cde604423ccf"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9892463499999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"19872894":{"subject":"PUBCHEM.COMPOUND:135398737","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:30103309","PMC3604003","PMC5372297","PMC3897763"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"The higher levels of IL-4 in patients treated with Clozapine might be due to effects of this antipsychotic drug on immune responses.|PMID:30103309|In stimulated blood from healthy donors, clozapine treatment increased levels of IL-4 and IL-17.|PMC3604003|Clozapine has previously been shown to decrease production of IFN-γ and enhance IL-4 and IL-10 in poly (I:C)-stimulated PBMC cultures from schizophrenia patients, which suggests an effect on CD4+ T cell differentiation.|PMC5372297|Haloperidol and quetiapine significantly increased the IL-4 levels (p<0.05) in LPS-stimulated PBMC cultures, while clozapine and quetiapine significantly enhanced the IL-4 levels (p<0.05) in poly(I:C)-stimulated PBMC 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administration leads to increased VEGF-induced phosphorylation of SHP-2 and this increased phosphorylation parallels the increased phosphatase activity of SHP-2.|PMID:19706677|Activation of the dopamine (Dp)/dopamine receptor 2 (Dp-r2) pathway was involved in the VEGF/VEGFR-2 signaling process and can reduce neoangiogenesis.|PMC6191968|Dopamine stimulation slightly decreased the surface expression of vascular endothelial growth factor receptor-2 (VEGF-R2) but induced the phosphorylation of VEGF-R2 through Src in HUVEC.|PMID:18470912","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"127160552":{"subject":"PUBCHEM.COMPOUND:5284583","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:12b267482ba8c1b1ddf2afc72eb2de60c41f2f9e7dbbbdf35a96a78d55138ff4","tmkp:f8b124324418e9c853ba4411af7637339e9b5ce62d3e9461f80224d2a8f52b4e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Levetiracetam (LEV) increased the levels of vascular endothelial growth factor (VEGF), hypoxia-inducible factor-1α (HIF-1α), and heat shock protein 70 (HSP70) in the cerebral cortex of middle cerebral artery occlusion (MCAO) rats on day 14.|PMC8161206|Levetiracetam (LEV) increased the levels of vascular endothelial growth factor (VEGF), hypoxia-inducible factor-1α (HIF-1α), and heat shock protein 70 (HSP70) in the cerebral cortex of middle cerebral artery occlusion (MCAO) rats on day 14.|PMC8161206","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.999299925","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8161206","PMC8161206"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"88416561":{"subject":"PUBCHEM.COMPOUND:439501","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Interestingly, ouabain suppressed the phosphorylation of ERK1/2 in the presence of CoCl2 (Figures 7E,F).|PMC7544989|Nevertheless, ouabain not only inhibited EGF-induced Erk1/2 and Akt signaling, but also reduced EGF-induced cell motility, and prevented the morphological changes in the actin cytoskeleton that were induced by EGF.|PMC4302666|Indeed, ouabain inhibited EGF-induced Erk1/2 and Akt activation and, moreover, prevented EGF-induced formation of actin stress fibers and cell motility, probably by activating a stress signaling response.|PMC4302666|However, in medulloblastoma cells, ouabain did not transactivate EGFR as has been reported in other cell lines, and ouabain inhibited EGF-induced Erk1/2 and Akt activation (Wolle et al.,).|PMC4362317|We show that while ouabain did not directly affect EGFR and ErbB2 phosphorylation, it inhibited EGF-induced activation of Erk1/2 and Akt 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decreased EGFr (total and activated), ERK1, ERK2, pERK and pP70S6k.|PMC4549030|However, Western blot reveals VPA significantly suppresses ERK2 phosphorylation in adult NSCs grown in proliferating culture conditions and that lithium co-treatment does not attenuate this 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recently reported similar observations for R-flurbiprofen and ibuprofen activation of p38 MAPK up-regulation of p75NTR dependent apoptosis in prostate cancer cells.|PMC2597303|In addition, we show that treatment with R-flurbiprofen or ibuprofen led to sustained activation of the p38 mitogen-activated protein kinase (MAPK) pathway.|PMID:18056468|Treatment with EGCG and ibuprofen also caused activation of MAPK, caspases and the inhibition of Bfl-1 expression, which were blocked by N-acetyl-L-cysteine.. 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In conclusion, our study revealed a regulatory function of camel milk on multiple parameters of inflammatory mediators, immunomodulators, antiapoptosis, and antioxidants, giving insight into the potential therapeutic benefit underlying the anti-HCV actions of camel milk.|PMID:26492130|Immunohistochemistry of Bax, Bcl-2 and proliferating cell nuclear antigen and TUNEL-immunofluorescence assay demonstrated that Lac16 and BSC10 exerted beneficial effects on cell apoptosis and proliferation, as indicated by the gene expression of down-regulated Bax and p53 as well as a significant upregulation of Bcl-2 (P < 0.05).|PMID:31064013|Molecular mechanism underlying apoptosis involved the modulation of Bax and Bcl-2 (Fig. 5f,g), as indicated by the increased Bax/Bcl-2 ratio in cells exposed to milk+δVB (P < 0.01 vs milk) 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we also found that indomethacin activated PKB/Akt and induced nuclear localisation of p21(Cip1/Waf1) and Akt2 isoform.|PMID:19433066|ER stress inhibitor alleviated indomethacin-induced p38 hyperphosphorylation, Akt, dephosphorylation, Mcl-1/FLIP downregulation, caspase 3 activation, and glioma cell viability loss.|PMC7013513|The inhibition of p38 by SB203580 alleviated indomethacin-induced PP2A activation, Akt dephosphorylation, Mcl-1 and FLIP downregulation, caspase 8 and caspase 9 proteolytic degradation, Bax mitochondrial translocation, caspase 3 activation, and cell viability loss.|PMC7013513|Common antioxidant PDTC and calcium chelator BAPTA-AM mimicked the actions of salubrinal to reverse indomethacin-induced p38 hyperphosphorylation, Akt dephosphorylation, Mcl-1 downregulation, FLIP downregulation (Figure 4D), cell viability loss (Figure 4E), and caspase 3 activation (Figure 4F).|PMC7013513|Pharmacological inhibition of ceramide synthase by fumonisin B1 and PP2A by okadaic acid moderately attenuated indomethacin-induced Akt dephosphorylation along with the apoptosis.|PMID:29470962","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"31066006":{"subject":"PUBCHEM.COMPOUND:5743","object":"NCBIGene:3172","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Prenatal dexamethasone exposure caused a permanent increase in hepatic Hnf4a mRNA.|PMID:16570165|Consistently, we observed that HNF4α is induced by dexamethasone in primary human hepatocytes, but not in hepatocyte tumor-derived cell lines.|PMID:24399729|Key to this global effect of Dexamethasone on hepatocyte maturation must be the combined induction of HNF4 (527% increase) and C/EBP α (356%).|PMC1913286|In terms of main findings, dexamethasone induces expression of both HNF4 and C/EBPalpha, essential transcription factors for hepatocyte differentiation.|PMID:12837037|In terms of main findings, Dexamethasone induces expression of both HNF4 and C/EBP-alpha, essential transcription factors for hepatocyte 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4 h after 500 μM ouabain treatment, expression in 15 genes was greatly upregulated (P < 0.05); these genes were Bcl10, Bcl2a1d, Bid, Birc3, Bnip2, Cflar, Nfkb1, Prok2, Ripk2, Tnf, Tnfrsf11b, Tnfrsf5 (CD40), Tnfrsf6 (Fas), Tp53, and Tp73l.|PMC3818842","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99934894","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"113375634":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9855294329411765","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In the same conditions, phosphorylation and activation of ERK-2 were also inhibited.|PMID:9045910|In contrast, the same treatment with paclitaxel resulted in a significant decrease of ERK2 kinase activity.|PMC2375254|At the same time point, the cells showed strong downregulation of YAP/TAZ, EGFR, and ERK2-3 mRNAs after antimiR-33a-3p transfection and Gefitinib co-treatment compared to Gefitinib treated cells (Figure 8B).|PMC6953103|The MEK inhibitor UO126 strongly and reproducibly reduced the expression of Snai2 in all cell lines tested (Fig. 3a) and the same effect was obtained upon ERK1 and ERK2 silencing (Fig. 3b).|PMC6262016|The same concentration of flavokavain A also inhibited the protein kinases Aurora B, DYRK1A, IKKβ, and MK3 more or to a similar extent, while approximately 40–70% inhibition was measured for ERK8, GSK3β, RSK2, MK2, MSK1, p70S6K, PDK1, PHK, PKA, PKB2, PLK1, p38δ, and 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all Cannabis sativa extracts, caspase-3 and caspase-9 were upregulated in all cell lines.|PMC5009497|Western blot revealed that Cannabis sativa hexane extract induced apoptosis via the activation of caspase-9 and caspase-3 when compared to untreated cells in all three cell 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male HFD-exposed rats, blood insulin levels in response to glucose challenge were significantly higher in offspring of nicotine-administered dams than in offspring of control dams.|PMC8220205|Insulin levels induced by glucose infusion were consistently and significantly higher in nicotine-treated mice than those in vehicle-treated mice (Fig. 1a).|PMC4390501|This might explain why acute nicotine treatment raised insulin levels when we observed no difference in insulin after DMPP injection.|PMC7228898|Among females, fasting insulin levels were higher in offspring from the nicotine-administered dams than in offspring of controls dams.|PMC8220205|There was no significant difference in fasting blood glucose among the groups ( Figures 3A, B ). 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OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|However, OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|VEGF protein levels were unaffected in Caki-1 cells treated for 16h with dDAVP, but were significantly reduced by Tolvaptan and OPC31260 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caspase-3 level significantly increased with sildenafil treatment, whereas Ki-67 expression failed to show any significant changes.|PMC5117873|In this study, tumor samples showed low expression of caspase-3 in untreated mice, whereas sildenafil induced significantly more expression of caspase-3 in the tumor cells.|PMC5117873|In contrast to VEGF and Ki-67, caspase-3, the apoptotic marker, was minimally expressed in control group (11.9±1.88); its level of expression was significantly increased in groups that received sildenafil, cisplatin, and combination therapy (45±6.81,|PMC5117873|Our laboratory first demonstrated that co-treatment with sildenafil potentiates antitumor efficacy of doxorubicin (DOX) in prostate cancer, which was mediated by enhanced generation of ROS, up-regulation of caspase-3 and caspase-9 activities, reduced expression of Bcl-xL, and phosphorylation of Bad.|PMC4826214|Caspase-3 and -9 activities were also increased following sildenafil and DOX co-treatment while overexpression of dominant negative procaspase-9 in DU145 cells blocked the enhanced cell killing 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also activates the mitogen-activated protein kinase family member, JNK1, in dose-dependent fashion.|PMID:10823417|However, paclitaxel treatment induced a rapid, although transient, activation (phosphorylation) of JNK1 and JNK2 (Fig. 3c).|PMC6842526|We show here that JNK1 activity is rapidly up-regulated and prolonged by specific mechanisms during apoptosis induced by paclitaxel- or ginsenoside-Rh2 in SK-HEP-1 cells.|PMID:14514687|In line with the predominant expression of JNK1 in astrocytes, we observed a stronger increase in the expression of this isoform after 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study showed that the mRNA and protein expression of GLUT3, rather than that of GLUT1 and GLUT4, were lower in the hippocampus and temporal lobe of young mice 24 h after the third exposure to sevoflurane than in those of control 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an inhibitor of p38MAPK and MEK1/2, inhibited the expression of VEGF protein and mRNA in the RPE cells stimulated with IL-1beta.|PMID:19011889|The inhibitory effect of clonidine on the secretion of VEGF protein stimulated with IL-1beta was blocked by alpha(2)-ADR antagonists.|PMID:19011889|In contrast, α2 adrenergic stimulation by clonidine has been shown to inhibit vascular endothelial growth factor expression in human retinal epithelial cells (Watanabe et al.,).|PMC3933766","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9993563499999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7978382","PMID:19011889","PMC6907244","PMC8234968","PMC3933766"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"36661643":{"subject":"PUBCHEM.COMPOUND:9871419","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999639685","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Further, ticagrelor, but not CAM reduced PAI-1 expression and enzyme activity in TNF-α-stimulated LAA endocardial cells.|PMID:28065908|Ticagrelor, but not CAM, reduces expression and activity of TF and PAI-1 in LAA endocardial cells isolated from patients with AF, indicating possible local antithrombotic 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that study, tamoxifen use was associated with an increase in serum VEGF levels; a result consistent with higher platelet derived VEGF levels in tamoxifen users as compared to nonusers.19|PMC5350889|Tamoxifen 1 g and 3 g resulted in a dose-dependent increase in VEGF and endothelin 1 levels, and ovarian follicle reserves were significantly reduced in our experimental model.|PMID:25848212|Vascular endothelial growth factor (VEGF) mRNA and protein levels were higher in MCF7 breast cancer cells and orthotopic tumors after treatment with tamoxifen, as compared with treatment with estrogen.|PMID:11929808|Vascular endothelial growth factor (VEGF) mRNA and protein levels were higher in MCF7 breast cancer cells and orthotopic tumors after treatment with tamoxifen, as compared with treatment with estrogen.|PMID:11929808|Hormonal regulation of VEGF expression has been demonstrated, and some reports indicate that tamoxifen, a partial estrogen receptor agonist, increases VEGF mRNA in breast cancer 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we showed a 6-fold increase of caspase-3 activity and 3-fold increase of DNA fragmentation with the same dose but shorter exposure (6 h) in our study.|PMC3038597|These same tumors showed increases in the cell death markers, TUNEL-positive cells (p < 0.05) and the enzyme caspase-3 (trend), as well as significant induction of PPAR type gamma (PPARgamma).|PMID:19500378|The same study revealed the up-regulation of pro-apoptotic Bax and caspase-3 and down-regulation of anti-apoptotic Bcl-2, indicating pro-apoptotic events in hepatocytes (Fig. 1).|PMC7781826|These same tumors showed increases in the cell death markers, TUNEL-positive cells (p < 0.05) and the enzyme caspase-3 (trend), as well as significant induction of PPAR type gamma (PPARγ).|PMC2703618|A dented anatomy of the HeLa cells was observed under fluorescence and confocal microscopy when they were incubated with L-glutaminase and in glutamine-free medium, as also a 3-fold increase in caspase-3 activity was observed under the same conditions.|PMID:25424834","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"122593659":{"subject":"UMLS:C4529301","object":"NCBIGene:2277","predicate":"biolink:related_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.0004783906666666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:38542ff18d63647085c9324487b73b4c4c52ac340df101c2160970011f2c9cbd","tmkp:21b0d11ebac964b7f404bf648535e436e532553f8c301d563fb58f16267a235e","tmkp:92ee8aa03ff403d51b7f43d94599a24757237cbb6cfda5b30be2086042b11156"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6501144","PMC6710319","PMC6501144"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Strategies have been developed to inhibit the VEGF signaling pathway including anti-VEGF antibody therapy (e.g., bevacizumab), anti-VEGFR antibody therapy (e.g., ramucirumab), inhibitors of VEGFR-2 tyrosine kinases (e.g., apatinib), and inhibitors of angiogenic receptor tyrosine kinases (e.g., sunitinib, pazopanib, sorafenib, and regorafenib).|PMC6501144|The patient was restaged as T2N0M1 of lung adenocarcinoma, and chose 6 courses of systematic chemotherapy (pemetrexed combined with nedaplatin) plus bevacizumab, a monoclonal antibody targeting vascular endothelial growth factor at 3 weeks intervals.|PMC6710319|Based on successful phase III trials, antiangiogenic therapeutics, anti-VEGF agents in particular (e.g., sorafenib, bevacizumab, and sunitinib), have entered the clinical practice in the USA and 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celecoxib has a greater inhibitory capacity than the rest of CL sample, the rhizome extract from MR-1 present only 36% less inhibition than celecoxib at the same concentration (3 µg/mL).|PMC7785433","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"95606948":{"subject":"PUBCHEM.COMPOUND:5988","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:363ce5df5619d93f9a83752f76888059ec2f7dc6495c73cc1a8f4462f987677f","tmkp:6263594815530e8b400d6c36024e2621ca8d6d112b5d431bdaf795cb4c264540","tmkp:1da7acdf69986e987a25a80a45191afd0a30cf666874f08be091c60da218203e","tmkp:663af7db871df8575bf6e7a5b3a1c0272a7a2778bd7d2a2bf1dda4cb01b8493e","tmkp:077f6595b4eae87553a9b5d8daa9a3943d454fdcc9186c8872f6ab23d5b3154c","tmkp:235f94eeb1988fedeb8f9bb168a604b809f6f3e0d716548ba708d09715628bac","tmkp:d55e5669061a7236492232c9ec8c80bfe21741faa97d0e9b9573a06db008801c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2775708","PMID:23775600","PMC6292393","PMC3954640","PMC5378956","PMID:27683267","PMC3579349"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.999017885","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In line with this notion, a recent report demonstrated that CASP3 activation was significantly enhanced in adipocytes from obese mice on either high-fat or high-sucrose diets compared with lean mice on a control diet.|PMC3579349|Feeding male Wistar rats either a high saturated fat diet or a high sucrose diet but not a high polyunsaturated fat diet resulted in significant increase in hepatic SFA as well as increased ER stress, caspase-3 activation and liver injury.|PMC2775708|We perfused mice when maximum caspase-3 activation (in one or more brain regions) is present (8 h) with a solution containing 4% paraformaldehyde and 4% sucrose in 0.05 M cacodylate buffer (pH 7.2), and the brains were further processed according to our previously described protocols.|PMC3954640|However, abnormalities of the testis and sperm in high- and middle-dose sucrose-exposed mice were related to the increased-cleaved caspase-3, but independent of T1R3 and/or Galpha.|PMID:27683267","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"36474644":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Ethanol paradoxically decreased the activity of stress-activated protein kinase-1 (SAPK-1) while increasing p44 and p42 mitogen-activated protein kinase (MAPK) activity.|PMID:11509022|Ethanol paradoxically decreased the activity of stress-activated protein kinase-1 (SAPK-1) while increasing p44 and p42 mitogen-activated protein kinase (MAPK) activity.|PMID:11509022|In rat heart, direct alcohol feeding led to a reduction of apoptotic cardiomyocyte death by reducing apoptotic signaling cascades, JNK-1 and c-Jun, and activating heat shock protein (HSP) 70, heme oxygenase and superoxide dismutase.|PMC2908373|Additionally, both wine and alcohol triggered a signal transduction cascade by reducing proapoptotic transcription factors and genes such as JNK-1 and c-Jun thereby potentiating an anti-death signal.|PMID:12074967|Acute exposure of cerebellar granule neurons to ethanol suppresses stress-activated protein kinase-1 and concomitantly induces AP-1.|PMID:11509022","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9988130164705882","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:11509022","PMC3432162","PMC2908373","PMC5374039","PMID:12074967","PMC5521807","PMID:20041771","PMC5739085"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dcb86727f9ec6513f5ab28762ce35e7fbeb3feca59f5fee07f69c36fc902c67f","tmkp:8178dcf18372e25670a5e48caa34b33d5c3097b0044a740e9b65ed4f6390c39b","tmkp:d57e124aeb66690fe3ea8a99355b7e275d33ae9cbf932cc21c336ebbbd02c36b","tmkp:2422a156948132bdc59a61b1b8374b088a3d173af28170c6203eed095cc0d34a","tmkp:b17ca1699c8d80595e8479a2f2a0d4865b51483d4a8b66c0c89fae7c35c879a8","tmkp:f3b18f2438f5b06e08967a7688def0e981c00bfc4fb53a046238808e2a0e4e3d","tmkp:898cb1dd0cf5fd550192251a1c9bcd75047a1e27de77703a09e87cb63b27959e","tmkp:c57e46a61a9a5cfb1e75c364b1b5c65b5e490763cdcccb066b863b90e250bb58","tmkp:b45d8ba93856567dc364790718d19a6aeba8d55e107b50fa19559326fbe49c6c","tmkp:17fed33dde4865762b03cfac20323afddaf894f236ab23f584a40450466bef58"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"50182853":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:a7f76ad84dcd229bffed4e565233f56df2d16f212fba750f9f6acefdeeb5e3ed","tmkp:613c5fa8a0baf3f57516f624831067dec78c980f8cff20a05c9198c5965b5fc2","tmkp:3b27681aa83a8f17fb9596b9b9bd079e56cfb8c11abe3acdf1a4425060d897d4","tmkp:337eb56ad1153c32d3ae2ea819fc6ab84957e7cab371db911a612f4e6f28fb1f","tmkp:96b18ae78709539538663b59bb71f0a29d93ec22b82d000eea4c9ff48adaacf6","tmkp:47e28c3de75e2960714e346c1398055ff46348fabf2be2dd60106e5e5d23dba4","tmkp:0b769b04c790b10ec3a5ef8a826d930e88724cbb41b9e596cd32b451d01377d3","tmkp:912f95427187f0d72e8fa561306e615d5ede58515188aefb6dfa2b375da67561","tmkp:d5d7d2305199938f9d78d8605f142b7ac380e9affb861e62db9495832cb375c0","tmkp:eca89e56d9f650c63a4b3255f197ecf5ea9496ca844dd1e59737f7356beec261"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Thus, we examined whether tamoxifen might suppress TGF-beta1 expression and consequently inhibit the process of hepatic fibrosis in vivo.|PMID:18564211|Tamoxifen seems to inhibit the process of hepatic fibrosis dose-dependently by suppressing the transcription of TGF-beta1 and TGF-beta RI in an experimental model of periportal hepatic fibrosis.|PMID:18564211|Tamoxifen at 3 and 10 microM down-regulated the secretion of TGF beta-1 from TSGH-8301 in a concentration-dependent manner, in contrast to the findings that tamoxifen was cytotoxic to the bladder cancer cells used and that tamoxifen up-regulated TGF beta-1 in a breast cancer model, suggesting that there may be a different mechanism of response to TGF beta-1 in these bladder cancer cells.|PMID:8653321|It has been reported that tamoxifen may affect hepatoma cell growth in vitro by suppressing transforming growth factor beta-1 (TGF-beta1) expression, suggesting that tamoxifen might also retard fibrogenesis.|PMID:18564211|There are indications that SERMs have an impact on cell‐extracellular matrix interaction which may subsequently affect invasiveness, for example, in breast cancer cells: Tamoxifen, a SERM, has been shown to reduce extracellular transforming growth factor‐beta 1 (TGF‐beta1) expression, while inhibition of matrix metalloproteinase (MMP) activity restored TGF‐beta1 levels in estrogen receptor‐positive breast cancer cells 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caused oxidative stress, decreased expression of neurotrophins, and inactivation of survival signaling proteins Ras, extracellular signal-regulated kinase (ERK 1/2), and protein kinase B (Akt).|PMID:15474364|In a cell-based assay, 2-(2'-amino-3'-methoxyphenyl)-4H-1-benzothiopyran-4-one (8b) showed a more potent inhibitory effect than the corresponding oxygen compound (PD98059, 1) on the Raf-induced activation of the ERK-MAP kinase pathway as well as cell proliferation.|PMID:15080936|The addition of the chemical inhibitor resulted in significant reduction of ERK1/2 activity in comparison with the controls upon oxygen exposure (Figure 4e).|PMC7091608","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ad17a53be820f62b73d8fba02d3734c68d9a0aba1eb095f33fb7c3c0ebeb56db","tmkp:e3e3ad05524411a5b3b3b2797c1166d0ece8928df154e094b436620b4399e314","tmkp:89a97fdb1440a6014aaa495846383085145673a8348bb19c0dd152eebe349073","tmkp:68fbfb98655c3fa0c3b3aaa4d7736ebf71d2cfdb88b821dc717115b7596425e6","tmkp:d46337b149cae054a8e7347fa214ae363c97360cd0940d32f825323295bf9ec2","tmkp:8cd5f2fc0fcdea2b0e329eca14cd3b274d5d810af49690182c2cabdaa174b020","tmkp:e5ef35f739bdab763bf8677c77e13a137fc77b7c412b76aae7c9cd3c68778196","tmkp:007974a9aff1b8a21bc9f0aa6e99918256f74c982e092971d96a01bd9b737693"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"84509150":{"subject":"PUBCHEM.COMPOUND:36314","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7ed431ebb1e5720f0e3000e25ef55c911fc45b9929889ff24a9be552b43fa324","tmkp:9d76bb2b5d6c409cb763bd556e2e19c99c1374323a05d4bdda1530ea25f886bd","tmkp:4db82dcf36e8462ec971e2613e796f90cb1a18c8eaf4d701b72b3c406b1d7aa7","tmkp:e9a586fa1e660d6a39d3b97a66a3cfce9e2a781db778b2cf30ef8e124279e34e","tmkp:c79d3c0f8376a86bc6aee013f81a8884da6c3e39be67bce09e4a2b786d90e8f5","tmkp:2daee1e965a2ab76867616c07e58381661fb0ec3df937f44afb77c993bc67ed7","tmkp:3d5bec206cd939c914b0584c32a0e88f35b74b01baa0d0654d54d650144c4c2f","tmkp:05dd8b616053b0654034ada8315b0c2bde7a1557e3d847568bf5d991939ca6b3","tmkp:4c5269f3cd31bd7817c855c99c1f87c6d9215176567c45b79734f58f31ac9c93","tmkp:afc457c324389fd02d22c70ddadf85708977585bbc93712712eba041c36678d1"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9980387333999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4145830","PMC4475536","PMC6320818","PMC8001342","PMC3899591","PMC6566430","PMC3508157","PMC4061164"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"A variety of inflammatory mediators and signaling pathways are upregulated in response to paclitaxel administration such as IL-1β, IL-8, IL-6, and vascular endothelial growth factor (VEGF)-A.|PMC4061164|Moreover, significant increases in a few inflammatory mediators—such as TNF-α, VEGF, and IL-2—were observed in paclitaxel-treated mice, especially with P. gingivalis administration.|PMC6566430|Further, the expression of VEGF, the growth factor responsible for endothelial-cell proliferation and permeability, appears to be increased, following implantation of sirolimus-eluting stents, paclitaxel-eluting stents, and zotarolimus-eluting stents, as compared to the everolimus-eluting stents and bare-metal stents.|PMC6320818|A variety of inflammatory mediators and signaling pathways are upregulated in response to paclitaxel administration such as IL-1β, IL-8, IL-6, and vascular endothelial growth factor (VEGF)-A.|PMC4061164|As shown in Figure 2A-1 and A-2 and in Figure 2B-1 and B-2, RT-PCR and Western blots analysis showed that SKOV-3 and A2780 cells constitutively expressed the mRNA and and protein of VEGF and survivin, and that LPS and paclitaxel significantly (P < 0.05) increased the expression of VEGF and survivin by SKOV-3 cells in concentration-dependent manner but not by A2780 cells; Treatment with AO-1 alone significantly decreased the constitutive mRNA expression of VEGF but not survivin by SKOV3 cells (Figure 2A-1 and A-2), and also markedly (P < 0.05) counteracted the paclitaxel-induced increased mRNA and protein expression of VEGF and survivin by SKOV-3 cells but not by A2780 cells in a concentration-dependent manner.|PMC3899591","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"96296670":{"subject":"PUBCHEM.COMPOUND:65028","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Enhanced cleaved caspase 3 expression was demonstrated in breast cancer cells treated with oseltamivir phosphate or in Neu1 knockdown mammary carcinoma cells.|PMID:31515676","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99880147","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:31515676"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0ab9d66525bafb2e4eeb434d90e52f3f37ee1169de54238285b011664d262223"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"62408069":{"subject":"PUBCHEM.COMPOUND:2726","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7178048","PMC5152916","PMC5152916"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9996574266666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a817672826d2b3f2804c4de285e20be27a5e617547ea5ee38ddaad3fec490a31","tmkp:a20b745633a9fb172b92d00429a49cafd4a796bad53a26988a7bca89de833f54","tmkp:489255beb96d19a052a5c5963acb02d18fac0e5a657675a48074cf48192abb56"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In fact, the inhibition of clathrin-dependent endocytosis with chlorpromazine and/or ML141, a CDC42/RAC1 GTPase inhibitor, significantly decreased EVs uptake by BMECs.|PMC7178048|Consistent with these studies, we observed that chlorpromazine treatment also reduced Rac1 glucosylation by TcdA in Caco-2 cells.|PMC5152916|Pretreatment of HeLa or HT-29 cells with chlorpromazine was shown to reduce Rac1 glucosylation and cell rounding by TcdA.|PMC5152916","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"67255614":{"subject":"CHEMBL.COMPOUND:CHEMBL2052016","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9944043792307693","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The aim of this study was to evaluate the results of photodynamic therapy (PDT), using verteporfin, for subfoveal neovascular age-related macular degeneration (ARMD) with retinal angiomatous proliferation (RAP) with pigment epithelial detachment (PED) and/or choroidal neovascularization (CNV).|PMID:16525824|To evaluate the efficacy of photodynamic therapy (PDT) with verteporfin for avascular serous pigment epithelial detachment (PED) in elderly Korean patients.|PMID:19696702|To assess the effectiveness of photodynamic therapy (PDT) with verteporfin for choroidal neovascularization (CNV) associated with retinal pigment epithelium detachment (PED) in age-related macular degeneration.|PMID:17460590|Prospective, comparative, nonrandomized pilot study included patients with PED comprising >50% of total lesion in subfoveal location with visual acuity (VA) 20/40-20/400 and lesions either previously untreated or treated only with photodynamic therapy/verteporfin.|PMID:20463807|Prospective, comparative, nonrandomized pilot study included patients with PED comprising >50% of total lesion in subfoveal location with visual acuity (VA) 20/40?20/400 and lesions either previously untreated or treated only with photodynamic therapy/verteporfin.|PMC2861946","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:16525824","PMID:19696702","PMID:17460590","PMID:20463807","PMC2861946"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:704d5a6dddc94bd00c49e23786e390d115e1dde6293829e41323f51205352778","tmkp:da043e2c684da99f2c9c4942d317d1b362d19a955de661c4c6b84a7396c08e1d","tmkp:7ba5c53db800d06e93f9b17c54bb6d0cd4ff8c9f077707c153129752ad1a54a6","tmkp:d333703b112fc76fcbc455586177aa8deffce99420172eccc9097fedb9f556eb","tmkp:1616dce701f97e2b9cff86e2987633fc35df2b73c2d866b19378e028faa1db1d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"41299680":{"subject":"PUBCHEM.COMPOUND:3672","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.997425898","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC3364991","PMC3364991","PMC3364991","PMC3364991","PMC3364991"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9c2e154e05f46f9bd88ab0cffce85c7b5346b424b5c988e7453ae05c66af6c22","tmkp:c45c35043546a6a2c907558386f5026913822e9078a9ba3018262c9c7aa9f3a0","tmkp:9a620e0ccd43cd0255f589ff50019f6ecec82942f8b375a7d353442a03289368","tmkp:54b074a23ded7e9d6383ca0645dba5abb98c7caccd734835bdf6d422c3906618","tmkp:855043b2167c2362702189cc4afdb52f77836d1f973ea3268103badc73448dd2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"We also observed that ibuprofen treatment reduced TGFB1 production, despite continued muscle loading, as well as CTGF and collagen matrix.|PMC3364991|Ibuprofen treatment also attenuated TGFB1 production.|PMC3364991|(C) Muscle from a 6-week HRHF rat treated with ibuprofen (6-wk HRHF+IBU) showing fewer TGFB1-immunostained cells than in panel B. (D) Muscle from a 6-week HRHF rat treated with anti-TNF-α (6-wk HRHF+anti-TNF) showing reduced TGFB1 immunostaining.|PMC3364991|The reduction in TGFB1 by ibuprofen likely contributed to the reduced CTGF; and reduced CTGF contributed to the reduced collage n production and deposition in the muscles.|PMC3364991|In contrast, TGFB1 decreased significantly with ibuprofen treatment, but not with anti-TNF-α.|PMC3364991","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"83421498":{"subject":"PUBCHEM.COMPOUND:3440","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"LAP was decreased in proportion to the dosage of furosemide, which did not significantly differ between IV and PO of the same dosages.|PMID:21314718|LAP was significantly decreased with all administrations of furosemide but not after placebo (P < .05,|PMID:21314718","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:21314718","PMID:21314718"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99970273","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:15e59dbcc8098b7fa1cdfeeb601c76e7af6474a7ab5c8933651777e567945182","tmkp:0f66e9e8dddb9005a616f211c36216aae46c74b5dff1da5f1e1dc6767a4e25c7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"66086017":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9978555728571428","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Alcohol treatment did not effect the body growth rate, but increased the DNA synthesis in lactotropes and reduced the levels of lactotropic growth inhibitory transforming growth factor-beta 1 (TGF-beta 1) protein and mRNA in the pituitary.|PMID:21552885|In primary cultures of pituitary cells, both ethanol and estradiol reduced TGF-beta1 release and increased TGF-beta3 and bFGF release at 24 hours.|PMID:18034699|The level of growth-inhibitory TGF-beta1 was reduced in the pituitary following ethanol and/or estradiol treatment for 2 and 4 weeks.|PMID:18034699|The amount of PDGF-AB, TGF-beta1, and VEGF released per platelet decreased significantly (p<0.05) with increasing ethanol concentrations but, however, not that of EGF.|PMID:19720546|Ethanol treatment of VL-17A cells also reduced the activity of leucine aminopeptidase 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uptake inhibited expression of Glut-1 and enzymes essential in the glycolytic pathway.|PMC5649203|Long-term exposure of ARG with or without CMP-C or L-NAME suppressed NO2-/NO3-, glucose uptake, GLUT-1, AMPK expression and activity below control, and increased overall cellular glucose, O2•- and ONOO-.|PMID:23718875|Long-term exposure of ARG with or without CMP-C or L-NAME suppressed NO2–/NO3–, glucose uptake, GLUT-1, AMPK expression and activity below control, and increased overall cellular glucose, O2•– and ONOO–.|PMC3680329|However, at least one-third fold decrease in GLUT-1 protein expression was seen in those cells exposed continuously for 7 days in medium containing 100 μM ARG or when combined with 30 μM of either L-NAME or CMP-C.|PMC3680329|Continuous (or chronic) cellular exposure to 100 μM ARG for 7 days in the presence or absence of 30 μM L-NAME or 30 μM CMP-C decreased 13C6 glucose uptake from the medium (A) and GLUT-1 expression 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chronic restraint stress during late gestation in rats reduces placental 11ß-HSD2 expression and expression of glucose transporter (GLUT) 1, with an associated reduction in fetal plasma glucose, whereas late gestation dexamethasone increases placental GLUT1 and 3 expression, and another synthetic glucocorticoid, triamcinolone, down-regulates placental GLUT1 and 3 protein and 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with ibuprofen or piroxicam in combination with l-dopa preserved the effect of l-dopa at the end of week 10, delayed the development of dyskinesia and decreased striatal COX-2 and VEGF levels.|PMID:27016022|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off at the end of week 10, delayed the development of dyskinesia, and decreased striatal cyclooxygenase-2 (COX-2) and vascular endothelial growth factor (VEGF) levels.|PMC8150526|When co-administered with l-dopa, a small molecule inhibitor of vascular endothelial growth factor signalling significantly attenuated the development of dyskinesia and completely blocked the angiogenic response and associated increase in blood-brain barrier permeability induced by the treatment.|PMID:21771855|Similarly, a study from Teema et al. showed in a rat model that treatment with ibuprofen or piroxicam in combination with l-dopa ameliorated wearing-off 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S7).|PMC4516794","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9701278","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4516794"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"124168932":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Alcohol Reduces Arterial Remodeling by Inhibiting Sonic Hedgehog-Stimulated Sca1+ Progenitor Stem Cell Expansion |PMC5711561|These data suggest that alcohol feeding attenuates neo-intima thickening by inhibiting resident Sca1+ progenitor cell expansion.|PMC5711561|In contrast, ethanol significantly decreased the numbers of cells that expressed cell-surface Sca-1, c-kit, CD133 and ABCG2.|PMC1249578|Alcohol intoxication may inhibit this phenotypic inversion by both impairing TNF-α production and suppressing the lin-c-kit+Sca-1- cell response to TNF-α.|PMC2731630|Alcohol suppresses the Sca-1 response in granulocyte lineage-committed precursors and restricts granulocyte production during septicemia, which may serve as a novel mechanism underlying impaired host defense in alcohol 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amount of PAI-1 mRNA significantly increased when the epithelial cells were exposed to the air.|PMID:15636194|We have previously reported a fivefold increase in plasma PAI-1 from rats exposed to 708 kPa hyperbaric air.|PMID:26109191|Compared with mice concomitantly exposed to filtered air, the CAPs exposed mice had a significant increase in white adipose tissue PAI-1 mRNA (Figure 1D).|PMC3073968|Urban air pollution increases plasma fibrinogen and plasminogen activator inhibitor-1 levels in susceptible patients.|PMC6397852|Urban air pollution increases plasma fibrinogen and plasminogen activator inhibitor-1 levels in susceptible 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the up-regulation of vascular endothelial growth factor (VEGF) and Prostaglandin D2 (PGD2) synthesis via the glucocorticoid receptor (GR).|PMC5297652|In addition, dexamethasone plays a neuroprotective role through the upregulation of the expression of neurotrophic factors and anti-apoptosis genes, such as nerve growth factor, basic fibroblast growth factor, and vascular endothelial growth 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further confirm the role of P-JNK in irisin-induced increase of telomerase activity, anisomycin, a JNK MAPK inhibitor, was administrated in aged primary hepatocyte.|PMC6959141|In addition, anisomycin potentially prevented the elevation of blood pressure by blocking MAPK signaling pathway.|PMC5704797|Upon stimulation with anisomycin, these matrix protein-stimulated cells further exhibited reduced IkappaBalpha expression and p42/44 MAPK activation, as well as became sensitized to JNK-increased anti-Fas/ActD killing.|PMID:10903887|Interestingly, pretreatment with the p38 MAPK activator anisomycin significantly abolished the effects of rhTrx, including inhibition of p38 MAPK phosphorylation, down-regulation of caspase-3 activity and the anti-apoptotic effect.|PMC5839490|Direct activation of p38MAPK with anisomycin facilitated barrier recovery in Dsg2-deficient cells, in which baseline p38MAPK activity was 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treatment of this condition involves laser photocoagulation (panretinal, focal, and grid), intravitreal anti-VEGF agents (aflibercept and ranibizumab), corticosteroids (dexamethasone and fluocinolone acetonide intravitreal implants), and vitrectomy in the case of vitreous 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inhibitors of PARP1 include the flavonoids myricetin, tricetin, quercetin, fisetin, rutin and naringin.|PMC6342515|Only quercetin seems to lower PARP-1 expression compared to high glucose incubation.|PMC4477254|In prostate cancer cells, quercetin significantly reduced the expression of ATM, PARP1, and DNA-PKcs.|PMC7710985|Quercetin has been reported to have an anti-inflammatory action in both human and model animals by inhibiting activities of cyclooxygenase, lipoxygenase, expression of cyclooxygenase and production of PGE2, diminishing production of interleukin (IL) -1α, PKC-dependent IgE-mediated proinflammatory mediator, IL-6 and IL-8, TNF-α, and poly (ADP-ribose) polymerase-1 (PARP-1), down-regulating vascular cell adhesion molecule-1 (VCAM-1) and cluster differentiation (CD) 80, etc. Quercetin also shows anti-oxidant actions via radical scavenging ability and by interacting with anti-oxidant enzymes, such as heme oxygenase-1 (HO-1), which protects oxidative stress H2O2-induced apoptosis, and reduces intracellular ROS production and mitochondria dysfunction.|PMC6155806|Treatment with quercetin along with LPS reduced the expression of PARP-1 in the adult mouse cortex and hippocampus (Figures 7A,B).|PMC6297180","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"91397497":{"subject":"PUBCHEM.COMPOUND:1130","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:663183be9d002db5f0769acb2eb1a1a26a22ef43e71b70ac6f49bcb373ebba3e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:16645728"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In 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1×-treated ARPE-19 cells showed upregulation of VEGF-A (1.12-fold, p = 0.67), HIF-1α (1.03-fold, p = 0.63), GPX3A (1.13-fold, p = 0.49), BCL2L13 (1.26-fold, p = 0.05), CASPASE-3 (1.21-fold, p = 0.04), CASPASE-9 (1.32-fold, p = 0.003) and IL-1β (1.38-fold, p = 0.22); and downregulation of SOD2 (0.76-fold, p = 0.14) and IL-18 (0.95-fold, p = 0.051), compared to untreated cells (Table 2, Figure 2).|PMC8069662|A recent study showed that in vitro VEGF-A concentrations increased in the retinal pigment epithelium after exposure to ranibizumab or aflibercept due to a compensatory response from the cells and suggested the possibility of differing responses according to the VEGF subtype.|PMC5348182|Real-time PCR analysis showed that treatment with 25 mg/kg BW aflibercept significantly upregulated the expression of fibroblast growth factor-2 (FGF-2), PlGF, VEGF, PDGF-BB, and transforming growth factor (TGF)–β mRNAs.|PMC4954942|Given the importance of the pro-angiogenic pathway downstream of VEGF, inhibiting the VEGF signaling axis has proven an effective therapy for patients with solid tumors and neovascular age-related macular degeneration; drugs such as bevacizumab and aflibercept which sequester circulating VEGF have shown efficacy in some of these clinical situations.|PMC5207393|In ARPE-19 cells, both aflibercept and ranibizumab induced VEGF-A mRNA expression after 24 h of treatment.|PMC8069662","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9862205657142857","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"7623672":{"subject":"PUBCHEM.COMPOUND:3715","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4467441","PMC4085328","PMC3493357","PMID:17410434","PMC3232537","PMID:23542713","PMID:17440234","PMC3612487","PMID:11282914","PMC6461401"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"We observed significantly higher mRNA levels for VEGF (1.73-fold), FGF-2 (5.6-fold) and TGFbeta receptor III (2.93-fold), PDGF receptor alpha (2.93-fold) and receptor beta (2.91-fold) in rats receiving indomethacin compared to rats given placebo (p < 0.05).|PMID:17440234|Indomethacin, a nonsteroidal anti-inflammatory drug (NSAID) with PPARγ activity, up-regulated VEGF expression, but acetylsalicylic acid, a NSAID without PPARγ activity, did not.|PMID:23542713|Infusion of fetal lambs with indomethacin for 48 hours constricted the DA and increased the thickness of the avascular zone of the DA, which in turn induced the expression of vascular endothelial growth factor, endothelial nitric oxide synthase (due to ingrowth of vasa vasorum), neointima formation, and loss of smooth muscle cells; moderate degrees of DA constriction in utero increased NO production, which inhibited DA contractility.|PMID:11282914|In addition, to determine the possible mechanism of the effect of E-cadherin on the PC invasion and metastasis, we found that the protein levels of metastasis-related factors (MMP-2, MMP-9, VEGF), which were increased in PC cells after Si-E-cad and treatment with indometacin 100 mg/L for 48 h.|PMC4085328|Indomethacin also increases the thickness of the avascular zone by causing constriction of circumferential and longitudinal muscle, decreasing blood flow in the vasa vasorum, and causing vessel wall hypoxia with release of vascular endothelial cell growth factor (VEGF).|PMC3232537","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7e913d869c39219769df78d237999a8a5693c2178646b648044e6376c2698182","tmkp:865cb13fa05e92e7b3a88389c346c5dbdf4eef4e8875dd73a735ba707c0ef390","tmkp:ab50bf918d18d8efe8d2cfff7f74aef16adb4e1a783f364d586cc1fe72dcb88d","tmkp:35bd7242c03af76992f8662c5dfe9ee2a35976887d401105e7fc678c3baedcff","tmkp:8302389e9bf1718655cd66a40f9c8ea99559b2c8da86d6b742d176b3f8e933c8","tmkp:51a9f97f843513a3ee748989ece31692580d464c061610d1d00ecfe3e4079da8","tmkp:c360cfd881d8a6fea9f99e765879b34fa1b9efd134c9a882957f8d0b0d3d6fa3","tmkp:4af3820fca0d5362658befed37ff8e83553a84470bb7e77ffabf53340aefe55d","tmkp:5be2067f585c1e1a657a31a213a41d5a611e9cf1365c85d8f6c5453fd5e89a57","tmkp:64f00859a2081ba3414bfa9815d3adf0ba6b63179213e28f9c4cc5adc720c85f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9913440175","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"72373131":{"subject":"PUBCHEM.COMPOUND:5865","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"These results suggest that in asthmatic patients after prednisone treatment raises PAI-1 activity, probability because of releasing of the increased amount of PAI-1 from activated platelet.|PMID:10765644|In 31 asthmatic patients (75.6%), after prednisone treatment, increased of PAI-1 activity together with platelet adhesion and aggregation were observed.|PMID:10765644|These results suggest that in asthmatic patients after prednisone treatment platelet activity appeared in a form of intensification of adhesion and of aggregation degree, also the activity of PAI-1 probably of the platelet origin increased.|PMID:9857661|In asthmatic group after 14 days of prednisone administration in a dose of 20 mg/d statistically significant (p < 0.05) shortening of APTT, and a significant increase of adhesion, aggregation and PAI-1 activity were found.|PMID:9857661|The results of our study suggest a stimulatory effect of CsA on tPA and PAI-I plasma activities as well as on uPA-Ant concentration, while prednisone in turn seems to enhance PAI-I activity in plasma and decrease uPA 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administration to immature neonates suppresses VEGF-A expression in the retina, resulting in the catastrophic vessel loss that initiates retinopathy of prematurity.|PMID:12840058|Oxygen can disrupt VEGF and NO signaling pathways via down regulation of eNOS.|PMC6008318|In postnatal phase 1 of ROP, increased oxygen exposure suppresses hypoxia-inducible factor 1 alpha (Hif1α) and vascular endothelial growth factor (VEGF), contributing to vascular attenuation.|PMC7568562|VEGF-A concentrations in the ocular fluid were reduced with exposure to 80% oxygen at P8 and P12 (Figure 3A).|PMC2958111|Compared to the intrauterine environment, the immature retina is exposed to a relatively hyperoxic environment after birth under oxygen supplementation, which leads to the down regulation of VEGF and IGF-1.|PMC7352796","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"92270850":{"subject":"PUBCHEM.COMPOUND:247","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:25080425","PMID:30805833","PMC7760816"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Bax/Bcl-2 ratio and Nrf-2/HO-1 expression of heat-exposed MAC-T were also reduced with betaine 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was no benefit from methotrexate therapy, and methotrexate therapy was associated with an earlier increase in insulin requirements.|PMID:10900154|Enhancement of synthesis by dexamethasone and insulin was associated with increases in the tri-, tetra-, and pentaglutamate derivatives of methotrexate, with little change in intracellular methotrexate and methotrexate diglutamate.|PMID:6370141|The activation of Ins by MTX was instantaneous and depended on the presence of extracellular Ca2+ ions.|PMID:7509442|Our results confirmed in vivo the results of previous in vitro studies showing clinical evidence that insulin potentiates methotrexate under conditions where insulin alone does not promote an increase in tumor growth.|PMID:14655024|Moreover, the anti-inflammatory effects and improvement in insulin sensitivity by MTX were dependent on endothelial 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the mRNA levels of MAPT, PIK3R1, CASP8, and DAPK1 were significantly decreased (Figures 8A–D, p < 0.05), and MAPK1 and CYCS were significantly increased (Figures 8E,F, p < 0.05), after treatment of these HT22 cells with quercetin for 48 h.|PMC7645061|Quercetin pretreatment in L6 myotubes revealed a significant upregulation of mRNA levels of both AMPK and its downstream target P38 MAPK.|PMC5462925|Nevertheless, treatment with both quercetin and LPS resulted in higher levels of phosphorylated p38MAPK as compared to that with LPS alone, especially at the 4 h time point (Fig 5C).|PMC4624710|When compared with the control group, the phosphorylation levels of p38 MAPK, ERK1/2 and JNK, the protein expression levels of ALP, COL I and BGP, and the mNRA expression levels of TGF-β1, BMP-2 and Cbfα1 were increased in the quercetin-treated group.|PMID:26136938|Also, the flavonol quercetin, which is structurally similar to chrysosplenol d, was shown to induce activation of ERK1/2.|PMC7312517","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7312517","PMC4624710","PMC7976442","PMC5462925","PMC7645061","PMC6470739","PMC8158719","PMID:26136938","PMC7446918","PMC7226806"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9892633378651685","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:034b4de89b6a76d4ba293b62c0669e057caeebddd94c58074b0862c849e5a757","tmkp:bf5f4edce37ff4fb0e0b74063693a96697d0bfcaedfd955f9b00c6595e2d0748","tmkp:f4c1faccdbd244ebc2d40a4a08753f5ecbaac2de4c43e2537e83c7a57f3021cd","tmkp:e1ba64098b79f857899d684b3962241d3076841fba3ff7b2a156bd04b3d145ef","tmkp:4d84ca4e89dab55e215aa94b684155bf4e05f9daa390d846f611e5b82f91897c","tmkp:201022f14c48c3eef626f51c5db5103e7d27664e844ff39ba10c2928af059b38","tmkp:2e57d681c6002b1deaea423a2bbb93e174c5152d7e9930cd545935c9928029bc","tmkp:ce4369d34ed9b9a74cc1e7a313d28acccc0d43b63b83985ae32a290df03a9068","tmkp:f132e2a295f507576469dd880b0125bc57b8220aaca120e7ffdd670e4d177eee","tmkp:3f2f8215f017229ac251730be868bf60cac534582b9d4556f8765d17accf9feb"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"42451588":{"subject":"PUBCHEM.COMPOUND:5743","object":"NCBIGene:6517","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"expression"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"10090","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"dct:description","value":"increases 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modulations of the DA–5-HT3 interactions in the mPFC and NAc core may form a basis for blocking the sensitization-associated behaviors and BDNF/ILK/Akt changes by a pergolide/ondansetron treatment regimen.|PMC4633640","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"125491426":{"subject":"PUBCHEM.COMPOUND:3016","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:b300c4f357906a0aba03f23b9f4de6f28a516096234d7bd7e4d8b067576bfe25","tmkp:d2af0250488315772c165505ef29d04aa0a04ce27122c166ab21d6d53c3b6f0c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:18239283","PMID:18239283"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99972458","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Like flavonoids, diazepam inhibited the release of vascular endothelial growth factor (VEGF) and granulocyte-macrophage-colony stimulating factor (GM-CSF) into supernatants of cultured in the SNU-C4 and MDA-MB-231 cells.|PMID:18239283|Like flavonoids, diazepam inhibited the release of vascular endothelial growth factor (VEGF) and granulocyte-macrophage-colony stimulating factor (GM-CSF) into supernatants of cultured in the SNU-C4 and MDA-MB-231 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the level of Mfn1 transcript significantly decreased (2.1-fold) in spermatozoa incubated with combination-prazosin + adrenaline, suggesting that ɑ1-ADRs could mediate more stimulatory effects.|PMC7544694|When inhibitors of this receptor are activated by adenosine diphosphate, adrenaline, collagen, or thrombin, they inhibit the expression of fibrinogen, von Willebrand factor, fibronectin, and vitronectin, thus directly reducing platelet aggregation by blocking the final aggregation 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arginine supplementation results in sustained wound nitric oxide production and reductions in vascular endothelial growth factor expression and granulation tissue formation.|PMID:16631200|Local arginine supplementation results in sustained wound nitric oxide production and reductions in vascular endothelial growth factor expression and granulation tissue formation|PMC4468226|In a published report, the culture of SKOV-3 and MDAH2774 ovarian cancer cells with L-NAME (an L-arginine analog) significantly reduced the ability of cells to produce vascular endothelial growth factor (VEGF) and completely blocked their capacity for angiogenesis, in the in vitro angiogenesis assay.|PMC6479373|L-Arginine further significantly increased MDA and NO, and decreased VEGF (P < 0.05 vs aortic IR).|PMID:18085359|C-terminal arginine-like compounds have established efficacy for inhibition of VEGF/Nrp 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activation of the IP3/Akt pathway, one of most relevant Mas-related signaling events acknowledged to date, might be on the basis of the protective effect of Ang-(1-7) against NOX-derived ROS formation and apoptosis in cerebral endothelial cells.|PMC5156706|Interestingly, to date, DOCK family proteins activate Rac or Cdc42 but not RhoA, although the structure of the RhoGEF catalytic DHR-2 domain bound to Cdc42 suggests that they may activate a broader spectrum of Rho GTPases.|PMC3124093|To date, in vitro studies have reported an up-regulation of Akt signalling and STAT1 phosphorylation with the familial TEK/TIE2 mutation, p.R849W, and the sporadic mutation, p.L914F.|PMC5167654|To date, GPCRs transduce signals into rapid changes on the actin-cytoskeleton via the activation of small GTP-binding proteins of the Rho GTPases family, such as Rho, Rac and 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cell exposure to cisplatin induced endoplasmic reticulum (ER) stress-associated apoptosis, and LAC treatment increased levels of cell apoptosis and the activation of caspase-3.|PMID:25323748|However, the induction of Caspase-3 mRNA by camel milk was completely abolished by Act-D, suggesting that camel milk increases the Caspase-3 mRNA level by increasing its de novo RNA synthesis.|PMC3359759|The lyophilized camel milk also induced the caspase-3 mRNA, activity level and the initiation of DR4 in BT-474 cells.|PMC8156492|They argued that camel milk inhibited the proliferation of HepG2 and MCF7 cancer cells by activating the caspase-3 mRNA and activity and the induction of death receptors in HepG2 and MCF7 cell lines.|PMC8156492|This inhibitory effect was also confirmed by resulted obtained from the in vivo rat model of breast cancer, which revealed a reduced size tumor, a higher level of DNA fragmentation (detected by a comet assay), and increased activity of the end result of apoptosis, caspase 3, in breast tumor tissues of rats treated with camel 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exposures to sevoflurane were shown to disrupt the tPA/PAI-1 signaling, causing inhibition of the cleavage of pro-BDNF to BDNF production in rats.|PMC8166894|Sevoflurane leads to learning and memory dysfunction via breaking the balance of tPA/PAI-1|PMC8166894","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9a00514e85af79a83941dfd51d30498b37f86ee1bb6a98600599b41eafe3b0e6","tmkp:2a8b60e9e1ace07544228f2d918303f44e504d2c052cf8c5d561980ee435f1c1"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9684831700000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8166894","PMC8166894"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"26800957":{"subject":"NCBIGene:7424","object":"PUBCHEM.COMPOUND:174","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4386807","PMC6364594"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995425675","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:39be1a73985db3bcd7bfb5841ea38b2883faf38dc2c6e73363d2fa5a388fd903","tmkp:4bfe22237e2174c671c98243be504441fde8d6ebd366ec382302e2418fc7942d","tmkp:8840bcaa2ab822024bf774f3a120169f54d26a0231cef45134a0783f54ee913d","tmkp:c4ee4decc25e266327da7f16e4f12879a4e2e000b2a9b3ca52b5817c67b72180","tmkp:aac90b6e100314da46967f0ee32f1030964469237c4c9e7f6e1dd9c98e3970a8","tmkp:189b1ccfca2ce179d55b0f119aa2093cc46ba688de9571263cf4d13d955d297b","tmkp:4d71315260ff87d9da748179f61e16a2a207c413eaa3aae8b57f09774e0331fb"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Consequently, M-MSN_VEGF siRNA@ PEI-PEG-KALA nanocarriers better inhibited VEGF expression, which fell to ~20%, compared with the Lipofectamine 2000 group, in which VEGF expression dropped to ~40%.|PMC4386807|Essentially, M-MSN_VEGF siRNA@PEI-PEG-KALA significantly suppressed expression of the VEGF gene, inhibited angiogenesis effectively, and cut off the supply of oxygen and nutrients, which finally inhibited tumor growth.|PMC4386807|Note: Synthesis of M-MSN_siRNA@PEI-PEG-KALA (top) and systemic administration of VEGF siRNA via this nanocarrier into orthotopic ovarian tumor-bearing mice led to effective silencing of VEGF gene expression in cancer cells and inhibited angiogenesis, ultimately leading to suppression of cancer growth.|PMC4386807|On observing that the M-MSN_VEGF siRNA@PEI-PEG-KALA delivery system achieved highly effective VEGF gene knockdown in SKOV3 cells, we then investigated whether this vector could inhibit tumor growth in vivo.|PMC4386807","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"32178058":{"subject":"PUBCHEM.COMPOUND:5284583","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Levetiracetam (LEV) increased the levels of vascular endothelial growth factor (VEGF), hypoxia-inducible factor-1α (HIF-1α), and heat shock protein 70 (HSP70) in the cerebral cortex of middle cerebral artery occlusion (MCAO) rats on day 14.|PMC8161206|Levetiracetam (LEV) increased the levels of vascular endothelial growth factor (VEGF), hypoxia-inducible factor-1α (HIF-1α), and heat shock protein 70 (HSP70) in the cerebral cortex of middle cerebral artery occlusion (MCAO) rats on day 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previous study suggested that the IMD pathway in D. melanogaster larvae induces c-Jun N-terminal Kinase (JNK)-dependent PDGFR and VEGFR receptor related (PVR) ligands such as PDGFR and VEGFR receptor related factor 2 (PVF2) and PDGFR and VEGFR receptor related factor 3 (PVF3) which in turn induce the proliferation of hemocytes.|PMC8019809","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8019809"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9990951","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"27353362":{"subject":"PUBCHEM.COMPOUND:89594","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:d32b1b6740b954e5f403c4e5e3c7c173b79500f7d38b30a0fd29543c92367e34","tmkp:0f9a12359c44834f7675a2af8d7e9523c120a1c1ad94b48d22fdd0a101a643b5","tmkp:5667a2a45433361173a4a8f9408fc1ff1b86bd1137c544106d7548f697b9adce","tmkp:ce63a5180a128afd5698baed45dcbcbe3f7ad189cff75f2f275d0b9409c00c67","tmkp:5ceb9b08d79a68c8783ae45e0f3973ae68a724bfc2bedc41625008f3c3448bdd","tmkp:7bccab3e3b7283ba2381f250573cef69825f371d1287d95f03e233fbebf286d2","tmkp:8c8d5cfb5a19e590426d2ec5ac29173ea5419d23916157925cf952ef1f97c8fd","tmkp:c6c3ab12d7f7c1d4b79d99ab08d86459022ad1e99bdbb8120e73817b9c60e177","tmkp:f84b00af24ad432d06c256e1f328c494c1c8996a9110010fb9afca66d17940f6","tmkp:a189978c0184b924eb0f6a85a16684e3fe9e8f87e5f1c40b4e9569bcd1b8289d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC7203434","PMC3897646","PMC3419772","PMC6141146","PMID:30472132","PMID:10230873"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9919840177777777","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Similar to CSE, nicotine diminished the proliferation of and IL-4 production by Th2 cells in concentration-dependent manners, though the effect on proliferation was relatively weak (Fig. 4B).|PMC7203434|Studies have demonstrated that Th2-cytokines, particularly IL-13, are key mediators of mucous cell metaplasia/hyperplasia and mucus production; however, in a rat allergic asthma model, chronic nicotine treatment strongly downregulated IL-4 and IL-13 production, but increased mucous cell metaplasia and mucus production in the lung.|PMC3419772|For the inflammatory response, nicotine could suppress the secretion of IL-1α, IL-4, IL-5, IL-10 and RANTES on day 6 and IL-17 on day 14 significantly after H9N2 infection compared with control mice (Fig. 8D).|PMC3897646|Nicotine is immunosuppressive and anti-inflammatory and our previous in vivo experiments indicated that chronic low-dose nicotine exposure significantly inhibited some parameters of allergic asthma, including a dramatic reduction in Th2 cytokines/chemokines such as IL-13, IL-4, IL-5, eotaxin, and atopy, yet the nicotine treated rats exhibited increased mucous cell metaplasia and mucus formation in the airways.|PMC3419772|The allergen-induced proliferation of and IL-4 production by Th2 cells were suppressed by CSE and nicotine, suggesting that the down-regulation of Th2 cell responses was involved in the mechanisms by which ETS diminished allergen-induced nasal eosinophilia and NHR.|PMC7203434","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"49591525":{"subject":"PUBCHEM.COMPOUND:5284371","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:ec62dcabf3dd7444c8b15ca84d56a94bb3fd39aa9c87087dcde8ee45efec761d","tmkp:8beaa539e80dfb5619be775592ea7eb55d2b578c92dfbdcbc695362c580f4ec9","tmkp:796cc0530ba897cb860e3fb14df140bb82513e08d8b3a3f53fa5f762393b6b30","tmkp:404ebc82291c973145cfa047f5bacafe272f9b92e5727fe8b93be84020194f2a","tmkp:5e4ab14a5b11bc2842e58393eef69b8933a0173755a2079dd138602f17bb0eae","tmkp:daf2246aab813215f606c726794e9c7168ab70ec176b5b72265d3292e1ad086e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9845228766666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Besides, the study demonstrates that redox imbalance-driven gonadotoxicity induced by codeine is accompanied by suppression of oestrogen concentration, as well as upregulation of caspase 3 activities and p53/Bcl-2 signaling pathway.|PMC7695972|Despite the adverse effects of codeine on testicular function, its cessation appears to partially restore oestrogen signaling, at least partly, thus enhancing testicular HER2, Ki67, and Bcl-2 expression, and down-regulating p53 pathway resulting in the maintenance of male fertility.|PMC7695972|Codeine cessation at the recovery phase up-regulated Bcl-2 expression in the testes (Figure 8).|PMC7695972","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7695972"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"13367947":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:2643","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:6542580"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9956649","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:50aa7064c2430dcb696da81557aaa22e9a40bcd682b131a7f33bd74dd4298d9d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"The results are as follows: The IC50 of MTX to cells of GCH-1, GCH-1 : RI and GCH-1 : RII was 4.5 X 10(-8)M, 7.5 X 10(-7)M and 9.5 X 10(-7)M, respectively.|PMID:6542580","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"95292561":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"A pilot compound library screen revealed that the topoisomerase II poison MTX (mitoxantrone) is an inhibitor of Rac1, and also inhibits RhoA and Cdc42 in vitro.|PMID:23181668|Because of the multi-inhibition of Rac1, RhoA, and Cdc42, 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and clonidine also increased by greater than two-fold the proportion of ERK-1 and ERK-2 in the phosphorylated active 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show that prednisolone not only suppresses reperfusion damage by reducing hypoxia induced signaling, namely vascular endothelial growth factor (VEGF)-A induced lung edema but also induces transdifferentiation of macrophages towards an anti-inflammatory phenotype, which in turn may play a significant role in long-term lung protection.|PMC3756949|Accordingly, prednisolone suppressed in vitro endothelial sprouting and tube formation in the aortic ring assay and reduced proliferating cell nuclear antigen (PCNA), Tie2, vascular endothelial growth factor (VEGF) and matrix metalloproteinase (MMP)-9 expression of murine endothelioma cells.|PMID:20186670|After treatment with melphalan-prednisolone therapy, the neurological symptoms improved along with decrease of serum VEGF levels as well as the size of pulmonary plasmacytoma.|PMID:11481854|After prednisolone therapy, PH disappeared with a dramatic decrease in serum VEGF.|PMID:11197800|Accordingly, prednisolone suppressed in vitro endothelial 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neurons in culture were exposed to formaldehyde, menthol, the ERK1/2 inhibitor PD98059 + formaldehyde, or PD98059 + menthol.|PMC6262987|However, we do show that the contribution of the spinal cord to the reduced behavioral effect is paramount since the activation of ERK1 and ERK2 is also decreased following formalin injection in the DN MEK mice relative to wild type littermates, and the behavioral and biochemical inhibition can be mimicked by intrathecal administration of MEK inhibitors.|PMC1382249|However, we do show that the contribution of the spinal cord to the reduced behavioral effect is paramount since the activation of ERK1 and ERK2 is also decreased following formalin injection in the DN MEK mice relative to wild type littermates, and the behavioral and biochemical inhibition can be mimicked by intrathecal administration of MEK inhibitors.|PMC1382249|Compared with formalin group, EA significantly inhibited the increased expression of phosphorylated ERK, JNK and p38 MAPK induced by formalin injection (P < 0.05), while subcutaneous rIL-33 administration further enhanced the increase (P < 0.05) (Fig 7).|PMC4466274|The lack of a CeA effect of corticosterone in females may be due to consistently high levels of corticosterone under naïve conditions (compared to male naïve levels), which may saturate CeA GRs and subsequently dampen any corticosterone effect on ERK2 phosphorylation or actually prevent ERK2 phosphorylation after formalin in the first 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human LECs, the levels of the  EMT markers α-smooth muscle actin (α-SMA) and fibronectin were drastically reduced by treatment with 2 mM aspirin.|PMID:31815277|The protein levels of the fibrosis markers (COL1A1, α-SMA, fibronectin), TGF-β1, p-Smad2/Smad2 and p-Smad3/Smad3, were significantly inhibited in the endometrium tissues in the aspirin and oestradiol valerate therapy group (group B; n=8) compared with the oestradiol valerate therapy group (group A; n=8) following treatment.|PMC7138280|Chronic aspirin treatment in diabetic rats significantly attenuated mesangial expansion, and effectively suppressed CTGF induction, as well as inhibiting the upregulation of TGF-beta1 and fibronectin expression.|PMID:14586741|Aspirin inhibits the protein expression levels of COL1A1, α-SMA, fibronectin and the TGF-β1-Smad2/Smad3 pathway in endometrial tissues.|PMC7138280|A new study reveals that salicylic acid, the major metabolite of aspirin, acts at the level of transcription to downregulate the 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of HIF-1 signaling by quercetin was confirmed by qRT-PCR which showed upregulation of the HIF-1 regulated genes EPO, VEGF, PGK1 and BNIP3.|PMID:19729006|A very mild increase in VEGF mRNA expression was observed in the rats treated with quercetin.|PMID:26281317|One study reported that 0.3% quercetin treatment of wounds accelerates healing by a variety of biological effects: rapid wound contraction, modulation of inflammatory and anti-inflammatory cytokines, increased VEGF and TGF-b1, increased antioxidant status, and enhanced fibroblast proliferation, with better collagen deposition.|PMC8186379|Quercetin up-regulated vascular endothelial growth factor (VEGF), an ulcer healing factor, not only in colon epithelial cell lines but also in the inflamed colonic tissue.|PMID:17377063|The gene and protein expression data suggest that quercetin treatment (100 micro M) significantly decreased EGF and cyclin D1, whereas VEGF was up-regulated in Ishiwaka cell 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expression was ~20% higher in EX brains than it was in SED brains (p < 0.05), and ~15% higher in LAC brains than it was in VEH brains (p < 0.05) (Fig. 8).|PMC4276250|Human milk levels of VEGF, IGF-I and b-FGF were significantly higher (p<0.001).|PMID:20202860|We found that bLF purified from milk increased the mRNA expression of vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF2) in murine osteoblast-like MC3T3-E1 cells and primary murine osteoblasts in a time- and dose-dependent manner.|PMID:21404021|We found that bLF purified from milk increased the mRNA expression of vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF2) in murine osteoblast-like MC3T3-E1 cells and primary murine osteoblasts in a time- and dose-dependent manner.|PMID:21404021|Bovine milk lactoferrin induces synthesis of the angiogenic factors VEGF and FGF2 in osteoblasts via the p44/p42 MAP kinase 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an inhibitor of matrix metalloproteinases and VEGF-driven angiogenesis, also had no significant effect.|PMC3881588|Doxycycline is a potential therapeutic agent which controls inflammation-induced lymphangiogenesis (ILA) by inhibiting the MMPs activity, resulted in decreased VEGF(vascular endothelial growth factor)-C/VEGF 3 signaling, and also reported to inhibit inflammatory cytokine expression, macrophage infiltration and VEGF-C-induced HDLEC proliferation in vitro.|PMC8105415|Additionally, doxycycline proved to increase tissue inhibitors of metalloproteinases-1 (TIMP-1) and stop human aortic smooth muscle cell (HASMCs) migration by inhibiting VEGF expression.|PMC7193389|In contrast, doxycycline has been found to eliminate angiogenesis indirectly as an MMP-9 inhibitor via suppression of VEGF expression in cerebral matrix of a mouse model.|PMC7193389|Our results showed that doxycycline treatment dramatically inhibited ILA in the mouse cornea (p<0.001), with a significant decrease in vascular endothelial growth factor (VEGF)-C/VEGF receptor 3 signalling, macrophage infiltration and inflammatory cytokine expression.|PMID:25268699","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"53532353":{"subject":"UMLS:C0724624","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6787513","PMC6726285","PMC7028200","PMC7673024","PMC6898858","PMC4823176","PMC3641722","PMC7782159"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"The results showed a remarkable decrease in expression of GLUT1, HK2, PKM2, LDHA, MCT4, HIF-1α, c-Myc and SIRT6 in tumours treatment with 5 and 10 mg/kg α-hederin compared to controls.|PMC7782159|Also, β‐elemene suppressed EGFR‐importin α5‐mediated nuclear translocation of PKM2 and expression of GLUT1, MCT1, MCT4 and LDHA |PMC6787513|Also, β‐elemene suppressed EGFR‐importin α5‐mediated nuclear translocation of PKM2 and expression of GLUT1, MCT1, MCT4 and LDHA |PMC6787513|Vldlr−/− mice treated with Ffar1 lipid agonists medium chain triglycerides (MCT; 8–10 carbons) or a second Ffar1 selective agonist TAK-875 had increased Glut1 suppression and more RAP-like lesions versus controls (Supplementary Fig. 8).|PMC4823176|Western blot results showed that compared to 0 µM α-hederin, 10 and 15 μM α-hederin significantly reduced the expression of GLUT1, HK2, PKM2, LDHA, and MCT4 (Figure 3).|PMC7782159","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d165d5f2ae48aea156dcc2dfd52e4421fd1e51f0dc73c246eaef27b034523f5d","tmkp:ef9c8780fa8594599e4da6630d5f8d1a61ba93bdca9b7424177cc61c030c2670","tmkp:3aa7f984e398a6c7d376e16435df9d232a56b185cbeeb8854c3a076084f26fd8","tmkp:44160f9ccf2fc3a3c02c422dd258e3eb65e7ea184ca6f50f071199ae8b2a5d8b","tmkp:69e04206593077745937a6e850c6b848bb0d8e9c3c71b7229bdd30574429b95a","tmkp:31dab2f3c00cd54da43aadc60452c69bda6c385f868ecd8f3a42d358d6b7612d","tmkp:2510cfb0725845a2a26ab195111f0e6563cc65ca7d22bc623bff4bb96e9b8c56","tmkp:2229bb606fa29ff3c23a43bc3e06b9452e364b7b8f5d3776c15c7ef7ac699e99","tmkp:e966cdf3723c86fa9591f1872aadc05d156251ff1af758c94377128b4ede1696","tmkp:3af668580a9159aa19b552f678edd0f3e61ace7c46598baa58e4bb5dc4124110"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999493895","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"38811173":{"subject":"PUBCHEM.COMPOUND:6468","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:7f7e74d9817b1bd94f7035567297b7fea608833c6d9d94f8f1a04ada42928a64","tmkp:62ae039e12c75fa51f5a2acb2db0863cc08fc4170a6660fca7c14c4797862413"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:11166517","PMC4605830"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Therefore, the decrease in phosphorylation of T386 in this dataset suggests ERK2 is less active after PCP treatment.|PMC4605830","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99965477","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"104654984":{"subject":"PUBCHEM.COMPOUND:24759","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Moreover, IL-4 antagonizes IFN-γ-induced hyaluronic acid synthesis and may have some effect on the tissue repair process.|PMC4451372","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4451372"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9836b2611c1a531ca5f2e339f6b2856f63c2d6521d99f850b67dc802049aa730"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9996978","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"13534249":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:63f1efa397fd5cb040a7468c190eea3ed87a4e116ad608db879fae1d2ef6626a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7459487"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99700755","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, in rat cardiac myocytes, dopamine, 5-methoxytryptamine, tryptamine, and serotonin administration intensified the transport of glucose, and this effect was paralleled by amplified cell surface GLUT4 and GLUT1 expression.|PMC7459487","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"90701236":{"subject":"PUBCHEM.COMPOUND:5816","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Akt phosphorylation increased in a time-dependent manner following application of 10 μM epinephrine, while phosphorylation of ERK1/2 was down-regulated by 10 μM epinephrine (Figure 3A).|PMC5641123|When the B2-adrenergic receptors are activated by epinephrine at higher concentrations, there is a negative inotropic effect on myocyte contraction; however, there is simultaneous activation of the phosphatidylinositol 3-kinase and protein kinase B (PI3K-AKT) pathway.|PMC6044494|The NO production induced by epinephrine and BRL 37344 was associated with the activation of the phosphatidylinositol 3-kinase/Akt pathway and phosphorylation of eNOS in serine 1177.|PMID:19429833|(A) Activation of Akt phosphorylation and inactivation of ERK1/2 following treatment with 10 μM epinephrine.|PMC5641123|Forskolin or epinephrine induced localized Rac activation dependent on Tiam1 and 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our work, Pld1 (phospholipase D1), Pld2 and Ppap2b (phosphatidic acid phosphatase 2b, LPP3) in interneurons are significantly increased by nicotine.|PMC5319194|Consistent with RNA-seq findings, Ppap2b, Pld1 and Crls1 were significantly up-regulated by nicotine in Sst neurons.|PMC5319194|In our work, Pld1 (phospholipase D1), Pld2 and Ppap2b (phosphatidic acid phosphatase 2b, LPP3) in interneurons are significantly increased by nicotine.|PMC5319194|Nicotine and LPS upregulated PLD1 and PLD2 mRNA expression in a dose-dependent manner in HPDLCs.|PMID:26334245|b Increased expression of Ppap2b, Pld1 and Crls1 are shown in nicotine treated Sst-neurons.|PMC5319194","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"124059327":{"subject":"UMLS:C2740799","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:6b7787cfb796fe8d49db706787e560a04fb025cafffb1094232633b26c545513","tmkp:66e7530208a5e92b864db7e3009143e8d307fff76b09431ef4fd59bcb8198a6d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9489131","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3375382","PMC8062492"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"To date, a number of small-molecule agents capable of suppressing the activity/expression of GLUT1 and/or other GLUT members have been reported, including resveratrol, naringenin, phloretin, fasentin, 8-aminoadenosine, and 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responders to initial prednisone therapy ('prednisone response') revealed significantly higher Bcl-2 expression levels [5.4 +/- 3.4 relative fluorescence intensity (RFI), n = 68] than poor responders (3.7 +/- 2.6 RFI, n = 42; P = 0.002).|PMID:10930993|Good responders to initial prednisone therapy ('prednisone response') revealed significantly higher Bcl-2 expression levels [5.4 +/- 3.4 relative fluorescence intensity (RFI), n = 68] than poor responders (3.7 +/- 2.6 RFI, n = 42; P = 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behavioral protection of long-term treatment with L-DOPA in AC5-KO mice was preceded by a decrease in the phosphorylation levels of PKA substrates ERK (extracellular signal-regulated kinase) 1/2, MSK1 (mitogen- and stress-activated protein kinase 1), and histone H3, levels of which were all increased in the lesioned striatum of wild-type mice.|PMID:25164669|In our study, treatment with HTHQ was able to reduce both sustained phosphorylation of ERK1/2 and JNK1/2 phosphorylation to baseline levels following l-DOPA-treatment (Figure 3 and Figure 4A,C).|PMC6429301","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:25164669","PMID:29120941","PMC6429301","PMC4464750"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"83914276":{"subject":"PUBCHEM.COMPOUND:38853","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:3fb447cc63ad72fcb8b370fc97d0ea489dab4d4cb6ca72a4c9a8586a83b1ba76","tmkp:e4f8289940f490e9cac7c5559e19024b4fb011a92789f9f6a2be82882b2ad2ae","tmkp:dc5d7ffe9e7f40aa13842a157f579d848987349e8df3a877cbc94930924aec17","tmkp:de5ceaba34f63ea8d14e7dc470570f4646d67524c8158e3c1cedec6bf92abe75","tmkp:9cc06006fe229b20369c3f880c368c725e418ade3fb8a2b14fbb2573a067f772"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Previous studies that have evaluated the use of photodynamic therapy (PDT) for AMD patients with PED have reported minimal improvement in terms of visual outcomes.|PMC5786863|Because this was a case report, further large and long-term prospective randomized studies are needed to determine the efficacy and safety profiles of aflibercept for AMD patients with PED.|PMC3699315|To quantitatively evaluate the change in pigment epithelial detachment (PED) morphology on spectral-domain optical coherence tomography (SD-OCT) 18 months after the transition to intravitreal aflibercept in patients with neovascular age-related macular degeneration (AMD) with PED recalcitrant to monthly intravitreal bevacizumab or ranibizumab.|PMID:26114844|Through inhibiting increased levels of VEGF, management of fluid withdrawal and reduction of neovascularization are intended in the treatment of PED in age-related macular degeneration (AMD).|PMC3971855|The aim of this study was to demonstrate the development of a macular 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reduces the level of cleaved caspase-3 and increases the ratio of Bcl-2/BAX in SH-SY5Y cells.|PMC5343851|VPA and SB suppressed reductions in a- and b-wave amplitudes of the ERG and attenuated the activation of caspase-3 in the RGCs, which was accompanied by upregulation in Akt and Erk phosphorylation in the retina.|PMID:22867974|VPA was shown to protect SH-SY5Y dopaminergic neuronal cells from 6-OHDA-induced toxicity thorugh down regulation of apoptotic caspases namely, caspase-3, caspase-7, and caspase-9.|PMC7194116|However, we found in our study that VPA administration increased the expression of the anti-apoptotic bcl-2 while decreasing the expression of the pro-apoptotic Caspase-3 protein.|PMC4418724|n-3 DPA is known to reduce the activation of microglia, sphingomyelinase, caspase-3 and oxidative stress in aged rats, and as a consequence to attenuate age-related deficit in spatial learning and long-term potentiation.|PMC6202571","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"30707334":{"subject":"PUBCHEM.COMPOUND:5206","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:74ddf8c71d63e7eef1a2e87e75795d75f7d241507015a0cc4dc8853352854917","tmkp:2b377bc4a60bb5d891eabb43f5f7eb93b8e92bdd64c328102d9c6182548b6b3c","tmkp:09cc802499b6278972c4aedd3c859be21ab62f49f1ca1a974a477e216edfa926","tmkp:b0a559783c68c151ba3e877e3fe9ff13cfa49b45611fca58f6ccc399e386ab74","tmkp:10f772df2f97cd2d142713c83938edb8e69f60db922de37fd2f15ebd8a46f797","tmkp:584bd7ad8adc6506c05b48267475ec2503124f4d3b85396ce751133af67db006","tmkp:beb877d181831a05fca44f26f55c4dd1884cc0cec7a592823da3852e2521c1a5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9859093800000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Glibenclamide significantly decreased glucose levels and significantly increased insulin levels under propofol anesthesia as well; however, insulin levels in rats pretreated with glibenclamide under propofol anesthesia were much higher than those in rats pretreated with glibenclamide under sevoflurane anesthesia.|PMID:22127813|Previous experimental studies have reported that sevoflurane and propofol induce insulin resistance, even in absence of surgical stress.|PMC6784668","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6784668","PMID:22127813","PMC4734237","PMID:12088955","PMC4146120","PMID:9174321"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"21397122":{"subject":"PUBCHEM.COMPOUND:3672","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:d44d5498318ed111f3eba636c3b95bdd7273617381e8d55c195a4fae7a063daf","tmkp:91c9708fb47b9a7a87d8a9c632f0f6a1f1d7c07c0037d2b0af4e7d8c36c85f16"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC2734968","PMC2746691"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99970433","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In a related study using PC-3 and DU-145 cells, hypoxia resulted in the upregulation of the hypoxia-inducible factors HIF-1α and HIF-2α; this upregulation could be inhibited by the NSAID ibuprofen, subsequently leading to the downregulation of the HIF-regulated proteins vascular endothelial growth factor and GLUT1.|PMC2734968|Moreover, hypoxia resulted in upregulation of hypoxia-inducible factors HIF-1alpha and HIF-2alpha that could be inhibited with the nonsteroidal anti-inflammatory drug Ibuprofen leading to cyclooxygenase-2 independent down-regulation of HIF-regulated proteins vascular endothelial growth factor (VEGF) and GLUT1.|PMC2746691","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"107516359":{"subject":"UMLS:C4529301","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999712815","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Bevacizumab 2× resulted in downregulation of VEGF-A (0.82-fold, p = 0.41), HIF-1α (0.63-fold, p = 0.001), GPX3A (0.91-fold, p = 0.63), IL-18 (0.86-fold, p = 0.02), and IL-1β (0.68-fold, p = 0.12); and upregulation of SOD2 (1.54-fold, p = 0.06), BCL2L13 (1.07-fold, p = 0.16), CASPASE-3 (1.04-fold, p = 0.39), and CASPASE-9 (2.16-fold, p < 0.0001) (Table 2, Figure 2).|PMC8069662|Treatment with bevacizumab 1× decreased the expression of VEGF-A (0.95-fold, p = 0.80), HIF-1α (0.85-fold, p = 0.26) and IL-1β (0.81-fold, p = 0.42), and increased the expression of SOD2 (1.8-fold, p = 0.009), GPX3A (1.28-fold, p = 0.23), BCL2L13 (1.8-fold, p < 0.0001), CASPASE-3 (1.5-fold, p = 0.003), CASPASE-9 (1.04-fold, p = 0.52) and IL-18 (1.33-fold, p = 0.0003) (Table 2, Figure 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ERK1 and ERK2 phosphorylation levels slightly decreased in sevoflurane-treated mice compared to their levels in controls.|PMC4764822|(e,f) ERK1 and ERK2 phosphorylation levels slightly decreased in sevoflurane-treated mice compared to their levels in the controls.|PMC4764822|(e,f) ERK1 and ERK2 phosphorylation levels significantly decreased in sevoflurane-treated mice compared to those of the controls.|PMC4764822|(c,d) ERK1 and ERK2 expression levels in sevoflurane-treated mice were not significantly different compared to 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female Wistar albino rats were divided into three study groups as follows: 1) control (C) rats; 2) rats with experimental periodontitis (PED); and 3) rats with PED that were treated with doxycycline (PED + LDD).|PMID:23786405|Thirty female Wistar albino rats were divided into three study groups as follows: 1) control (C) rats; 2) rats with experimental periodontitis (PED); and 3) rats with PED that were treated with doxycycline (PED + LDD).|PMID:23786405","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:db56862b62c86d32e0c0e0c3ccf6f20a08efc0e26b5da3e964c0c469e532f6b8","tmkp:325afc4fe4c8dec127c0b6a7d3734cba35180a0c3fc0b2f4242f612d5a58b9ad"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:23786405","PMID:23786405"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"52283835":{"subject":"PUBCHEM.COMPOUND:135398748","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Here, we showed that PCV2 infection induced ASK1 phosphorylation which preceded activation of JNK1/2 and p38 signaling in the cultured cells, and that the phosphatidylinostol 3-kinase (PI3K)/Akt signaling triggered by PCV2 infection limited the extent of JNK1/2 and p38 activation and thereby apoptotic cell 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inhibits the IL-1β-induced expression of COX-2 in HEI-OC1 murine auditory cells through the inhibition of ERK-1/2, JNK-1 and AP-1 activity |PMC6437450|Prednisone inhibits the IL-1β-induced expression of COX-2 in HEI-OC1 murine auditory cells through the inhibition of ERK-1/2, JNK-1 and AP-1 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hypothesis was diclofenac-mediated apoptosis is associated with inhibition of PI3K/Akt/MAPK signaling axis.|PMID:30406888|We found that both single agent and combined treatments of DFMO (p = 0.05) or diclofenac (p = 0.03) and DFMO+diclofenac (p = 0.001) significantly reduced the phosphorylation-dependent activation of ERK1/2 (Figure 3B) as compared to vehicle-treated control (Figure 3B).|PMC3832653|We found that both single agent and combined treatments of DFMO (p = 0.05) or diclofenac (p = 0.03) and DFMO+diclofenac (p = 0.001) significantly reduced the phosphorylation-dependent activation of ERK1/2 (Figure 3B) as compared to vehicle-treated control (Figure 3B).|PMC3832653|DFMO+Diclofenac downregulates ERK/MAPK signaling|PMC3832653|Depending on the characteristics and the type of tumor, PDT can be applied in combination with immunomodulatory (Imiquimod) and chemotherapeutic (5-fluorouracil, methotrexate, diclofenac, or ingenol mebutate) agents, inhibitors of some molecules implicated in the carcinogenic process (COX2 or MAPK), surgical techniques, or even 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it was concluded that diclofenac inhibits the proliferation of TNBC cells by inhibiting glycolytic enzymes such as GLUT1 and HK.|PMC8027724|Diclofenac significantly inhibited cell proliferation, downregulated GLUT1 and c-Myc expression, and decreased HK activity in TNBC cells compared with non-TNBC cells.|PMC8027724|Diclofenac significantly decreased glucose transporter 1 (GLUT1), lactate dehydrogenase A (LDHA), and monocarboxylate transporter 1 (MCT1) gene expression in line with a decrease in glucose uptake and lactate secretion.|PMC3706586|As the most invasive breast cancer subtype, TNBC exhibits higher levels of GLUT1 compared with other subtypes of breast cancer; however, diclofenac can significantly decrease GLUT1 expression and glucose uptake.|PMC8027724|In summary, the present study results provide evidence that diclofenac can decrease the protein expression of GLUT1 and HK activity in cancer cells by downregulating the expression of c-Myc, lowering glucose uptake, preventing the supply of energy and inhibiting glycolysis, eventually inhibiting the growth of TNBC cells.|PMC8027724","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8027724","PMC8027724","PMC3706586","PMC8027724","PMC8027724"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"109435332":{"subject":"NCBIGene:1892","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Paroxysmal exercise-induced dystonia within the phenotypic spectrum of ECHS1 deficiency.|PMID:27090768|The phenotype associated with ECHS1 mutations might be milder than reported earlier, compatible with 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this end, the PLD1 inhibitors quercetin, ML298, and ML299 decrease U87 glioblastoma cell invasion in in vitro assays.|PMC4381264|Quercetin significantly suppressed the expression of PLD1 at the transcriptional level.|PMID:21867678|Taken together these data demonstrate that quercetin abolishes PLD1 expression and subsequently inhibits invasion and proliferation of glioma cells.|PMID:21867678|Quercetin suppressed NFκB-induced PLD1 expression via inhibition of NFkB transactivation.|PMID:21867678|Quercetin, a flavonoid that is known to downregulate matrix metalloproteinase protein 2 and 9 (MMP-2 and MMP-9), which are found at increased levels in tumors, downregulates PLD1 activity in these cancerous 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the baseline, we established that epinephrine stimulation of the endogenous beta(2)AR in HEK293 cells (20-30 fmol/mg) caused a rapid and transient activation of ERK1/2 with an EC(50) of 5 to 6 nM.|PMID:12391272|Epinephrine and norepinephrine increased proliferation in vitro, as well as increasing tumour growth in vivo through activation of ERK1/2 by adrenergic signalling.|PMC7825104|The action of epinephrine is mediated by the activation of ERK1/2 and possibly transcription factors Sp-1 and Ap-2.|PMC3241883|In all cases we detected robust ERK1/2 activation in response to isoproterenol and epinephrine, further confirming that this effect is mediated by G protein, rather than arrestins.|PMC3236217|New research shows that epinephrine activation of β2AR and ERK1/2, JNK, and cAMP signaling is necessary for mucin 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clinical effect of the AMT in treating BK could be explained by its natural production of pro-inflammatory cytokine antagonists such as IL-ra, sTNF antagonist and VEGF-R.|PMID:22220428","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"43985130":{"subject":"PUBCHEM.COMPOUND:23985","object":"MONDO:0000188","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:81662f64cf3ef89f5742a3a269d0166261bee8e59a6b25add0eda8e8b4a7ce7e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"The potential use of KD in pathological conditions characterized by chronic hypoglycemia is further strengthened by the fact that KD is the gold standard in the treatment of GLUT1 deficiency syndrome, which can be considered a metabolic phenocopy of hepatic GSD, since blood glucose cannot be transported into 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with a protective effect of the MSC on cancer cells regarding drug-induced apoptosis, we observed a significantly lower expression of cleaved-caspase 3 and cleaved-PARP-1 by the sorted-SCC and MSC/SCC fused cells, compared to naïve SCC-25 by western blotting in a time dependent manner with paclitaxel treatment.|PMC7732973|The level of cleaved caspase-3 expression decreased by 19% following treatment with gemcitabine and by 28% following treatment with paclitaxel under both stromal cell co-culture conditions, indicating that PSC co-culture contributed to drug resistance and no resistance was further conferred by the presence of TAMs in the culture (Figure 6B).|PMC7762293|As presented in Fig. 4A and B, while single treatment with paclitaxel only led to low cleaved caspase-3 and cleaved PARP expression, combined shikonin and paclitaxel treatment markedly enhanced expression levels of cleaved caspase-3 and cleaved PARP.|PMC6704285|When numbers of viable cells were determined in cultures exposed to amyloid peptide with or without paclitaxel for 24 or 96 h, the percentage of surviving cells was significantly higher in paclitaxel-treated cultures, and activation of the apoptosis-associated protease CPP32 was significantly reduced.|PMID:9523579|(C) The expression levels of caspase-3 in paclitaxel-treated A549-F10 cells were lower compared with the untransfected A549 cells and A549-mock cells 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found that IL-4 mRNA and protein levels were significantly higher in aspirin-treated PBMCs from AERD patients compared with that in aspirin-treated PBMCs from ATA patients (Figure 7).|PMC4686698|This result indicates that aspirin induces IL-4 expression at least, in part, through the increased synthesis of NFATs.|PMC4686698|Aspirin induced IL-4 expression and activated the IL-4 promoter in a report assay.|PMC4686698|The present study indicates that aspirin is directly linked with IL-4 production in the context of AERD pathogenesis as (i) aspirin induced IL-4 expression and activated the IL-4 promoter in cell types relevant to AERD pathogenesis, indicating that IL-4 may be a direct target of aspirin; (ii) aspirin-induced IL-4 production was accompanied by the activation of biochemical and molecular pathways leading to IL-4 transcription; (iii) aspirin-induced higher levels of IL-4 transcription in PBMCs from patients with AERD compared with those from patients with ATA.|PMC4686698|The present study indicates that aspirin is directly linked with IL-4 production in the context of AERD pathogenesis as (i) aspirin induced IL-4 expression and activated the IL-4 promoter in cell types relevant to AERD pathogenesis, indicating that IL-4 may be a direct target of aspirin; (ii) aspirin-induced IL-4 production was accompanied by the activation of biochemical and molecular pathways leading to IL-4 transcription; (iii) aspirin-induced higher levels of IL-4 transcription in PBMCs from patients with AERD compared with those from patients with ATA.|PMC4686698","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"63424376":{"subject":"PUBCHEM.COMPOUND:5206","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.994384924736842","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Sevoflurane treatment activated the MAPK/NF-κB signaling pathway in hippocampal neuronal cells |PMC7065510|Sevoflurane post-conditioning protects isolated rat hearts against myocardial I/R injury and inhibits cell oncosis and apoptosis via activation of the ERK1/2 pathway.|PMID:25345742|Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway.|PMID:25345742|Sevoflurane post-conditioning protects 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treatment of the colon cancer cell lines SW480 and DLD-1 with paclitaxel resulted in increased activation of the MAPK pathway, which was blocked by PD98059, a MEK inhibitor.|PMID:19331159|All three mitogen-activated protein kinase (MAPK) family members, c-Jun N-terminal kinase (JNK), p38 MAPK, and extracellular signal-regulated kinase (ERK) were activated upon paclitaxel treatment.|PMID:11278851|These findings suggest that the bortezomib/paclitaxel regimen induces a significant activation of stress-dependent kinases (JNK & p38 MAPK), while the cytoprotective kinases ERK1 & ERK2 are only activated at higher concentrations (Figure 2).|PMC3796452|Thus, the treatment of SW480 and DLD-1 cells with paclitaxel resulted in increased activation of the MAPK pathway.|PMC7431588|A rationale for combining paclitaxel with other treatment regimens, such as the proteasome inhibitor bortezomib, was elegantly illustrated in tumors in which the H-ras/MAPK pathway is 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doses of risperidone (0.3-3.0 mg/kg i.p.) prevented increased inflammatory parameters induced by LPS in brain cortex [expression of inflammatory cytokines, interleukin (IL)-1β and tumour necrosis factor (TNF)-α, activity of the inducible inflammatory enzymes nitric oxide synthase and cyclooxygenase, p38 mitogen-activated protein kinase (MAPK) and inflammatory nuclear transcription factor κB] and restored anti-inflammatory pathways decreased by LPS challenge (deoxyprostaglandins and peroxisome proliferator activated receptor 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1 treatment also resulted in a 35% decrease in oxygen consumption, 50% inhibition of Na(+)-K(+)- ATPase activity, and a 57% decrease in gluconeogenesis.|PMID:8853432|β-LAP also inhibited reactive oxygen species (ROS) production by suppressing the expression and/or phosphorylation of NADPH oxidase subunit proteins, such as p47(phox) and gp91(phox).|PMID:26173397|β-LAP also inhibited reactive oxygen species (ROS) production by suppressing the expression and/or phosphorylation of NADPH oxidase subunit proteins, such as p47phox and gp91phox.|PMC4502557|In the first 24-48 h, TGF-beta 1 mRNA levels decreased steadily in both oxygen environments.|PMID:1940433|However, production of active oxygen molecules was suppressed by TGF-beta 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mRNA and protein expression was significantly reduced after CIH compared with CCH or normal oxygen rats, 0.002 +/- 0.002 vs. 0.039 +/- 0.009, P < 0.001; 0.642 +/- 0.073 vs. 1.000 +/- 0.103, P = 0.035.|PMID:20193488|Our findings indicate that the expression of GLUT4 and the phosphoenolpyruvate carboxykinase 1 decreased because of the lack of oxygen, but inhibition of miR-27 and miR-195 was able to reverse GLUT4 downregulation (Figure 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was associated with a lower thrombus uPA/PAI-1 antigen (Ag) ratio than the vehicle, reduced by 20% (P < .05,|PMC2997482|Indeed, we observed that the expression of several claudin-low-enriched transcripts, ALDH1A1, IL8, SERPINE1, VCAM1, and CD44, was decreased in doxycycline-treated SUM159PT_shADAM12 cells versus SUM159PT_shControl cells (Fig. 6e).|PMC5288940|Conversely, doxycycline was associated with reduced thrombus uPA/PAI-1 ratio at 2 and 7 days.|PMC2997482|Although we found that the uPA to PAI-1 balance was affected by both treatments, being decreased in the thrombus with doxycycline and elevated in the vein wall with both LMWH and doxycycline, this also did not appear to affect the overall thrombus size.|PMC2997482","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"53268463":{"subject":"UMLS:C3536832","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9930526325","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The evaluation of insulin sensitivity demonstrated higher HOMA-insulin resistance indices, and lower M values (P < 0.001 and P < 0.05, respectively), while both the AIR and the insulinogenic index were lower in patients with SCA1 compared to controls (P < 0.001 and P < 0.05, respectively).|PMID:20669273|The increase in partial pressure of oxygen (ppO2) and normobaric air can suppress the expression of caspase-3 and will inhibit the apoptosis of gastric mucosal cells.|PMC6437737|Further, we checked for the expression levels of total caspase-3 and cleaved caspase-3 in these lysates and our results strongly supported our hypothesis indicating that ASK-1 protein expression is significantly inhibited in the Ad-SOCS-1 mice even in room air and hyperoxia which is further associated with a significant decrease in cleaved caspase-3 when compared to Ad-GFP control mice.|PMC4457693|The number of activated caspase-3 positive cells increased from PND 10 to PND 13 in the neocortex while the number of activated caspase-3 positive cells in the hippocampus of air-exposed controls decreased over time (figure 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discuss the value of integrating human factors into the design process for a PPT for PED.|PMC7501580|This study details the integration of human factors into the design process for a PPT and PPA for a PED.|PMC7501580|A prototype version of the PPT has been developed and implemented in the PED.|PMC7501580|This case study presents the development of a patient prioritization tool (PPT) and of the related patient prioritization algorithm (PPA) for a pediatric emergency department (PED), relying on a human-centered design process.|PMC7501580","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"86058541":{"subject":"PUBCHEM.COMPOUND:977","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7834967","PMC7834967"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c1a9f1fbefe815bc559802705db437206c5642f677597aab6e46b1577be85e15","tmkp:dfb3f25bbb3a318bbd5464cf805e241ed5eb836769bac95c7e5091cbcf8dfae7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"↑, an increase in target protein; ↓, a decrease in target protein; PARP, poly ADP-ribose polymerase; ERK, extracellular regulated protein kinases; TGF-β1, transforming growth factor-β1; MMP, mitochondrial membrane potential; AQP1, aquaporin 1; VEGF, vascular endothelial growth factor; AMPK, AMP-activated protein kinase; EMT, epithelial-mesenchymal transition; PI3K, phosphoinositide-3-kinase; JNK, c-Jun N-terminal kinase; NF-κB, nuclear factor-κB; PCNA, proliferating cell nuclear antigen; COX-2, cyclooxygenase-2; HIF-1α, hypoxia-inducible factor-1; ROS, reactive oxygen species; STAT3, signal transducer and activator of transcription 3 Rac1, Rac family small GTPase 1; MAPK, mitogen-activated protein kinase; TNF-α, tumor necrosis factor α; PKC-α, protein kinase C system -α; LC3I, the protein expressions of light chain 3I; LC3II, the protein expressions of light chain 3II; Atg7, autophagy related 7; AKT, protein kinase B; GSK3β, glycogen synthase kinase 3β; P-gp, P-glycoprotein; MDR1, multidrug resistance protein 1; α-SMA, alpha-smooth muscle actin; LncRNA-ATB, long non-coding RNA activated by transforming growth factor-β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; HSP, heat shock protein; GRP78, glucose regulated protein 78; Bip, binding immunoglobulin protein; XIAP, X-linked inhibitor of apoptosis protein; MCL1, myeloid-cell-leukemia 1; cFLIP, cellular FLICE-like inhibitory protein; mTOR, mammalian target of rapamycin; B7-H3, GPI-linked CD59 and costimulatory molecule CD276; CTL, cytotoxic T lymphocytes; IDO-1, indolemaine-2,3-dioxygenase-1; CREB, cAMP-response element binding protein; GNF, gastric normal fibroblast; GCAF, gastric cancer-associated fibroblast; IFN-γ, interferon-gamma; MNNG, N-methyl-N′-nitro-N-nitrosoguanidine; TIGAR, TP53-induced glycolysis and apoptosis regulator; PLGC, precancerous lesions of gastric carcinoma; NOX, NADPH oxidase; iNOS, inducib|PMC7834967|↑, an increase in target protein; ↓, a decrease in target protein; PARP, poly ADP-ribose polymerase; ERK, extracellular regulated protein kinases; TGF-β1, transforming growth factor-β1; MMP, mitochondrial membrane potential; AQP1, aquaporin 1; VEGF, vascular endothelial growth factor; AMPK, AMP-activated protein kinase; EMT, epithelial-mesenchymal transition; PI3K, phosphoinositide-3-kinase; JNK, c-Jun N-terminal kinase; NF-κB, nuclear factor-κB; PCNA, proliferating cell nuclear antigen; COX-2, cyclooxygenase-2; HIF-1α, hypoxia-inducible factor-1; ROS, reactive oxygen species; STAT3, signal transducer and activator of transcription 3 Rac1, Rac family small GTPase 1; MAPK, mitogen-activated protein kinase; TNF-α, tumor necrosis factor α; PKC-α, protein kinase C system -α; LC3I, the protein expressions of light chain 3I; LC3II, the protein expressions of light chain 3II; Atg7, autophagy related 7; AKT, protein kinase B; GSK3β, glycogen synthase kinase 3β; P-gp, P-glycoprotein; MDR1, multidrug resistance protein 1; α-SMA, alpha-smooth muscle actin; LncRNA-ATB, long non-coding RNA activated by transforming growth factor-β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; HSP, heat shock protein; GRP78, glucose regulated protein 78; Bip, binding immunoglobulin protein; XIAP, X-linked inhibitor of apoptosis protein; MCL1, myeloid-cell-leukemia 1; cFLIP, cellular FLICE-like inhibitory protein; mTOR, mammalian target of rapamycin; B7-H3, GPI-linked CD59 and costimulatory molecule CD276; CTL, cytotoxic T lymphocytes; IDO-1, indolemaine-2,3-dioxygenase-1; CREB, cAMP-response element binding protein; GNF, gastric normal fibroblast; GCAF, gastric cancer-associated fibroblast; IFN-γ, interferon-gamma; MNNG, N-methyl-N′-nitro-N-nitrosoguanidine; TIGAR, TP53-induced glycolysis and apoptosis regulator; PLGC, precancerous lesions of gastric carcinoma; NOX, NADPH oxidase; iNOS, inducib|PMC7834967","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99956924","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"44403993":{"subject":"PUBCHEM.COMPOUND:439501","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999437965","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"A novel observation was the fact that ouabain induced IL-10 and VEGF as well.|PMC4034513|Nevertheless, the levels of IL-10 and VEGF measured in the supernatants of cells cultured for 24 hours in the presence of ouabain were also higher than control levels (Figures 6(c) and 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with L-Dopa and dopamine agonists is associated with lower levels of anti-apoptotic Bcl-2 in the blood, and higher densities of the peripheral benzodiazepine receptor PBRs.|PMC2828394|On the contrary, resistance exercise or levodopa treatment suppressed Bax expression and enhanced Bcl-2 expression in PD mice (P< 0.05), causing in decrement of Bax to Bcl-2 ratio.|PMC8103184|The study by Dorszewska and Kozubski demonstrated that PD patients treated with L-dopa had significantly increased level of PARP protein and significantly decreased levels of Bax and Bcl-2 proteins.|PMC3958954|Patients treated with L-Dopa and dopamine agonists showed the lowest values of Bcl-2, coupled with the highest density of PBRs, while increased levels of Cu/Zn SOD were found in the group under monotherapy with L-Dopa.|PMID:15254790","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9996466525000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"79558136":{"subject":"PUBCHEM.COMPOUND:10607","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2774782","PMID:19628068","PMC6875004","PMID:22142990"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9995448","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Contrary 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combination of salbutamol and prednisolone resulted in a partial, but statistically significant inhibition of ERK1 phosphorylation and IκB phosphorylation (Fig. 9).|PMC3682954|The beneficial effect of prednisolone on this GN may be partially mediated by the suppression of MAPK, followed by the suppression of AP-1.|PMID:9697658|SB-681323 inhibited the p38 MAPK pathway to a greater degree than prednisolone 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Representative immuno-blots that demonstrate the suppression of the mitogen-activated protein kinase (MAPK) pathway by camel milk, as evidenced by lowered expression of phospho-p38 (p-p38) MAPK (Thr180/Tyr182)/total p38 MAPK, phospho-c-Jun N-terminal kinase 1/2 (p-JNK1/2 (Thr 183/185)/total JNK1/2, and phospho- extracellular signal-regulated kinase 1/2 (p-ERK1/2 (Thr202/Tyr204)/total ERK1/2 ratios.|PMC8156933|In perspective, camel milk has shown remarkable efficacy for inhibiting the MAPK pathway in rodent models of 5-fluorouracil-induced renal injury, rheumatoid arthritis, and LPS-triggered respiratory distress.|PMC8156933|Interestingly, camel milk demonstrated multi-pronged anti-inflammatory effects against cyclosporine-evoked renal injury, as proven with significant suppression of the upstream p38 MAPK, JNK1/2, and ERK1/2 pro-inflammatory components of the MAPK pathway.|PMC8156933|These findings propose that camel milk may be a promising agent that inhibits cyclosporine-triggered renal inflammation via curtailing the p38/ERK/JNK MAPK and NF-κB pathways, matrix metalloproteinases, and pro-inflammatory cytokines.|PMC8156933|Parallel to the NF-κB pathway inhibition, camel milk also counteracted the activation of renal MAPK signaling, as seen by downregulated expression of p-p38MAPK/total p38 MAPK (by 53.9%), p-JNK1/2/total JNK1/2 (by 39.1%), and p-ERK1/2/total ERK1/2 (43.3%), relative to the renal injury group.|PMC8156933","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"30460581":{"subject":"NCBIGene:6513","object":"MONDO:0012805","predicate":"biolink:genetic_association","attributes":[{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop","infores:pharos"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:uniprot","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"}]},"11115798":{"subject":"PUBCHEM.COMPOUND:10297","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:31764844","PMC6882595","PMC5209272"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.999251","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Lastly, serum vascular endothelial growth factor (VEGF) C concentration was significantly higher in the GA group than in the PPA group.|PMC5209272|Lastly, serum vascular endothelial growth factor (VEGF) C concentration was significantly higher in the GA group than in the PPA 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the precursor of EPA and DHA, suppressed high-glucose-induced VEGF secretion in streptozotocin-induced diabetic animals.|PMC5016593|Moreover, ALA treatment has been shown to suppress expression of vascular endothelial growth factor (VEGF), angiopoietin 2 and erythropoietin via blockade of superoxide formation.|PMID:23790257|In an extension of this study, we noted that ALA, the precursor of EPA and DHA, suppressed high-glucose-induced VEGF secretion in streptozotocin-induced diabetic animals, implying that pathological VEGF secretion is inhibited by ALA, similar to EPA and DHA.|PMC4296072|Cells incubated with ALA had a statistically significantly lower production of VEGF, RANTES, ICAM-1, MCP-1 and IL-6 compared to cells incubated without additional ALA.|PMID:30661600|ALA significantly modulated the growth kinetics of the cells and reduced cell migration with concomitant decrease in the expression of VEGF, MMP-2, and MMP-9 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we demonstrate that VEGF mRNA levels are increased by anisomycin, a strong activator of stress-activated protein kinases.|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 3'-UTR).|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 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serum insulin concentration was significantly higher in dexamethasone-treated horses than control horses on days 7, 14, and 21.|PMID:17605611|In the dexamethasone group, there was an increase in serum insulin and homeostatic model assessment of insulin resistance, while total bone mineral density decreased.|PMC6604092|In the same study by these authors, administration of dexamethasone to another group for two days resulted in an increase in fasting insulin and HOMA-IR without a significant change in serum visfatin concentrations.|PMC3386777|Dexamethasone administration resulted in an increase in fasting insulin (from 11.6 +/- 6.8 to 17.1 +/- 7.2 muU/ml; p = 0.003), and an increase in HOMA (from 2.73 +/- 1.74 to 4.02 +/- 2.27; p = 0.015), although without a significant change in RBP-4 levels (119 +/- 26.8 vs. 117.5 +/- 24.8 mg/ml, p = ns).|PMID:18777500|Furthermore, in fetal sheep, both glucose and insulin are able to upregulate muscle GLUT4 protein expression and, therefore, the dexamethasone-induced increments in plasma glucose and insulin are likely to contribute to the increase in muscle GLUT4 seen in the present study.|PMC3530600","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"105454734":{"subject":"PUBCHEM.COMPOUND:4946","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Furthermore, propranolol and SP600125, which are LPIN1 and JNK1/2 inhibitors, respectively, strongly suppressed IL-33-induced colony formation in breast cancer cells and mammary gland tumor development.|PMC8124251|After administration of a nonselective β-adrenergic receptor blocker (propranolol) before induction of cerebral ischemic injury, hepatic adrenergic transduction, TNF-α expression, ER stress, and the activation of the JNK1/2, IKK-β, and NF-κB pathways, and serine phosphorylation of IRS-1 were all attenuated.|PMID:24437486|Tau hyperphosphorylation shown by Tg2576 mice was also decreased in the hippocampus of propranolol-treated mice, an effect probably related to an increase of GSK3β phosphorylation (inactive form) and a decreased JNK1 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Triamcinolone acetonide could prohibit proliferative scars through inhibiting cell proliferation and TGF-beta1 expression, as well as inducing apoptosis.|PMID:19408724|The modulation of Col-1, VEGF, TGF-beta1 and MMP-2 expression by triamcinolone and 5-fluorouracil alone or their combination varied between individual cell lines; the trend is to promote a reduction in Col-1 and TGF-beta1 but up-regulation of MMP-2 expression.|PMID:23810214|While the effect of inducing apoptosis was stronger than that of triamcinolone acetonide, the effect of inhibiting TGF-beta1 expression was weaker than those of triamcinolone acetonide and IFN alpha-2b.|PMID:19408724","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:19408724","PMID:23810214","PMID:19408724"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"76718666":{"subject":"PUBCHEM.COMPOUND:86287518","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9932641414999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4aa2b69fd6deb6648892a024f2369578f3993b2f2a70c190539faffe68fc9211","tmkp:84a4b9ef6ef102c4b6d71412c90259655ef5bdb78657099ff7645ad708374d2b","tmkp:8a47218230b77cef7a6db3c9103411253dba54c1a13422be584c8ea67eef5959","tmkp:5927499dd16d2ca592386ff116f4ac1516de5907b82525bce69571338e2d5259","tmkp:7dbcbbe5686c0d0c43c1e96f17c8f94423658c38aa25eb2bd3216e6e34032b86","tmkp:109c3f70d9f6f1dbb64a12c46cc8cb85c0b243e670decbd1cfb0f6332848f1ad","tmkp:7ada375a638bfe8d699defd6e318804e9a48fff208504cac43db002139cbb766","tmkp:2190dc01c4debda84f68380ae77e477d49dd1ac6652d328117a02c9992b35484","tmkp:77606540604eb32f896b7e927a6bf82789647f51a77fb609afd5c9b235a48bec","tmkp:561652860ead10d818e77b9dec51a06af88c3e58638c1e388387ba09fb2402e6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"IMD also upregulated the protein and mRNA expression levels of VEGF and VEGFR2 and downregulated the expression level of MMP2, MMP9 and ET-1.|PMC7666991|Both CLR/RAMP1 and CLR/RAMP2 appeared to mediate the pro-angiogenic effect, which was associated with a significant increase of vascular endothelial growth factor (VEGF) mRNA expression 18 h following IMD administration, indicating that the observed pro-angiogenic effects are related, at least in part, to an increased synthesis of this growth factor promoted by the peptide.|PMID:20596610|Both CLR/RAMP1 and CLR/RAMP2 appeared to mediate the pro-angiogenic effect, which was associated with a significant increase of vascular endothelial growth factor (VEGF) mRNA expression 18 h following IMD administration, indicating that the observed pro-angiogenic effects are related, at least in part, to an increased synthesis of this growth factor promoted by the peptide.|PMID:20596610|However, compared to the IRI group, the IMD group had significantly higher expression levels of VEGF and VEGFR2, although they were still lower than those in the sham group.|PMC7666991|Therefore, we may conclude that IMD could promote neovascularization by upregulating the expression of VEGF and VEGFR2 in the kidney after ischemia reperfusion.|PMC7666991","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:25205865","PMID:25637316","PMID:20596610","PMC7435801","PMID:26905334","PMC4364779","PMC7666991"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"111840735":{"subject":"PUBCHEM.COMPOUND:1032","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9991516","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC7999574"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The Propylamylatin formula solution containing the propionic acid/isoamyl hexanoate electrolyte mixture was administered to tens of animals suffering with PED to assist in rehydration and electrolyte balance.|PMC7999574","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4f4ca90989e20eddfc205132db5ee475e3b114f7c31ebc465f5ed269962c253e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"15315944":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:24","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:30590389"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.986073","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a6be6c713768d35ef45d93ad81f573b9c4e0497c42f2f2772f050cb1e373dec0"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"To investigate the role of RMP in cardiac function, Cre-loxP recombinase technology was used to generate tamoxifen-inducible cardiomyocyte-specific Rmp knockout mice.|PMID:30590389","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"65816961":{"subject":"PUBCHEM.COMPOUND:4943","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9964964123376624","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4244672","PMC6278392","PMC3050912","PMID:28478273","PMC7445405","PMID:19703415","PMC6662450","PMC3854382"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"In this study, with similar expression of total Akt, the expression of p-Akt, which is essential in the protective signaling pathway in cardiomyocytes, was much higher in the propofol treated group.|PMC6662450|PI3K and p-Akt protein expression was detected in all lung tissue samples from control and experimental rats, as shown in Figure 4. Compared to the control group, PI3K and p-Akt protein expression levels were significantly decreased in the LPS and wortmannin groups; however, the levels of PI3K and p-Akt protein expression were elevated in the propofol group (P<0.05 or P<0.01, n=6 animals per group).|PMC4244672|Our study indicates that propofol pretreatment attenuated LPS-induced ALI, partly by activation of the PI3K/Akt pathway.|PMC4244672|Here, we report that propofol protects cardiac H9c2 cells from hydrogen peroxide (H(2)O(2))-induced injury by triggering the activation of Akt and a parallel up-regulation of Bcl-2.|PMID:19703415|Propofol either alone or with prior nobiletin treatment had down-regulated TLR4 and TLR4-mediated NF-κB signaling and caused activation of Akt/mTOR 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administration of vitamin B1 (50 mg per day) dramatically improved his symptoms in a few days and the level of VEGF returned to nearly normal.|PMID:15199756","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.97696483","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"42632004":{"subject":"PUBCHEM.COMPOUND:4927","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:5ed9c5aca5ec6700dc976c9cecc987ed7406c99e1025287b417c6189fa28fd7a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"As expected from an mPT 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water extract (25, 50, 100, and 200 µg/ml) dramatically suppressed β-HB-induced increases in both fibronectin and bioactive TGF-β in a dose dependent manner.|PMC3493576","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b5551ac270619b677ce5dc723ea2847cdd04b12443a50c9956bcb6b8ebf33427"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3493576"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9995989","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"24101713":{"subject":"PUBCHEM.COMPOUND:3715","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996859","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The different concentrations of indomethacin decreased FN and PAI-1 secretion in the 2.5% glucose or the LPS group within 24 h (P < 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expression of Bcl-2 in the finasteride-loaded microspheres-treated group was increased, whereas the expression levels of cleaved-PARP, cleaved-caspase-3, TGF-β2 and Bax were lower than those in the microspheres-treated group (Fig. 5A and B).|PMC6488187|Both azelaic acid and finasteride increased the expression of BCL-2 protein (p < 0.05) and decrease the expression of bax protein (p < 0.05).|PMC3813161|The results for azelaic acid and finasteride were converse, and the expression of BCL-2 was increased in these groups to more than weak (+/-) in approximately 51.5% and 60% of them, respectively (p < 0.05).|PMC3813161","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"85310673":{"subject":"PUBCHEM.COMPOUND:3715","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9996159","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Our research suggests that BAD-Indomethacin's inhibition with the other two hub proteins, MAPK8-6MNA, MAPK10-Rofecoxib might play cumulative actions by inactivating the RAS signaling pathway against COVID-19.|PMC8100301","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC8100301"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d641f8ae09b4f10749121b03c82b6a5d5ec3cad74aed2c1c204993bdda1ee601"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"61711740":{"subject":"PUBCHEM.COMPOUND:10607","object":"NCBIGene:994","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop","infores:hetionet"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:lincs","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"}]},"64646478":{"subject":"PUBCHEM.COMPOUND:2802","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6368667","PMC7969896","PMC7969896"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99889691","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Nobiletin and clonazepam upregulated PI3K/Akt signaling following PTZ-induced seizure.|PMC6368667|Moreover, the administration of nobiletin and clonazepam can significantly upregulate the phosphoinositide 3-kinase/protein kinase B (PI3K/Akt) signaling.|PMC7969896|Moreover, the administration of nobiletin and clonazepam can significantly upregulate the phosphoinositide 3-kinase/protein kinase B (PI3K/Akt) signaling.|PMC7969896","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:633485570fd7c96708efe202b0190b78bed93a5b57b5fd87f6ade5bc5031fb45","tmkp:16541c80a5f2f7b905fd6e860fd653972489e36538267f20291aaa3daf7fb17f","tmkp:d184b2501bf6960c8657284977cf5eeabcb315d909cf8b718b0ba902ac09d15b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"20936487":{"subject":"PUBCHEM.COMPOUND:5743","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:6daa71145bdffb0569731b7b6aed09c98a67f6b595df938a3abd666eb10680cd","tmkp:586862c61693739cd193f5352fb2ca026b5742f3435c4188f377f16a2b0c74ab","tmkp:db0c8829266fba8f9480f062d00b5d639d6334a5cf9158f436977dd713b473d9","tmkp:f62a42275864ac82a9da845c435c0781160b65489f24e5ac7bfeae8b65b82658","tmkp:34da2caffc551dea01a5bf9dbcc4bba4564e7a0902ed3a77dc9e0e4e8ae042cd","tmkp:f76bbbed22a16d303b87065182755b38476b5d5d688161721d00667c00b54a72"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Stable transfectants of the SV40-transformed hamster cell line CO60 were used: COM3 cells contain a construct to overexpress the poly(ADP-ribose) polymerase (PARP-1) DNA-binding domain (DBD) when induced by dexamethasone, as well as a construct for the constitutive overexpression of the human glucocorticoid receptor (Hg0).|PMID:11258844|COM3 rodent cells carry a construct for the dexamethasone-inducible overexpression of the DNA-binding domain of PARP1 and exhibit greatly impaired DSB rejoining after irradiation.|PMID:17889269|We measured rejoining of DSBs in a cell line, COM3, conditionally expressing PARP-1 DBD under the control of a dexamethasone-inducible promoter (Supplementary Figure 2A).|PMC1693894|However, in COM3 cells treated with dexamethasone to induce PARP-1 DBD overexpression, the fast component of the rejoining kinetic was largely reduced, and residual fragmentation increased concomitant with the increased damage fraction in slow rejoining.|PMID:11258844","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC1693894","PMID:11258844","PMID:17889269","PMC6466787"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.95621435","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"62363923":{"subject":"PUBCHEM.COMPOUND:5280343","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996428838983051","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC7910826","PMC2826114","PMC7459988","PMC7587811","PMID:27008429","PMC7996139","PMID:12431781","PMC6839267"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, quercetin is known to ameliorate the pathogenic process of asthma by decreasing IL-4 and IFN-γ synthesis and by regulating Th1/Th2 balance.|PMC7996139|Although it has been reported that quercetin can inhibit the ability of human peripheral-blood mononuclear cells to spontaneously produce IL-4, but not IFN-γ in vitro via inhibition of cytokine mRNA expression, the precise mechanisms of quercetin’ on cytokine production are not well understood.|PMC7459988|Additionally, quercetin demonstrates an immunosuppressive effect on dendritic cell function, downregulating Th2-derived production of interleukin 4 (IL-4).|PMC7910826|Further, quercetin treatment also increased the phenotypic expression of IFN-γ positive cells and decreased IL-4 positive cells.|PMC2826114|Further, quercetin treatment increased the phenotypic expression of IFNgamma cells and decreased IL-4 positive cells by FACS analysis, which corroborate with protein secretion and gene expression 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interferes with lymphotoxin α signaling, necrostatin-1 inhibits necroptosis pathway, hyaluronan blocks MAPK pathway, and paclitaxel suppresses AP-1 activity which contribute to chondrocyte dysfunction in rheumatoid arthritis.|PMC7038065|In an in vitro study, Albano et al. found that only high molecular weight form of sodium hyaluronate efficiently inhibited the IL-17A-mediated activation of ERK1/2 and nuclear factor kappa B and production of reactive oxygen species in human nasal epithelial cells.|PMC6032683|Hyaluronic acid targets CD44 and inhibits FcRI signaling involving PKC, Rac1, ROS, and MAPK to exert anti-allergic effect|PMC5200957|Small size hyaluronan oligomers suppressed the MAPK and PI3K/AKT pathways in multidrug-resistant tumor cells and sensitized cancer cells to a variety of chemotherapeutic drugs.|PMC4504107|In an in vitro study on human nasal epithelial cells, Albano et al. observed that only high-molecular-weight form of sodium hyaluronate efficiently inhibited the rhIL17Amediated activation of ERK1/2, IkBa phosphorylation and NF-kB signal pathway activation, ROS production, IL-8 and NOX-4 proteins, and mRNA levels, therefore exhibiting an anti-inflammatory/anti-oxidative 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our microarray experiments, we found that acute ethanol rapidly induces several genes that regulate the cellular immune response and participate in the production of inflammatory soluble intermediates, including Pea15, Rsg16, Cd97, Entpd2, Gas6, and Fdz5.|PMC3607153|The hyperoxidative state produced by ethanol in astrocytes can trigger apoptosis in some functionally impaired cells, and accordingly, we found that ethanol induced several apoptosis regulation genes in our microarray study (Col18al, Rtn1, Pea15, Idb4, and Insl6).|PMC3607153","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"99871548":{"subject":"PUBCHEM.COMPOUND:23985","object":"MONDO:0011724","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"The potential use of KD in pathological conditions characterized by chronic hypoglycemia is further strengthened by the fact that KD is the gold standard in the treatment of GLUT1 deficiency syndrome, which can be considered a metabolic phenocopy of hepatic GSD, since blood glucose cannot be transported into neuron.|PMC4101992","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99013805","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:98cdd66f27539bf1e594eba17aeda514e740d0f39401429f0fc9edee4cf3ce59"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC4101992"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"52453644":{"subject":"PUBCHEM.COMPOUND:6957673","object":"NCBIGene:355","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3924998"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"These effects are reversed upon treatment with PFTα, which protects against CIN-induced apoptosis of HepG2 cells and results in decreased levels of p53, CD95, Bax, and PARP cleavage.|PMC3924998","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9997236","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:12edef15e3be21a53da0d6c98226633db3a27876c2e518083b096c16cd6b547c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"30795517":{"subject":"PUBCHEM.COMPOUND:3033","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99809557","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:db8c238fbdc353572212d4302d354f35f87bca74a2402de2b6b52ecb95f5b5e2","tmkp:90f0a9ccc3216af991d3ef0262ead9f5718c6e83fa6d2f03b58c9cced0aae416"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6099564","PMID:11992736"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The results showed that diclofenac sodium had the ability to increase the level of IL-4 and IL-10.|PMC6099564|Collectively, these data suggest that diclofenac: (i) induces a T-cell-dependent direct PLN reaction that; (ii) provides non-cognate help for IgG AFC production when co-injected with TNP-Ficoll, possibly through the formation of neo-antigens; and (iii) possesses intrinsic adjuvant activity that selectively induces IL-4 mediated production of IgG(1) and IgE against co-injected TNP-OVA.|PMID:11992736","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"11557210":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9987970658333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:804faa4daf38666233db70c4dc36a1ab0c5f528d100ecd770b6721a360c75b2f","tmkp:4cdd2ec6c42cc5e4c45c964040528008fe244986a02b328f359ec224e7d172aa","tmkp:e75afe8bb3aed2587da8a1d2020bce4fec1cc0b5a850b325ec19cfae09156176","tmkp:331b7feee761c21ea20db499331542edccc12cc425336d0046afe151c6078685","tmkp:6f21db9a48d487521ed1f973d9c7ff51e5833658d04c28c87de0092ea343f7bd","tmkp:baed5715ecfb5a3dcd3cf58682c63533ce4d4ec357cf6256c88e6f425d35cbe9","tmkp:92f16fa7e4ebd60146f0273977136fca53f48c52c8eb01d4083f3aaad38216b6","tmkp:38214d99bd515333dd930d3735d47eaddd5a6a75602a01a40f603debb7b0f1ad","tmkp:72a14e6c0a3a81f66cb08ed75af6beab68d07d314e23d899994fb6189105544a","tmkp:76fd27483af087277d855785da1d74640eec2b975c749e97005029597b75634e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The current study provides the first evidence that MMC induces p-Akt, which in turn induces resistance to MMC and enhances the migration abilities of aggressive CL1-5 cancer cells.|PMC5346766|In sum, the present study revealed that the level of p-Akt is an important factor underlying MMC resistance and that MMC seemed to enhance the migration abilities of aggressive CL1-5 cancer cells through the induction of p-Akt.|PMC5346766|Therefore, we hypothesized that the activation of p-Akt in CL1-5 cells after MMC treatment might play a crucial role against MMC-induced cytotoxicity.|PMC5346766|Thus, the MMC-induced high level of p-Akt might either inhibit pro-apoptotic proteins or activate pro-survival genes to reduce MMC induced cytotoxicity in CL1-5 cells.|PMC5346766|However, CL1-5 cells had both a higher level of endogenous p-Akt (S473) and strong activation of p-Akt after MMC treatment compared to CL1-0 cells (Figure 3B).|PMC5346766","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4607229","PMC6030503","PMC5346766"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"94797948":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"At the same time, Bcl2 expression was increased, whilst the protein expression of Bax was reduced.|PMC4541019|The same treatment also significantly increased the apoptosis level of HK-2 cells, as shown by the increased Bax-to-Bcl2 ratio and expression of cleaved Caspase 3 (Figures 3D,E).|PMC7508261|We also confirmed an increase in Bcl-2 protein levels in a time dependent manner under the same conditions (Fig. 1C).|PMC4469911|Additionally, the expression levels of P‑gp and p‑P65/P65 were significantly reduced following the addition of the miR‑146a antagonist, whereas the expression levels of Bcl‑2/Bax significantly increased under the same conditions.|PMID:29363732|Additionally, p53 and Bcl-2 pro-apoptotic genes were upregulated in the same region, accompanying with the decrease of p53 inhibitors SirT2 and 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ductal endothelial cells, ibuprofen significantly induced vascular endothelial growth factor and its receptor 2, but not receptor 1, whereas indomethacin did not alter the expression levels of the vascular endothelial growth factor system.|PMID:29198223|In contrast, ibuprofen significantly induced vascular endothelial growth factor and its receptors 1 and 2 in aortic endothelial cells, whereas indomethacin only induced vascular endothelial growth factor receptor 2.|PMID:29198223|Prophylactic Use of Ibuprofen Significantly Suppresses Serum Levels of MCP-1 While Increasing VEGF and MMP-9 Expression|PMC6566430|The mechanism underlying this increase in VEGF with the combined administration of P. gingivalis and paclitaxel is not clear; however, we suspect that the reduced paclitaxel resistance in mice administered ibuprofen may be due to the increase in VEGF, which can help deliver paclitaxel to the tumor mass.|PMC6566430|In addition, VEGF was increased in the presence of ibuprofen, especially in paclitaxel-treated and/or P. gingivalis-treated mice.|PMC6566430","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2746691","PMC4391471","PMC6566430","PMC8150526","PMID:29198223","PMID:27016022","PMC6335784"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"54390083":{"subject":"PUBCHEM.COMPOUND:5743","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Further, dexamethasone reduced the cellular content of GLUT-1 when insulin and glucose were absent (p < 0.05), but did not significantly affect the expression of GLUT-4 in the presence of insulin (p > 0.05).|PMID:17072757|In both systems, insulin increased and dexamethasone decreased GLUT1 messenger RNA (mRNA) and protein, an effect inhibited by the glucocorticoid antagonist RU 38486.|PMID:7588207|In 3T3-L1 adipocytes treated with dexamethasone, the GLUT1 protein expression level was decreased by 30%, which possibly caused decreased basal glucose uptake.|PMID:11016454|As shown in Fig. 1A, both doses of dexamethasone (10 and 100 μM) reduced the expression of several HIF-1 targets at mRNA level, such as VEGF, Glut1 and LDHa in our colorectal carcinoma model.|PMC5021256|Dexamethasone blunted the increase of GLUT1 mRNA abundance and increased the liver PEPCK mRNA abundance.|PMID:8774068","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9995885000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5021256","PMID:9541032","PMID:11016454","PMID:8774068","PMID:11250642","PMID:1596083","PMID:7588207","PMID:7818550","PMID:9468291","PMID:17072757"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:13d945910241db0a89cf96909637dee1f0bcdf91400c87f4922a197ecbc4284c","tmkp:940795909304b305cf256cb7bcf4d434fd5ffc73e71b8fb18af172c991b42c62","tmkp:21325e5dd3331ecc91040ecaedc668b290cf773f96a8d28b1f00a60c70221202","tmkp:a8e39edd3d6fa91838a62fec402d36fa6984e730bac64130695d613722a0888d","tmkp:521aac020a7e1b3d97856b99569d8d83fd50bea0453034e9e12fac45808bcb43","tmkp:de769e89f7234c148d64ea580e00af1331d822245f689a596f2cfd22aaa6a811","tmkp:00016f176dd2a8490f67f3f2d49a387c58736f7516ca9f4ce9d1516c41b90a9e","tmkp:50466771752c3df250e296df97f92bc6550b9bfab2a9dad2bb62ff19acef4004","tmkp:8aef932ead55a3f57f733177ae6019e16640be01e64fa9fe70849243178c0914","tmkp:a71531fbfba5618e674dc45420c27e26a8443a67327732d378520fdcb1cc0d19"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"119216450":{"subject":"PUBCHEM.COMPOUND:31307","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9939161","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3f468bd13416143cead7c89ac18e28ea0241ae9043ffe040a1b604c1b4abc747","tmkp:16144b21e42af258dedfa20477109589d963b3e5d236593202550ef3197d1789","tmkp:faa4b349110e5e3dacef5fa3a513e1eae5d619b26aa50a5b616b04729591ea06","tmkp:c3f99f0e68163ed356e91c776f75dc19ff435b228e66e818828ff25eb215c0de","tmkp:e24ca1fe950c8bab019b221cdcf35e57c93a219b6fd3109c164e364de0710b40","tmkp:e935296dc1e2937a8e0e9ae720efda87e775be26c85d49dbc1409f407b53cd2b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3428247","PMC3573139","PMID:18299840","PMC3508742"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"With the aid of the literature, it is known that triamcinolone acetonide regulates VEGF in a concentration-dependent manner, such that triamcinolone acetonide exerts a biphasic effect on retinal pigment epithelial cell proliferation, stimulating cell growth at lower concentration (lower than 1 μM, ie, 0.44 μg/mL) but inhibiting cell growth at higher concentration (higher than 100 μM, ie, 44 μg/mL).|PMC3428247","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"88473087":{"subject":"NCBIGene:142","object":"PUBCHEM.COMPOUND:5746","predicate":"biolink:decreases_response_to","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:28757444"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"dct:description","value":"decreases response 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ibuprofen.|PMID:19609076","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99928963","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"27887538":{"subject":"UMLS:C5242471","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4728290","PMC8156933"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9760548652941177","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:95b604e2b8a41ecff99d67de55c79ab5bf806e74689f3281325e437cc9ac492a","tmkp:b8025e8fd46f1757a1cece7f2e797541cb33651410bdf9c293cacdc645fa11d7","tmkp:296c1454793c903e802dc6a47911d0d770a5e1f13ce10113597142f6964000d7","tmkp:b0311726942726e4bd15081d21bf0d18fd29aa48ee393bb6575c3c272b2f0b12","tmkp:b8058741455221137db39596b34436c5fd5286c54a0486dcfb05e0de6cf45f09","tmkp:68fd43cad950fadb433cf57471a5376f44dcd7e6c8f6055e51f0659157d3778a","tmkp:2ff3797d1d253ba25466e31b672c292fb4c09fb1224e12b4f2f38b8842cb896f","tmkp:2eede5deacd7c86bbe75480a0f1ce44ecbaf6c034c09d262db2d16dd41207055","tmkp:e36cbc548771c5550ce577b92818339ea9e5da45c0c8c840ecab4eea6982ef28","tmkp:a279231239f03fb8f5ed4fe247f1f86ed30d81b64506894d23cf2ea89d7bae17"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Interestingly, camel milk demonstrated multi-pronged anti-inflammatory effects against cyclosporine-evoked renal injury, as proven with significant suppression of the upstream p38 MAPK, JNK1/2, and ERK1/2 pro-inflammatory components of the MAPK pathway.|PMC8156933|Parallel to the NF-κB pathway inhibition, camel milk also counteracted the activation of renal MAPK signaling, as seen by downregulated expression of p-p38MAPK/total p38 MAPK (by 53.9%), p-JNK1/2/total JNK1/2 (by 39.1%), and p-ERK1/2/total ERK1/2 (43.3%), relative to the renal injury group.|PMC8156933|According to the current findings, the proposed mechanisms pertaining to the attenuation of cyclosporine-evoked nephrotoxicity are: (A) Camel milk inhibited the upstream pro-inflammatory p38/ERK/JNK MAPK pathway, as revealed by lowered phosphorylation of the three subfamilies of MAPK (p38 MAPK, ERK1/2, and JNK1/2).|PMC8156933|(A) Representative immuno-blots that demonstrate the suppression of the mitogen-activated protein kinase (MAPK) pathway by camel milk, as evidenced by lowered expression of phospho-p38 (p-p38) MAPK (Thr180/Tyr182)/total p38 MAPK, phospho-c-Jun N-terminal kinase 1/2 (p-JNK1/2 (Thr 183/185)/total JNK1/2, and phospho- extracellular signal-regulated kinase 1/2 (p-ERK1/2 (Thr202/Tyr204)/total ERK1/2 ratios.|PMC8156933|Parallel to the NF-κB pathway inhibition, camel milk also counteracted the activation of renal MAPK signaling, as seen by downregulated expression of p-p38MAPK/total p38 MAPK (by 53.9%), p-JNK1/2/total JNK1/2 (by 39.1%), and p-ERK1/2/total ERK1/2 (43.3%), relative to the renal injury group.|PMC8156933","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"82866240":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9954498948611111","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5644366","PMC7961436","PMC2898903","PMC4626203","PMC1382249","PMC3101953","PMC6262987"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:1e8295f26f9dfc6eb2211f2267f65fd16a7f5399914c4ea9203a83b36cb7f378","tmkp:0f953d3d84d53c4e69651ec9a04bef760253d5b6c24d36c27f8ea358876e03b0","tmkp:de6788781616dc851a05d5f114988b54849263be3e36e1350d01e91fddd3dfea","tmkp:1956d348a14e125f76eeeb94e4722c1f112fc2fcee0b943a3ea17985b865b009","tmkp:d28564c03416df07cfe7f303878d6dbdcd99c93af95de29a668a53cc09e802ca","tmkp:774ff0fcafde7548d4db810524a5996481a1231ca2a3e412a554de8d5ef77197","tmkp:cd627362c67ccef21461c4fcf56fa25cd147261cc2d9ad1e3d3b15517a1ce6cf","tmkp:25a2a9c30c8136ca52d5113a94a2e969433fa127ad0b939e8dd69bd46eb60668","tmkp:c83a9ece7be03cb6f55ce4259216fe45329204de5a3e8b9eacf820c6cebd790c","tmkp:0bd820d6ae9957c1cf678d5f195a416f306f8ccd15d68ffdba3eb8e356acd95d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Formalin injection results in spontaneous pain behaviors and increases the expression of the mu-opioid receptor, c-Fos, and phosphorylated extracellular signal-regulated kinase (p-ERK1/2), which participates in MAPK signaling in the ipsilateral trigeminal ganglion (TG).|PMC7961436|Activation of ERK1/2 was enhanced after formalin challenge in the spinal dorsal horn neurons, whereas the inhibition of ERK1/2 reduced nociceptive response in the late phase of formalin test.|PMC5644366|At 30 minutes following injection, ERK1 and ERK2 phosphorylation was significantly higher in formalin-injected rats than in either normal control rats or saline-injected control rats (p < 0.05, p < 0.01; Fig 5a–5c).|PMC4626203|In the wild type mice, blots of tissue taken from the side of the spinal cord ipsilateral to the formalin injection showed significant stimulation of both ERK1 and ERK2 when compared to the contralateral side (Fig 5a and 5b), whereas ERK activation in the spinal cords from the DN MEK mice was not significantly different from their contralateral sides.|PMC1382249|ERK1/2 activation in the hypothalamic paraventricular nucleus (PVN) has also been reported after intraplantar formalin or i.t.|PMC3101953","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"63415060":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6525159"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:cc94a175c8088656c3388738e36c7c9c7a16a13069c4985182ea3439c7f80a98"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"On the contrary, it was observed that, after stimulation with anti-CD3 and anti-CD28, there was a significant increase in CD4+ T cells of a regulatory phenotype (CD25hiFoxP3+LAP+) in untreated psoriasis patients compared with the group treated with methotrexate (p = 0.03) (Fig. 4F).|PMC6525159","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9987011","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"43703615":{"subject":"PUBCHEM.COMPOUND:89594","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Nicotine may promote carcinogenesis through activation of extracellular signal-regulated kinase/cyclooxygenase-2/vascular endothelial growth factor signaling pathway.|PMID:16054976|Moreover the nicotine treatment resulted in the increased expression of ERK1/2 in NGF withdrawn SCG neurons implicating ERK1/2 involvement in neuroprotection.|PMC6312731|Acute nicotine injections following extinction sessions upregulate the active form of ERK1/2 in the ventral hippocampus but have no effect on JNK1 phosphorylation|PMC5698137|Furthermore, the expression of nicotinic acetylcholine receptor (nAChR) α4/β2, the phosphorylation of extracellular regulated kinase 1/2 (ERK1/2) and Ets-like protein-1 (Elk-1), and the expression of early growth response-1 (Egr-1) were increased in the nicotine groups.|PMID:29486207|As shown in Figure 2, cells exposed to 3 min of incubation with nicotine resulted in maximal induction of 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an increased expression of the mRNA coding for the membrane Glucose Transporter-1 (GLUT-1) and a decreased expression of mRNA coding for the negative modulator insulin-like growth factor-binding protein-4 (IGFBP-4) were induced by in vitro treatment with L-carnitine and L- acetylcarnitine separately and in combination; in fact, the effects observed were far more pronounced following concomitant treatment with both compounds.|PMID:15114520","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"48986461":{"subject":"PUBCHEM.COMPOUND:6137","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In MCF-7 cells, one study reported an increase in VEGF expression after MET treatment.|PMC5405996|Expression of VEGF, iNOS, MMP-2, and MMP-9 in aneurysmal walls was also increased by methionine treatment.|PMID:21382440|Western blotting revealed significantly upregulated VEGF, MMP9, and Cadherin 5 levels in the MET group compared with controls (p = 0.021, p = 0.021 and p = 0.033, respectively; Fig. 2E-J).|PMC6367544|c-MET also stimulates angiogenesis through the induction of vascular endothelial growth factor (VEGF) expression (Abounader et al.,), and resistance to bevacizumab, an anti-VEGF monoclonal antibody, occurs by c-MET activation of pro-survival and invasion mechanisms (Lu et al.,).|PMC3619126|The present study demonstrated that c-Met signaling activates both the MEK-ERK and PI3-AKT signaling pathways leading to up-regulation of VEGF expression in the synovial cell 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IL-4 levels were raised equally by both pioglitazone and prednisolone.|PMC3086159|Finally, tissue protein expression of the anti-inflammatory IL-4 was significantly upregulated in prednisolone-treated lungs (2672 ± 96.09 mean pixel density) when compared to Perfadex-treated animals (923.1 ± 50.30 mean pixel density; P<0.001) or shams (662.1 ± 11.89 mean pixel density; P<0.001) (Figure 7A).|PMC3756949|(B) Prednisolone-treated cats with FIV exhibit similar changes in cytokine expression (increased Fas, IL-4, IL-8 and decreased Flt-3L, IL-12 p40, SCF) at 5 days of treatment.|PMC6783960|The rebound phenomenon was confirmed after discontinuation of chronic treatment with prednisolone in chronic CHR in mice, i.e. by evidence of flare thickening of the ear, enhanced expression of mRNA for IL-4 and IL-10 and increased serum IgE.|PMID:12811023|It was shown that GCR subjects had elevated cell numbers expressing IL-2 and IL-4 before prednisolone treatment as compared to the GCS 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mRNA and protein expression level of PCSK9 significantly decreased following treatment with ticagrelor, accompanied with upregulation of B‑cell lymphoma (Bcl) 2 and downregulation of Bcl‑2 associated X, apoptosis regulator, caspase‑3, p38, phosphorylated‑(p) p38, p‑c‑Jun N‑terminal kinases (JNK), p‑extracellular signal‑regulated kinases and the ratio of p‑JNK to JNK.|PMID:30592271|In our study, our results demonstrated that ox-LDL led to increased expression levels of Bax and caspase-3, and decreased the expression level of Bcl-2 in our model, and the Bcl-2/Bax ratio was significantly decreased, and these changes were improved following exposure to 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6 normal subjects, L-dopa (500 mg PO) and apomorphine (0.6 mg sc) increased circulating growth hormone and suppressed prolactin levels in a parallel and quantitatively similar fashion, but only L-dopa induced a rise in plasma glucagon, glucose, and insulin levels.|PMID:591612|Possible mechanisms of a stimulating action of L-DOPA and insulin are 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Western blot results revealed that PPT decreased the expression of Bid, Mcl-1, and Bcl-2, and increased the expression of Bax, apoptotic protease activating factor-1(Apaf-1), and cleaved Poly (ADP-Ribose) Polymerase (c-PARP) in the ESCC cells.|PMC7369713|In addition, the estrogen receptor (ER)α agonist propylpyrazole triol (PPT) prevented a decrease in the ratio of Bcl-2 to the pro-apoptotic protein BAD in mice treated with the neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) (; cf.).|PMC3708543|When CaMKII activity within PPT neurons was reduced coincident with periods of decreased W and increased REM sleep, there were 8 genes involved in cell death whose expression in the PPT was also reduced (Bax, Bcl2, Bcl21, Birc1b, Birc3, Brca, Ei24, and Nfkb1).|PMC2809126| ↑ upregulation ↓ downregulation 5-FU 5-fluorouracil ABC ATP-binding cassette transporter proteins ABCB1, ABCG1 isoforms of ATP-binding cassette transporter proteins ARE antioxidant response element ABT-263 small molecule that inhibits Bcl-2; 4-(4-{[2-(4-Chlorophenyl)-5,5-dimethyl-1-cyclohexen-1-yl]methyl}c-1-piperazinyl)-N-[(4-{[(2R)-4-(4-morpholinyl)-1-(phenylsulfanyl)-2-butanyl]amino}-3-[(trifluoromethyl)sulfonyl]phenyl)sulfonyl]benzamide ABT-737 small molecule that inhibits Bcl-2; 4-{4-[(4′-Chloro-2-biphenylyl)methyl]-1-piperazinyl}-N-[(4-{[(2R)-4-(dimethylamino)-1-(phenylsulfanyl)-2-butanyl]amino}-3-nitrophenyl)sulfonyl]benzamide AKT protein kinase B ALDH aldehyde dehydrogenase ALP autophagy lysosomes systems AMPK AMP-activated protein kinase APAF1 apoptotic protease activating factor 1 APR-246 drug that binds to p53 (restoring p53 function) and depletes glutathione; PRIMA-1, 2-hydroxymethyl-2-methoxymethyl-aza-bicyclo[2.2.2]octan-3-one AR androgen receptor ATR serine/threonine protein kinase Axl, Tyro3 receptors for tyrosine kinase BASE base excision repair Bax Bcl-2-associated X protein/Bcl-2-like protein 4 Bcl-2 B cell lymphoma 2 protein Bcl-XL B cell lymphoma extra-large protein BCRA1, 2 breast cancer susceptible genes BCRP breast cancer resistant protein BER base excision repair BH Bcl-2 homology domain BIM Bcl-2 like protein 11 BNDQ quercetin and doxorubicin co-encapsulated biotin receptor-targeting nanoparticles BPIS bound polyphenols of inner shell from foxtail millet bran BRAF serine/threonine-protein kinase B-Raf C catechin CAB carboplatin CAPE caffeic acid phenethyl ester CAR constitutive androstane receptor caspase-3, 8, 9 cysteine aspartic proteases-3, 8, 9 CBZ cabazitaxel CD44, 24, 133 cluster of differentiation 44, 24, 133 CDF difluorinated curcumin CDK 2,4,6 cyclin-dependent kinases 2,4,6 CDPP cisplatin CE|PMC7013436| ↑ upregulation ↓ downregulation 5-FU 5-fluorouracil ABC ATP-binding cassette transporter proteins ABCB1, ABCG1 isoforms of ATP-binding cassette transporter proteins ARE antioxidant response element ABT-263 small molecule that inhibits Bcl-2; 4-(4-{[2-(4-Chlorophenyl)-5,5-dimethyl-1-cyclohexen-1-yl]methyl}c-1-piperazinyl)-N-[(4-{[(2R)-4-(4-morpholinyl)-1-(phenylsulfanyl)-2-butanyl]amino}-3-[(trifluoromethyl)sulfonyl]phenyl)sulfonyl]benzamide ABT-737 small molecule that inhibits Bcl-2; 4-{4-[(4′-Chloro-2-biphenylyl)methyl]-1-piperazinyl}-N-[(4-{[(2R)-4-(dimethylamino)-1-(phenylsulfanyl)-2-butanyl]amino}-3-nitrophenyl)sulfonyl]benzamide AKT protein kinase B ALDH aldehyde dehydrogenase ALP autophagy lysosomes systems AMPK AMP-activated protein kinase APAF1 apoptotic protease activating factor 1 APR-246 drug that binds to p53 (restoring p53 function) and depletes glutathione; PRIMA-1, 2-hydroxymethyl-2-methoxymethyl-aza-bicyclo[2.2.2]octan-3-one AR androgen receptor ATR serine/threonine protein kinase Axl, Tyro3 receptors for tyrosine kinase BASE base excision repair Bax Bcl-2-associated X protein/Bcl-2-like protein 4 Bcl-2 B cell lymphoma 2 protein Bcl-XL B cell lymphoma extra-large protein BCRA1, 2 breast cancer susceptible genes BCRP breast cancer resistant protein BER base excision repair BH Bcl-2 homology domain BIM Bcl-2 like protein 11 BNDQ quercetin and doxorubicin co-encapsulated biotin receptor-targeting nanoparticles BPIS bound polyphenols of inner shell from foxtail millet bran BRAF serine/threonine-protein kinase B-Raf C catechin CAB carboplatin CAPE caffeic acid phenethyl ester CAR constitutive androstane receptor caspase-3, 8, 9 cysteine aspartic proteases-3, 8, 9 CBZ cabazitaxel CD44, 24, 133 cluster of differentiation 44, 24, 133 CDF difluorinated curcumin CDK 2,4,6 cyclin-dependent kinases 2,4,6 CDPP cisplatin 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inhibits the expression level of PEA15 in hippocampal neurons.|PMC6625386|Propofol inhibits the expression level of PEA15 in hippocampal neurons|PMC6625386|Furthermore, propofol significantly decreased the mRNA expression level of PEA15 in a time-dependent manner (Fig. 1E).|PMC6625386|The present results suggested that propofol significantly decreased PEA15 expression levels in hippocampal neurons.|PMID:31257496|The western blotting suggested that the protein expression level of PEA15 was decreased following treatment with propofol for 6, 12 and 24 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by 3-methyladenine and ammonium chloride, an autophagy and a lysosomal inhibitor, respectively; therefore, the authors speculated that MDA might act on VEGF secretion through the autophagy–lysosomal pathway.|PMC8145578|The finding that the hypoxia-mediated secretion of soluble factors like VEGF, FGF2, IGF-1, and HGF is sensitive to PI3K inhibitor 3-methyladenine (3-MA) in mBMSCs, apparently, supports the concept that a hypoxia-responsive AKT/PKB-mTOR-EIF4EBP1 pathway participates in the translation of cytokines/growth 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studies have shown that dexamethasone (Dex) induces the expression of TGF-beta1 in androgen-independent prostate cancer both in vitro and in vivo.|PMID:16887915|In addition, dexamethasone decreased cell growth, up regulated TGF beta 1 mRNA, and down regulated uPA mRNA expression in prostate cancer cells.|PMID:9179184|The results showed that dexamethasone caused an increase in TGF beta production and a dose-dependent two to fourfold increase in TGF-beta 1 mRNA in activated as well as in unstimulated T cells, 1 h after exposure of the cultures to the steroid.|PMID:1939646|Dexamethasone administration before general sensitization reduced the symptom score, OVA-specific IgE, and eosinophil infiltration and increased the serum level of TGF-beta1 significantly.|PMID:17762268|The increase in TGF-beta 1 mRNA levels by dexamethasone was further potentiated two to threefold by cycloheximide, suggesting that the steroid effect may be due to inhibition of the synthesis of proteins that decrease 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with basic fibroblast growth factor alone or in combination with dexamethasone 10(-9) M for 48 hr induced an enhancement of glial fibrillary acidic protein, vimetin, and ERK2 expression.|PMID:26469526|We observed that dexamethasone strongly dephosphorylates Erk1 and Erk2, which could be antagonized by mifepristone (data not shown), whereas TGF-β induced their phosphorylation.|PMC1868771|We demonstrated that dexamethasone, which enhances steroidogenesis by up-regulation of the p450scc enzyme system, stimulates the MAPK cascade by phosphorylation of ERK1, ERK2 as well as by Akt phosphorylation within 1-5min with no effect on p38 MAPK phosphorylation.|PMID:14623288|We demonstrate that exposure of post-confluent 3T3-L1 preadipocytes to insulin, isobutylmethylxanthine (MIX), dexamethasone (DEX), and fetal bovine serum induces a rapid but transient activation of MEK1 as indicated by extensive phosphorylation of ERK1 and ERK2 during the initial 2 h of 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ticagrelor treatment also significantly increased the IL-10 protein level and decreased VEGF protein level in ischemic tissues.|PMC8052144|Furthermore, ticagrelor treatment significantly increased the IL-10 protein expression and inhibited the VEGF protein expression in ischemic tissues of IL-10+/+ mice.|PMC8052144|Furthermore, the possible mechanisms underlying the effect of ticagrelor were associated with its functions of attenuating the expression levels of VEGF and EGF, as well as suppressing the phosphorylation activation of ERK1/2, P38 and nuclear factor-κB P65.|PMID:29042978|The major results of the study showed that IL-10 negatively adjusts angiogenesis induced by ischemia, and ticagrelor inhibits the angiogenesis and blood reperfusion recovery, significantly increases IL-10 level, and reduces the VEGF expression in the IL-10+/+ mouse ischemic hindlimb, which were abolished in IL-10−/− mice.|PMC8052144|In addition, ticagrelor significantly decreased the ulcer-stimulated expression levels of EGF, VEGF, phosphorylated extracellular signal-regulated kinase (ERK), phosphorylated P38 mitogen-activated protein kinase and nuclear factor-κB P65 at the ulcer margin (P<0.05).|PMID:29042978","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"76097879":{"subject":"UMLS:C5242471","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:53e77ec704ae1e098a71c3a05afca9434665282c1ec87431a4d935021718ef64","tmkp:412eb9278dca4130eeceab7e1d0c2d1d020205a1649a46219a1bf4428fb52401","tmkp:c72a861e36515fa054f359614d3be34088e817bc5105ad6bbeb28736390ee177","tmkp:7181e0d921814a0325658d164ef54347ebf1e88068acd71a07ee3099508096f9","tmkp:3ffecea1cc5cec79c186db5edcdde48676bd681561b4818002cf0199ef9ad0d2","tmkp:0cf79b4ee217d047ec23bb070c6fd9a7723da945184577b8b3a3adcf6d9ad68a","tmkp:8f0054a041a245fd370169d121429f3f12895ece9fd2c9db7b3c6c75b21f4122","tmkp:f3c5c744ce42889a19843f9aea0706d325b4d32e4d7cb8486526992a796eb609","tmkp:af3a86fe85f038a79295224dfec9111a1c6c2a54a9885352163b549b17424ba6","tmkp:17f55426bcc5855d925b1af293c2ccbce363a6ec934051c00bea1a99b500f07e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6484084","PMID:19426601","PMID:24686517","PMC5581320","PMC6374775","PMC2868273","PMC7228999","PMID:27771084"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9984698433333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"IL-4 and IL-13 production after ex vivo restimulation of lung T cells with HDM was also reduced by both milk types.|PMC5581320|IL-4 and IL-13 production after ex vivo restimulation with house dust mite (HDM) was inhibited by raw milk.|PMC5581320|Horse-milk administration decreased the mRNA levels of IL-4 and resulted in higher transcripts of TLR-4 in all treatment groups; however, the levels of MCP-1, TNF-α, and TLR-2 were unaltered.|PMID:27771084|however, the level of Th2-type cytokines IL-4 in camel milk drinking group was significantly lower than that in the non-drinking camel milk group (P<0.01).|PMID:19426601|We found that the levels of IFN-γ and IL-10 increased, but the levels of IL-17A and IL-4, decreased in lamina propria of colon in immune milk-fed mice as compared with those in control milk-fed mice.|PMID:24686517","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"115052230":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:355","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:4844325a24b524baa59dc8b3c42d4166bd0d55e75a3b9c1ec820292b82452a1c","tmkp:9643163142d4a1f84c120d6b64f64b9ca288eef72ed7e91e3336de014e6c4dfc","tmkp:36fe613d7448033ef814cbb91a336ca7004d80dfda04ca9141547e3db1751f76","tmkp:1296c10175f05aa4de09edde5f09eb60cb284d59ebdd7da259a8f8b4629afd33","tmkp:b60c76f97606116e4278a0f78d71538a2071fdc123d0dd6f7dc5e22f28e4a36d","tmkp:6fca7e07f900aea7175b34a81ce263272c1eea8310e19e151700e35be5d7f6a5","tmkp:dc87a4d36feb397ca92335bc3ee2586616ad6dfd05a78083ee3a21dcbd404660"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In fresh CTCL lines, the level of FAS promoter methylation was reduced at 6 distinct CpG sites in response to MTX treatment in the two lines with high baseline methylation (HH, SZ4) but not the two with low baseline methylation (MyLa, Hut-78) (Figure S4).|PMC4331060|Consistent with these in vitro findings, the level of FAS promoter methylation was significantly reduced at these same six CpG sites within both tumor cells and normal keratinocytes microdissected from FFPE lesional skin biopsy specimens of CTCL patients treated with MTX (Figure 2).|PMC4331060","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC2212386","PMC4331060","PMID:23799623"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99969785","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"85980222":{"subject":"UMLS:C3536832","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Exposure to ambient air fine particulate matter prevents VEGF-induced mobilization of endothelial progenitor cells from the bone marrow|PMC6257429|Exposure to ambient air fine particulate matter prevents VEGF-induced mobilization of endothelial progenitor cells from the bone marrow|PMC4069084|Exposure to ambient air fine particulate matter prevents VEGF-induced mobilization of endothelial progenitor cells from the bone marrow|PMC8126292|Exposure to ambient air fine particulate matter prevents VEGF-induced mobilization of endothelial progenitor cells from the bone marrow|PMC6188890|Exposure to ambient Air fine particulate matter prevents VEGF-induced mobilization of endothelial progenitor cells from the bone marrow|PMC4456050","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:25554261","PMC4456050","PMC8126292","PMC6257429","PMC6188890","PMID:16500767","PMID:14521929","PMC7673239","PMC4069084"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:1dba60268762e07633efd2e419b193e16f439ec61eca204618c36d91f69f9a3e","tmkp:326e2bdf9f82a01015ff7e0f7b292f0a0faf90683e12de04992913efac940d22","tmkp:4f597cdd033df6871ff28460fbc39677c12ffa7d516226ade5c9074530af3414","tmkp:5280bf0e9151d0079b6696a23d730ba6628b47e33fa95ab4cca7ccd2f882926c","tmkp:92baa500bbd1d0ae368535d9fb09eceea6d2ef85e2abeeef88f74cab5d457964","tmkp:6b9664c7c7ad531b3ebe4b7b3a689e73fbd9c5a92b79d7344752d7f763a0f8a5","tmkp:17736368d2770903c164202c1be5ad95dda1749f273ec4e33b975a04f4e91730","tmkp:96cd942d18cfd786851e53626ae6aa003189fff103450eb679414dd2df87180e","tmkp:a689f0c293478bca8aa2b03a3cdec9179a95521d6627b47b9c9cdcfafc3027fc","tmkp:e8bef9cbfd146f0479a3378817f55b8692b2f2ae2abd8ff115fb3862873c6d12"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9934131214285715","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"117353137":{"subject":"PUBCHEM.COMPOUND:3715","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:8557642"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:894e541b3d089f4584da56274448e47c5c31c9835e6692c5ec40ba95af4f4d1d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Compatible with a cyclooxygenase mediated event, the AA-induced suppression of GLUT4 mRNA was abolished by pretreating the cells with the inhibitor, 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plasma insulin level was significantly higher after tamoxifen treatment (p = 0.01) in tamoxifen-treated rats than in control rats.|PMID:15542935|The plasma insulin level was significantly higher after tamoxifen treatment (p = 0.01) in tamoxifen-treated rats than in control rats.|PMID:15542935|(e) HNF4α and insulin gene expression were upregulated when E47 was induced by tamoxifen in T6PNE which has a low level of insulin and HNF4α expression at baseline.|PMC3447631|Induction of E47 by tamoxifen resulted in a potent and dose-dependent upregulation of insulin gene expression (Fig. 1C,D) but still approximately 1000-fold lower than in primary β-cells, in which insulin mRNA constitutes close to 10% of the mRNA.|PMC3374493|HbA1c (Fig. 1j), fasted insulin (Fig. 1k), triglyceride and free fatty acid serum concentrations (Fig. 1l) were significantly higher in tamoxifen-treated mice compared to controls 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patients with persistent epithelial defects (PED) and 30 patients with sterile corneal ulcers (CU) were treated either with 5% AED or 0.1% hyaluronan eye drops (HED) 8 times daily until complete epithelium 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compared with the sham treatment control group, levels of insulin, pancreatic duodenal homeobox-1 (PDX-1), GLUT2, and insulin receptor substrate-2 were upregulated in the islets of MET-treated mice, whereas the phosphorylation of JNK, nuclear translocation of forkhead box class O-1 (FOXO1), and nuclear factor-κB p65 were reduced.|PMC4216407|After four weeks, fasting blood glucose decreased, while body weight change and serum insulin level increased significantly in MP, Met and MP + Met treated diabetic groups compared to diabetic control (DC) group.|PMID:30026088|Islets periphery was improved, and down-regulation of glucagon and up-regulated insulin protein expressions were found after Met treatment.|PMID:25757281|Although insulin administration prevented hypermethioninaemia in streptozotocin-diabetic rats, discontinuing insulin treatment resulted in a time-dependent increase in the plasma methionine level.|PMID:6391990|After four weeks, fasting blood glucose decreased, while body weight change and serum insulin level increased significantly in MP, Met and MP + Met treated diabetic groups compared to diabetic control (DC) 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transfected cells were selected on solid minimal medium (EMM2) lacking leucine and supplemented with 2 μM thiamine to repress GFP-Er-MAPK1 constructs expression, and cultured in EMM2 without thiamine to induce GFP-Er-MAPK1 constructs 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GR-mediated, metabolic side effects of glucocorticoids.|PMC6371196|A single injection of prednisolone or cortisone to 5-day-old rats caused a transient elevation of the blood level of insulin and a prolonged decrease in that of growth hormone.|PMID:744153|More specifically, BGL was significantly higher at 17:00 and 21:00, but not significantly higher at 07:00 and 12:00 In addition, the daily insulin dose was significantly higher in the prednisolone-treated group than in the control group, especially at 12:00 and 17:00.|PMC6549610|As lipolysis is more sensitive to small changes in insulin concentration than EGP, and plasma NEFA levels are closely correlated with changes in lipolysis, we hypothesise that decreased basal lipolysis and NEFA levels in individuals receiving prednisolone 30 mg may be because of the observed prednisolone-induced 80% increase in fasting plasma insulin levels.|PMC3131514|Compared to placebo, prednisolone treatment tended to lower fasting Angptl4 levels (P = 0.073), raised fasting insulin levels (P = 0.0004) and decreased fasting nonesterified fatty acid concentrations (NEFA) (P = 0.017).|PMID:22972030","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d8630d68ea10afe1dbebe22a57c56bda9e01d1d05965917862c1ee0c7a5dcf71","tmkp:daad599081cf04c691f756436c13147c3cc52827d9fac99e6e8b542c248f115b","tmkp:5ac142a95601d760df89293982a95c49ae2396dbc9262e55b8ac65f51e028296","tmkp:dc0edd8a58c538400e866f8101d61aabc92e231bfa7fe8a9184f68ce44f45dbd","tmkp:9dd7e61ae7d8cf936b41e3d487613a02b7203da0e45cc01796bd60ef2f3f2d3a","tmkp:0ae2a47ee6c61eba5756e95fa311164482ea3b22490ec1319ad032c597acea89","tmkp:63efebd29ca97313ba39b89c6632e479c3de4fc8f834a2eb37952a2ff409d10e","tmkp:046a8918487e1e8ca7a59a0bb8e0815655d43c31efdc94a31963dfec06463c7f","tmkp:496283ed81edb0a06ca4bc00a4df8ba7dd0cdc250cc1b7ef401037eaa748c31e","tmkp:cf8eff4a8a23328571b1e96cd1072400e2ff0f5db680cdec06dbb8a4d01e4273"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"77654385":{"subject":"PUBCHEM.COMPOUND:24759","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In the conscious state, with addition of hyaluronic acid, the area under the curve of plasma insulin concentration was significantly increased (1842 +/- 383 vs 75 +/- 24 m units min L-1, P < 0.01).|PMID:7837049|Hyaluronic acid stimulates the endogenous growth factor, epidermal growth factor, insulin growth factor, tumor necrosis factor, and vascular endothelial growth factor in a reported animal study.|PMC5127212|Consistent with this, treatment of cultured β cells with exogenous high molecular weight hyaluronan has been shown to increase insulin secretion and content, and hyaluronan treatment decreased oxidative stress and neutrophil activation in a rat model of pancreatitis, suggesting that hyaluronan may be beneficial for islet/pancreas function.|PMC3524560|In contrast, insulin significantly increased hyaluronan content in the medium of SMIGFIRKO VSMC (Fig. 7c).|PMC6765023|In addition, insulin also increased hyaluronan content in the culture media of WT VSMC, whereas SMIRKO VSMC did not 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the liver of HIS-HUHEP infected mice, we also observed increased expression of Fas/CD95, TRAIL, and TRAIL-R (Figure 6C).|PMC5733397","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"83726116":{"subject":"UNII:15C2VL427D","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4954942","PMC5454820","PMID:27314606","PMC4211604","PMC5207393","PMC7027529","PMID:25458604","PMC6893275"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99867736","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:feddd2f7c25964f9a41bbfeeabca7681da793083ad3b8514898e83fb014be247","tmkp:e99d2684b2ccb9a5cc491431ca2f87cb351d21fe161076217bb6802b0133edee","tmkp:3eff45400f83dbd8003e3b6187f16ead17b5e7cc17fe2e05c8796b19a4d87e66","tmkp:3554507db58f01f301d49c3836de37c805447c34d61c2c0c8c0e334d12b895d8","tmkp:8765f5c574d0470a2611ae783718fbeff7ea3c05eca0e9c7458133b986c51fb7","tmkp:e475e90e70c950f802977cd4330c7be1f03cb69bea70a5d1ed6b06bf373a9362","tmkp:249bf0ae3065bff46ec453a39ad5aa3f02d2db7b3e3f2369588380b5a6dae821","tmkp:e66212760b05464237a24fb10188df31d96f9c7f6e639e0f3e8317c97b111836","tmkp:e0678c90d6926a14508b5f1e106758207a80e06b6deab96b77d789c64ac66ed1","tmkp:3394b4281af0baf51a43b5eeeed11f0dd9e4ae793f163b19343da045cc35adad"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Real-time PCR analysis showed that treatment with 25 mg/kg BW aflibercept significantly upregulated the expression of fibroblast growth factor-2 (FGF-2), PlGF, VEGF, PDGF-BB, and transforming growth factor (TGF)–β mRNAs.|PMC4954942|Given the importance of the pro-angiogenic pathway downstream of VEGF, inhibiting the VEGF signaling axis has proven an effective therapy for patients with solid tumors and neovascular age-related macular degeneration; drugs such as bevacizumab and aflibercept which sequester circulating VEGF have shown efficacy in some of these clinical situations.|PMC5207393|In tumor tissues of Hepa1-6 cells, aflibercept significantly suppressed the phosphorylation of VEGFR-1 and -2 and upregulated the expression of HIF1-α, VEGF, and PlGF (Figure 4, A and B).|PMC4954942|Our results also showed that aflibercept upregulated HIF1-α expression in tumor tissues, in addition to the expression of VEGF, PlGF, FGF-2, PDGF-BB, and TGF-α.|PMC4954942|Thus, the proposed dose escalation of aflibercept was expected to achieve serum levels in excess of circulating VEGF levels reported in cancer patients as well as exceed the concentrations associated with preclinical studies.|PMC4211604","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"34822969":{"subject":"UNII:15C2VL427D","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9987736125","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9d324426efb1d79e2808d2b1250acb78a8e4710b63dc39c3caa75850275e888e","tmkp:46155ee53a17ed6b47251762e795ad4e35c1c682b92647c7e3a67f298ab9be95","tmkp:f3dbb60c102e7c903d4e111972f7e72eb32a25e63bd98934d83eb57e93be47c1","tmkp:0c0edd15bf0ef339d7f69ed11fb13df3225821107f641f25e52d2b80736a463f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5338630","PMC5338630","PMC5338630","PMC5338630"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Furthermore, as expected, both aflibercept and ranibizumab blocked VEGF-induced activation of Akt, but this blocking was less effective than that with K12-sgRNA/SpCas9–mediated depression of Akt activation (Fig. 3C).|PMC5338630|These data indicate that the CRISPR/Cas9-mediated depletion of VEGFR2 expression is alternative to that of either aflibercept or ranibizumab in blocking VEGF-induced activation of Akt in HRECs.|PMC5338630|In addition, there were lower levels of Akt phosphorylation in HRECs with VEGFR2-sgRNA/SpCas9 than those with LacZ-sgRNA/SpCas9, and there was less VEGF-stimulated Akt activation, proliferation, migration, or tube formation in the VEGFR2-depleted HRECs than those treated with aflibercept or ranibizumab.|PMC5338630|We next compared the efficiency of editing the genomic VEGFR2 locus using CRISPR/Cas9 with aflibercept (800 μg/mL) or ranibizumab (200 μg/mL) in blocking VEGF-induced activation of Akt and its downstream effectors (e.g., p-BAD and Caspase 9).|PMC5338630","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"32378971":{"subject":"PUBCHEM.COMPOUND:9287","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6823312"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b653030e7910f44698e8f7399be4872d936767ed0e670159c35c7d5181276400"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99914396","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"We found that median levels of MyD88 and MAPK1 are both increased in onset/AMT-hot tubers (Fig. 2d, e), and we previously reported NF-kB activation.|PMC6823312","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"17038034":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:30350305"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Dopamine promotes cathepsin B-mediated amyloid precursor protein degradation by reactive oxygen species-sensitive mechanism in neuronal cell.|PMID:30350305","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9986994","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dfed0c96eb89ebbb4a5152a39fb4c1782af7126aab95a61394b6e95de780d811"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"78622587":{"subject":"PUBCHEM.COMPOUND:5988","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:41f9bebafd743e17fe911fafd9aaf13687e5f805b0566a1d0b7125b40b346531","tmkp:5599c561ec2ae9473c786ed5a7719b4e072c9faf7509f17d6f1e67e30f40ad38","tmkp:daf5b6b39195b57ae175b668c8f115a9d5a35cc37792ccba709f08241374762f","tmkp:8061bc6de3e40b967720ff2e222fe6085840f6f65913a3c7f0ac8ad887486766","tmkp:9cd3fa70b8689be8d95de1fa8d5802ca56e9c619c0772ec41b94b9f1416d9743","tmkp:1b102d50750fb5eca116f3507d6850f40781c23579e1ba4f061c726fe623d0c2","tmkp:9eab17ecbcc1a89e0553d718b6c8eb7fffd7b8576f131ab89dbd9c57216a5bba","tmkp:74951c5f2098aa33e6046fdbeccd7340c1865e49100c457f30695cbc7d21f850"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:27965359","PMC5363518","PMID:27342664","PMC6664608","PMC8017331","PMC6433667","PMID:16586065"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"For example, sucrose induces autophagy via inhibiting Akt/mTOR pathway in human chondrocytes.35|PMC6433667|Western blot analysis indicated that sucrose feeding: (1) inhibited insulin-stimulated phosphorylation of insulin receptor and Akt; (2) enhanced protein-tyrosine phosphatase 1B (PTP1B) expression; and (3) suppressed endothelial nitric oxide synthase (eNOS) and Na+-Ca2+ exchanger expression without affecting peroxisome proliferator-activated receptor gamma (PPARgamma), sarco(endo)plasmic reticulum Ca2+-ATPase isozyme 2a and phospholamban.|PMID:16586065|Our further analysis revealed that sucrose diet intake significantly suppressed Akt phosphorylation, as well as downregulated levels of HO-1, PGC-1α and Sirt3 (p < 0.05 vs. starch group for all these indices) without any overt effect on pan Akt levels.|PMC5363518|Mice fed a high fat/sucrose diet exhibited attenuated Akt phosphorylation in the retina as compared with mice fed normal chow.|PMID:27965359|Moreover, the phosphorylation of Akt, a substrate of mTORC2, was remarkably reduced under sucrose stress (Fig. 6), indicating that mTORC2 is suppressed under hyperosmotic stress.|PMC6664608","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999620006","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"94358199":{"subject":"PUBCHEM.COMPOUND:57363","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:78f85a2f454143e508eff4545aaa0872560e8193535a8df0d2e23f739643626f","tmkp:e3c2ead5a7964f79e3fa0e0fea6c53c668c43d8cda20ae501c428016d0ac8f5b","tmkp:d6bb0fb6fc096908f9fd62d024846a292c2d1e3b75ade94433dab405238e5c01","tmkp:0555ceac34aebe7314ebab724cfb8666011763dfcc6b1fa48107adece3092b6b","tmkp:c8e41ee97ce11a5014a1323a59e56e7b28615a68cfecf32f3925f2a2e4a7c688","tmkp:cfae85c7f5156fcb5d28f38a384342e717dd76a5df0e0e786e028568a09fa448","tmkp:1a5bf727ce04ff7546cd6e33e6cd2b2760cd5a3561f11a0bad6052190579ee3b","tmkp:db63e36a031a97f64b64700576b0fd8070d64c6ff6115f1dd985b227a3102cfb","tmkp:18944013f044771c1e1bc6b0563b9d880f10092c8f62273982dc76cdbb2ce776","tmkp:51bd73b39837de71a9a4b33c7ef81e2472cf6ff97df87d3e150cbec162d66b68"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Although finasteride promotes the expression of p-AKT and p-ERK1/2 in epithelial cells maintained in mono-culture, finasteride represses p-AKT and p-ERK1/2 expression in epithelial cells that are co-cultured with fibroblasts.|PMC5308847|Finasteride inhibited p-Akt and p-ERK1/2 in mono-culture of LNCaP (PC3) cells (Figure 5), but when LNCaP (PC3) cells were grown with mouse fibroblasts or HPF in co-culture transwells, finasteride up-regulated p-Akt and p-ERK1/2 in LNCaP and PC3 cells (Figure 5).|PMC5109888|However, when LNCaP (PC3) cells were grown with fibroblasts or HPF in co-culture transwell, Finasteride upregulated the expression of p-Akt and p-ERK1/2 in cancer cells.|PMC5109888|(A) Finasteride stimulated the expression of p-AKT, p-ERK1/2, cyclin D1 and cyclin D3 in a concentration-dependent manner in BPH-1 mono-culture.|PMC5308847|Finasteride promoted the expression of p-Akt and p-ERK1/2 in LNCaP (PC3) cells when co-cultured with fibroblasts in vitro|PMC5109888","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9972423","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5109888","PMC5308847"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"3807943":{"subject":"PUBCHEM.COMPOUND:22833565","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9735825","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9286e60f485a361a80620918cf2738986e062c0405fdd0da996762f5b7e4f4fe"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6469915"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Pedal edema and ascites reduced, and he was started on injection of unfractionated heparin as per weight 6 hourly for thrombus.|PMC6469915","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"35398871":{"subject":"PUBCHEM.COMPOUND:4649","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9933316","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Indeed, pronounced glomerulosclerosis was present in glomeruli of 5/6Nx mice without treatment and this was attenuated by Rac-1 and ROCK inhibition as demonstrated with the PAS staining.|PMC3820652","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC3820652"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e35931aa8d070b7b8f0d8d83d8b346f5cf1ad1e8f73f2841fd8159dd7088ee37"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"62778642":{"subject":"PUBCHEM.COMPOUND:6137","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:fc3dd398b4044ffadb7bafaa606333753e45f9d41d4388e60bb02e0b56c7809d","tmkp:e8802611e8fd05d29e51bcc60225b684d3160ae1ed03aa3216a9d8e96fa921d2","tmkp:99390718b61de7d05ee5b60868f5a31e26919773979099e4b80a0ade34eaba37","tmkp:0ea30d7a6f8ff51c02163774ee3462a7d6f3648cdbaa21d6242292260325a6d1","tmkp:dd708558e29bf3c84e6837f8d3ddcd91b03a5ae68a8974bcc5338cab9481ca3d","tmkp:2e333b42b5cfdc4ba1036781a9e3cf564fc377b06891f4a51f799db7929eb1ec","tmkp:c9c7b689bf6ac0833b76fce1c4faa02bc88f9afba0a9efb059db7ddd357196be","tmkp:0af8a3b0a10b3aa76a53cd4d59d951ccfef759f8aa8e7b250776333c47459c73"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"The administration of Se-Met effectively decreased the production and deposition of Aβ by inhibiting β-site amyloid precursor protein cleaving enzyme 1 (BACE1)-regulated amyloid precursor protein (APP) processing and reduced the level of total tau and phosphorylated tau, which depended on depressing the activity and expression of glycogen synthase kinase-3β (GSK-3β) and cyclin-dependent kinase 5 (CDK5).|PMC5085628|A simple and rapid method discriminating between placental and non-placental leucine aminopeptidases (LAP) existing in pregnancy serum is described, which includes technics of heat inactivation at 60 degrees for 30 minutes and inhibition by 0.02 M L-methionine.|PMID:1248106|Considering an example of cancer, from Fig. 3 and tabular forms of the regulome description, it can be observed that hsa-miR-200b: (i) forms a feed-back loop with TGFB1, (ii) P53 activates and TGFB1 inhibits its expression, (iii) inhibits MAPK, WNT, and AKT signalling pathways, (iv) inhibits cell cycle and cell proliferation by targeting cell cycle regulators and oncogenes like CCND1, VEGFA, MYC, NOTCH1, MET, EGFR etc. (v) is involved in cancer associated pathways, (vi) is downregulated in response to arsenic carcinogen, (vii) is upregulated by chemotherapy drug Gemcitabine and downregulated in Docetaxel-resistant cancers, and (viii) is downregulated in several cancers (Fig. 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example, Schwarte- Waldhoff and his colleagues reported that the restoration of SMAD4 in SW480 colon cells reduced expression levels of the endogenous urokinase-type plasminogen activator and plasminogen-activator-inhibitor-1 (PAI-1) genes, involved in the degradation of extracellular matrix proteins and the control of tumor cell migration and invasion.|PMC4007528|Interestingly, one of the p53 mutants (273his) inhibited PAI-1 promoter activity.|PMID:7479001|For example, Schwarte- Waldhoff and his colleagues reported that the restoration of SMAD4 in SW480 colon cells reduced expression levels of the endogenous urokinase-type plasminogen activator and plasminogen-activator-inhibitor-1 (PAI-1) genes, involved in the degradation of extracellular matrix proteins and the control of tumor cell migration and 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activation of p38 MAPK with anisomycin prevented both the LPS-induced stimulation of ERK1/2-mediated NF-kappaB activity and associated changes in ASM responsiveness.|PMID:16581829|As shown in Figure 3, compound 1 was able to achieve greater than 50% reduction in the phosphorylation of MNK1 in response to anisomycin stimulation without reducing the level of phosphorylated/activated p38 or ERK1/2, a closely related MAPK family member.|PMC7480010|In the two cell lines, anisomycin (4 μmol/L) activated p38 MAPK and JNK, and inactivated ERK1/2.|PMID:22684030|For instance, inhibition of mTORC1, MNK1/2, cap-dependent translation, or general translation by local administration of rapamycin, cercosporamide, 4EGI-1, or anisomycin, respectively, reduces injury-induced changes in nociceptor excitability and mechanical hypersensitivity.|PMC6004100|Western blot results showed that p38/AGF blocked the phosphorylation of Mnk1 and eIF4E under anisomycin treatment (Figure 2B, lower panel), implicating 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stress.|PMC2817461","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC4834478","PMID:16581829","PMID:9155018","PMID:22684030","PMC7480010","PMC2817461","PMC6019702","PMC6004100"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"112907880":{"subject":"PUBCHEM.COMPOUND:86287518","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9930295865","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ee010116b263d606d07c29d96e1b4f4ef2cf8449b113480c6a7765a8ffd0e3c1","tmkp:21c5513dfde216153a4de3ed87d8ecd6dd6053aea5e53f2982beeea1cabb9289","tmkp:e214f7c44fb6f6b33789e9a1cc318b68ff4bb4c34fd077d3147083f5bd9af22b","tmkp:e1b6c81d1989b36a713a8bdad1e8708acb2d8523293527865f07db401c08068e","tmkp:f75908e756e3a5ad0754ad37bff73f88f730a2238696f13b563a968997f4f29b","tmkp:6dee7e4511c32b04c9d7f5658eb5844380e9e25dbec03ab6733ceefa4b3bcbba","tmkp:37abffbda25f5639ef43f8a3ac213cae584143d4182c36c037f0de13118927c6","tmkp:99eb7f098626fe7a67200e33c7b5a57436f15d1141147e305bc9047e4fe60c8f","tmkp:6f964422563bb8bcd0c424eb927f7a4ec25d26a1c27531be5592af8758c336c0","tmkp:a60cf4c3cbf20fa0ed22e3a9a731c03e846585d8e261668a31be15148c168d7c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"During the research on IMD, we have found that IMD can activate ERK1/2 by inducing Src phosphorylation in more than 20 kinds of cells (including tumor cells such as liver cancer cells, breast cancer cells, glioma cells; and normal cells such as endothelial cells, fibroblasts, smooth muscle cells, etc.).|PMC7803743|We found that IMD induced the formation of a signaling complex containing CRLR and Src and promoted this complex internalizing into cytoplasm in a clathrin-dependent manner to activate downstream ERK1/2.|PMC7803743|IMD activates an ERK1/2-EGR1 signaling cascade, through which HCC cells acquire highly invasive abilities and a survival benefit.|PMC7803743|The treatment of IMD did not affect the expression of the 3 genes may be due to that the IMD-induced of ERK1/2 phosphorylation increases cell growth and invasive ability, but it will not induce UPR, therefore it will not affect the expression of the ER-stress sensor proteins (Fig. 7k–m).|PMC7803743|On the other hand, the treatment of IMD did not seem to affect the expression of the ER stress sensor genes, which may be due to that the IMD-induced of ERK1/2 phosphorylation increases cell growth and invasive ability, but it will not induce UPR, therefore it will not affect the expression of the ER-stress sensor proteins.|PMC7803743","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC5685717","PMID:18829738","PMID:30229842","PMC7803743","PMID:25951228"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"112695627":{"subject":"PUBCHEM.COMPOUND:31307","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"These results show that triamcinolone acetonide inhibits growth of NEL-M1 human melanoma cells in serum-free defined medium, medium supplemented with insulin and 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Western blots (left) show the efficiency of Rac1 and Rac2 protein deletion in resting B cells, 3 days after the last tamoxifen-injection.|PMC5635268|Mice were given tamoxifen (5 mg in 50 µl) by gavage for 5 days in a row to delete Rac1 and sacrificed on days 3 or 4 after the final tamoxifen treatment.|PMC5635268|Thus, inhibition of Rac1 may represent a new therapeutic opportunity in the treatment of ER positive breast cancer even in the setting of tamoxifen 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patterns, spikes, polyspikes and periodic epileptiform discharges (PED) have been reported in electroencephalograms (EEGs) during anaesthesia induction with sevoflurane in healthy adults and children.|PMID:19032567","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:19032567"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"35959962":{"subject":"PUBCHEM.COMPOUND:439501","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999437965","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0f765e10690a4bc6ff8b4e1a584371cdaa1c0a47acb5f494dac3bb1ab7984f00","tmkp:3493a2566e088ffef5622497e81cd61e58b0d62e9077c2ae544444e104ef5ca7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"A novel observation was the fact that ouabain induced IL-10 and VEGF as well.|PMC4034513|Nevertheless, the levels of IL-10 and VEGF measured in the supernatants of cells cultured for 24 hours in the presence of ouabain were also higher than control levels (Figures 6(c) and 6(e)).|PMC4034513","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC4034513","PMC4034513"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"127482683":{"subject":"PUBCHEM.COMPOUND:2554","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:21273730","PMC4822806","PMC4807443","PMC6912407","PMID:9949555","PMID:9804957","PMC7720859"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"CBZ induced a rapid increase in the serum concentration of insulin.|PMID:21273730|These results indicate that the expression of insulin signaling was increased due to enhanced differentiation, along with the increase in the number of adipocytes by carbamazepine treatment.|PMC6912407|The indirect response model was applied to account for the CBZ-induced increase in insulin secretion and the subsequent decrease in serum glucose.|PMID:21273730|Given the similarity between carbamazepine and sulfonylureas in their effects on KATP channels, it would be predicted that carbamazepine would also stimulate insulin secretion.|PMC7720859|Collectively, our studies suggest that carbamazepine or derivatives, regardless of the exact molecular mechanism or mechanisms, may hold promise for increasing insulin production, promoting β-cell differentiation, and/or protecting β-cells from 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these findings demonstrated that ketamine attenuated the expression of VEGF and cell migration ability in colorectal cancer cells, probably via blockage of NMDA receptor.|PMID:30817910|In chronic ketamine abusers, peripheral blood serum vascular endothelial growth factor (VEGF) protein is reduced.|PMC8228861|compared with NMDA-induced rats (228 ± 18% of control), and VEGF was decreased (133 ± 14%, 133 ± 16%, and 127 ± 20% of control, resp.)|PMC5660823|In accordance, Figure 5(e) presented that the IVB (0.25, 2.5, and 25 mg/ml) treatment decreased the expression of VEGF in the retinas of rats treated with NMDA (168 ± 11%, 137 ± 11%, and 140 ± 18% of control, resp.)|PMC5660823|In chronic ketamine abusers, peripheral blood serum vascular endothelial growth factor (VEGF) protein is 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neurons, nicotine‐derived nitrosamine ketone could inhibit the insulin receptor and Akt pathway, leading to loss of insulin‐mediated neurotropism and neuronal dysfunction37.|PMC6400172|Nicotine expands the neutrophil lifespan by inhibiting the diphospho-inositol pentakisphosphate (InsP7) and Akt pathway, contributing to cell accumulation and tissue damage in emphysema and bronchitis.|PMC7023896|Nicotine suppressed insulin-stimulated Akt phosphorylation at Ser473 (pAkt) in skeletal muscle, liver, and WAT (Fig. 2j).|PMC4390501|We conclude that prenatal nicotine exposure attenuates the phosphorylation of PDGFR, Akt and Bad-136 during hypoxia in the CB of developing rats.|PMID:20447445|PI3K levels were upregulated, but Akt1/2 and eNOS levels were remarkedly reduced by 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level of VEGF expression in the osteocytes, osteoblasts, and cells of bone matrix and endothelial cells increased first 1 week after and then decreased after the prednisone administration in Group A, and decreased after the prednisone administration in Group B, however, without significant differences between these 2 groups.|PMID:17064544|Conversely, corticosterone, prednisone, and dexamethasone similarly inhibited cell invasion and expression of related genes, including MMP-9, VEGF, and IL-6, in GR-positive lines.|PMID:24880571|With respect to subgroup analyses, comparison between the MTX monotherapy and MTX + prednisone subgroups revealed significant decreases in IL-7, IL-8, IL-10, and VEGF in the latter subgroup post-therapy, but only IL-8 in the former, possibly supporting the role of low-dose corticosteroids in the management of early RA.|PMC4446850|Following prednisone therapy (B), VEGF level was reduced but it was still higher than in the control group.|PMID:16825140|The one pretreated for 6 months with moderate-dose steroid (prednisone 20–30 mg daily) exhibited low VEGF levels throughout the study period following primary POEMS syndrome treatment (transplantation).|PMC4654348","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9995045016666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"11268899":{"subject":"PUBCHEM.COMPOUND:56603655","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"To review clinical data on the sequential use of the non-selective vascular endothelial growth factor (VEGF) inhibitors (ranibizumab and bevacizumab) and the selective VEGF inhibitor (pegaptanib) in the treatment of neovascular age related macular degeneration (n-AMD).|PMID:22283373|There are many other drugs that may play a role in DR therapy in coming few years such as somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|A number of drugs may play a role in DR therapy in the coming few years; eg, somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|Nowadays, VEGF-inhibitors like bevacizumab, ranibizumab, pegaptanib, are the first choice in therapies for the treatment of neovascular ocular diseases.|PMC6249906|In this way, the effect of VEGF inhibitors (pegaptanib, bevacizumab, ranibizumab) on primary cultures of human REC and CEC was evaluated by Stewart et al.. Significant differences between retinal and choroidal microvascular cells were observed, which highlights the need for specific treatment interventions in RNV or 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F344 control rats, CASP3 (41%, P=0.039), IL5 (213%, P=0.037), IRF4 (33%, P =0.026) and IRF9 (41%, P=0.002) were upregulated following nicotine treatment and only IL1α (36%, P=0.023) was downregulated.|PMC4985440|It is worthy to note that nicotine toxicity induced significant increments in the protein expression levels of nuclear factor kappa B as well as caspase-3.|PMID:30217256|Increased caspase 3 expression was detected in human gingival fibroblasts treated with nicotine due to decreased cell integrity and increased apoptosis.|PMC6025719|Nicotine induces oxidative stress through the apoptotic pathway via activation of caspase-3 due to mitochondrial damage.|PMC8189814|In addition, it has been demonstrated that nicotine acts by reducing mRNA and protein levels of Bcl2, as well as upregulating p53 and caspase-3 mRNA, including protein levels, that adversely affects the germinal epithelium in adult 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inflammatory mediators.|PMC2756477|In HAECs treated with 500 nM nicotine, the expression of ICAM1, VCAM1, MCP1, PAI1, MMP1, MMP9, MMP10, TIMP2 and TIMP4 were significantly upregulated, while eNOS was downregulated (Figure S2).|PMC7196288|Interestingly, nicotine was found to up-regulate PAI-1 in patients with COPD, with PAI-1 protein concentrations increased in sputum of COPD patients.|PMC8231800|We demonstrated that TSP-1, TGF-β1 and PAI-1 increased after nicotine administration.|PMID:21494021|These target genes have been shown to play vital roles in TGFβ/SMAD canonical signaling and TGFβ-induced epithelial–mesenchymal transition (EMT) may be inhibited by SKIL binding to SMAD In this study, we found increased protein abundance of PAI-1 in WT mice exposed to PG with nicotine, but PAI-1 was further reduced in nAChRα7 KO 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and CBZ treatments caused a decrease in β-Catenin and VEGF levels in SW480 colon cancer cell lines.|PMC5291934|We have shown here that VPA and CBZ decreased the hypoxia-mediated induction of VEGF secretion in the SW480 cell lines.|PMC5291934|CBZ is a small molecule that targets MET, AXL, and VEGF receptors and has recently been approved for treating advanced RCC patients.|PMC7272308|Treatment of SW480 cells with 5 μM of CBZ and 2.5 mM of VPA decreased the VEGF protein levels by 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the same time, the expression levels of MFN1 and MFN2 were restored by quercetin, indicating the protection of mitochondria against excessive stress-induced fission and reduced fusion.|PMC7412508|In conclusion, periodic treatment with quercetin is effective in reducing IAV infection, and differentially regulates the expression of key proteins, including heat shock proteins, fibronectin 1, and prohibitin to reduce IAV replication.|PMID:27157719|Transfection with miR-21 mimics inhibited the quercetin-induced anti-fibrotic effects, increasing the expression of collagen I, fibronectin, α-SMA and E-cadherin at the mRNA (Fig. 3B) and protein levels (Fig. 3C and D).|PMC6122524","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"80652291":{"subject":"PUBCHEM.COMPOUND:54729367","object":"NCBIGene:5594","predicate":"biolink:related_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.05827557","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4cc59171bc32507e48a1ec89fbae63f18d74ae1ef7c9f6e172f36952a4854e00"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"As shown by western blot for p-ERK1/2 and p-MEK immunostaining (as readout for Ras/MAPK pathway activation), all three obtained cell lines showed inducible Ras pathway activation upon doxycycline and 4OHT stimulation 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of HIF-1 signaling by quercetin was confirmed by qRT-PCR which showed upregulation of the HIF-1 regulated genes EPO, VEGF, PGK1 and BNIP3.|PMID:19729006|A very mild increase in VEGF mRNA expression was observed in the rats treated with quercetin.|PMID:26281317|One study reported that 0.3% quercetin treatment of wounds accelerates healing by a variety of biological effects: rapid wound contraction, modulation of inflammatory and anti-inflammatory cytokines, increased VEGF and TGF-b1, increased antioxidant status, and enhanced fibroblast proliferation, with better collagen deposition.|PMC8186379|Quercetin up-regulated vascular endothelial growth factor (VEGF), an ulcer healing factor, not only in colon epithelial cell lines but also in the inflamed colonic tissue.|PMID:17377063|The gene and protein expression data suggest that quercetin treatment (100 micro M) significantly decreased EGF and cyclin D1, whereas VEGF was up-regulated in Ishiwaka cell 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vitro studies in cultured podocytes showed that treatment with Bevacizumab induces podocyte apoptosis through activation of the p38/MAPK pathway.|PMC3789480|(B) FOLFIRI/Bevacizumab treatment increases MKNK1 protein level (MAPK-interacting kinase 1), the target of RAS/RAF/ERK and MKK/p38 MAPK signaling, regulating the activation of eIF4E.|PMC7215415|In contrast, the basal-like tumor responded to bevacizumab treatment by activating several pathway components (Figure 3B), with MEK, MAPK/ERK, STAT3, AMPK, TSC2 and AKT as potential critical nodes.|PMC4326070|Therefore, when the ETV5+ CRCs received Bevacizumab treatment, the secretion of CCL2 induced by upregulation of ETV5 continued to activate angiogenesis-related pathways, such as the PI3K/AKT and p38/MAPK signaling pathways in HUVECs and this resulted in persistent angiogenesis.|PMC7585575","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"27876343":{"subject":"PUBCHEM.COMPOUND:2726","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:f42722894a2e944d70e2e3ffa48bce2185003fde5fa15478b262ae17e4025c28","tmkp:47bf85b8282a32ec45d88f951d8a024e53a20a549eb1a5addfbb0384449bcf4c","tmkp:d191c6a248a143210507b46bb7febdc98a6439e170b68b509f2ec1afef36493d","tmkp:7e1f257134e5c2cd516f43c16b2ce11af5791b8fcc461c517c7a0269492892e5","tmkp:68d9a47729f725211b3472a7712c02ccf98d3c26c9660777800acdcab3ad7fc2","tmkp:05c19dccd29ee5bf9b6d48cda5c19c0deb850470187e3f6cdf33e4a298cf2bae","tmkp:1259ed4bf0d8b37d81e0992fddd84b2061ee7e6bf6f41a27fd28aedfa7d7a3e6","tmkp:1cd59ef751788d182d5ea6bf7a5c49db4224a29ea37aacd37654ae98ea1d0580"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9983575666666665","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6129591","PMC6206841","PMC7061211","PMC7265959","PMC5547051","PMID:16205782","PMID:16845229","PMC4557281"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Inhibition of the proliferative capability of splenocytes by chlorpromazine and clozapine resulted mainly from the activation of PI3-K/Akt pathway.|PMID:16845229|Clozapine and chlorpromazine action on CRH activity operates mainly through activation of the PI3-K/Akt pathway.|PMID:16205782|Although mild hypothermia (S&H) (P < 0.01) or a low dose of chlorpromazine and promethazine alone (S&D) (P < 0.01) elevated p-Akt expression at both 6 and 24 h after reperfusion, the elevation of p-Akt expression was largely and significantly enhanced by their combination (S&HD) (P < 0.01) at 6 h (F (4,25) = 22.032) and 24 h (F (4,25) = 8.639).|PMC5547051","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"38839095":{"subject":"PUBCHEM.COMPOUND:247","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"We previously reported that choline and betaine supplementation reduced the expression of macronutrient transporters such as FATP1 and GLUT1 in GDM mice at mid-gestation and speculated that trophoblast uptake and transport of nutrients would decrease accordingly.|PMC6213524","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6213524"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:228d57ffb44d530e6bf269bb9d363d2cd353df4554487939801860f35250c070"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99968123","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"121503807":{"subject":"PUBCHEM.COMPOUND:5206","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:25555490","PMC5333720","PMC4678156","PMC7976445","PMC4382529","PMC6880526","PMID:16678324","PMC7684862","PMC7295720","PMID:23186353"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Previous studies have shown that sevoflurane reduces the protein expression levels of caspase-3 in the fetal brain.|PMC7976445|We propose, therefore, that sevoflurane can inhibit apoptosis by decreasing levels of caspase-3 and cleaved-caspase-3, blocking apoptosis at its final stage.|PMC5333720|Sevoflurane-delayed post-conditioning significantly increased levels of phosphorylated Akt-Ser473 and GSK-3β-Ser9 in the mitochondria and inhibited the activities of caspase-3 and -9, showing an improved neurological deficit score and a decreased infarct size.|PMID:25555490|In the study of Zhou et al. sevoflurane could activate HIF-1α expression and inhibit caspase-3 expression to ameliorate myocardial I/R injury in the heart of rats.|PMC6880526|I/R injury increased the levels of cleaved caspase-3, and sevoflurane post-conditioning decreased the cleaved caspase-3 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elevated autophagy mediated by IL-17 enhanced ubiquitin-proteasome system activity and B cell anti-apoptotic ability by Beclin-1 and p62 through Erk1/2 phosphorylation, and these changes brought by IL-17 could be also inhibited with 3-methyladenine.|PMID:24269624","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:24269624"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ba6bc327904ad602b339d0510bf02b436b7ba59224bde696c30b3801853992c7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"64095331":{"subject":"PUBCHEM.COMPOUND:5280343","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Consistent with this, western blot data showed an up-regulation of the major pro-apoptotic protein Bax and a down-regulation of the major anti-apoptotic protein Bcl2 after quercetin exposure in A549 cells.|PMC4379472|Similarly, desatinib and quercetin can act in concert to clear senescent adipocyte and endothelial cells in atherosclerotic lesions, by inhibiting the cell death regulator Bcl-2.|PMC5651105|Other naturally occurring compounds such as curcumin and quercetin have been reported to reduce the effects of EMT by inhibiting key proteins associated with migration (SNAIL, MMP-2/9), anoikis tolerance (BCL2), cell-to-cell adhesion (N-cadherin), and signaling cascades (JAK/STAT, ERK).|PMC8137940|Quercetin increased the expression of Bax, phospho-JNK, phospho-p38 and phospho-ERK1/2, cleaved poly-ADP ribose polymerase and decreased Bcl-2 in a concentration-dependent manner.|PMID:31348906|Quercetin inhibits the invasion and mobility of murine melanoma B16-BL6 cells through inducing apoptosis via decreasing Bcl-2 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including dexamethasone, prednisone, prednisolone and methylprednisolone dramatically down-regulate VEGF-A secretion by HemSC and this suppression was sufficient to block blood vessel formation in vivo.|PMC3707963|The level of VEGF expression in the osteocytes, osteoblasts, and cells of bone matrix and endothelial cells increased first 1 week after and then decreased after the prednisone administration in Group A, and decreased after the prednisone administration in Group B, however, without significant differences between these 2 groups.|PMID:17064544|Conversely, corticosterone, prednisone, and dexamethasone similarly inhibited cell invasion and expression of related genes, including MMP-9, VEGF, and IL-6, in GR-positive lines.|PMID:24880571|With respect to subgroup analyses, comparison between the MTX monotherapy and MTX + prednisone subgroups revealed significant decreases in IL-7, IL-8, IL-10, and VEGF in the latter subgroup post-therapy, but only IL-8 in the former, possibly supporting the role of low-dose corticosteroids in the management of early RA.|PMC4446850|Following prednisone therapy (B), VEGF level was reduced but it was still higher than in the control 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addition, USP21 over-expression did not significantly alter FOXM1 mRNA levels in MDA-MB-231 cells transduced with a pINDUCER20 lentivirus to introduce a doxycycline-inducible USP21 transgene (Figure S3A).|PMC6425951|(A–D) Cells with stable inducible expression of wild type USP21 (A), OTUD3 (C) or inactive versions (B, D, respectively) were induced or uninduced with doxycycline (Dox, 2 μg/ml) for 16 hr followed by UV 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importantly, ALA/l-Car also significantly blocked the activation of ERK1/2, JNK1, and p38MAPK in skeletal muscle of mdx 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staining revealed significantly increased Ki67, prolyl 4-hydroxylase, and vascular endothelial growth factor expression, and suppressed CD45 expression in the higher molecular weight hyaluronic acid plus povidone-iodine group when compared with the other groups.|PMID:30807498|Furthermore, it accelerated the wound-healing process by promoting angiogenesis in skin wounds with the hyaluronan oligosaccharide-mediated enhanced expression of vascular endothelial growth factor.|PMID:30519937|Hyaluronic acid stimulates the endogenous growth factor, epidermal growth factor, insulin growth factor, tumor necrosis factor, and vascular endothelial growth factor in a reported animal study.|PMC5127212|Indeed, hyaluronan with 6–10 residues has been described as: (i) promoting the proliferation of HUVEC, (ii) inducing angiogenesis in the chicken chorioallantoic membrane assay and (iii) increasing VEGF mRNA levels in HUVEC.|PMC3822652|In vitro, the treatment of Mo/MØ with lysates and conditioned media 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or 5 μmol/l) of the Bcl-2 inhibitor ABT-263, dexamethasone, or dexamethasone plus ABT-263 for 24–48 h.|PMC6708234|In INS-1 cells, dexamethasone increased the number of transferase-mediated dUTP nick-end labeling-staining positive cells, caspase-3 activity, and poly-(ADP-) ribose polymerase protein cleavage; decreased Bcl-2 transcript and protein abundance; dephosphorylated the proapoptotic protein of the Bcl-2 family (BAD) at serine155; and depolarized mitochondria.|PMID:16644695|The present case demonstrates the ability of a combination regimen incorporating Bcl-2 inhibition with daratumumab, bortezomib, venetoclax, and dexamethasone to induce a rapid and very deep hematologic response in a pPCL patient with t (11;14), even in a setting of very refractory disease.|PMID:29064593|Although dexamethasone induced differentiation and down-regulated bcl-2 expression, it did not sensitize the cells to induction of apoptosis and inhibited the apoptosis sensitizing effect of the cytokines and dibutyryl cyclic AMP.|PMID:7517174|In our study, dexamethasone stimulated ROS production in C2C12 cells, increased Bax protein levels, and attenuated Bcl-2 protein expression in dexamethasone-treated C2C12 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minutes after the intraperitoneal injection of glucose, the propofol treatment showed elevated insulin levels in rats at both 2 (by 207.8% increase, p < 0.05) (Figure 4C) and 7 (by 93.2% increase, p < 0.05) (Figure 4D) months of age.|PMC7397023|In propofol group, the levels of serum insulin and C-peptide significantly increased compared with those in conscious group.|PMID:24814617|Herein, we found that the improvement of postload glucose levels caused by propofol, as seen in both the IPGTT (Figure 3B,C,E) and OGTT (Figure 3D), was accompanied by increased plasma levels of FGF-21 (Figure 4B) and insulin (Figure 4D).|PMC7397023|At T2, T3, T4, serum cortisol and blood glucose in propofol group were having less increasing pattern, and were lower than those in isoflurane group (all p<0.001), while insulin levels in propofol group were higher than those in isoflurane group (all p<0.001).|PMID:30823941|Anesthesia involving propofol in unstressed rats slightly induces insulin resistance due to the tumor necrosis factor α (TNF-α) elevation and acute lipid load, whereas in stressed rats and rhesus monkeys, propofol increases insulin secretion and improves glucose metabolism, and reduces TNF-α-induced hepatic insulin 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exerted two opposite effects on apoptosis; compared to controls, the expression of activated-caspase-8 was higher in treated rats, while the expression of apoptosis inhibitors survivin, Bcl-2 and c-Flip was lower.|PMID:21224497|Amiodarone was identified as a compound possessing synergy with the Bcl-2 inhibitor 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of phosphorylated ERK1/2, p38 MAPK were significantly increased in the propionic acid group compared to the control group (P < 0.05).|PMC5364657|Furthermore, the expression levels of phosphorylated ERK1/2 and p38 MAPK were increased in propionic acid group.|PMC5364657|We concluded that continuous oral administration of propionic acid during lactation may increase its concentration in the proximal colon and promote epithelial barrier function of proximal colon by enhancing the expression of ZO-1, Claudin-8, Claudin-1 and Occludin via increases in the expression of ERK1/2 and p38 MAPK.|PMC5364657|But, the mechanism underlying the propionic acid activation of ERK1/2 and p38 MAPK remains to be further elucidated.|PMC5364657|In this study, we showed that phosphorylated ERK1/2 and p38 MAPK were more strongly expressed in colonal mucosa after the oral administration of 200 mM propionic acid during lactation compared to the control 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level of VEGF expression in the osteocytes, osteoblasts, and cells of bone matrix and endothelial cells increased first 1 week after and then decreased after the prednisone administration in Group A, and decreased after the prednisone administration in Group B, however, without significant differences between these 2 groups.|PMID:17064544|Conversely, corticosterone, prednisone, and dexamethasone similarly inhibited cell invasion and expression of related genes, including MMP-9, VEGF, and IL-6, in GR-positive lines.|PMID:24880571|With respect to subgroup analyses, comparison between the MTX monotherapy and MTX + prednisone subgroups revealed significant decreases in IL-7, IL-8, IL-10, and VEGF in the latter subgroup post-therapy, but only IL-8 in the former, possibly supporting the role of low-dose corticosteroids in the management of early RA.|PMC4446850|Following prednisone therapy (B), VEGF level was reduced but it was still higher than in the control group.|PMID:16825140|The one pretreated for 6 months with moderate-dose steroid (prednisone 20–30 mg daily) exhibited low VEGF levels throughout the study period following primary POEMS syndrome treatment 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NIR-II fluorescent molecular probe, indocyanine green (ICG) conjugated bevacizumab (Bev-ICG) that targets vascular endothelial growth factor (VEGF), is successfully synthesized and evaluated along with the NIR-II endoscopy imaging 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the sucrose preference test, sucrose preference in Model+PAI-1group and Model+PAI+EA group was distinctly decreased compared with the Model+EA 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plasma insulin levels were decreased, and the rate of glucose uptake into hindlimb muscles and abdominal fat was increased in the clenbuterol-treated rats.|PMID:11254461|On day 40 clenbuterol-treated pigs had lower levels of thyroxin, tri-iodothyronine, insulin, urea and higher levels of lactate and creatine phosphokinase activity.|PMID:7941835|The results of the clamp tests showed that clenbuterol induced a transient decrease in insulin sensitivity.|PMID:9787491|In fact, serum insulin was reduced in clenbuterol-treated mice during the experiment (by 38%, p < 0.05, Fig. 7b, similarly to Fig. 5b).|PMC7351816|We also excluded enhanced insulin secretion as a contributing factor since fasting plasma insulin concentrations were significantly reduced upon prolonged low-dose clenbuterol treatment and since plasma insulin levels rose to a similar extent in treated vs non-treated mice upon glucose administration during OGTTs.|PMC7351816","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:7941835","PMID:9787491","PMID:8277227","PMID:8266894","PMC7351816","PMID:1975743","PMID:11254461"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:613f384e6a0e554a13c2e8a829a30929fb913a2017842bfa86b5c3e6fc067058","tmkp:b801e0248bf0f219620add4174590538bfbc676617e046f6b4571d36b5c177cb","tmkp:c8010d379ae02f050a508462106a077b1b73d7b0e1e4c799b9e77c30a451170c","tmkp:15234b43b577086f878e597655ffc443e228a1043d3916bde9260d1f82add418","tmkp:937d8a0cd32d8925387338627e69463192d50395ba668d7412de44379535ef2c","tmkp:ffcf8bbc2ef5eb514ef67d27402529195699d6c4f9455faeda6034804c289247","tmkp:ef6ed581dfcb015c8808c2bb800da4c19305b3279781d9c735d5bcc416d5fa96","tmkp:9b2016b7d2273815f664338c30dcf24d0983ccd659a377a9e25a73f9c6761071","tmkp:0e2ec4de0797f75ede1944b71190da81248eef2fc9221809fd010b6726953994","tmkp:6dad012a6fdd446c95afee0c9403199e09565a3b7e6d30aa227eef45126a9d56"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"83393348":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5361596","PMC5361596","PMC5361596","PMC5361596"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"(F) Western blot and densitometry quantification (n = 3) showing activation of MAPK8/9/10 and its target JUN after a time course treatment of sorafenib (20 µM) in Ishikawa cells.|PMC5361596|(G) Activation of MAPK8/9/10 and JUN by western blot in sorafenib-treated primary EC biopsies.|PMC5361596|Sorafenib induces autophagy through ER stress and MAPK8/9/10 activation.|PMC5361596|3J and S3H, targeted deletion of Mapk8/9 in MEFs completely abrogated MAPK8/9 and JUN activation in response to sorafenib and significantly delayed LC3B-II accumulation.|PMC5361596","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:267ae04efddd9efa9e9dd997e087cb282626cf91b78fb5f2e2e99f3a5110f807","tmkp:62d894bdc9daf25b5def77d12718d1a6f2513f41f85d817e4b77c4336b399991","tmkp:03dc7ee2fc2ea28034a8a51a4eaa940ce3d08ae1294992984f475af2f4c435c9","tmkp:0d8ed9b43a5c0c572d36ae2264d81544d0057d5b10b799cf17422aefe930c2d4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9991150175","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"42651252":{"subject":"PUBCHEM.COMPOUND:3121","object":"NCBIGene:355","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In addition, valproic acid was neuroprotective in an intracerebral hemorrhagic model of stroke by HDAC inhibition and transcriptional activation, and displayed anti-inflammatory actions by down-regulating proinflammatory factors, including Fas-L, IL-6, and MMP-9.|PMC2771446|In addition, VPA treatment had the following expressional effects; it activated the translations of acetylated histone H3, pERK, pAKT, pCREB, and HSP70; up-regulated bcl-2 and bcl-xl but down-regulated bax; and down-regulated the mRNAs of Fas-L, IL-6, MMP-9, MIP-1, MCP-1, and tPA.|PMID:17398106|It is noteworthy that the expression level of FAS (fatty acid synthase) was significantly suppressed when the cells were cultured in medium containing 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analysis showed the stimulatory effect of phenytoin in expression of vascular endothelial growth factor and basic fibroblast growth 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stimulation of cells with doxycycline (DOX)-induced expression of PLD1 caused a twofold increase in CPA production, which was similar to that observed for WT cells (Fig. 3a).|PMC3446787","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"9580583":{"subject":"PUBCHEM.COMPOUND:5280343","object":"NCBIGene:142","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"degradation"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"10090","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"dct:description","value":"increases degradation 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with or without nicotine exposure reduced the protein abundance of fibronectin in WT female and nAChRα7 KO mice compared to air control (Fig. 7a).|PMC7301079|PG with or without nicotine exposure reduced the protein abundance of fibronectin in WT female and nAChR α7 KO mice compared to air control (Figure 6A).|PMC7336696|Previous investigation indicated that maternal nicotine exposures induce decreased fibronectin expression in lung parenchyma.|PMID:23755407|The present results showed a decrease in the expression of fibronectin in newborns’ kidneys, simultaneously receiving nicotine and vitamin C. Our present data were in general conformity with previous studies suggesting that vitamin C maintained the morphology of cells and down-regulated gene expression.|PMC4166096|Similarly, 24h treatment of WI38 cells with nicotine following 1h pretreatment with calphostin completely blocked the nicotine-induced up-regulation of LEF1 and fibronectin (Fig. 5), indicating the central involvement of PKC activation in nicotine-induced up-regulation of Wnt 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the SMMC-7721 cells only incubated with PFT-α had reduced Bax, increased Bcl-2, and reduced apoptotic percentage (3.87%|PMC4163890|Our data shows that PFT exerts the following: 1) inhibition of tumor incidence and tumor growth; 2) inhibition of cellular proliferation via a marked decrease in the expression of tumor marker PCNA; 3) arrest of the tumor cell cycle in the sub-G0/G1 phase, signifying apoptosis; 4) induction of apoptosis in cancer cells via a mitochondrial-dependent pathway as indicated by the up-regulation of p53 expression, increased Bax/Bcl-2 ratio, decrease in the polarization of MMP, and caspase-3 activation; and 5) immunomodulation with an increase in the number of infiltrating CD4+ and CD8+ T cells and an enhancement of TNF-α expression within the tumor.|PMC7189677|As shown in Fig. 7B, pre-treatment with PFT-α attenuated expression of the pro-apoptotic molecule, Bax, and increased the expression of the anti-apoptotic molecule, Bcl-2, compared with the group treated with RSV alone (P<0.05).|PMC7473753|PFT-α inhibits the germ cell apoptosis caused by the experimental cryptorchidism via increasing the expression of bcl-2 and decreasing the expression of p53 and bax.|PMID:24748186|As expected, when PRF-α was added to the PD/Ex527/PFT-α group, apoptosis was reduced markedly, accompanied by reduced expression of Bax and the cyto/mito ratio of cytochrome C and increased expression of 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ironically blunt its own effectiveness by inducing elevated insulin levels that modify the expression and functions of dopamine transporters and receptors.|PMC4698431|An increase ( approximately 25%) in the insulin response to hyperglycemia and a decrease ( approximately 18%) in the insulin sensitivity index were observed after treatment with olanzapine and risperidone.|PMID:12050274|At the end of the initial 12-month, double-blind phase, treatment with risperidone was associated with statistically significant increases compared to lurasidone in weight, BMI, waist circumference, prolactin levels, glucose, and insulin.|PMC7201608|Subsequently, two clinical studies in healthy male subjects demonstrated that mifepristone significantly attenuated not only the side effect of weight gain caused by the antipsychotic medications olanzapine and risperidone, but also attenuated the increase in fasting plasma insulin and triglycerides levels caused by the risperidone.|PMC3819252|Some studies also 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of sorafenib (multi-kinase inhibitor of vascular endothelial growth factor (VEGF), platelet-derived growth factor (PDGF), and Raf kinases) was the first systemic therapy to conclusively demonstrate an improvement in overall survival in patients with advanced HCC.|PMC6697704","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"57094964":{"subject":"PUBCHEM.COMPOUND:253602","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In mouse macrophages, anisomycin-mediated JNK signaling antagonized Akt activity, and loss of Jnk1 gene obliterated this effect.|PMID:27102962|Fao or HepG2 cells exposed to TNF, anisomycin, or sphingomyelinase demonstrated rapid transactivation of ErbB receptors leading to PI3-kinase/Akt activation and IRS-1 serine phosphorylation.|PMC3064087|Neither insulin or anisomycin, 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showed that the expression of VEGF in PFT-α-treated rats was significantly higher than that in vehicle-treated rats (Fig. 4C,D), and the results were confirmed with Western Blot assays (Fig. 4A,B).|PMC4876321|PFT-α induced VEGF expression in vivo and vitro |PMC4876321|Given the degree that VEGF was elevated after the administration of PFT-α, we next investigated importance of VEGF in PFT-α-induced neuroprotection after cerebral ischemia.|PMC4876321|Since upregulation of VEGF promoted angiogenesis and neurogenesis, which further improved physiological functions after cerebral ischemic injury, it is reasonable to propose that PFT-α promotes neurogenesis and angiogenesis, at least in part, through the upregulation of VEGF expression.|PMC4876321|Results demonstrated that PFT-α could improved ischemic stroke outcome by inducing neurogenesis and angiogenesis through the upregulation of VEGF 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both VEGF and PDGF were significantly downregulated after completing a full CMP rush IgE desensitization.|PMC4065666|Both PDGF and VEGF were significantly downregulated (P < 0.05) 6 months after completion of the CMP desensitization process and remained significantly decreased 12 months 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nitrous oxide (N2O) is used increasingly as a sedative and analgesic in the paediatric emergency department (PED).|PMC5843010|to assess the safety and the effectiveness (analysing the behaviour of the patient) with the use of nitrous oxide during the performance of painful procedures in the Paediatric Emergency Departments (PED); secondary objectives: to evaluate the manageability of the method and its acceptance by both the medical team and the patient.|PMID:21440518|Inhaled nitrous oxide (N2O) is used increasingly as a sedative and analgesic in the paediatric emergency department 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MCF-7 cells, one study reported an increase in VEGF expression after MET treatment.|PMC5405996|Expression of VEGF, iNOS, MMP-2, and MMP-9 in aneurysmal walls was also increased by methionine treatment.|PMID:21382440|Western blotting revealed significantly upregulated VEGF, MMP9, and Cadherin 5 levels in the MET group compared with controls (p = 0.021, p = 0.021 and p = 0.033, respectively; Fig. 2E-J).|PMC6367544|c-MET also stimulates angiogenesis through the induction of vascular endothelial growth factor (VEGF) expression (Abounader et al.,), and resistance to bevacizumab, an anti-VEGF monoclonal antibody, occurs by c-MET activation of pro-survival and invasion mechanisms (Lu et al.,).|PMC3619126|The present study demonstrated that c-Met signaling activates both the MEK-ERK and PI3-AKT signaling pathways leading to up-regulation of VEGF expression in the synovial cell line.|PMC4192143","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3619126","PMC5405996","PMC7694406","PMC6367544","PMC4192143","PMID:21382440","PMC6180630","PMC4068350","PMC3366283"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9948216375675675","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:db93695d5500d1a5057fc3ce657d61abc80de04c95e0ee30574ddaf76180337e","tmkp:bb7961a5861c9cf2c9373a33ca1b33ee994e10038376541807d1ceab9f26ca35","tmkp:f4a911649ceda86e21420788e5a9db156975c88e6b2b70dc11e20f84f9a1770a","tmkp:9a04d772a96616eb106015cec841e5ca626a245ffa56e02a154c69b1eaa3d239","tmkp:95a51737d54d490f877c94a6f53480aeb94b0cdc6a60f6849005767fc2e56bdb","tmkp:37749ae93016b4c88fdcbfb2645c8554f3ff20b61117211678d21647bf127bf0","tmkp:f09c717c399d8b6b1de506e32761fb40f5396177343e6a787ff089cfcb9c61db","tmkp:2cfa907e534141326bfcecce8678856966289231a0c5d0f0e22357cf2a0bc49f","tmkp:79a16c8b66de51598b0c98034bf36c63a61b2e0981be556c53dbd64cf0021e21","tmkp:dd68296dcc617d5f1d8e7146c6170ac3b3b13b96541492db28fab31ebdffd350"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"81637460":{"subject":"PUBCHEM.COMPOUND:24759","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"TGF-beta 1 also promoted secretion of glycosaminoglycans into culture medium by BASMC with a preferential increase in hyaluronan secretion (4.5-fold) after 24 h.|PMID:8997260|The TGF-beta1 treatment stimulated productions of hyaluronic acid and laminin, and significantly decreased the secretion of hepatocyte growth factor in LI90 cells.|PMID:9622588|Collagen and hyaluronic acid increased secretion of TGF-beta1, a growth factor involved in bone remodeling.|PMID:11453237|This paper provides evidence that chondrocytes synthesize the appropriate proteoglycan matrix under TGF-beta 1 stimulation: (i) there is a coordinated increase in hyaluronic acid and proteoglycan monomer synthesis, (ii) link-stable proteoglycan aggregates are assembled, (ii) the hybrid chondroitin sulfate/keratan sulfate monomeric species is synthesized, and (iv) there is an increase in protein core synthesis.|PMID:1910291|Furthermore, TGF-beta1 added to SAVIC cultures increased the production of sulfated glycan and hyaluronic 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we report that S-ibuprofen pretreatment of THP-1 cells leads to a dose-dependent inhibition of fAβ-mediated Rac translocation to the membrane (Figure 6A).|PMC2980562","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9982482","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2980562"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:adfe18f1e197d97b733dedbeaadefc826ff2ad9ac826e4853863620cad608d18"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"49767962":{"subject":"PUBCHEM.COMPOUND:6274","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The results revealed that Ki-67 expression was decreased in the His-treated groups compared with the vehicle group, while the cleaved caspase-3 and p-eIF2α expression levels were increased (Fig. 5F).|PMC7160559|His team also mentioned the dose-dependent cytotoxicity to C6 glioma cells and enhanced ROS (Reactive Oxygen Species) accumulation with an increase in cytochrome c and caspase-3 protein level proving enhanced anticancer effect on C6 glioma cells.|PMC7783214|However, the significant reduction by histidine in both ultrasonically induced apoptosis and caspase-3 activation clearly suggests that some ultrasonically generated active species, which can be deactivated by histidine, stimulated the apoptotic signaling pathways through caspase-3 activation.|PMC3475214|A significant reduction in the number of UVA-induced apoptotic cells and caspase-3 activation was observed when histidine was present, which suggested that photodynamically-generated singlet oxygen is an important mediator of apoptosis.|PMID:29061826|Similar findings reported by Fouad and his colleagues in 2017 showing a marked increase in caspase-3 protein levels and Bax/Bcl-2 ratio in rat testis treated with 10 mg/kg cisplatin, in addition, our research team reported before marked expressions of caspase-3 and Bax in rat kidney treated with 6 mg/kg 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VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab ist seit Oktober 2019 in den USA und seit Februar 2020 in Europa zur Behandlung der neovaskulären altersabhängigen Makuladegeneration (nAMD) zugelassen.|PMC7935813|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|In den Phase-III-Zulassungsstudien HAWK und HARRIER zeigte der VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab (8- oder 12-wöchentliche Gabe) im Vergleich mit Aflibercept (8-wöchentliche Gabe2) nach 48 Wochen eine Nichtunterlegenheit in Bezug auf den Visus.|PMC7935813|Consistent with this focus, laser therapy, VEGF inhibitors like bevacizumab (off-label), ranibizumab, aflibercept, and brolucizumab, and corticosteroids such as dexamethasone intravitreal implant comprise the current therapies for DRD.|PMC8003049","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f808cbc09343fd93e4ce84fd299b4b0d8a57415e24b6488bad9aee4cb48d7e19","tmkp:c46a2b530d7c7b126984582e7b87405969fb014947d0c9742b640d13f9020a9b","tmkp:4fd85d389e8ae0846e550b389c7e6a7a81b6a5977af5f09cb6db4be2ee7557d5","tmkp:fbdffedb6dcddaf0298048bcf60ae18bd7de8173bbecff59ffe67693d943b9d2","tmkp:2c8b1a0f0fcb6f767bef5e7ced11e32b817e5e6445db3687f04468bf33d28f13"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC7935813","PMC7263271","PMC7263271","PMC7935813","PMC8003049"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"1140369":{"subject":"PUBCHEM.COMPOUND:1775","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:769588531b9070ea7621102dd48271c01b22e37dafb354d158970afa4f2afcb9","tmkp:766e3195c2209fdcdc07918a399ac9ce427294a435ec7aabcfd84f7feb41cc38","tmkp:5588d9558e77b6bd18577538f8fd9822e81153d2077be2977f7093bb20e0c79b","tmkp:2b61c2f2344d6c3e6efdf349874c1cef80914a837826d12a681d6cbd60ae151f","tmkp:d6b3792ae4d4b380ccc4ddf9aa7d4d681932ce86ba10825949cddff08ee81c0a","tmkp:5fb8c2b01de88be226565c66058c32727452e5be849ab740f02dbd2c69081f51","tmkp:6e91e4ce86b3f5e70ad90a3c0f2bc2b5d10fdb06a3dd6190806a24d904646de8","tmkp:249667372f10ca012d8f85129ae23bd875d197ac7fe03fa857845c4556eb9627","tmkp:274d75d5d254d69628373c9d4987e719c9a7ff76e92431e0f83e5c941ac8386b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:2673162","PMID:7040499","PMID:323000","PMC3371484","PMID:4904710","PMID:4558084","PMID:6759243","PMC4422883"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.996786975","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Serum glucose concentrations rose immediately after the infusion of phenytoin followed by a significant increase in serum insulin values (P less than 0.05).|PMID:7040499|Islets cultivated at 5 mM glucose and at 20 mM glucose with the inhibitors mannoheptulose or atropine lost the responsiveness to glucose and theophylline whereas such islets cultivated at 20 mM glucose alone or with diphenylhydantoin (DPH) or 5.3 mg Mg++ showed a stimulation of insulin secretion by glucose and theophylline.|PMID:323000|Phenytoin sodium has been used to treat muscle cramps of diverse causes, and is known to increase insulin sensitivity during long-term use.|PMID:2673162|Phenytoin-induced improvement in muscle cramping and insulin action in three patients with the syndrome of insulin resistance, acanthosis nigricans, and acral 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expected, control and paclitaxel treated mice showed high levels of insulin and IGF-1 receptor activation in the primary breast cancer tumors, whereas the xentuzumab and xentuzumab with paclitaxel treated groups showed markedly reduced levels of insulin and IGF-1 receptor activation, confirming that xentuzumab has reached the tumor and has blocked IGF signaling (Fig. 5b).|PMC5895608","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"6420318":{"subject":"PUBCHEM.COMPOUND:6322","object":"NCBIGene:5594","predicate":"biolink:related_to","attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6746280"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:af4bffc21c4f0328d9ec4d908ebb508adab686aecd4d831a97e79d97d4c19afc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.00041603","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"OMT 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aspirin.|PMID:11376496|Paradoxically, this research group also reported an increase in VEGF expression in aspirin-treated female mice.|PMC6136175|Rats treated with ASA404 also produced elevated tumor tissue concentrations of cytokines and chemokines, including TNF, VEGF, IL-6 and IL-1α, MIP-1α (CCL3), KC (CXCL1) and IP-10 (CXCL10).|PMC3583340|In summary, ASA VI promotes angiogenesis of HUVECs in vitro via up-regulating the HIF-1α/VEGF pathway, and efficiently enhances the vascularization in regenerated tissue and facilitates wound healing in vivo.|PMID:29219948|The vascular endothelial growth factor level was significantly higher in the letrozole-treated group than aspirin-treated group (0.49 ± 0.26 vs 0.42 ± 0.22, P = 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proteins after transferring on nitrocellulose membranes were blocked using PBS (0.1%) and nonfat containing dry milk (5%) for COX-2, ERK-2, Bcl-2 and β-actin, for pERK-1/2, PBS-Tween (0.1%) containing non-fat dry milk (5%) and NaF (50 mM).|PMC6078184|In some cases, the membranes were stripped using a stripping buffer (140 μl β-mercaptoethanol in 20 ml of 60 mM Tris/2% SDS (pH 6.8) buffer) under gentle shaking for 30 min at 50 °C in a water bath, washed for 1 h in TBST, blocked with 5% low-fat milk in TBST for 1 h at room temperature, and probed with the pan antibodies for PKD1, PKD2, JNK, AKT, ERK1/ERK2, and p38 MAPK, p65-NF-κB, c-Jun, STAT1, and STAT3.|PMC5735906|Aliquots (30 µg cellular protein) were electrophoretically-separated, transferred to nitrocellulose, membranes blocked in 5% milk in 0.05% Triton-X 100/PBS, incubated overnight with specific antibodies to rat PAI-1 (American Diagnostica), EGFR, pEGFRY845, pSMAD2Ser465/467, SMAD2/3, pSMAD3Ser423/425, pp60c-src-pY416 (Cell Signaling); pERK1/2, ERK2, pSMAD 2/3, FAK, RhoA, TGF-βRI (Santa Cruz Biotechnology), phosphotyrosine (4G10, Upstate Biotechnology), caveolin-1, phospho-caveolin-1Y14 (BD Bioscience), pFAKY397, pFAKY577, pFAKY861 (Biosource), and human PAI-1 (#9163) in blocking buffer and washed three times in 0.05% Triton-X 100/PBS prior to incubation with secondary antibodies.|PMC3145778|The ERK2 (# sc-154) and phospho–ERK1/2 (#sc-7383) antibodies were purchased from Santa Cruz (Santa Cruz, CA) and used at a 1/5000 dilution in 5% milk and 1% BSA blocking solutions, respectively.|PMC3392522|After a blocking treatment for 1h with 5% of milk, the nitrocellulose filters were probed with primary antibodies specific for ERK1/2 (sc-7383 Santa Cruz, Italy), ERK2 (sc-1647 Santa Cruz, Italy), pAKT (Ser 473) (#9271, Cell signalling, Italy), AKT (#9272, Cell signalling, Italy), pp70S6k (#9206, Cell signalling, Italy), p70S6k (sc-8418, Santa Cruz, Italy), PARP (#9542, Cell signalling, Italy) and β-actin (A4700; Sigma Aldrich, Italy) overnight; subsequently, filters were hybridated with peroxidise-conjugated secondary antibodies and immunoreactive bands were detected by ECL 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this case, VEGF induced a transient reaching 1.2030 ± 0.0005 (p < 0.01; n = 6 Figure 2C), which was larger than the ratio induced by VEGF in the presence of CPZ (p < 0.05; n = 6; Figures 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with saline-treated controls, the combination therapy of VEGF and NGF significantly reduced infarct volume, water content, neural cell apoptosis and the expression of caspase-3, up-regulated the expression of Bcl-2 and improved functional recovery (both p<0.01) when administered 5 or 8 hours after ischemia.|PMID:29756589","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996966","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3170324","PMC5739168","PMC5581548","PMC6939309","PMC7223834","PMC6288198","PMID:29756589","PMC3951730","PMID:12545262","PMC3940779"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"2505530":{"subject":"PUBCHEM.COMPOUND:3672","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9996085333333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:24833778","PMID:24833778","PMID:24833778"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:47081e2b67e751ec6628bb77e48cd8bf36ca63c83c4357041384c3a54d79f365","tmkp:01be81c2ba0f52a8755548360c447216635d1e4651f23f9a004e8362a1eaf42d","tmkp:0ff830a61df2b831390afe561c3f42bb05cbc9e253b523e11c2cc3d0fe7cdf55"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Ibuprofen treatment prevented sustained elevation of MEK-ERK signaling at 3 h (p-ERK1/2, p-RSK, p-Mnk1, p-p70S6K Thr421/Ser424) and 24 h (p-ERK1/2) postexercise, and this was associated with suppressed phosphorylation of ribosomal protein S6 (Ser235/236 and Ser240/244).|PMID:24833778|Ibuprofen treatment prevented sustained elevation of MEK-ERK signaling at 3 h (p-ERK1/2, p-RSK, p-Mnk1, p-p70S6K Thr421/Ser424) and 24 h (p-ERK1/2) postexercise, and this was associated with suppressed phosphorylation of ribosomal protein S6 (Ser235/236 and Ser240/244).|PMID:24833778|Ibuprofen treatment prevented sustained elevation of MEK-ERK signaling at 3 h (p-ERK1/2, p-RSK, p-Mnk1, p-p70S6K Thr421/Ser424) and 24 h (p-ERK1/2) postexercise, and this was associated with suppressed phosphorylation of ribosomal protein S6 (Ser235/236 and Ser240/244).|PMID:24833778","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"107095221":{"subject":"PUBCHEM.COMPOUND:174","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Both phosphorylated Akt (p-Akt) and VEGF level were significantly elevated by PEG-Ex4 treatment (Fig. 6B).|PMC4279188|Furthermore, ASCs encapsulated within 3D polyethylene glycol/hyaluronic acid (PEG/HA) hydrogels showed significantly higher secretion of vascular endothelial growth factor (VEGF) and placenta-derived growth factor (PDGF) compared to cells cultured on top of 2D hydrogels.|PMC5521188|Moreover, the expression level of VEGF and bFGF in the groups treated with MF‐Lip10@PEG, MF‐Lip20@PEG, and MF‐Lip40@PEG was significantly higher than those in the control group.|PMC6364594|Moreover, the expression level of VEGF and bFGF in the groups treated with MF‐Lip10@PEG, MF‐Lip20@PEG, and MF‐Lip40@PEG was significantly higher than those in the control group.|PMC6364594|In the present study, PEG-Ex4 increased VEGF level in both failing heart induced by MI and cultured HUVECs while VEGF inhibition abolished the survival and functional benefit of PEG-Ex4 treatment and increase of tube formation, confirming that PEG-Ex4 increases VEGF production by endothelial cells and this effect plays a key role in mediating the cardioprotection of 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had already published that indomethacin caused proteolytic degradation of PARP-1 and a reduction of Akt phosphorylation in glioma 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pilot study was conducted to prospectively compare symptomatic improvement following a single injection of intramuscular dexamethasone (IMD) to a 3-day regimen of oral prednisone (OP) for children with mild to moderate wheezing episodes that are responsive to nebulized medications in the Pediatric Emergency Department (PED).|PMID:9350159|This study examines caregiver preferences of single-dose dexamethasone (DEX) versus 5-day oral prednisolone in treating acute asthma exacerbation in a pediatric emergency department (PED).|PMID:25009118|This clinical experience suggests that we should rethink dexamethasone implantation for patients with PED and pachychoroid and should be cautious in using the above treatment.|PMC6685827","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.980293","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"8521858":{"subject":"PUBCHEM.COMPOUND:2726","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:de0fdfde46ef611aaf4e294ce128c1495cce4034f22bcfd58b0f354cbb85644a","tmkp:9f8a684ffa20f9538ae5a028a878b3918907eb81bceba2dd0c9d0253c9bec9f5","tmkp:612015de3fbe5b8484c0a0c75e0f0703baab09dd3a9cebd097736d89e4b54626","tmkp:df287af0db1d77fe35935e3ebee71ee041c9973543ecf6be20fce1365a4b2f2e","tmkp:623fb4879c06870c4c1438ce9be736cf2fe6591192bfd367948463550059bb17","tmkp:28ad52d79bb7a41e3bfdab1ab27b40c1293b215d44a24dbb2585728519567e9f","tmkp:b9761f3dd7e47c22f27208a92580979b916a08c1c9ab581a47420357753000ac","tmkp:26fe70eb670cb9438ad90f5f1492aba3f133c552c3404e127f543d0327980860","tmkp:d6bb2eebbe1472061c9b86aefcc691d3d1a1a847583f20c9a29a490805cb3109","tmkp:b59f0647e087a3f1b82ec22c0b01a344ec722861ebb3b09c084dfe2be6cbdf7c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9988403691666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:26592196","PMC3136481"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Western blot analysis showed a substantial increase in the level of Bcl-2 upon treatment with CPZ at 20 mg/kg (Figure 4B).|PMC3136481|Interestingly, we found that the Bcl-2 level was increased in the brain of rats injected with CPZ either once in isolation or continuously for two weeks, which is consistent with previously published data indicating that antipsychotic treatment can raise cortical Bcl-2 levels in schizophrenic patients.|PMC3136481|Furthermore, in another independent rat model of apoptosis, compared with the group administrated with alcohol only, the brains of the CPZ-pretreated rats showed lower expression of cleaved caspase-3, cytochrome c and Bax, but higher expression of Bcl-2 and TF.|PMID:26592196|The results showed an increase in Bcl-2 and a decrease in Bax expression (Figure 4C) in the CPZ-treated group.|PMC3136481|Compared to the group injected with ethanol only, the brains of the CPZ-pretreated rats had fewer apoptotic cells, lower expression of cleaved caspase-3, cytochrome c and Bax, and higher expression of Bcl-2.|PMC3136481","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"60274314":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:19053028","PMC4929690","PMC4260762","PMC6400119","PMID:3611064","PMC7290481","PMID:8262151","PMC7400414","PMC7926795"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:72220aa5012c28d8021cfa885b36b2dbf31761fc029166de38f4327d0839dec0","tmkp:b438b8433557953dd44a3d5ec91200e3bc003c14e68b82c969f689cdbd0ee7c4","tmkp:ef18571684e7c2ae398c7d73b9fd42d66181b1bea7de0dcbb541057b4688ed47","tmkp:3e698dfe47ffc22df48c7bf139abe95311c39f442dca48067e9ce7fbd1a85993","tmkp:495b1b7c9f923ea5bc3e7bcc1780b682d47469d62c279f1f63f5e58f0af6d1f8","tmkp:338fc3357da471f2d952daa84cbaa2a1ad1400f731fb41b6cdc8f9d775a524d8","tmkp:822935f32cd8ec22655dece0abc2d7624f974c436f23c8d9d8ecfe3670a7ded7","tmkp:f5fab8ba3fcdf82364398eae9717f230c6746720b22c58f22bd35aa63babaff1","tmkp:a1949c7e8a9f3fda56b75df500a6f1a26636e799fc5404afcabbff765df3fd6f","tmkp:ec79d264917dc99eb41f4de085ede91c5d6e46fc6b0775e2d9f5a9a74bcd8ff5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9924471536","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Consistent with the mitochondrial membrane depolarization that we observed, we noted significant mitochondrial accumulation of PINK1, Parkin and p62 in HCb24h compared with Ctrl mice; in contrast, the level of Mfn1 was significantly reduced in the same mitochondrial preparation (P<0.01,|PMC4260762|Authors found that Alba (same as in study above) and Romina cultivars presented the best results, with decreased collagen 1A1, fibronectin, versican, and activin A mRNA expression in UF cells.|PMC7290481|Moreover, SAMe treatment attenuated transforming growth factor-β (TGF-β)-induced fibronectin expression in cultured fibroblasts.|PMC4929690|We next confirmed that SAMe significantly reduced TGF-β1-induced fibronectin expression in the human fibroblast cell line, MRC-5 (Figures 8a and b).|PMC4929690|The same concentration of BFA completely blocked accumulation of secretory proteins, e.g., fibronectin into the culture medium, probably due to retention in ER.|PMID:8262151","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"59544160":{"subject":"PUBCHEM.COMPOUND:3672","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Indomethacin (1 mM) and ibuprofen (1 mM) significantly reduced Bcl-2 expression in the cancer cell lines tested and might be thought responsible for the observed increase in apoptosis.|PMID:11813903|Capsaicin stimulation of the pulp also significantly increased the Bax:Bcl-2 ratio and activated caspase-3 in the hippocampus (P<.01), which was inhibited by ibuprofen pretreatment (P<.05).|PMID:26485387|In contrast, pretreatment with celecoxib, indomethacin and ibuprofen (2.5 and 5 μM) in PC12 cells treated with 6-OHDA decreased Bax/Bcl-2 to a level similar to the related control (Figure 4).|PMC6556502|Cell pretreatment with celecoxib, indomethacin and ibuprofen decreased Bax/Bcl-2 to a level near that of control and the Bax/Bcl-2 ratio is slightly similar for all three drugs.|PMC6556502","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99969175","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:11813903","PMID:26485387","PMC6556502","PMC6556502"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:9dce6c29abb71c9f0dbaa4b5b1c5ddd06f46df1116b954d5c276512c4c0e14b9","tmkp:a96c23bfaec4eb96b739b290486310ba90a17a49af0fd46db7a425088e3833bd","tmkp:058c925fbd138ce31f6effb52706ef8e146ff54d1abfc87a979c83ceb0f88704","tmkp:9b967997445d4a8fc894b0f3f25fd604d796c12ead2b2170761e864a7b6b7a6e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"47804502":{"subject":"PUBCHEM.COMPOUND:135398744","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Moreover, sildenafil dramatically decreased the expression of transforming growth factor-β1 (TGF-β1), vascular endothelial growth factor (VEGF), and α-smooth muscle actin (α-SMA) in the grafted aortas and increased the concentrations of cyclic guanosine monophosphate (cGMP) and endothelial nitric oxide synthase (eNOS) in serum.|PMID:29218089|Sildenafil also increased serum levels of TAC and Flt-1 and decreased TOS, OSI, and VEGF.|PMID:25541842|Moreover, sildenafil dramatically decreased the expression of transforming growth factor-β1 (TGF-β1), vascular endothelial growth factor (VEGF), and α-smooth muscle actin (α-SMA) in the grafted aortas and increased the concentrations of cyclic guanosine monophosphate (cGMP) and endothelial nitric oxide synthase (eNOS) in serum.|PMID:29218089|Moreover, we were able to demonstrate that sildenafil strongly diminished chronic inflammation in the metastatic LN indicated by a drastic reduction of IL-1β, VEGF, GM-CSF, CCL2, CCL3 and S100A9 production.|PMC3564242|However, contrary to the findings by Koneru et al. and Liu et al., sildenafil citrate rather decreased VEGF levels in fertile women and had no influence on idNK cell VEGF production in RPL patients.|PMC8112925","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9990461468181819","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:16716755","PMC8112925","PMID:25541842","PMC3564242","PMID:29218089","PMC3828881"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c607cb1eced8f41fe816f9feea5f45ad04a18652ecae13ec7bd34297f2082cae","tmkp:ff8a635a6e50d58f7594ce6c3813e9bc66d62b54a98b3394eaf1612ee689bce7","tmkp:75b2b17ec728618b170a3eda858f8b6bbbfee03b7798b6284317680464321ed2","tmkp:ecba9df3fe36bcd1a828064a42df0c892f2afcc90cee9a6c7a44bd473fb0258f","tmkp:4c7c60f9a24cf93f9284e627b4f23611b19335596ea49d9f458661ff106b3cfc","tmkp:9d527060c42ba64f56f71254c19c9fedc2df1afe2a753690069b2f662c964cc0","tmkp:723ca5a39d81eecba96c69e5e08da8076ce326dd4cce23419d320ae03607e6f8","tmkp:1281ffa9fb0b83978b3c8d2e6054210d6db52854fab249888ed91407c47e44bf","tmkp:0153bd90151a7f03e2f1dc556e42c4735bdaaa1feca13463c34b9af2c9804987","tmkp:12a2a80e33b19513bc07feb3c459b0a9c80cb4fd104639f48234d6de4319f5ec"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"39678144":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Combined treatment with IL-4 and other known inhibitors of breast carcinoma cell growth [transforming growth factor-beta 1 (TGF-beta 1) and the antiestrogen tamoxifen] showed additive inhibition.|PMID:1728401|Similar studies have shown that the SERM tamoxifen and toremifene inhibit the GM-CSF and IL-4 supported differentiation of human DCs from peripheral blood monocytes and synovial fluid macrophages.|PMC3415586|We observed such behaviour for IL-1, IL-2, IL-4, IL-9, IL-17 and IFNγ, all of which were reduced to low levels following tamoxifen induced nuclear localisation of GFP-Foxp3-ERT2 in cFoxp3-transduced Marilyn CD4+ T cells.|PMC3467196|Expression of both IL-4 and IL-13 decreased in total kidney homogenate after tamoxifen administration (Figure 2a).|PMC5548101|Moreover, iCre-/+IL-4Rα-/Lox mice treated with tamoxifen produced significantly less IL-4 and IL-13 after re-stimulation with either N. brasiliensis antigen (NbAg) or mitogen compared to control mice (Fig 4G).|PMC5501681","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8ac5440185392c7d1f026618858a90bc3432260e2d5c9ed9a24d520205c82323","tmkp:98850018ed0520966d146d2756db93e365c9a43f68649da5354f105589437a2b","tmkp:fbd3e24e7b6a574e3ed740394f6c5f1236e75f51ff5d44f722d3d12a00349cab","tmkp:4e75a8e3207451ad39ae82c0baab336b3871b2a42fe0af88273d917cd6c68d3e","tmkp:17ab8d7dcc86ce67c6c362961e6de7e7258683396be61f0b46ff602c70191fea","tmkp:5f3e0b6e42aef94b368b32df21515f2c8eae2652364ebfebf835f144d86ef083","tmkp:c801c8d8718b0735a26118dcb98e1e9b629d7548899526089460180607d359f3","tmkp:07bb8930d7a7d2821bb8c6d24cfbdc9838600ce361bf7c794547ecc36396976c","tmkp:963256fd5c37bbdba08611644a2064b479c65a657c219b5899ce13c6ffc2801f","tmkp:91e1924888f4962d02d899c60f7319552af6469d5938c24bc083d42bd15e117e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC2896666","PMC3467196","PMC7589740","PMID:28395712","PMC5548101","PMC2667209","PMID:1728401","PMC5501681","PMC3415586","PMC8231265"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9995945666666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"18496387":{"subject":"PUBCHEM.COMPOUND:135398744","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99768372","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:edb5a9328fa19745a4fe003500cd7ac08288465f599fc50d569196c5bb5de1db","tmkp:092d677ffaab17a16092d1bff00744b04a1b75effb5a715983dc607d1b3ed29e","tmkp:d26c4a84dc4d4f8e58cb96a2f1c7a4fe2ff4ab0767a67a53237acaf9171ccee6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"We investigated for the first time whether three clinically relevant polymorphisms in the VEGF gene are associated with altered responsiveness to sildenafil treatment in postoperative erectile dysfunction (PED) and clinical erectile dysfunction (CED).|PMID:23007311|Our results indicate that VEGF polymorphisms affect the responsiveness of PED and CED patients to sildenafil.|PMID:23007311|Sildenafil poor responders have shown higher plasma arginase activity in PED and higher arginase 1 levels on CED groups.|PMID:28374859","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:23007311","PMID:23007311","PMID:28374859"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"74490918":{"subject":"PUBCHEM.COMPOUND:56603655","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"To review clinical data on the sequential use of the non-selective vascular endothelial growth factor (VEGF) inhibitors (ranibizumab and bevacizumab) and the selective VEGF inhibitor (pegaptanib) in the treatment of neovascular age related macular degeneration (n-AMD).|PMID:22283373|There are many other drugs that may play a role in DR therapy in coming few years such as somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|A number of drugs may play a role in DR therapy in the coming few years; eg, somatostatin agonists (sandostatin), corticosteroids (triamcinolone, dexamethasone, fluocinolone), vascular endothelial growth factor inhibitors (pegaptanib, ranibizumab), hyaluronidase and plasmin enzyme.|PMC2701130|Nowadays, VEGF-inhibitors like bevacizumab, ranibizumab, pegaptanib, are the first choice in therapies for the treatment of neovascular ocular diseases.|PMC6249906|In this way, the effect of VEGF inhibitors (pegaptanib, bevacizumab, ranibizumab) on primary cultures of human REC and CEC was evaluated by Stewart et al.. Significant differences between retinal and choroidal microvascular cells were observed, which highlights the need for specific treatment interventions in RNV or CNV.|PMC6321100","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9945540733428571","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:656765128aaadad30ff66a2452e5ecd5e5a1d5d186d1caf2609b14a2da1b94ef","tmkp:74d9042b489c2110bcd270dab137a5c551d78d533ef9175e73da13464909c039","tmkp:dbe957d93ebed88053dcab82e5bc817f08fd456d0ed41d444f819d84b2fb80fd","tmkp:dc150fdaf0bb3f8d5cdebec9d7a7369c8220db63dcf82612b5d9ec69809e0e24","tmkp:1c68d027b824904be284f59c6afdb000ff690acca78d8bb4375417532418bb4e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:22283373","PMC2701130","PMC2701130","PMC6249906","PMC6321100"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"23068030":{"subject":"PUBCHEM.COMPOUND:6957673","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:3136a1b67e43df185467f371887e8cc691a96eb8dd389700f877de2e216232da","tmkp:69a0ecc4d517d6a1b30ca373287f0d11cc98d16a7628a10c8934c9b858bceaf1","tmkp:99a06921fd8e0f69bc55721098cda58e4dfeb7ece01dc3e00187044ed822763f","tmkp:3792cff98a52268e3a545a3a2cab758b9ba6227035f5ececec72ab7310c3ffe9","tmkp:5ee42b3f55a6fef8de5e120a44a48f29c982e367fdd97f688d8f3f7dc4518531","tmkp:3ddae518fc71548fccce11f0c49d12ee19b1421c1371e1769271d3916c4851ee","tmkp:29f860e97693dc41e4d8f0ff993d52004f67e39fe7826530b5971b0760fa18a5","tmkp:1888f9d7cd6e66e25f836292b9dbb244325cefa329f8f2133cc14fbbb5fdab71"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9994304342857143","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Results showed that the expression of VEGF in PFT-α-treated rats was significantly higher than that in vehicle-treated rats (Fig. 4C,D), and the results were confirmed with Western Blot assays (Fig. 4A,B).|PMC4876321|PFT-α induced VEGF expression in vivo and vitro |PMC4876321|Given the degree that VEGF was elevated after the administration of PFT-α, we next investigated importance of VEGF in PFT-α-induced neuroprotection after cerebral ischemia.|PMC4876321|Since upregulation of VEGF promoted angiogenesis and neurogenesis, which further improved physiological functions after cerebral ischemic injury, it is reasonable to propose that PFT-α promotes neurogenesis and angiogenesis, at least in part, through the upregulation of VEGF expression.|PMC4876321|Results demonstrated that PFT-α could improved ischemic stroke outcome by inducing neurogenesis and angiogenesis through the upregulation of VEGF expression.|PMC4876321","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC4876321"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"38731008":{"subject":"PUBCHEM.COMPOUND:54729367","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3575099","PMID:16202406","PMC6959564","PMID:15557436","PMID:15728539"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9875069059999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"One mechanism by which doxycycline decreases the production of MMP-9 is its ability to inhibit the intracellular p38 and C-Jun-N-terminal kinase mitogen-activated protein kinase signaling cascade.|PMC3575099|SB202190, PD98059 and doxycycline markedly suppressed the levels of p-JNK-1/p-JNK-2 and/or p-ERK1/p-ERK2, as well as IL-1beta, TNF-alpha and IL-8 mRNAs and proteins stimulated by hyperosmolar media.|PMID:16202406|In order to confirm ablation of JNK1 from lung epithelial cells following administration of doxycycline (dox), single cell suspensions were prepared for flow cytometric evaluation as described previously.|PMC6959564|The p-JNK inhibitor SB202190 and doxycycline markedly inhibited the stimulation of p-JNK-1, p-JNK-2, and p-c-Jun, as well as MMP-9, -1, -13, and -3 at both the mRNA and protein levels in the cells exposed to hyperosmolar media.|PMID:15557436|Doxycycline markedly inhibited the TGF-beta1-induced production of MMP-9 and activation of the Smad, JNK1/2, ERK1/2, and p38 signaling 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may block immunologic escape in the treatment of 3LL bearing mice partly through up-regulation TAP-1, TAP-2 and eliminating Treg cells.|PMID:20959065|[Paclitaxel blocks immunologic escape through up-regulating TAP-1, TAP-2 and eliminatiing Treg cells in 3LL-bearing mice].|PMID:20959065|was remarkably higher in paclitaxel-pretreating 3LL group than that in 3LL bearing mice group with TAP-1 (1.93%+/-0.25%),|PMID:20959065|Exposing tumor cells to other drugs such as paclitaxel and doxorubicin increases the expression of the antigen processing machinery via the cytosolic route, such as TAP1, tapasin, and 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combined treatment with MMC and RAPA reduced the expression of caspase3 and caspase8, while increasing the expression of LC3 II and ATG5.|PMC8165251|We previously showed that one MMC treatment in FancC −/− mice reduced the BM cellularity by 70%, decreased the short-term reconstituting cells (Lin−c-Kit+Sca1+CD34+ stem cell population) by 85% as compared to untreated mice, and decreased colony forming cells (CFCs) and long-term culture-initiating cells (LTC-IC) to levels of 16% and 33% of untreated mice, 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higher value of AIR indicates an increase in insulin secretion.|PMC3485446|The insulin (panel C) is higher for the AIR individuals, whereas the glucose profiles are the same (panel D), the same pattern seen in the IVGTT (Figure 6).|PMC8100339|The patients treated with insulin (especially with CSII) had higher remission rates and better improvement of AIR at 1 year follow-up irrespective of the recruiting FPG (CSII or MDI vs OHA: 57.1%, 51.8% vs 32.8% in stratum A, P < 0.05; 44.4%, 38.7% vs 18.6% in stratum B, P < 0.05).|PMID:20356473|Exposure to particulate matter (PM) air pollution, but not NO2, during pregnancy was associated with increased levels of cord plasma insulin at birth among 590 newborns in Belgium, suggesting that prenatal exposure could increase the risk of cardiometabolic dysfunction later in life.|PMC6876847|For example, air pollution has been associated with adverse lipid changes and higher fasting glucose and insulin as well as higher childhood body mass index (BMI) 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the normal men, insulin administration resulted in a significant decline of basal plasma glucagon and C-peptide levels and in a clear-cut decrease in the arginine-induced glucagon response.|PMID:3286673|In women levels of cGMP rose and levels of L-arginine decreased significantly during insulin infusion, consistent with an increase in nitric oxide production.|PMID:8932993|In perfused control pancreas, the priming effect of D-glucose resulted in a time-dependent potentiation (TDP) of insulin release during subsequent L-arginine stimulus, whereas L-arginine induced a time-dependent inhibition (TDI) of insulin release during subsequent D-glucose stimulus.|PMID:1513806|Our results show the inhibitory effects of arginine on the initial aggregation kinetics of bovine insulin over a range of insulin concentrations and quench temperatures.|PMC3400368|Although the insulin levels in all BMI categories were higher in the 2nd trimester, such levels during weeks 24-27 were suppressed only in normal-weight women after l-Arg 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administration leads to increased VEGF-induced phosphorylation of SHP-2 and this increased phosphorylation parallels the increased phosphatase activity of SHP-2.|PMID:19706677|Activation of the dopamine (Dp)/dopamine receptor 2 (Dp-r2) pathway was involved in the VEGF/VEGFR-2 signaling process and can reduce neoangiogenesis.|PMC6191968|Dopamine stimulation slightly decreased the surface expression of vascular endothelial growth factor receptor-2 (VEGF-R2) but induced the phosphorylation of VEGF-R2 through Src in 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this methodology, Elokdah and colleagues identified Tiplaxtinin as a potent and selective PAI-1 inhibitor, which became one of the most studied PAI-1 inhibitors to date.|PMC5345237|The most intensively studied PAI-1 inhibitor to date is tiplaxtinin (also referred to as tiplasinin or PAI-039).|PMC7817699|We have also reviewed the range of SERPINE1 inhibitors available to date and stressed, despite promising results, the need for further development for some existing therapeutics.|PMC7997307|Small molecule inhibitors of plasminogen activator inhibitor (PAI)-1 have been reported to date but their clinical effects still remain 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with 10 microM unconjugated bilirubin (UCB)/human serum albumin in a molar ratio of 3:1 and 250 microg/mL ibuprofen caused additional loss of cell viability and increased LDH release (p < 0.01), DNA fragmentation, and activated caspase-3.|PMID:19127220|Ibuprofen selectively increased the cytotoxic potency of MMC and caspase-3 activity in both malignant cells lines but not in 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novel observation was the fact that ouabain induced IL-10 and VEGF as well.|PMC4034513|Nevertheless, the levels of IL-10 and VEGF measured in the supernatants of cells cultured for 24 hours in the presence of ouabain were also higher than control levels (Figures 6(c) and 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also significantly decreased Mfn1 to 75% of the level in controls, but did not decrease expressions of Mfn2 and Opa1 (Fig 4A, 4B and 4C).|PMC5085033|It was also recently shown that diclofenac treatment decreased mitochondrial membrane potential in both rat and human hepatocytes in vitro, accompanied by mitochondrial fragmentation due to decrease in the mitochondrial fusion protein Mfn1.|PMC6261533|Specifically, acetaminophen and diclofenac down-regulated the mito-fusion proteins Mfn1, Mfn2 and Opa1, but did not affect the activity of fission protein Drp1.|PMC5085033|(A) Treatment with acetaminophen or diclofenac significantly decreased Mfn1 expression.|PMC5085033|As observed following DFMO+diclofenac treatment, Akt inhibition also down-regulated the expression of EMT-regulatory proteins such as N-cadherin, fibronectin and EMT-associated transcription factors slug and twist (Figure 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1 month of follow-up, increased fibronectin and collagen alpha1 (IV) mRNA were present in the retina of diabetic and galactosemic animals, and the bosentan-treated groups exhibited mRNA levels similar to the control 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highly effective in suppressing EVs containing mRNA encoding CD63 and TGFB1 by CD90+ CSCs, which may be related to the ability of sorafenib to prolong overall survival in advanced HCC patients and suppress de novo metastasis.|PMC5596021|Sorafenib can directly inhibit tumor proliferation, neovascularization, and promote apoptosis by inhibiting RAF/mitogen-active protein kinase/extracellular signal transduction pathways, vascular endothelial growth factor, PDGFRβ, c-kit, Flt-3 and p38 tyrosine kinase transfer, 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VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab ist seit Oktober 2019 in den USA und seit Februar 2020 in Europa zur Behandlung der neovaskulären altersabhängigen Makuladegeneration (nAMD) zugelassen.|PMC7935813|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|In den Phase-III-Zulassungsstudien HAWK und HARRIER zeigte der VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab (8- oder 12-wöchentliche Gabe) im Vergleich mit Aflibercept (8-wöchentliche Gabe2) nach 48 Wochen eine Nichtunterlegenheit in Bezug auf den Visus.|PMC7935813|Currently used anti-VEGF agents (ranibizumab, bevacizumab (Genentech), aflibercept, and brolucizumab (Novartis, Basel, Switzerland) inhibit VEGF-A or VEGF-A, B and placental growth factor 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arginine supplementation results in sustained wound nitric oxide production and reductions in vascular endothelial growth factor expression and granulation tissue formation.|PMID:16631200|Local arginine supplementation results in sustained wound nitric oxide production and reductions in vascular endothelial growth factor expression and granulation tissue formation|PMC4468226|In a published report, the culture of SKOV-3 and MDAH2774 ovarian cancer cells with L-NAME (an L-arginine analog) significantly reduced the ability of cells to produce vascular endothelial growth factor (VEGF) and completely blocked their capacity for angiogenesis, in the in vitro angiogenesis assay.|PMC6479373|L-Arginine further significantly increased MDA and NO, and decreased VEGF (P < 0.05 vs aortic IR).|PMID:18085359|C-terminal arginine-like compounds have established efficacy for inhibition of VEGF/Nrp 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anesthetic doses that produced loss of righting reflex, isoflurane, propofol, and ketamine all reduced phosphorylation of the activating residue T183 of ERK2 (but not of ERK1); S897 of the NR1 NMDA receptor subunit; and S831 (but not S845) of the GluR1 AMPA receptor subunit in cerebral cortex.|PMID:17826804|It was important to optimize the concentration of NMDA used in our experiments, as exposure of neuronal cultures to relatively high concentrations of NMDA (70-100 μM) had been previously reported to cause inactivation of ERK2 via binding to and activating extrasynaptic NMDA receptors.|PMC2693081|n = 4, p<0.01 vs. NMDA, p = 0.09 vs. cont), it also completely abolished any dopamine induced ERK2 activation as well (0.97±0.05, n = 4, p<0.001 vs. dopamine, p = 0.61 vs. cont) (Fig. 4A).|PMC1762427|Addition of a calcium ionophore or 100 microm NMDA decreased phospho-ERK2 in the presence of 1 mm extracellular calcium but enhanced phospho-ERK2 in 0.1 mm extracellular calcium.|PMID:11062237","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9911453225","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:5afa1db1906ac35ab95af6bebba803edc6349e3722fa9ce6778528deca87e80a","tmkp:ca9151940533746c6d7489bb0e54ae896ce61d1aea811fdd42b779d719e26389","tmkp:40bad7cb470ac2bdeafaa6f99ac7b2d0c74defe7500f615e472fc4f94fbabd07","tmkp:58f46fb52dbdc8bf4666e65475b013206705000987350c631f41af8264dc1059","tmkp:d7977c75f48b4e0b1d0ca577f14d32c127b3b9b9a102691a39e238a28fd42f96","tmkp:31421f56a1058e944e4e6c4985ebaba825edc63fa314f55ab0d10952777e68c3","tmkp:1505e45861a0859b26f683c63abbb05f3453918d81a02fe578624bf811f47d1c","tmkp:a322eaac93393e9c46d95214c9c83f5cd93e9a1afa45d619bb7933a31bfb0ce7","tmkp:7ab45246b4b81950ea0c28fb402f186fa08c25c91c63738f21dca0f99e3a913b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"31200216":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9983685846666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Ethanol exposure resulted in reduced VEGF-induced cord formation on collagen and reduced capillary network structure on Matrigel in vitro.|PMID:18469146|VEGF prevents the apoptosis of primary cultured SECs induced by ethanol, through at least in part, inhibition of ethanol-induced down-regulation of Ets-1 protein expression and ethanol-induced up-regulation of Casepase-8 activity in SECs.|PMID:18269875|A model of in utero exposure of lambs to maternal alcohol was developed demonstrating reductions in lungs of preterm lambs of hypoxia-inducible factor (HIF), vascular endothelial growth factor (VEGF), and surfactant protein A (SpA) (Lazic et al.).|PMC7223741|In utero alcohol exposure resulted in a 32% ± 9% decrease of VEGF-A (p < 0.05; Fig. 1e), whereas PLGF was undetectable by Western blot (Fig. 1f).|PMC5461764|A model of in utero exposure of lambs to maternal alcohol was developed demonstrating reductions in lungs of preterm lambs of hypoxia-inducible factor (HIF), vascular endothelial growth factor (VEGF), and surfactant protein A (SpA) (Lazic et al.).|PMC7223741","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC3213039","PMID:11404314","PMID:18469146","PMC4081417","PMC6218769","PMID:18269875","PMC7223741","PMC5461764"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:234dc1c070e479ed374b1aca3b63fe3f4e6fc0e66c3d53ab4d73e9258b794671","tmkp:798c5c76a6093b1bd7250fe0a69f9c1531721cc0f83480ca38f4e69acc0ea793","tmkp:b92714927a0a35c5780da27cb8a6c4cfbe4e368ff4b41ecafdc136242030eb61","tmkp:8d2d0f7e556d432335b2888b8674d35661d9b05f739b37e01f4ecb737abe2ff2","tmkp:1969040dcaed002be61e7eb618878aeae27e5962f076323ecfb0e993243e258c","tmkp:3d9a82441496f9256778e912df1d7bbe4896390b5c22c07f77d21484f9542923","tmkp:9f55a6b18d2b346145b4005abd0f7e322090c42fdb32ca7082d207e932f0f5cd","tmkp:ce295e303e1c990f3c0d05c5a4b49ece82617bd9d9295713ba09213519d48255","tmkp:ba7b5e7ddf9703c23ab0a6d082cae30ae0f0bc2f3ef9f8fc237cd2d24d85a10a","tmkp:f6887c3950a275c146293983699a9e7be95edce77f6d729cf2275d17a614b162"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"34088117":{"subject":"CHEMBL.COMPOUND:CHEMBL292268","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:ec7189f7bdfc9342b1a3a8a63eb8f3b825e7ed5668c6611491393f6cdd2175e4","tmkp:ab910a6f13375c1f969a6dcc3b76a53cff45d48ee62ca2ee4c4fb7c6f9fe108e","tmkp:1fbb09653bd8166337730f8c684b7fc1526420458edadde6a99921015fd58fbe","tmkp:6995d05630a7357904186e7b4fbb881c61d2a9acc373806a6e2b7756618779d3","tmkp:1f10d87c910cde47c7edc15e5be924a5079c5d936a62c43398caa08478d3a0d6","tmkp:c42e20d81f6e73dbfe790ba07121e6951e62bbe7ae856b3f2db9f9b989b3f286"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Additionally, the differences in myocardial PI3K protein, mTOR protein, p‐PI3K/PI3K, p‐Akt/Akt and p‐mTOR/mTOR in the 3‐methyladenine group were not statistically significant (P > 0.05) compared to the model group, but Akt protein expression was significantly up‐regulated (P < 0.01).|PMC7576289","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7059812","PMC3355994","PMC5225378","PMC7576289"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9993518","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"3331146":{"subject":"PUBCHEM.COMPOUND:10607","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:24216299","PMC5514346","PMID:26780219","PMID:30096284","PMID:25791936"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Then the administration of selective ERα agonist PPT partly reversed Aroclor 1254-induced alteration in Bcl-2, caspase-3 and cyclin D1 protein expression while selective ERβ agonist DPN accelerated it.|PMID:24216299|We found that ERα and/or ERβ activation using their agonists (0.5 mg/kg E2, PPT or DPN) ameliorate memory impairment in the Morris water maze (MWM) and Y-maze tests and suppress apoptosis as evidenced by decreased caspase-3 activity and increased ratio of Bcl-2/Bax.|PMID:30096284","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e860090e321b1a5edfe43fa83d69ebb239426c352077a8e4946cf68cdd29a72e","tmkp:f80958b8ef4e8c5aea1a7c01eb8e72418a6dac96cfeea6e03e176d6b3d48501f","tmkp:3f3bbfbe2c0c853a04260275a49abb4c32cf9e49904a85178fde54bbf0b31c5c","tmkp:926d4ad295f200bb1ade6129298628ac227ad787d1eca50f6f951ff779b4ac78","tmkp:b467eaa49cef121fdcfef400058d9003b7354718a8b436c726787d6f1c935200","tmkp:d82de66006501d11343ce768209a7968ab506095a15acc22780d4c371b10f99f","tmkp:4b9b3869a160100adcc0951b558a757a6968336f3917458ccf1b4706904475d6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9966611000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"116094408":{"subject":"PUBCHEM.COMPOUND:36314","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:6c51206585412f093b0f867caf855640e6356c196c7fbd381f2d0aa1df08a648"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.98056567","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"As shown in Fig. 6a, this inhibitor reduced the glucose uptake under both normoxic and hypoxic conditions, as a consequence of HIF-1α and GLUT-1 down-regulation (Fig. 6b); most importantly, the sequential combination with paclitaxel potentiated these effects.|PMC6736958","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6736958"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"6972770":{"subject":"PUBCHEM.COMPOUND:2803","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9984689275","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Levels of p-ERK1/2 in LC of animals treated with clonidine (60 μg/kg, i.v.) or ethanol (1 g/kg, i.v.) were increased compared to saline treated animals (Fig. 4A), though the difference was only significant for ethanol treatment.|PMC3770283|In MEFs expressing both spinophilin and arrestins, activation of the α2BAR by clonidine induced transient ERK1/2 activation, which was desensitized after 20 min of stimulation (Fig 4).|PMC4526467|The Western blot analysis showed that clonidine stimulated phosphorylation of ERK1/2 in the cultured cells; activation peeking after 10 min of exposure (Fig. 7).|PMC3933766|Moxonidine and clonidine also increased by greater than two-fold the proportion of ERK-1 and ERK-2 in the phosphorylated active form.|PMID:11739604|Moxonidine and clonidine also increased by greater than two-fold the proportion of ERK-1 and ERK-2 in the phosphorylated active form.|PMID:11739604","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:29074416","PMID:19011889","PMID:26704560","PMC3770283","PMC3933766","PMID:11739604","PMC4526467"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:64d09b768c877fb11aca928107c72ccf5342ec6c170db099a58a786db7063c20","tmkp:d6b4f4220fa50776763348440ae4815cb81c60743bc39305ec7b48d4d05f912f","tmkp:8dfbb199155e9cab2096c28b5d15a1cc3b5c3772db7322694c1e8159136e6462","tmkp:b8ba2e44971f027b480e5bc606f054aaa2a8cae636cda8c448789f6055747e54","tmkp:103557400d8d402defebd3cfd7376051f6434c8d731546e75b3fe30a12217d23","tmkp:711a3ef9b2514947620ab3e76610ad1d37bd91243d14130f25bdd44e1736d161","tmkp:0cb60bb281e1a8b49746e0f444a13530c1541d8b072ad70c54d6c4cc057ffaa4","tmkp:72f5f356575f0a59cd9d6da4deba50ceba644bbed9225f7e16247e4625957187","tmkp:27104bc65f670cd77ee2cb68870aea90325d23fa2a8ed5fda3ec7a2a5766dfa3","tmkp:64ed56496a7a3ce0a544d8e44c4d848d3a33fcfd3c90cf602a53a8fd92cade8f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"73172086":{"subject":"PUBCHEM.COMPOUND:2783","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:11720783","PMID:11720783","PMID:10499369","PMID:11720783","PMID:11720783"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In the hippocampus neuroprotection by clenbuterol (0.5 mg/kg) was accompanied by increased TGF-beta1 immunoreactivity as early as 3 h, and remained elevated up to 2 days after ischemia.|PMID:11720783|In parallel with the up-regulation of TGF-beta1 immunoreactivity, LTBP-1 levels in the hippocampus were considerably increased by clenbuterol from 3 h to 2 days after ischemia.|PMID:11720783|The increase in the mRNA level of nerve growth factor (NGF), basic fibroblast growth factor (basic FGF), and transforming growth factor-beta1 (TGF-beta1) mRNA in cortical and hippocampal tissue occurred earlier after middle cerebral artery occlusion and was more pronounced in animals treated with clenbuterol than in controls.|PMID:10499369|In the present study, we demonstrated that intraperitoneal administration of clenbuterol, a lipophilic beta(2)-adrenoceptor agonist, caused an increase in TGF-beta1 expression in non-ischemic rats and further enhanced TGF-beta1 protein levels in rat CA1 pyramidal neurones after transient forebrain ischemia.|PMID:11720783|In the present study, we demonstrated that intraperitoneal administration of clenbuterol, a lipophilic beta(2)-adrenoceptor agonist, caused an increase in TGF-beta1 expression in non-ischemic rats and further enhanced TGF-beta1 protein levels in rat CA1 pyramidal neurones after transient forebrain 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have further reported that air exposure under hypoxic conditions can increase proliferation and inhibit the abnormal epidermal differentiation of corneal limbal epithelial cells through activation of the Notch signaling pathway and inhibition of the p38 MAPK signaling pathway.|PMC4813266|Molecular analysis of pathways involved in cell proliferation and invasion revealed that AIR significantly reduced phosphorylation of ERK1/2 and upregulated cMET expression in A549 cells.|PMID:27096542|There was no significant difference in total p38 MAPK expression in mice treated with CO or room air for 7.5 hours sham conditions or 7.5 hours I/R (Figure 5A).|PMC3315834|Blocking p38 and JNK MAPK also suppressed parasympathetic nerve activity in air exposed animals, suggesting p38 and JNK MAPK contribute to acetylcholine release by airway parasympathetic 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level of VEGF expression in the osteocytes, osteoblasts, and cells of bone matrix and endothelial cells increased first 1 week after and then decreased after the prednisone administration in Group A, and decreased after the prednisone administration in Group B, however, without significant differences between these 2 groups.|PMID:17064544|Conversely, corticosterone, prednisone, and dexamethasone similarly inhibited cell invasion and expression of related genes, including MMP-9, VEGF, and IL-6, in GR-positive lines.|PMID:24880571|With respect to subgroup analyses, comparison between the MTX monotherapy and MTX + prednisone subgroups revealed significant decreases in IL-7, IL-8, IL-10, and VEGF in the latter subgroup post-therapy, but only IL-8 in the former, possibly supporting the role of low-dose corticosteroids in the management of early RA.|PMC4446850|Following prednisone therapy (B), VEGF level was reduced but it was still higher than in the control group.|PMID:16825140|The one 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293(PED) cells, decreased apoptosis induced by anisomycin and H(2)O(2) was also accompanied by block of JNK1/2 and p38 phosphorylations, respectively.|PMID:11790785|To suppress and activate the c-Jun N-terminal kinase (JNK) pathway, SP600125 (SP, 10 μM) and Anisomycin (Ani, 10 μM) (both from Selleck Chemicals, Houston, TX, USA) were used, respectively to treat the cells for ~2 h at room 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induced a moderate increase in Akt activation, which was significantly augmented by PARP inhibition, suggesting that PARP inhibition-induced Akt activation could be responsible for the cytostatic resistance.|PMID:19426673|Paclitaxel appears to activate NF-κB and Akt, which have critical roles in regulating cell survival, proliferation, invasion and metastasis.|PMC3918531|Many nature products could induce autophagy through the inhibition of Akt/mTOR pathway, while paclitaxel has been reported to upregulate Akt pathways to compromise its antitumor activity.|PMC7138813|However, gemcitabine, paclitaxel, or cisplatin treatment enhanced the Akt activation, heterodimer formation of EGFR with HER3, and secretion of amphiregulin, indicating that the presence of gemcitabine promoted the activity of targeted molecules including amphiregulin, Akt, and HER3 for pancreatic cancer therapy.|PMID:20726858|Furthermore, the combination of paclitaxel and AVE1642 resulted in a sequence-dependent increase 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treatment with insulin or ICI222155, an aldose reductase inhibitor (ARI) previously shown to prevent spinal polyol accumulation and formalin-evoked hyperalgesia in diabetic rats, prevented elevated spinal COX-2 protein and activity in diabetic rats.|PMID:17287466|Although hypoglycemic doses of insulin (0.24-7.5 U/kg s.c.) did not significantly change acetic acid-induced writhing in mice, they dose-dependently attenuated formalin-induced nociceptive responses, and their effects were more potent on the second phase (ID50 = .62|PMID:9103512|Study showed that ICV injection of insulin through the activation of central dopaminergic, serotonergic, and opioidergic pathways attenuated specifically the second phase of formalin-induced nociception in non-diabetic mice.|PMC6760484|Some studies showed that ICV injection of insulin reduced nociception in the formalin test which was inhibited by dopamine and serotonin antagonists ( ).|PMC8019850|Insulin attenuates formalin-induced nociceptive 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mellitus.|PMID:9103512","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9942117275","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"113688858":{"subject":"PUBCHEM.COMPOUND:10607","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop","infores:hetionet"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:lincs","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"}]},"66956651":{"subject":"PUBCHEM.COMPOUND:3715","object":"NCBIGene:142","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"degradation"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"dct:description","value":"increases 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inhibition in macrophages prior to treatment with IL-4 resulted in reduced levels of arg-1 and IL-10 protein levels (Figures 2a and 2b).|PMC3141401|After exposure to IL-4 for 24 h, MIF-knockdown RAW264.7 cells had reduced expression of Ym-1, Fizz-1 and Arg-1 compared with that in cells transfected with scramble controls (Figures 3E,G).|PMC8020258|Dietary supplementation of malarial-parasite-infected mice with L-arginine or L-citrulline reduced levels of ileal transcripts encoding interleukin-4 (IL-4), a key mediator of intestinal mastocytosis and macromolecular permeability.|PMID:23690397|To further investigate the function of p38α MAPK in AAM polarization, we challenged BMDMs from p38α MAPKLyz2-KO mice with IL-4, in which p38α MAPK-deficient macrophages displayed a significant reduction in expression of Arg1, Ym-1, Fizz-1, and CCL17 (Figure 1G–J).|PMC6934154|In contrast, IL-4 reduced M2 polarization of these cells from PD-1 deficient mice by decreasing their expression of Arg1 and CD206.|PMC4121443","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"19264061":{"subject":"PUBCHEM.COMPOUND:126941","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In the db(+)/db(+) mice, MTX treatment was associated with a ∼2-fold increase in skeletal muscle GLUT4 protein concentration and a >4-fold increase in GLUT4 mRNA expression (P < 0.01, all), as compared to vehicle-treated mice; no significant differences were noted in controls.|PMID:22778921|In the db(+)/db(+) mice, MTX treatment was associated with a ∼2-fold increase in skeletal muscle GLUT4 protein concentration and a >4-fold increase in GLUT4 mRNA expression (P < 0.01, all), as compared to vehicle-treated mice; no significant differences were noted in controls.|PMID:22778921|In the db +/db + mice, MTX treatment was associated with a ∼2-fold increase in skeletal muscle GLUT4 protein concentration and a >4-fold increase in GLUT4 mRNA expression (P < 0.01, all), as compared to vehicle-treated mice; no significant differences were noted in controls.|PMC3384889|In the db +/db + mice, MTX treatment was associated with a ∼2-fold increase in skeletal muscle GLUT4 protein concentration and a >4-fold increase in GLUT4 mRNA expression (P < 0.01, all), as compared to vehicle-treated mice; no significant differences were noted in controls.|PMC3384889|In db +/db +  MTX-treated mice, there was a ~2-fold increase in total skeletal muscle GLUT-4 protein concentration as compared to those treated with vehicle (P < 0.01), whereas the difference between MTX- and vehicle-treated groups was not significant in controls (db +/+ m).|PMC3384889","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9993151347058823","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:958028ff6d0dc30ef66ec9c54c2b13b955b6eaa7bd278b810c10ab5746edac36","tmkp:00106f9d15c59e95a38ac515ff9c76e3fa74e711a030522266ee5d9a15c28a96","tmkp:7e38863fa52be14e50675718f87a5b56752b7891c67b2eb04b92ab1fd8ca5893","tmkp:d8e69f3bb90e1349eae89686312394729cd92402654eb258096a73c0c6341b80","tmkp:fce98fc601b60b18082b52c4d651e2f3e46085d3ca52f5ee050908af74ee42fa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:22778921","PMID:22778921","PMC3384889","PMC3384889","PMC3384889"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"120461175":{"subject":"PUBCHEM.COMPOUND:3033","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC2939880","PMID:11815376","PMID:21739277","PMID:12826271"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Treatment with diclofenac resulted in nuclear condensation (a morphological change due to apoptosis of NSCs) 24hr after the treatment and activated caspase-3 after 6 hr, indicating that diclofenac may cause apoptosis of neuronal cells via activation of the caspase cascade.|PMID:12826271|Comprehensive protein and gene expression profiling of Diclofenac treated AML cells revealed transcriptional activation of GADD45α and its downstream MAPK/JNK pathway as well as increased protein levels of the caspase-3 precursor.|PMID:21739277|B, Caspase-3 activation in tumor homogenates of 4 untreated and 3 diclofenac treated mice was measured as described in Materials and Methods, one out of two experiments.|PMC2939880|This finding was further supported by an enhanced presence of cleaved caspase 3 in homogenates from tumors excised from diclofenac treated mice (Fig 2B).|PMC2939880","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dcc3bd05070b44db9c2c3104bd54afa43752d7ab5e2e4a4babef38bae0532bf0","tmkp:b884f90b30b2420a157810f9293748f713ef6879c39f6f30b4b7fbd318f41cea","tmkp:f35bb06c59bb1fb6b4f161f88f281abcaba3755e918856bec2b6ddf47c4a3d64","tmkp:9c8cd6c55ef2482be6e6ebf31f01b7661bbd9ab2b5adaa544eefc9f5f4c09dac","tmkp:88712c3c3a9419aa929a313f7316b5ef87ca2d9192d33266588905a5ea711f51"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9989615125","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"50414437":{"subject":"PUBCHEM.COMPOUND:10297","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:23011634","PMID:23011634"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8661925fdab8d3fb575af600ec05b324ba71a1437ceb1c005b6ec841db543fd8","tmkp:64fb4bb6cad6c99d89fae13fa8d9ea0a78e13777b89733b646cd1d302de3a55e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.999503045","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"PPA-treated animals had suppressed airway resistance, eosinophil and lymphocytes infiltration, and IL-4 and IL-17 secretion.|PMID:23011634|Our data suggest the therapeutic mechanism by which PPA effectively treats allergic inflammation on reductions of airway responsiveness, eosinophil infiltration, IL-4 and IL-17 secretion, and improvements of epithelial functions.|PMID:23011634","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"110713437":{"subject":"PUBCHEM.COMPOUND:439501","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999437965","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"A novel observation was the fact that ouabain induced IL-10 and VEGF as well.|PMC4034513|Nevertheless, the levels of IL-10 and VEGF measured in the supernatants of cells cultured for 24 hours in the presence of ouabain were also higher than control levels (Figures 6(c) and 6(e)).|PMC4034513","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC4034513","PMC4034513"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:65e7d780287b9e1f3eacccc49f910a2678c4eb05b56c15496492fd6744654b4e","tmkp:2b74dfbfbebfdf3677cf1738b1081d944218e24e03eb20ba7efb494821dcff91"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"93948257":{"subject":"PUBCHEM.COMPOUND:86287518","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:25205865","PMID:25637316","PMC7435801","PMID:20596610","PMID:26905334","PMC4364779","PMC7666991"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994845928571429","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Immunohistochemical staining of excised tumors revealed that IMD-0560 suppressed VEGF expression, tumor angiogenesis, and cancer cell proliferation.|PMID:26905334|In a xenograft model, the treatment of IMD-0354 significantly inhibited peritoneal dissemination with a marked reduction of intratumoral blood vessel formation followed by the inhibition of VEGF expression from cancer cells.|PMID:25637316|In our study, VEGF levels in lung homogenates and angiogenesis of mice exposed to Dp were decreased by IMD-4690 treatment.|PMC4364779|Systemic administration of IMD-0354 for 6 weeks to week-6 diabetic mice caused significant reduction in the loss of retinal ganglion cells and apoptotic signaling, with preservation of retinal vascular integrity and suppression of retinal VEGF expression.|PMID:25205865|In rat suture-induced CoNV, systemic IMD0354 significantly suppressed CoNV, decreased inflammatory cell infiltration, expression of inflammatory chemokines (CCL2, CXCL5, Cxcr2), and attenuated expression of angiogenic factors (VEGF) and inflammatory mediators (TNF-α).|PMC7435801","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:829db1c9df575a2853b195e156affcd3158ab70db353c0c6d62a31d7a4847158","tmkp:82fa170637e8cf7d99288a180f07e294fe4c6a2502dcf514888ecab7787df759","tmkp:93a13ba56c82fa80da0e9292fc3f0193475fdcd7e86cd16175c626cddf7fa058","tmkp:fb056ed132db44aac3881686fb00a4697bccd32279a9fc109c0ed5cb571a3926","tmkp:6b267f8e685336eb70c4f88b2117da07d4de7b118e7ee1e076528ab47ce28110","tmkp:c643292647e6b11a98349be36e80f7432da8fa06c414882c9c156cce2cc4fc37","tmkp:527bc2ebe3a75144dbeb7abac1c3aa7e4b8e0d90749cd4357f101dca4e8c2df3","tmkp:be6344163a8f3c848600944571a89035b7cb6030dc51be8a355e4b3aebe30748","tmkp:021b231b575bb97bca05f718c7e634e4a64a6803d14b76cae0bceeb722764c00","tmkp:920728203e2a43176c5b8126c9e4b60a5686f3b6f3ca4faa6fe0b52447878f84"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"11028798":{"subject":"PUBCHEM.COMPOUND:2244","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Previous studies have demonstrated the ability of ASA VI to promote the expression of BMP-2 and the activation of p38 and ERK1/2, confirming that its role in promoting osteoblast differentiation is dependent on the BMP-2 pathway.|PMC5069473|The combination of sorafenib and aspirin increases activation of ERK1/2 and the phosphorylation of the AMPK substrate acetyl-coenzyme A carboxylase (ACC).|PMC7352732|The treatment of HMC-1 cells with aspirin for 4 h resulted in a dose-dependent activation of ERK1/2 (Figure 3a).|PMC4686698|Our data demonstrate unequivocally that aspirin activates ERK1/2, supporting the involvement of ERK1/2 in aspirin-mediated IL-4 induction (Figure 3).|PMC4686698|In conclusion, ASA VI may induce osteoblast maturation and differentiation, and then increase bone formation via increasing BMP-2 synthesis, and activating p38 and ERK1/2.|PMID:21452371","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c0fb682b43183076b3c7157ef7b3c1faa123010354face2da23c8214f7289dc3","tmkp:9c95d2ad0dd744a5e15ef61c806b3cd6bdd06a46627b398913c21c7e1df4fe0c","tmkp:e58522389f7ed774dd902fed06dea25c276e60f1d9ddd9344c5e13ab62b918b7","tmkp:55d7b621ad0e56100c196eb0705566b3c68d901a6ce7ae7c453a1bba9062363d","tmkp:51dc8ded03a223d2a56dfa6d3e0b88b84c6b8846d7c321044449815dad4b5fbe","tmkp:bc2fb92b9e95966ab2ec505c18ee9d111f03e1d664fe06fd2f7f1cb280b4f8ca","tmkp:eba12b27b76f3a3e047ed8a8043d87ab82d42d8391f9e50740c4e9bd1244b542","tmkp:f5605e9e6a1faf5df0ec310b6de1534025c4b0673c7767f6eab0887200137cba","tmkp:dde91cd51b2d4bba1238968e15fd7ab0a315f5a18873aa11d7470dd49debe23b","tmkp:24a3ee8a6bb4c96900be2e9c26dc42361a10edfbe755eaf0eef91a012d9b58b0"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9926405384375","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:28055284","PMC7429043","PMC5069473","PMID:29518782","PMC2408682","PMC7352732","PMC7138280","PMID:21452371","PMC4686698"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"34858422":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Here we show that in prolactin-secreting GH4ZR7 cells and primary pituitary cells, dopamine treatment leads to a rapid, pronounced, and specific decrease in activated ERK1/2.|PMID:12121979|Dopamine (DA) prevents impairment of cerebral autoregulation in male and female newborn pigs via inhibition of upregulation of ERK mitogen activated protein kinase (MAPK) after fluid percussion injury (FPI).|PMC5538381|It has been suggested that dopamine diminishes T-cell activation via inhibition of Erk1/2 phosphorylation and reduced nuclear translocation of NFκB or by limiting the expression of the upstream tyrosine kinases Lck and Fyn and induces T-cell quiescence by up-regulating Krüppel-like factor-2 expression.|PMC7773816|Our results provide a novel mechanism for dopamine D2S-induced inhibition of ERK1/2 and indicate that RASA3 links Galphai proteins to inhibit Gq-induced Ras/ERK1/2 activation.|PMID:18952607|Upon siRNA-mediated PDGFRβ suppression, both dopamine (1 μM) and PDGF-BB (10 ng/ml) treatment showed approximately 50% reduction in ERK1/2 phosphorylation compared to 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antiepileptic agents such as phenytoin and valproic acid can aggravate hyperglycemia by inhibiting insulin release or inducing insulin resistance, and seizures can be refractory to antiepileptic drugs in nonketotic hyperglycemia unless the hyperglycemia is properly controlled.|PMC7541982|In group III (VPA exposed rats), the percentage of insulin-positive cells was significantly decreased, and the percentage of glucagon positive cells was significantly increased in comparison to control groups (p < 0.001).|PMC7564314|VPA treatment significantly reduces glucose-stimulated insulin secretion in|PMC6719693|Consequently, a reduction of glucose-stimulated insulin secretion is observed following VPA exposure.|PMID:30145684|The results showed that at the age of 32 weeks, the offspring of pregnant rats administered with 250 mg VPA on days 10, 13, and 16 of pregnancy had higher serum glucose concentrations and lower serum insulin concentrations, followed by decreased concentrations of RNA, and 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with this result, in present study, lower mRNA and mature protein expressions of HMGCR and SREBP-2 were observed in FO+ALA-PS group but not in FO group.|PMC4477243|Transcriptome analysis of hPSCs derived hemogenic endothelial cells showed that ALA promoted endothelial‐to‐hematopoietic transition by up‐regulating RUNX1, GFI1, GFI1B, MEIS2, and HIF1A and down‐regulating SOX17, TGFB1, TGFB2, TGFB3, TGFBR1, and 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milk levels of VEGF, IGF-I and b-FGF were significantly higher (p<0.001).|PMID:20202860|We found that bLF purified from milk increased the mRNA expression of vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF2) in murine osteoblast-like MC3T3-E1 cells and primary murine osteoblasts in a time- and dose-dependent manner.|PMID:21404021|We found that bLF purified from milk increased the mRNA expression of vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF2) in murine osteoblast-like MC3T3-E1 cells and primary murine osteoblasts in a time- and dose-dependent manner.|PMID:21404021|Bovine milk lactoferrin induces synthesis of the angiogenic factors VEGF and FGF2 in osteoblasts via the p44/p42 MAP kinase pathway.|PMID:21404021|Bovine milk lactoferrin induces synthesis of the angiogenic factors VEGF and FGF2 in osteoblasts via the p44/p42 MAP kinase pathway|PMC3692204","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"107558130":{"subject":"PUBCHEM.COMPOUND:3016","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3230766","PMC7039622"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Specifically, treatment with the BDZ drug diazepam has been shown to increase the levels of ERK1/2 in the rat hippocampus, and the administration of the SSRI fluoxetine similarly enhances ERK1/2 signaling across different brain regions, including the hippocampus; brain circuitry that is activated during both stress and anxiety 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protein expressions of Bcl-2, Bax, Caspase-8, Caspase-9 and Caspase-3 were significantly increased in response to Bosentan treatment after IR.|PMID:24276417|Comparing with the control group, expression of caspase-3 was prominently enhanced in CSE groups, but both BQ123 and bosentan treatments markedly inhabited the increases of the cleaved caspase-3 protein levels in rats injected with CSE.|PMID:20646409|Bosentan's effects on migration are not attributable to increased cell death, as assessed by activated Caspase-3 immunostaining (Fig. 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has been linked to the pericentromeric region of chromosome 16, PNKD is associated with mutations in the myofibrillogenesis regulator 1 (MR-1) gene on the long arm of chromosome 2 (2q32-36 locus), and PED is associated with mutations in the glucose transporter gene, GLUT1, responsible for glucose transport across the blood-brain barrier.|PMID:19364451","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:589ec1b01e506a03804a6d33dc8244a8f9f12abb48879afd579ea14d45bffb43"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9979329","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:19364451"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"22746209":{"subject":"PUBCHEM.COMPOUND:443894","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:01e3286e6b0e575ea4e7e172ac2e234051d1cb0b8e9bf7c30263d4f034d28905","tmkp:2b1e01e0c7006c79656ae15b1d3946e09093e3aa262eed992c74359fe5820dbb","tmkp:df681ff097a651c4b9a3be3150f2a2ec15532abf2d4fea9737867d0867324fbf"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7007354","PMC7007354","PMC7007354"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9947236833333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"However, OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|However, OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|VEGF protein levels were unaffected in Caki-1 cells treated for 16h with dDAVP, but were significantly reduced by Tolvaptan and OPC31260 (Fig-5G).|PMC7007354","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"72758411":{"subject":"UMLS:C5242471","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"After blocking membranes with 5% skimmed milk for 1 h, primary antibodies against ITGA9, Ras-related C3 botulinum toxin substrate 1 (Rac1), Ras homolog family member A (RhoA), cell division control protein 42 homolog (CDC42), collagen type 1, fibronectin, cyclin-dependent kinase 2 (CDK2), cyclin E, cyclin-dependent kinase 4 (CDK4), cyclin D1, B-cell lymphoma 2 (BCL2), Bcl-2-associated X protein (BAX), cleaved caspase-3, cleaved poly (ADP-ribose) polymerase 1 (cleaved PARP1), α-tubulin and β-actin, were incubated overnight at 4 °C.|PMC7432329|Membranes were incubated overnight at 4°C with the following primary antibodies diluted in blocking solution (5% milk/PBST): Catalase, Mfn-2, MnSOD, Nrf-1, UCP-2, UCP-3, VDAC-1/Porin (Abcam); Bcl-2 (BD Transduction Laboratories); Phospho-AMPKα (Thr172), AMPKα, Cytochrome C, Phospho-p38 (Thr180/Tyr182), p38, SIRT3 (Cell Signaling); Fis1 (Enzo Life Sciences); tFAM (GenWay Biotech); ATP Synthase (Invitrogen); SIRT1 (Millipore); PGC-1α (Millipore and Novus Biologicals); Nrf-2 (R&D Systems); GAPDH, GLUT4, Mfn-1 (Santa Cruz).|PMC3706566|After blocking with 5% milk in TBST for 4 h at room temperature, the rat monoclonal antibodies specific for rat Opa1 (A9833, ABclonal, USA), Mfn1 (A9880, ABclonal, USA), Mfn2 (A5750, ABclonal, USA), Drp1 (A2586, ABclonal, USA) and Fis1 (GTX111010, GeneTex, USA) and alpha Tubulin (GTX628802, GeneTex, USA) were incubated at a concentration of 1: 500 (for Opa1, Mfn1, Drp1), or 1: 1000 (for Mfn2, Fis1, and Tubulin) in 1×TBST overnight at 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proinflammatory and proangiogenic factors, including G-CSF, stroma-derived factor (SDF), TGF-β, tumor necrosis factor (TNF)-α, VEGF, IL-1β, and IL-6 were found to be increased in sorafenib-treated mouse orthotopic liver tumors.|PMC6511249|Increases in serum VEGF have been noted in patients treated with sorafenib in phase II and III trials.|PMC6626665|In the sorafenib cohort, VEGF levels increased, whereas sVEGFR-2 and TIMP-1 levels decreased.|PMC3461173|During sorafenib treatment alone, there was a significant increase in plasma VEGF, PlGF, VEGF-D, sMET and TNF-α (at days 3 and 15), and sVEGFR1, CAIX and the fraction of CD8+ T cells (at day 15) and decrease in plasma sVEGFR2 and the fraction of CD56Dim NK cells (at day 3) and plasma sVEGFR2 and s-c-KIT (at day 15) compared to baseline (all p<0.05,|PMC6320284|In addition, sorafenib demonstrated significant activity against several receptor tyrosine kinases involved in neovascularization and tumor progression, including vascular-endothelial growth factor (VEGFR)-2, VEGFR-3, platelet-derived growth factor (PDGFR)-beta Flt-3, and c-KIT.|PMID:16474853","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"123917388":{"subject":"PUBCHEM.COMPOUND:54729367","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9976009914583334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In the 1205 Lu TetR siGRM1-9 derived tumors, treatment with doxycycline led to a statistically significant increase in cells positive for cleaved Caspase-3 over the no treated controls with p<0.05 (Figure 6D, left panel).|PMC3501593|It also showed increased caspase 3 transcripts in HT 29 cells treated with doxycycline compared to control (p = 0.21).|PMC2628910|The results revealed increased caspase 3 gene expressions and activities in HT 29 cells treated with cisplatin, oxaliplatin and doxycycline; however the combination of doxycycline with cisplatin and oxaliplatin did not report increased caspase 3 gene expressions and activity compared to cisplatin and oxaliplatin alone.|PMC2628910|RT-PCR and western blot assays proved that apoptosis induction effect of doxycycline was achieved via inducing the expression of caspase-3 and bax, as well as attenuating the expression of survivin and bcl-2.|PMID:26846275|The relative activity of caspase-3 was significantly increased when cells were treated with the PVT1 shRNA induced by 1 ug/ml doxycycline (P < 0.01 in two cell lines) (Figure 5C and 5D).|PMC4747399","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC2753283","PMC2628910","PMC3501593","PMC2958174","PMC3386503","PMID:26846275","PMC4134396","PMC4747399"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2142c54513d940e7a2387e4c81cd10f00341a6cdf656cd60803172d42960ed9f","tmkp:16c98f018a45d196d895a7a55e6c2427b3ae1b36584ed54933b951c769ea3862","tmkp:b4c6644bddeb4b6dcda8d22ef68b783d00bafb52d98c06651685ea6b8ceeb5ba","tmkp:a0c157587a906940d26a4f0a154071cc4f3f60ac231f50b6db7d1f44c0bc077f","tmkp:7b78c4e96f610e0e11a88f7a33a2b371ee2bee22f146289f8b257c48e98f1295","tmkp:91ddb9d963f37d3590ecac3e2481e6125d1dfb5937ae1b2b6aaadb359798e44d","tmkp:fe4ffe3cfc54de24c638ea00f0921809236fdaf6782d305df37a4b2d89746a5c","tmkp:f24ba4d2e97ef5ad783134f86b174c5a4bc482f605ad1068d03a07f688b779bf","tmkp:f5a143757495043540f69ed51a36e8b68893beab9fcc366a99ea95f4a3c62583","tmkp:cefe461ae31ad70de4583f15ba2ec3a1084fa3d797178bef710384c10ee7b3d3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"21210104":{"subject":"PUBCHEM.COMPOUND:6957673","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:28863286"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:06b99d34e1c00493ce73f475af94dded4abcfc34579f6566447fcd122d0962ae"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.99375594","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"More prospective studies are needed to compare the efficacy of different APT agents and reach conclusions regarding use of PFT and platelet reaction values in order to decrease hemorrhagic and thromboembolic complications associated with the PED.|PMID:28863286","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"77031383":{"subject":"PUBCHEM.COMPOUND:10607","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Treatment with PPT showed no significant effect on PDGF-induced proliferation, whereas WAY interestingly suppressed proliferation via inhibition of ERK1/2, Akt, and p38 signaling.|PMC6120801|Estradiol's or PPT's inhibition of the fluvoxamine-induced slowing of 5-HT clearance mediated by ERα, was blocked after inhibition of either MAPK/ERK1/2 or PI3K/Akt signaling pathways.|PMID:24423185|It was found that P-A (0.5 μM) and PPT (0.05 μM) significantly suppressed the phosphorylations of ERK1/2 and AKT in MKN-45 and BGC-823 cells, respectively, and they did not alter the phosphorylation of STAT3 and mTOR.|PMC6154554|However, both PPT and DPN significantly (p < 0.05) increased Akt (Fig. 7A), but only PPT decreased ERK1/2 (Fig. 7B) phosphorylation, and these effects were reversed by ethanol (Figs.|PMC5272804|Estradiol’s or PPT’s inhibition of the fluvoxamine-induced slowing of 5-HT clearance mediated by ERα was blocked after inhibition of either MAPK/ERK1/2 or PI3K/Akt signaling 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anti-inflammatory effects of arginine and glutamine were associated with decreased activation levels of signaling molecules known to be involved in mast cell cytokine expression such as MAPK family members extracellular signal-regulated kinase, c-Jun N-terminal kinase, and p38, and the protein kinase B (Akt).|PMID:22527286|Representative of n=3 replicates D) Treatment of SKNAS neuroblastoma cells with recombinant cytokines leads to upregulation of ARG2, which is inhibited by ERK1/2 and p38 inhibition.|PMC6420118|RESULTS Our results demonstrated that L-Arg significantly activated PKG II and effectively ameliorated xenograft tumor development through inhibiting cancer growth, angiogenesis, and metastasis, which was partially dependent on blocking of epidermal growth factor receptor (EGFR) activity, as well as downstream signaling pathways such as Erk1/2.|PMID:29401205|The NO synthase inhibitor Nomega-monomethyl-L-arginine, as well as the guanylate cyclase inhibitor 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results indicated that the expression of p-Akt was obviously enhanced and that of caspase-9 significantly decreased in the group treated with CBZ and SXC together, which might have inhibited the apoptosis of neuronal cells.|PMC6366425|Simultaneously, p-Akt expression was obviously enhanced in the combined group compared with the CBZ group (p < 0.01).|PMC6366425|Carbamazepine Alleviates Retinal and Optic Nerve Neural Degeneration in Diabetic Mice via Nerve Growth Factor-Induced PI3K/Akt/mTOR Activation.|PMID:31736682|In addition, our results showed that the carbamazepine treatment promoted adipocyte differentiation, and increased the levels of insulin signaling proteins, such as Akt, insulin receptor (IR), insulin receptor substrate 1 (IRS1), and glucose transporter type 4 (Glut4) during differentiation (Figure S3A).|PMC6912407|PHx surgery induced the expression of several cyclins and activated Akt/mTOR signalling pathways, all of which were enhanced by CBZ 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found this for erythrocyte GLUT1 during my PhD studies and much later after I moved to Bath, when Bill Rees looked at the same side-specific inhibitors for adipocyte GLUT4.|PMC6243331|The same treatments also decreased the glycosylated fraction of GLUT4-eGFP fusion protein associated with the vesicles, further suggesting that in glioblastoma cells PARP1 has a role in GLUT/SLC2As trafficking.|PMC7290719|On the other hand, while some members of the flavonoid family were reported to stimulate the expression of Slc2A4 gene and glucose transport, other phytochemicals of the same family were identified as inhibitors of glucose transport mediated by GLUT1 and/or GLUT4.|PMC8073144|And at the same time, downregulation of GLUT4 expression leads to lower insulin-dependent glucose uptake in the adipocytes.|PMC6127149|There was some variability in the protein levels between the samples within the same feeding group (Fig. 4C), but quantification demonstrated that GLUT1 and GLUT4 proteins were reduced by ~50 and 30% respectively after 14 days of HFD compared to chow (Fig. 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in BALB/c mice fed a high-fat, high-sugar diet, only low-dose ALA supplementation (150 mg/kg vs. 300 mg/kg) was protective against TNBS-colitis resulting in significantly lower colonic IL-1, IFNγ, IL-4 and IL-2 cytokine production.|PMC7884479|④ ALA could suppress production of interferon-γ (IFN-γ) and interleukin -4 (IL-4).|PMC6446120|④ ALA could suppress production of interferon-γ (IFN-γ) and interleukin -4 (IL-4).|PMC6446120|ALA could ameliorate the impaired mitochondrial function of CD4+T cells of acquired immunodeficiency syndrome (AIDS) patients, downregulate the expression of CD4 molecules of human peripheral blood T cells, inhibit nuclear factor kappa B (NF-κB) activation induced by tumor necrosis factor-alpha (TNF) in Jurkat T cells (Figure 1, ③), suppress production of interferon-γ (IFN-γ) and interleukin-4 (IL-4) (Figure 1, ④) by CD4+T cells to reduce the severity of atopic dermatitis lesions in mice model, and induce lymphocyte progression from G0/G1 to S phase (Figure 1, ⑤), which might be related to restore the function of immune system in advanced cancer patients.|PMC6446120|A marked decrease in inflammatory markers (INF-γ, TGF-β, ICAM-1, and IL-4) was observed in ALA-treated animals in a study published by Khalili et 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also led to an increase of the active form of caspase-3 and reduced the intracellular concentrations of AKT and ERK1/2 in NALM-6 cells.|PMC3255249|PFT induces apoptosis in HL60/AR cells associated with activation of caspase 3, decreased expression of Bcl-2 and decrease in the polarization of MMP.|PMC3928472|Determination of caspase-3 activation revealed a dose-dependent increase of the cleaved, active form of caspase-3 in NALM-6 cells after treatment with 3, 4 and 5 μ PFT-μ for 24 h (Figure 2c).|PMC3255249|Cell cycle arrest, apoptosis and caspase-3 activation induced by PFT-μ in NALM-6 and KG-1a cells.|PMC3255249|In the present study, pre-treated HepG2 cells with PFT-α and SIN co-treatment resulted in upregulation of p62, cleaved PARP, and cleaved caspase-3 proteins and further downregulation of p-AMPK and LC3B-II expression as compared with only SIN 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bosentan induced a marked increase in vessel density at 3 and 28 days (1.4-fold and 1.7-fold, respectively, compared with no treatment; P<0.05), which was associated with an increase in VEGF and endothelial NO synthase levels in ischemic legs (by 31+/-8% and 45+/-23%, respectively, at 3 days and by 65+/-13% and 55+/-15%, respectively, at 28 days; P<0.05 versus nontreated rats).|PMID:11597932","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"28848551":{"subject":"PUBCHEM.COMPOUND:22833565","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9959169259999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a1d617d1923a8cfdf9e6788106943a7eb8dc4d9ed345c09bfb2b57547249fb82","tmkp:fbab5cf1f4806174de0aa626286358f78877ab63a174d216ccc9e6636c424053","tmkp:a4f04324d117d311f3e78e83d7a62a94bf8b7bd031f609520a626bca43bd3981","tmkp:f7752bda879d16e0d8068a68f0594240180dc79decc502d21ecc48360756846c","tmkp:43ea803a3026a1e28132820e8bf2f30157dfdfef79edf8572a676de149351892","tmkp:232626400399a9667b8df815550d76835e78dab20710564cdbe87446b74cdd11","tmkp:90871fff1d5c90fe9bb74b1bd9650a2d93c11ca0bf6f4b3bc11e32227fa80ed1","tmkp:93755fd64c5441c43271c588d4fa69e9ac69be37b7fd3bab017ca7827e5621e2","tmkp:8e8c196e852b19d5d1608d62c6fdc41251b69c36a6a3c1b54d482699b2dc848a","tmkp:d2a5c8b9368b1551033d7f5012e55aa0bc4830b26e491a4b20e27f98c7ed440a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"In villous trophoblast, heparin increased Bcl-2 and cytokeratin 18 protein expression.|PMID:15671997|Heparin and ADM appear to interact in a synergistic manner, which may be related to the over-expression of p53 and p21 mRNA and the elevated ratio of Bax/Bcl-2 mRNA.|PMID:11866879|In parallel with the data obtained from western blotting analysis, our PCR results also showed that, although the ratio of Bax/Bcl-2 gene expression was dramatically increased in the cells of the histone group, the ratio decreased in samples from the heparin intervention group.|PMC7738632|Western blot analysis showed that levels of bcl-2, bax and c-myc were significantly overexpressed by treatment with the increase of heparin concentrations.|PMID:11787776|Consistent with the data obtained from western blotting analysis, our PCR results also showed that, although the ratio of Bax/Bcl-2 gene expression was dramatically increased in mice of the sepsis group, the ratio decreased in samples from the heparin intervention 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to \"Amiodarone induces cell proliferation and myofibroblast differentiation via ERK1/2 and p38 MAPK signaling in fibroblasts\" 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observed significantly higher mRNA levels for VEGF (1.73-fold), FGF-2 (5.6-fold) and TGFbeta receptor III (2.93-fold), PDGF receptor alpha (2.93-fold) and receptor beta (2.91-fold) in rats receiving indomethacin compared to rats given placebo (p < 0.05).|PMID:17440234|Indomethacin, a nonsteroidal anti-inflammatory drug (NSAID) with PPARγ activity, up-regulated VEGF expression, but acetylsalicylic acid, a NSAID without PPARγ activity, did not.|PMID:23542713|Infusion of fetal lambs with indomethacin for 48 hours constricted the DA and increased the thickness of the avascular zone of the DA, which in turn induced the expression of vascular endothelial growth factor, endothelial nitric oxide synthase (due to ingrowth of vasa vasorum), neointima formation, and loss of smooth muscle cells; moderate degrees of DA constriction in utero increased NO production, which inhibited DA contractility.|PMID:11282914|In addition, to determine the possible mechanism of the effect of E-cadherin on the PC invasion and metastasis, we found that the protein levels of metastasis-related factors (MMP-2, MMP-9, VEGF), which were increased in PC cells after Si-E-cad and treatment with indometacin 100 mg/L for 48 h.|PMC4085328|Indomethacin also increases the thickness of the avascular zone by causing constriction of circumferential and longitudinal muscle, decreasing blood flow in the vasa vasorum, and causing vessel wall hypoxia with release of vascular endothelial cell growth factor (VEGF).|PMC3232537","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9913440175","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"81095923":{"subject":"PUBCHEM.COMPOUND:6274","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The activation of PARP-1 follows his binding to the DNA strand breaks and enables PARP-1 to synthetize poly(ADP-ribose) (PAR) and also to increase its own 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of tears in the retinal pigment epithelium (RIP) has been described as a possible complication following anti-vascular endothelial growth factor (VEGF) antibody therapy with substances which have been available for years when treating pigment epithelium detachment (PED) in eyes affected by age-related macular degeneration (AMD).|PMID:24062151|Atrophy may complicate eyes with PED and nAMD after anti-VEGF therapy, especially in association with complete PED resolution.|PMID:29697591|Development of tears in the retinal pigment epithelium (RIP) has been described as a possible complication following anti-vascular endothelial growth factor (VEGF) antibody therapy with substances which have been available for years when treating pigment epithelium detachment (PED) in eyes affected by age-related macular degeneration (AMD).|PMID:24062151|RPE tears may develop during the course of anti-VEGF therapy for age-related macular degeneration-related PED.|PMID:17558312|Atrophy may complicate eyes with PED and nAMD after anti-VEGF therapy, especially in association with complete PED 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PCV showed reduced stress responses (decrease in cortisol levels and increase in insulin levels), and even improved right ventricular function.|PMC6646045|Basal acid output and the insulin-stimulated acid secretion were significantly increased from 1 month to 1 year after PCV, while there was no such increase after SV + P.|PMID:364625","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:20b379597549566e887e62e26c87e3c1bc103aa6e80baaff6297f9ab9429480d","tmkp:c43cdc9748ce21cf3d58ee41282858bd5a2cc9d3b4d8691c1cdc26cff161d951"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC6646045","PMID:364625"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.998858085","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"113255387":{"subject":"PUBCHEM.COMPOUND:5073","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9936655971428571","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Additionally, the increase in lean mass may be due to increases in insulin-like growth factor 1 and Akt, both of which are increased by risperidone.|PMC3657586|IL-6 levels significantly increased the risperidone-induced expression of AKT1, DICER1, DROSHA, and COMT mRNA.|PMID:26491028|Similarly AA such as clozapine, olanzapine, risperidone, quetiapine, and ziprasidone, have been shown to activate Akt or mimic its activity by increasing GSK3α and GSK3β phosphorylation in the striatum, cortex, and hippocampus (Alimohamad et al.,; Li et al.,; Beaulieu et al.,).|PMC3167352|Furthermore, it has been shown that atypical antipsychotics clozapine, olanzapine, quetiapine, risperidone, and ziprasidone can either activate Akt or mimic its activity by increasing phosphorylation of GSK3α and GSK3β (Alimohamad et al.,; Li et al.,).|PMC3206544|Risperidone can activate the Akt-GSK3β signaling pathway in the U251 cells, and PI3K is a common regulatory site in Akt-GSK3β signaling and D2 receptor gene 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results of our present study indicate that the synergistic overexpression of c-Myc and bcl-2 oncoprotein may be related to the pathogenesis of gingival hyperplasia induced by nifedipine and phenytoin, especially to the morphogenesis of hyperplastic 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oxygenase-1; IκBα: inhibitory κBα; iNOS: inducible nitric oxide synthase; IL-1β: interleukin 1β; IL-6: interleukin 6; IL-10: interleukin 10; JNK: c-Jun N-terminal kinase; Keap-1: Kelch ECH-associated protein-1; LPS: lipopolysaccharide; MAPK: mitogen-activated protein kinase; MTT: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetrazoliumbromide; NF-κB: nuclear factor-κB; NO: nitric oxide; NQO-1: NAD(P)H quinone dehydrogenase-1; Nrf2: nuclear factor erythroid 2-related factor 2; PCR: polymerase chain reaction; PG: prostaglandins; PGE2: prostaglandin E2; P/S: solution of penicillin and streptomycin used for cell culture; ROS: reactive oxygen species; RT-PCR: reverse transcription PCR; TNF-α: tumor necrosis 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edema associated with clozapine use|PMC6964462|Pedal edema associated with clozapine use|PMC4904752|Pedal edema associated with clozapine 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Ang Il-induced GLUT1 expression was significantly inhibited by the EGF-R inhibitor AG1478 (approximately 80% inhibition), by inactivation of ERK by PD98059, and by pretreatment with heparin and the metalloproteinase (MMP) inhibitor 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addition, given the excellent PAI efficacy of DSPE-PEG-Bi NPs in vitro, the capability of DSPE-PEG-Bi NPs for PAI enhancement in vivo was further 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the case of MTX, the caspase-3 inhibitor had no protective effect on undifferentiated SH-5YSY cells, although MTX was shown to activate caspase-3 in H9c2 cells.|PMC6027466|Caspase-3 and 8-OHdG expression was mild in hepatocytes in the CAS+MTX group and Caspase-3 expression in the MYR+MTX group was less.|PMC6312684|Mtx + quercetin group revealed significantly lower histopathological damage and APOI and caspase-3 expression decreased when compared to Mtx group.|PMID:27005763|Mtx + quercetin group revealed significantly lower histopathological damage and APOI and caspase-3 expression decreased when compared to Mtx group.|PMID:27005763|A significant decrease in enterocyte apoptosis in ileum of MTX-PMG rats (vs MTX) was associated with a decrease in caspase 3 protein expression as well as increased cell proliferation, which was correlated with elevated p-ERK protein 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GED patients were prescribed antibiotics (41% versus 27%, P = 0.002), while more PED patients were treated with oseltamivir (6.7% versus 0.4%, P < 0.001).|PMID:24982807|More GED patients were prescribed antibiotics (41% versus 27%, P = 0.002), while more PED patients were treated with oseltamivir (6.7% versus 0.4%, P < 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mineralization in dexamethasone or vitamin D3-induced ASCs correlated with both increased ERK1/2 and JNK1/2 activation.|PMC6200338|These suggest that dexamethasone-induced JNK1/2 and p38 MAPK activation are not crucial to the induction of apoptosis.|PMID:11012613","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC3242752","PMID:9794429","PMID:28871941","PMC6200338","PMID:31629215","PMID:11012613"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.998869375","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"31682284":{"subject":"PUBCHEM.COMPOUND:4943","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9838244625","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Similarly, serum level of VEGF also increased in mice treated with sevoflurane compared to propofol with statistical significance obtained at one day after surgery (p = 0.03, two-way ANOVA + Dunnett’s post hoc tests).|PMC6994546|It was noteworthy that the ERK activator (phorbol 12-myristate 13-acetate [PMA]) treatment increased the MMP-9/VEGF levels after propofol treatment, and led to significant increase of proliferation, invasion and angiogenesis.|PMID:24089228|The expression of HIF‐1α and VEGF was increased by hypoxia and was alleviated by propofol.|PMC6515893|The expression of HIF-1α and VEGF was increased by hypoxia and was alleviated by 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reduces MMP-9 expression by inhibiting IL-17-stimulated ERK1/2 activation in C2C12 cells.|PMC5155103|Interestingly, in the same model when compared to losartan, doxycycline was able to both inhibit MMP-2, limiting latent TGF-β release, as well as prevent the phosphorylation of ERK1/2.|PMC4912448|Pretreatment of macrophages with 10 µM doxycycline prior to A. actinomycetemcomitans LPS stimulation resulted in a marked decrease in the phosphorylation of extracellular signal-regulated kinase 1/2 (- 76%).|PMC3282276|SB202190, PD98059 and doxycycline markedly suppressed the levels of p-JNK-1/p-JNK-2 and/or p-ERK1/p-ERK2, as well as IL-1beta, TNF-alpha and IL-8 mRNAs and proteins stimulated by hyperosmolar media.|PMID:16202406|Pretreatment of macrophages with 10 microM doxycycline prior to A. actinomycetemcomitans LPS stimulation resulted in a marked decrease in the phosphorylation of extracellular signal-regulated kinase (ERK) 1/2 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, 8 Recently, certain quinone compounds (such as mitomycin C, E09, RH1 and β‐lapachone) have been shown to be cancer‐specific drugs in tumors with high‐NQO1, 6 , 7 , 8 , 9 and have provided greater efficiency of treatment when combined with other drugs, such as PARP1 inhibitors.|PMC7894015|As expected, UAF1 depletion led to hypersensitivity of cells to MMC and olaparib, the latter being an inhibitor of polyADP-ribose polymerase 1 (PARP1) (Fig. 4b).|PMC6599204|Next, we tested whether the difference in HR capacity is reflected by sensitivity to PARP1 inhibition by olaparib or MMC treatment in the colony formation assay. Figure 2F shows cellular survival after increasing concentrations of olaparib (left) and MMC (right) for the four cell lines studied.|PMC7017274|Similar to bleomycin treatment, the parp1-2 and parp2-1 mutants exhibited moderately or markedly increased sensitivity to mitomycin C, respectively (Fig 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μg/mL).|PMC3428247","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"59299065":{"subject":"UNII:15C2VL427D","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4954942","PMC5454820","PMID:27314606","PMC4211604","PMC5207393","PMC7027529","PMID:25458604","PMC6893275"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:99799e52e74aa4dce9eeefb58b6c96fd73f95d846fe3add3f7b60e083e9fe371","tmkp:1e336bed7ab31cd2db5017e91b941567f696d1113387ee3f63c07a2a02f4afe3","tmkp:0d69e08ec030aa34e5e32976309ba78b5ef9ba8be4dbcc571d36532d6d6da598","tmkp:e0ebc1c7ac20385cd3c232541da3a41d1bda8848a047093e3197f6b2ce89ade8","tmkp:eca300ded82ba3ae153c396f049eadaccfc2a90d6be990dc1e48e0b314efa31c","tmkp:cfcd6db15168078dfc9b4c7ee2e0c1697e9a0c7ba6c20424f9c8f06565b062a8","tmkp:7ed6324f6f5762c8b7a8b071a14b068b1a75c0147b1e05513be7dcc3dc0c6781","tmkp:11d1a829679c0af27bf975c6def89c5d7739fa28e162a5982e51f2d7513c355d","tmkp:ef162d8226d9749f4fa08ab233523db3d3e868fa814c05cce1186f65099f72e6","tmkp:e9751b84f867295ae9afcfd11c07ab1d4d84298cdb99fe4124caa39bbafdffa9"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99867736","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Real-time PCR analysis showed that treatment with 25 mg/kg BW aflibercept significantly upregulated the expression of fibroblast growth factor-2 (FGF-2), PlGF, VEGF, PDGF-BB, and transforming growth factor (TGF)–β mRNAs.|PMC4954942|Given the importance of the pro-angiogenic pathway downstream of VEGF, inhibiting the VEGF signaling axis has proven an effective therapy for patients with solid tumors and neovascular age-related macular degeneration; drugs such as bevacizumab and aflibercept which sequester circulating VEGF have shown efficacy in some of these clinical situations.|PMC5207393|In tumor tissues of Hepa1-6 cells, aflibercept significantly suppressed the phosphorylation of VEGFR-1 and -2 and upregulated the expression of HIF1-α, VEGF, and PlGF (Figure 4, A and B).|PMC4954942|Our results also showed that aflibercept upregulated HIF1-α expression in tumor tissues, in addition to the expression of VEGF, PlGF, FGF-2, PDGF-BB, and TGF-α.|PMC4954942|Thus, the proposed dose escalation of 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for glucose transporter type 1 deficiency (G1D): Modulation of human ictogenesis, cerebral metabolic rate, and cognitive indices by a food supplement|PMC5796071|Fanny Mochel holds a patent on the use of triheptanoin in Huntington disease and GLUT1 deficiency syndrome.|PMC5625655|Triheptanoin: Orphan Drug designation for treatment of glucose transporter type-1 deficiency syndrome.|PMC7575481|Triheptanoin: orphan designation for the treatment of glucose transporter type-1 deficiency syndrome.|PMC7575481|Long-term follow-up in an open-label trial of triheptanoin in GLUT1 deficiency syndrome: a sustained dramatic 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heparin treatment markedly inhibited the mesangial matrix expansion for a variety of ECM proteins, including laminin, type I and IV collagen, fibronectin and entactin.|PMID:8441232|Heparin has been shown to inhibit GBM cell-attachment to laminin and fibronectin, two ECM proteins.|PMC4582077|Heparin could obviously reduce HSC growth, inhibit the synthesis of type I procollagen and fibronectin protein, and the gene expressions of type I procollagen, fibronectin and MT-MMP.|PMID:10951616|Northern blot analysis also showed that interleukin-1 antisense decreased the expression of matrix genes such as type I collagen, fibronectin, and decorin similar to downregulation after heparin/endothelial cell growth supplement treatment.|PMID:10614876|Heparin could obviously reduce HSC growth, inhibit the synthesis of type I procollagen and fibronectin protein, and the gene expressions of type I procollagen, fibronectin and 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molecular markers of senescence, including pATM, pCHK2, p53, p21, ApoJ, fibronectin, γ-H2AX, SA β-Gal, collagenase, and MMP9.|PMC6018655|Finally, treatment of lung alveolar epithelial cells (A549) with ouabain also resulted in the downregulation of TGFβR2, the inhibition of TGF-β-induced Smad phosphorylation and of the expression of mesenchymal markers, vimentin and 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acid targets CD44 and inhibits FcϵRI signaling involving PKCδ, Rac1, ROS, and MAPK to exert anti-allergic effect |PMC7397973|Hyaluronic acid targets CD44 and inhibits FcRI signaling involving PKC, Rac1, ROS, and MAPK to exert anti-allergic effect|PMC5200957|Hyaluronic acid targets CD44 and inhibits FcepsilonRI signaling involving PKCdelta, Rac1, ROS, and MAPK to exert antiallergic effect|PMC2784008|Hyaluronic acid targets CD44 and inhibits FcepsilonRI signaling involving PKCdelta, Rac1, ROS, and MAPK to exert anti-allergic effect|PMC4205896|Hyaluronic acid targets CD44 and inhibits FcepsilonRI signaling involving PKCdelta, Rac1, ROS, and MAPK to exert anti-allergic 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beta-GPA in combination with clenbuterol enabled training to elevate GLUT4 protein concentration and citrate synthase activity, with the increase in GLUT4 being greater than that observed for the TR animals.|PMID:10072100|Clenbuterol treatment did, however, increase citrate synthase activity and GLUT-4 protein in soleus.|PMID:7559215|The increase in muscle glucose uptake could not be ascribed to an increase in the glucose transport protein GLUT-4 in clenbuterol-treated rats.|PMID:11254461|Providing beta-GPA in combination with clenbuterol enabled training to elevate GLUT4 protein concentration and citrate synthase activity, with the increase in GLUT4 being greater than that observed for the TR 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to other protein misfolding diseases, the majority of CLC5 mutants studied to date cause decreased expression of the mature protein, rapid degradation by the proteasome, mislocalization and reduced or abolished Cl− conductance.|PMC7812281","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"68609638":{"subject":"UNII:ZL1R02VT79","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5348182","PMC4648717","PMID:22283373","PMC7127926","PMC8069662","PMID:27106625","PMC5732636","PMC2701130","PMC7391612"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9857806378947369","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In another larger trial assessing plasma VEGF in patients with treated with anti-VEGF therapy (bevacizumab, ranibizumab, and aflibercept) for DME found that the median plasma VEGF concentration increased by +0.20 pg/ml (IQR −5.00 to +4.90) 4 weeks after the first injection of ranibizumab.|PMC7127926|In contrast to MacTel 1, macular edema caused by vein occlusions respond favorably to bevacizumab, ranibizumab, or aflibercept therapy, which may be linked to the relative elevation of both VEGF-A and PlGF in the ocular media of these patients.|PMC5732636|After two intravitreal ranibizumab injections, reductions in the levels of circulating cytokines IL-1β, IL-13, G-CSF, IFN-γ, IP-10, MIP-1α, and TNF-α were measured, with increased levels recorded for IL-9, MIP-1b, VEGF, and sVEGFR-1, after correcting for the multiple comparisons.|PMC7127926|A recent study showed that in vitro VEGF-A concentrations increased in the retinal pigment epithelium after exposure to ranibizumab or aflibercept due to 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may promote carcinogenesis through activation of extracellular signal-regulated kinase/cyclooxygenase-2/vascular endothelial growth factor signaling pathway.|PMID:16054976|Moreover the nicotine treatment resulted in the increased expression of ERK1/2 in NGF withdrawn SCG neurons implicating ERK1/2 involvement in neuroprotection.|PMC6312731|Acute nicotine injections following extinction sessions upregulate the active form of ERK1/2 in the ventral hippocampus but have no effect on JNK1 phosphorylation|PMC5698137|Furthermore, the expression of nicotinic acetylcholine receptor (nAChR) α4/β2, the phosphorylation of extracellular regulated kinase 1/2 (ERK1/2) and Ets-like protein-1 (Elk-1), and the expression of early growth response-1 (Egr-1) were increased in the nicotine groups.|PMID:29486207|Therefore, nicotine may modulate γ oscillations through NMDAR-mediated Ca2+ influx, activating 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activity of","value_type_id":"EDAM:data_0006","original_attribute_name":"description"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"91706492":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3199064","PMC3477707","PMC3477707","PMC5095960","PMC7409331"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Our preliminary data indicated that a high content of apigenin was detected in the water-based extract of GJH (Figure  1 of Supplementary Material available at doi: 10.1155/2012/935860), and in GJH-induced cytoskeleton rearrangement through downregulation of Rac 1 expression (Figure  2 of Supplementary Material).|PMC3199064|ACM were infected with Nox2 shRNA or control lentivirus (MOI 5 for 48 h), Ad.N17rac1 (MOI 50 for 24 h) or treated with the Rac1 inhibitor NSC (100 nM in water for 21 h) prior to Ang-II addition (10−7M for 1 h).|PMC3477707|ACM infected with Nox2 shRNA or control lentivirus (MOI 5 for 48 h), Ad.N17rac1 (MOI 50 for 24 h) or treated with the Rac1 inhibitor NSC (100 nM in water for 21 h) were exposed to Ang-II (10−7M for 1 h).|PMC3477707|It has been recently shown that water soluble polysaccharides extracted from Bupleurum chinense inhibited fMLF-induced HL60 cell recruitment and involved the inhibition of rac-1 activation.|PMC5095960|Rac1-specific inhibitor NSC 23766 (dissolved in water; ab142161, Abcam, Cambridge, UK) and Cdc42 specific inhibitor ML-141 (dissolved in DMSO; ab145603, Abcam) were used at final concentrations of 100 μM and 80 μM, 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(300 microg/mL and 600 microg/mL) also stimulated TGF-beta1 mRNA expression by normal skin (12% to 53%) and hyperplastic scar fibroblasts (33% to 52%), with statistical significance (P < 0.05) at various time points.|PMID:18443513|Modification of neuronal cell adhesion by heparin induces important morphological changes in rat cultured neurones and increases the genetic expression of the A4 amyloid peptide precursor.|PMID:2471577|Heparin stimulates production of bFGF and TGF-beta 1 by human normal, keloid, and fetal dermal fibroblasts.|PMID:12640331|Heparin stimulates production of bFGF and TGF-beta 1 by human normal, keloid, and fetal dermal fibroblasts|PMC4211176|Heparin (300 and 600 microg/ml) also stimulated TGF-beta1 production by normal skin (26% to 83%) and hyperplastic scar fibroblasts (63% to 85%) with statistical significance (P < .05) at various time 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superiority was attributed to the more potent antiplatelet effect of clopidogrel, and its more efficient inhibition of hyperreactive diabetic platelets: only 15.6% of diabetic patients on clopidogrel therapy developed the composite vascular primary endpoint vs 17.7% of those on ASAtherapy alone (p = 0.042); the insulin subgroup showed greater absolute 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camel milk demonstrated multi-pronged anti-inflammatory effects against cyclosporine-evoked renal injury, as proven with significant suppression of the upstream p38 MAPK, JNK1/2, and ERK1/2 pro-inflammatory components of the MAPK pathway.|PMC8156933|Parallel to the NF-κB pathway inhibition, camel milk also counteracted the activation of renal MAPK signaling, as seen by downregulated expression of p-p38MAPK/total p38 MAPK (by 53.9%), p-JNK1/2/total JNK1/2 (by 39.1%), and p-ERK1/2/total ERK1/2 (43.3%), relative to the renal injury group.|PMC8156933|According to the current findings, the proposed mechanisms pertaining to the attenuation of cyclosporine-evoked nephrotoxicity are: (A) Camel milk inhibited the upstream pro-inflammatory p38/ERK/JNK MAPK pathway, as revealed by lowered phosphorylation of the three subfamilies of MAPK (p38 MAPK, ERK1/2, and JNK1/2).|PMC8156933|Parallel to the NF-κB pathway inhibition, camel milk also counteracted the activation of renal MAPK signaling, as seen by downregulated expression of p-p38MAPK/total p38 MAPK (by 53.9%), p-JNK1/2/total JNK1/2 (by 39.1%), and p-ERK1/2/total ERK1/2 (43.3%), relative to the renal injury group.|PMC8156933|(A) Representative immuno-blots that demonstrate the suppression of the mitogen-activated protein kinase (MAPK) pathway by camel milk, as evidenced by lowered expression of phospho-p38 (p-p38) MAPK (Thr180/Tyr182)/total p38 MAPK, phospho-c-Jun N-terminal kinase 1/2 (p-JNK1/2 (Thr 183/185)/total JNK1/2, and phospho- extracellular signal-regulated kinase 1/2 (p-ERK1/2 (Thr202/Tyr204)/total ERK1/2 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recent evidence on upstream signaling revealed that Akt activation, iNOS upregulation, and viability loss in ALA/light-treated U87 cells were all strongly inhibited by added L-histidine, consistent with primary 1O2 generation by photoactivated mitochondrial PpIX.|PMC7263973|In addition to strongly blunting iNOS upregulation, exogenous histidine inhibited PDT-induced upstream phosphorylation-activation of PI3K and Akt, and oxidative inactivation of PTEN (intramolecular -S-S- formation).|PMC6526063|Phosphor-GSK3β, NFATc1, and Mcl-1 expression increased with the over expression of a constitutively active Akt, which were inhibited by treatment with His-MDA-7.|PMC7598934|Preincubation of SK-BR-3 cells with Δ15HER2-His protein resulted in a dose-dependent reduction of phosphorylated Akt (Fig 5A), suggesting the PI3K pathway activation was inhibited.|PMC2671679|PTEN has mostly been studied as a tumor suppressor in various cancers due to his ability for shutting down Akt-mediated cell 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insulin growth factor 1 (IGF-1) was found upregulated in tumor and stromal cells in the two ovarian xenograft models treated with bevacizumab.|PMID:22700681","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"65894397":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9955722255263157","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The identities of the three EC growth inhibitors were confirmed by demonstrating that recombinant human OSM, LIF, and TGF-beta1 were inhibitory in the same concentration range.|PMID:8798767|The same peptides also inhibited the activity of TGF-beta1 in endothelial cell proliferation assays.|PMID:12755614|This suggests that TGF-beta 1 is inhibiting the same protein-tyrosine-phosphatase required by IL-4 to transduce its mitogenic signal.|PMID:7948747|In treatment groups, SAM provided significant protection from the liver injury induced by alcohol, resulting in a decrease in serum TNF-alpha, TGF-beta1 levels, lipid peroxidation, and the expressions of TNF-alpha and TGF-beta1 mRNAs in the livers, as well as an increase in GSH levels.|PMID:19669264|TGFB1 is one of the candidates in the most significantly decreasing genes by SAM treatment in both cell lines (1 mmol/L SAM vs. control: FCHT-29 = 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inhibits neuronal apoptosis via PI3K/Akt signaling pathway in rats with cerebral infarction.|PMID:31389591","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"124028986":{"subject":"UNII:XSZ53G39H5","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Der VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab ist seit Oktober 2019 in den USA und seit Februar 2020 in Europa zur Behandlung der neovaskulären altersabhängigen Makuladegeneration (nAMD) zugelassen.|PMC7935813|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|When brolucizumab became commercially available in late 2019, the retinal community was enthusiastic about this newest vascular endothelial growth factor (VEGF) inhibitor for the treatment of exudative age-related macular degeneration (eAMD).|PMC7263271|In den Phase-III-Zulassungsstudien HAWK und HARRIER zeigte der VEGF(„vascular endothelial growth factor“)-Inhibitor Brolucizumab (8- oder 12-wöchentliche Gabe) im Vergleich mit Aflibercept (8-wöchentliche Gabe2) nach 48 Wochen eine Nichtunterlegenheit in Bezug auf den Visus.|PMC7935813|Consistent with this focus, laser therapy, VEGF inhibitors like bevacizumab (off-label), ranibizumab, aflibercept, and brolucizumab, and corticosteroids such as dexamethasone intravitreal implant comprise the current therapies for 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response to tolbutamide was significantly augmented after ASA (p less than 0.01) while GH response to hypoglycemia was reduced (p less than 0.05).|PMID:481213|Arginine stimulated insulin levels were increased after ASA (p is less than 0.01 at 15 min; p is less than 0.05 at 30 min; p is less than 0.05 at 45 min), whereas glucose values were lower than under basal conditions at all times, with significant differences at 105 (p is less than 0.02) and 120 (p is less than 0.05) min.|PMID:669099|In 14 normal subjects, treatment with acetylsalicylic acid (ASA, 3.2 g daily for 3 days) a well known inhibitor of prostaglandin synthesis, caused a slight but significant decrease (p is less than 0.05) in basal plasma glucose levels; by contrast, basal insulin rose from 5 +/- 1 to 8 +/- 1 muU/ml (p is less than 0.01) after ASA.|PMID:669099|Insulin concentrations were increased during the glyburide plus aspirin treatment.|PMID:8773160|Concentrations of serum insulin in the hyperglycaemic state prior to arginine infusion were increased during treatment with ASA, whereas increments of serum insulin induced by 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have blocked PLD-1 pathway downstream phosphatidic acid production, using propranolol, which inhibits PLD-1-dependent production of diacylglycerol (DAG).|PMC4260953|To this end, Ins-1EPED/PEA-15 and Ins-1ECTRL cells were incubated with 15 µM propranolol, a specific pharmacological inhibitor of PLD-1 pathway, before treatment with hydrogen peroxide.|PMC4260953|Pretreatment of Ins-1E with propranolol, a well known inhibitor of PLD-1 pathway, abolishes PED/PEA-15 ability to block hydrogen peroxide-induced apoptosis.|PMC4260953|Interestingly, the preincubation with propranolol, an inhibitor of the pathway of PLD-1, a known interactor of PED/PEA-15, responsible for its deleterious effects on glucose tolerance, abolishes the antiapoptotic effects of PED/PEA-15 overexpression in Ins-1E beta-cells.|PMC4260953","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC4260953","PMC4260953","PMC4260953","PMC4260953"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"78494473":{"subject":"UMLS:C3536832","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Further analyses illustrated that among COPD patients, air pollution exposure was associated with reduced levels of serum eotaxin, interleukin 4 (IL-4) and IL-13 and was correlated with increased serum IL-2, IL-12, IL-17A, interferon γ (IFNγ), monocyte displacing protein 1 (MCP-1) and soluble CD40 ligand (sCD40L).|PMC6993429|Further analyses illustrated that among COPD patients, air pollution exposure was associated with reduced levels of serum eotaxin, interleukin 4 (IL-4) and IL-13 and was correlated with increased serum IL-2, IL-12, IL-17A, interferon γ (IFNγ), monocyte displacing protein 1 (MCP-1) and soluble CD40 ligand (sCD40L).|PMC6993429|Furthermore, we found evidence of associations between air pollution and decreased levels of circulating eotaxin, IL-4 and IL-13 and increased levels of IL-2, IL-12, IL-17A, IFNγ, MCP-1 and sCD40L in COPD patients.|PMC6993429|IL-4 was significantly lower in the phosgene-exposed mice than in the air-exposed mice from 4 to 8 h after exposure.|PMID:12754690|AIR645, developed by Altair Therapeutics, is another ASO drug that is designed to target IL-4α for both Th2 cytokine IL-4 and 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it suggests that co-targeting of PED may improve the efficacy of sorafenib.|PMC5682677|PED may be a novel target for HCC therapy and serve as a predictive marker for treatment response against sorafenib.|PMC5682677|PED may be a novel target for HCC therapy and serve as a predictive marker for treatment response against sorafenib.|PMID:29072691","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"124016523":{"subject":"PUBCHEM.COMPOUND:6274","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Imidazole propionate is a histidine-derived bacterial metabolite that can inhibit insulin signaling at the insulin receptor-substrate level during T2D.|PMC8110751|His blood glucose levels gradually decreased after a daily dose of insulin of 0.7 U kg−1, suggesting insulin resistance.|PMC4650454|HIS fed rats had higher glucose and triacylglyceride levels (p < 0.01), and lower plasma insulin (p < 0.01).|PMID:15971156|While it is possible that there was spontaneous resolution of insulin antibodies, we speculate that his prednisolone and immunosuppressant therapy may have suppressed insulin antibody production.|PMID:29588555|In a supplementation trial, His significantly decreased markers of insulin resistance, waist circumference, fat mass, serum NEFA, serum inflammatory cytokines, and oxidative 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to 20% oxygen significantly increased signal for both ERK1 and ERK2 (ERK1: P < 0.01; ERK2: P < 0.01; Fig. 5).|PMC4331663","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"93583988":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"These same three strains decreased Th2 cytokines production such as IL-4 and IL-5 in lymph node cell cultures.|PMC3773919|The same study also observed a decreased release of cytokines such as IL-4, IL-5, IFN-γ, IL-1β, and IL-12, indicative of enhanced Th1 response, suggesting that TLR9 activation may suppress the Th2 response via promoting a Th1 response.|PMC4870363|The inhibitory effect could be observed at a concentration of 100 U/ml and was near to maximum at 1,000 U/ml in acute phase, whereas the same suppressive action of IL-4 was reached at 100 U/ml in recovery phase.|PMID:12569762|IFN-γ induces the class-switching of IgG2, at the same level of inhibition of IL-4 induced production of IgG1.|PMC7532904|At the same time there is a decrease in type 2 cytokines (IL-4, IL-5, IL-13 and 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data indicated that the serum levels of testosterone, insulin and zinc were significantly increased (P<0.01) in testosterone-administrated and finasteride groups, but the level of chromium was decreased in both groups (P<0.01).|PMID:23279835|Prostatic involution in men taking finasteride is associated with elevated levels of insulin-like growth factor-binding proteins (IGFBPs)-2, −4, and −5 |PMC3174339|The study demonstrates that testosterone and finasteride increases insulin and zinc levels and decreases chromium levels in the serum of male adult rats.|PMID:23279835","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"71417747":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:225689","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999655","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:cbdabbd696a96885cdd944be71264b2e36b25227eadf74557618ccc9d7ecc81e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Working stocks of JNK Inhibitor III, SB202190, Tyrphostin, and PD98059 were prepared directly in DMSO as a vehicle, while a working stock of ERK2 Inhibitor was prepared in 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c-Met mediated inhibition of the Akt and ERK1/2 pathways can lead to cell cycle arrest (Fig. 2B).|PMC3407171|Reduction of phospho-AKT and phospho-p44/42 MAPK levels was also observed with MET treatment in these cells, suggesting MET’s influence on kinases that control expression of genes involved in growth regulation.|PMC7077930|For the first time, we have shown that the downregulation of Met by Met-specific shRNA leads to differential effect on the tyrosine phosphorylation sites of EGFR, Her2 and Her3 (Figure 5) suggesting that Met plays a crucial role in activating ErbB family receptors especially EGFR, as the activation of EGFR is drastically affected with concomitant inhibition of Erk1/2 and Akt activation.|PMC2661782|According to all the above results, we concluded that MET can upregulate the expression of miR-7 by mediating AMPK signaling in NSCLC A549 cells and then by inhibiting the AKT/mTOR, Erk, and NF-κB signaling pathways to suppress the growth, migration, and invasion of A549 cells.|PMC7077962|These data indicated that Met suppressed the LPS-induced activation of MAPK signaling in RAW 264.7 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another larger trial assessing plasma VEGF in patients with treated with anti-VEGF therapy (bevacizumab, ranibizumab, and aflibercept) for DME found that the median plasma VEGF concentration increased by +0.20 pg/ml (IQR −5.00 to +4.90) 4 weeks after the first injection of ranibizumab.|PMC7127926|After two intravitreal ranibizumab injections, reductions in the levels of circulating cytokines IL-1β, IL-13, G-CSF, IFN-γ, IP-10, MIP-1α, and TNF-α were measured, with increased levels recorded for IL-9, MIP-1b, VEGF, and sVEGFR-1, after correcting for the multiple comparisons.|PMC7127926|In addition to the reduced concentrations of certain cytokines, we found that at 28 days after two consecutive monthly intravitreal ranibizumab treatments IL-9, MIP-1b, VEGF, and sVEGFR-1 were elevated in the serum.|PMC7127926|There was then a rebound increase of 67% in total plasma VEGF levels following a further injection, which remained above baseline for 12 weeks despite two further intravitreal ranibizumab injections.|PMID:25657041|One approach to achieve this goal may be combination therapy of ranibizumab with verteporfin-PDT since after PDT the production of VEGF is 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PEG, significant elevations of IL-4, IL-6, IL-8, IL-16, CCL13, CCL15, CCL22, CCL24, CXCL13, and CXCL16 were found.|PMC6162267|IL-4 production was significantly increased in the spleen of PEG-treated mice compared with that of PBS-applied mice.|PMID:18270494|Peg-IFN-α therapy resulted in higher levels of IFN-γ, IL-12p70, IL-7, IL-8, IL-16, IL-4 and IL-13 in the responders (elaborated in next section), before the detectable loss of HBsAg.|PMC8018960|Peg-IFN-α treatment resulted in higher levels of IL-27, IL-12p70, IL-18, IL-13, IL-4, IL-22 and GM-CSF prior to HBsAg loss.|PMC8018960|Notably, the production of both IFN-γ and IL-4 was significantly increased in PEG-GO-treated groups (Figure 4).|PMC4162634","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"54622948":{"subject":"PUBCHEM.COMPOUND:3121","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Trophic factors assessment, following treatment revealed the mRNA expression level of BDNF, GDNF and VEGF could be significantly up- regulated at various time points, mainly by 1 mM VPA.|PMID:30904572|VPA enhances postischemic angiogenesis via upregulation of HIF-1α and the downstream pro-angiogenic factors VEGF and MMP-2/9.|PMC6248271|In addition to enhancing HDAC inhibition, VPA potentiated MCAO-induced HIF-1α accumulation and upregulated VEGF protein levels and MMP-2/9 activities in the ipsilateral cortex on days 7 and 14 post-MCAO.|PMC3429729|The transcription factor hypoxia-inducible factor-1α and its downstream proangiogenic factors, vascular endothelial growth factor and matrix metalloproteinase-2/9, were upregulated after middle cerebral artery occlusion and significantly potentiated by VPA in the ipsilateral cortex.|PMID:22811460|As shown in Fig. 2a, the expression levels of 6 secreted proteins (GCSF, GM-CSF, M-CSF, PDGF Rα, PDGF Rβ, and PDGF-AA) were decreased and those of 4 secreted proteins (AR, EGFR, TGF-β2, and VEGF) were increased in VPA-treated cells, compared with the 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also increased the expression of Bax, decreased the expression of Bcl‐2, and activated PARP (Fig. 3b).|PMC5378285|Inhibition of YAP1 with verteporfin also interrupted Bcl2 and BAX expression and reversed TNBC taxol resistance through the EMT pathway.|PMC6361558|Moreover, expression of Bcl2 was inhibited and that of Bax was increased in the verteporfin treatment group (Figure 4C).|PMC6361558|Verteporfin treatment inhibited the transcription of BCL-2 and C-MYC|PMC5787498|Mitochondrial-localizing PSs such as benzoporphyrin derivative mono acid A (BPD, verteporfin) and protoporphyrin IX have been shown to be especially potent in triggering apoptosis through mitochondria membrane depolarization, cytochrome c release, and the destruction of the anti-apoptotic proteins BCL-2 and 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can inhibit retinal angiogenesis via suppressing VEGF expression in an OIR mice model with exposure to relative hypoxia.|PMID:29464332|These results suggest that high-concentration sevoflurane can regulate NSC apoptosis by inhibiting the VEGF/PI3K/AKT pathway.|PMC6126114|Sevoflurane minimised bronchoconstriction and cell infiltration, and decreased tumour necrosis factor-α, transforming growth factor-β, vascular endothelial growth factor, sirtuin, catalase and glutathione peroxidase, while increasing nuclear factor erythroid-2-related factor 2 expression.|PMID:24666314|Together, our findings indicate that exposure to a high concentration of sevoflurane (3.5%) in mid-gestation decreases VEGF, PI3K and p-AKT protein levels and induces neural stem cell apoptosis, thereby causing learning and memory dysfunction in the offspring.|PMC6126114|The present study showed that in human neuronal SH-SY5Y cells, the expression of BDNF and VEGF decreased after LPS and sevoflurane exposure for the 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Schematic representation of the in vivo model design used to compare the efficacy of paclitaxel delivered intravenously (intravenous) to the paclitaxel eluting device (PED) treatment.|PMC4849535|(A) Schematic of localized therapeutic approach with a paclitaxel eluting device 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PAs.|PMC6558377","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9994336","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"86885450":{"subject":"PUBCHEM.COMPOUND:57363","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9994944666666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Furthermore, the finasteride-loaded microspheres increased the activities of phosphoinositide 3-kinase/protein kinase B and Wnt/β-catenin in relation to hair follicle cell growth signaling in mouse skin, and suppressed the apoptosis of hair follicle cells by reducing the expression of transforming growth factor-β2 and caspase-3, which are indicators of apoptosis.|PMC6488187|The expression of Bcl-2 in the finasteride-loaded microspheres-treated group was increased, whereas the expression levels of cleaved-PARP, cleaved-caspase-3, TGF-β2 and Bax were lower than those in the microspheres-treated group (Fig. 5A and B).|PMC6488187|Finasteride treatment significantly increased apoptosis (activated caspase-3 expression) in hippocampal CA3 and CA1, and cerebellar molecular and granular layers, an effect abolished by co-infusion of alfaxalone and 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is of interest that in our study increase in ERK2 phosphorylation is more pronounced than ERK1 in the chronic-ethanol binge group.|PMC3204341|The increase in the levels of phospho-ERK2 were more marked (4.0 fold increase) in chronic ethanol – three binge group, modest in control-binge group.|PMC3204341|While our finding on ethanol activation of RVLM ERK2 is consistent with findings in other tissues, studies on the effect of ethanol on p38 and JNK signaling produced conflicting data.|PMC3812351|Elevated activation of ERK1 and ERK2 accompany enhanced liver injury following alcohol binge in chronically ethanol-fed rats|PMC5533086|Elevated activation of ERK1 and ERK2 accompany enhanced liver injury following alcohol binge in chronically ethanol-fed 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Bcl-2.|PMC5220214|This study has reported that caspase-3 and -9, HIF-1alpha, Bcl2, Cox2 and the phosphorylated AKT were enhanced upon PDT with ALA.|PMC4125699|Neither had an effect on Bcl-2; however, IHG-induced apoptosis was significantly attenuated by ALA treatment, as evidenced by decreased Bax, Caspase-3, and increased Bcl-2 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shown in Figure 2 , at concentrations below 40 × 10−6 m, the MF‐Lip40@PEG could significantly increase the expression level of VEGF and bFGF in a dose‐dependent manner.|PMC6364594|32 In the present study, we found that following treatment with MF‐Lip@PEG leaching liquor for 7 d, the expression levels of VEGF and bFGF in HUVECs increased significantly in a dose‐dependent manner at concentrations below 40 × 10−6 m (Figure 2b,c).|PMC6364594|In this study, vascular endothelial growth factor (VEGF)-small interfering RNA (siRNA) was encapsulated into a magnetic mesoporous silica nanoparticle (M-MSN)-based, polyethylenimine (PEI)-capped, polyethylene glycol (PEG)-grafted, fusogenic peptide (KALA)-functionalized siRNA delivery system, termed M-MSN_VEGF siRNA@PEI-PEG-KALA, which showed significant effectiveness with regard to VEGF gene silencing in vitro and in 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treatment of this condition involves laser photocoagulation (panretinal, focal, and grid), intravitreal anti-VEGF agents (aflibercept and ranibizumab), corticosteroids (dexamethasone and fluocinolone acetonide intravitreal implants), and vitrectomy in the case of vitreous hemorrhage.|PMC6681039","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.000122313","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"27599532":{"subject":"PUBCHEM.COMPOUND:36314","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999474685","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:cae296a974791036acd69c943cf0c4542e475b38deff68e024eebbdfdf345190","tmkp:e1b3ce2cee0a9baabbbfff36119258c2c6474e0b90595d0d86b8df22f2ba8a47","tmkp:5ac95effb22a6a5737f2fdfedd3e6ae2a63b3563afc1baa8a39b98e0424ed646","tmkp:c4ad6867ad933a93f6a480a1ad2dd58693591740b1423eba9a25bc42932e5835","tmkp:f59cf4e15e494dbc94f10e527206fa6428514a0088dc43ea7409ae4ecce2428d","tmkp:f9a9138c580e96ca0d2afdd54e327a07e3abfdf1293af0e06fed89f538d5b1f2","tmkp:ff35c03b3d063785f22a5d229340ed1a6ca027c396db3489a41059c08a8b2bf6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"The mRNA expression level of TGFB1 was increased by paclitaxel in vivo as previously reported (Supplementary Figure 2A).|PMC4741946|Low-dose (∼50 nM–10 μM) paclitaxel treatment of HK-2 cells for 24 h caused prominent G2/M arrest (Fig. 5d), with upregulation of mRNA expression of TGFB1, CTGF, COL4A1 and COL1A1 and increased CTGF protein secretion into the supernatant (Fig. 5e).|PMC3928013","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5411865","PMC5282965","PMC3928013","PMC7462997","PMC7262989","PMC4274046","PMC4741946"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"21519195":{"subject":"PUBCHEM.COMPOUND:36314","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"FR-targeted liposomes loaded with paclitaxel and imatinib have shown effectiveness in promoting cell death and suppressing vascular endothelial growth factor (VEGF) expression in folate-receptor-overexpressing cancer cell lines.|PMC8001342|FR-targeted liposomes loaded with paclitaxel and imatinib have shown effectiveness in promoting cell death and suppressing vascular endothelial growth factor (VEGF) expression in folate-receptor-overexpressing cancer cell lines.|PMC8001342|In murine studies, paclitaxel was able to reduce new vessel formation at low, noncytotoxic doses (0.3 and 6 mg/kg per day in mice) by suppressing VEGF expression.|PMC4475536|Paclitaxel inhibits radiation induced VEGF secretion and enhances radiosensitizing effects in human colon cancer cell HT29|PMC4145830|Paclitaxel inhibits radiation induced VEGF secretion and enhances radiosensitizing effects in human colon cancer cell HT29|PMC3508157","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:173f2059466cec68b9774a3b228709d3f5de5c76480ba780ca8f0ae9368967bb","tmkp:76c9dba6ae0cad50dd8b38deb5ff3cf9a561f9f5874d57b3fa603023cb06386e","tmkp:9539c2ea50caf1017bbf29680462d75f203d89a249dc408a732084a53b0bedd7","tmkp:56d99f3ce3c3f2d2b7b6c2644f1537ee077632ae7d8b7235b0dd8b2aafdb3fbe","tmkp:a672feb10f87d18fc3d42d07039594d54cd823ace91031da4504dd09f2e8542e","tmkp:5ca121fdb42597058214d4676c4a5f273e703a0821efe6090cd0ea0389dc617d","tmkp:c834461bc6af2f4c1352daaf3d6c9157cf73edc277f1c8128eae97a4e9e56ef3","tmkp:b61c71731018a973f923fceda0c8f63ee211838a06575c936718e76fc15f5b1b","tmkp:22079d2c6c4ad223d86ee13c5a55de5f7798031d3478f2f6c9bf07e779730eac","tmkp:d7c8d632e71a59af57f80a10078f7f8f39cfaae0486e192291e34ad5f7728a0e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4145830","PMC4475536","PMC6320818","PMC8001342","PMC6566430","PMC7883871","PMC3508157","PMC4061164"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9965584944755245","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"32422447":{"subject":"PUBCHEM.COMPOUND:702","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"The objective of this study was to determine feasibility and acceptability of a brief pediatric emergency department (PED) prevention intervention to delay/prevent initiation of alcohol use in 12-to 14-year-olds.|PMID:24168879|The objective was to determine if adolescents presenting to a pediatric emergency department (PED) for an alcohol-related event requiring medical care differ in terms of substance use, behavioral and mental health problems, peer relationships, and parental monitoring based on their history of marijuana use.|PMID:20078438|The association of PED with alcohol consumption showed a somewhat similar pattern (Table?4).|PMC5641269","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9927196199999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d7be8eba9737ff207bae332d639932c9f81a9f3dedfe8ddb38454c0ac3920dc0","tmkp:148ad2f4fb8ca8fc83ec40d917e4709039ff71e46f1cf5fd2273f942e7071add","tmkp:9d8e5c5e046d49b2ba98e65b7a93a927d9d444f2a6929dc7e710dfcc867135cc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:24168879","PMID:20078438","PMC5641269"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"118866715":{"subject":"NCBIGene:2335","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ab229bb9bc58b698435e7b8243bca3002d7743f2fd633fd0a568dca3adc3d246"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:26312620"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"To report 2 cases of corneal perforation associated with a persistent epithelial defect (PED), which were treated with eye drops containing the fibronectin-derived peptide PHSRN (Pro-His-Ser-Arg-Asn).|PMID:26312620","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99525166","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"100920943":{"subject":"PUBCHEM.COMPOUND:439501","object":"NCBIGene:142","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"degradation"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"increased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"9606","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"dct:description","value":"increases degradation of","value_type_id":"EDAM:data_0006","original_attribute_name":"description"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:ctd","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:24124520","PMID:31436044"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"63514085":{"subject":"UMLS:C2740799","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Oral administration of lyophilized Ajwa date extract (250 and 500 mg/kg body weight) downregulated the expression of pro-inflammatory cytokines (interleukin [IL]-6, IL-10 and tumor necrosis factor-alpha [TNF-α]) and apoptotic markers (caspase-3 and Bax) in injured Wistar rat heart tissue, further supporting the anti-inflammatory and anti-apoptotic potential of dates against ISO-induced myocardial damage.|PMC8125345|Treatments tested to date include overexpression of BCL-2, inhibition of caspases (e.g., caspase-3 and caspase-8) and CD95, and most recently the use of noncaspase protease inhibitors.|PMC3684427|The interaction between the enzyme and a ligand (substrate/inhibitor) would thus only involve a single domain (A/B chain) of the protein with the ligand, as confirmed by our survey of the 38 crystal structures of caspase-3 in complex with inhibitors deposited in the PDB to date.|PMC2767110","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9984009433333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC8125345","PMC3684427","PMC2767110"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:970915f9301abcabbaec02988f6ff6509096939a0e645241cd11e957a7ae1669","tmkp:6158246e2fcb1ec2eee21c7faa70a017de18c9634b6000320dd664073cfe57b6","tmkp:a1225f13ca6430e5c45afac5b4ff1a2de3f1ee54f2d3add13fd183ecaea3db93"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"54011275":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:25953","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"While alcohol or caffeine ingestion are the most consistent triggers of human PNKD associated with PNKD mutations, dogs rarely ingest alcohol and methylxanthines are toxic to dogs, so whether they would trigger episodes in dogs is unknown.|PMC5243907","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC5243907"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:5d76e6df0db17b2cc530ce852e860a9a869643eca3cfe0ab1b9e8fa8db79d771"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.99752325","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"96133097":{"subject":"UMLS:C2740799","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Increased expression of VEGF has been demonstrated in most human tumors examined to date, including tumors of the lung, breast, thyroid, gastrointestinal tract, kidney, bladder, ovary, and cervix, as well as angiosarcomas and glioblastomas.|PMC2783916|Similar results of upregulation of VEGF mRNA expression have been reported for the vast majority of human tumors examined to date, including carcinoma of the lung, breast, gastrointestinal tract, kidney, bladder, and ovary.|PMC3383312","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:22c75006ae50eabffa3070923fc7fb9ff49105676a8d9e81a80c7e50830e628d","tmkp:a35192241f49cfec5ec26deda2c85a982ab04ca841c81c1a8ca4a8df556644ec","tmkp:88f1a882e753b495022c1d441a7ed73a169254dbc195052e4988a856606a79bd","tmkp:8e0f20b754c18c0f0945115aa0e1a7a081d4bb09792be0bcbc0acdccb5a319fa","tmkp:9534088534a5191422dc0ef9b60c5e25db7a697738e5dcff71b4ca92ef3d1b6c","tmkp:b96d91e615dc9fc8467d5ca5a0faf1c4c6fbcf67b4197a6b0386098d1a8a2152","tmkp:3a660aac29f6d06bc3d92eb5d698a0e5ba06c64e12abc17d92d127e697830a55"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC3563266","PMC8230848","PMC3383312","PMC2669548","PMC2783916","PMID:12177445"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9987033000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"51498177":{"subject":"PUBCHEM.COMPOUND:5284583","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9993531833333332","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC7995356","PMC7995356","PMC7995356"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:efde692b14adcc073151bc6116292d366fa92cfe1d9fe59b5f05a16fba28e210","tmkp:29ab3fd25ee9e76055259a1ea3d719efc320382d14e045b26158559b68e8296e","tmkp:74393983fafe7d2a0ce636ddc203f0e74cc1e3fac748974bcfc1a703c6e9c6be"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"4 , 5 , 56 Here, we report PED in a Welsh Terrier and long term management with levetiracetam.|PMC7995356|56 Levetiracetam was efficacious in the treatment of PED in this dog, and there were no long?term adverse effects after 47?months.|PMC7995356|This is a report of PED in a Welsh Terrier that describes a successful therapeutic approach to the long?term management using the novel AED levetiracetam.|PMC7995356","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"65627911":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:52256bb09af2fbc197b79f3bdbd71163490412b38547e0366412fa12ce7a510e","tmkp:7b44844f51298ab05390c21c6f132e0317bd60f4317500e33f7f452575efd161","tmkp:376005e26ce60608c5d50c02d3a37244d92ab3d5fc4cc2dccd1479c4879ca8ac","tmkp:e4226dfac8311982e9d71477cc9f57bb4f0f4a6fcfd9eabe8de7b609309d6c32","tmkp:7771dd00c2b32ea5ee2c048b73136854b00940d764deceb533f4b11c0af0fc00","tmkp:110fb8ba0362b0361fb40b23e6baffea148411ec455cacf71331dbdd4cc017b7","tmkp:58c483a057ec44fc9dc0d7d1f84b33830f6dbc1cac13faf0e15046681cd25a06","tmkp:83127749729ef71db1606b408590f5117f527f5247054ea6154783dbc7705b1b","tmkp:2f95989dcb7171d9d7a838d30ca50783914e403fac3baa5052f22edf34bbaeaa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9969096166666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC7238550","PMID:23726868","PMID:24558828","PMC6539586","PMC3131400","PMID:21195670","PMC2831074"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"To demonstrate this, we induced gene silencing of tgfβ1 in the lungs of wild type and IL10 knockout mice using a non-invasive aerosolized intrapulmonary delivery of siRNA targeting TGFβ1 Five days after the last treatment with siRNA, the levels of tgfb1 transcripts and TGFβ1 protein were reduced when compared with control groups treated with RNase free water or non-targeting siRNA.|PMC7238550|Under LAP, the boiling point of water decreases, which accelerates the evaporation of moisture.|PMC6539586|Five days after the last treatment with siRNA, the levels of tgfb1 transcripts and TGFβ1 protein were reduced when compared with control groups treated with RNase-free water or non-targeting 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upregulation by pro-inflammatory stimuli, IFNγ, DNCB or formaldehyde is preceded by the production of IL-8, an acute inflammatory phase cytokine.|PMID:25617811|There was significant upregulation of IL-1α,IL-1β, IL-5, IL-17A, leptin, NGF, VEGF, CXC and CC chemokines (*p < 0.05, unpaired t test) in formalin injected prostate, while expression of BDNF, IFNγ, G-CSF, IL-2, IL-4, IL-10, IL-12p70, IL-13, TNFα remained unchanged between the 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studies have shown that VEGF expression levels decrease after exposure to nitrous oxide during urological surgery.|PMC5513670|according to Pre-operative 0th min VEGF levels decreased (28%) more in the group who were given nitrous oxide than the group (11%) who were not given nitrous oxide suggests that the decrease occurred due to nitrous oxide.|PMC3955540|according to Pre-operative 0th min VEGF levels decreased (28%) more in the group who were given nitrous oxide than the group (11%) who were not given nitrous oxide suggests that the decrease occurred due to nitrous oxide.|PMC3955540|Compared with preop levels, VEGF levels were found to be low at postop 4 and 24 hours in the 30 patients who had mastectomy operation under general anasthesia using nitrous oxide but no statistically significant difference was 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27 hpf, tgfb1a expression is downregulated in the DA and PCV, whereas tgfb1b is still clearly present (Figures 1B and 1C).|PMC4998007","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99923897","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"40388416":{"subject":"PUBCHEM.COMPOUND:135398748","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:bb03eae85786c75518378c6029e9fbf83c49f705369e3fe97c7d03961dae756c","tmkp:2936c9c1add9f9d85d711f57fdc44eef048fe07dcd23ebcf4fe76695cd2ddaa0","tmkp:ad351d0954043e655beb99963e4b1eb60686f7a9a5d048f0e82336439ffc2bbd","tmkp:3f9bcc92d62baa92cf6e434ca77d9b6faddfe14a40e392d427b516999b879f0d","tmkp:8470a167b1cc4fabe63f91564c4fe7323fe84516021cbc9fd47db60c41b27274","tmkp:c5acc3dd809315ee6d48307dae08d91a9c5b9a1a37c1b0f131d85b187321e6f3","tmkp:957abff050eed7e7fd379cceca5edeaa17492542a2046d9da5eef930129c9382","tmkp:0249ad03b5c165fb13eab80afe992af897dd53bf3ce332824ad8b290d5e1d038"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9644474000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, PCV2 induces autophagy by repressing mTOR in a cascade of phosphorylated proteins involving TSC2, ERK1/2, and AMPK and enhances the replication of autophagic machinery in PK-15 cells.|PMC4363047|This observation is consistent with an earlier report that p-ERK1/2 and Cap proteins were significantly decreased in PCV2-infected PK15 cells transfected with ERK siRNA.|PMC7126689|PCV2 specifically activates the c-Jun NH2-terminal kinases (JNK1/2) and p38 in infected PK15 cells, and inhibition of these MAPK pathways significantly hindered viral transcription, viral protein synthesis, viral progeny release, and virus-induced apoptosis.|PMC4391141","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7047418","PMC4391141","PMC7103411","PMC4363047","PMC7126689","PMC6039236","PMC7058596"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"49666073":{"subject":"PUBCHEM.COMPOUND:6274","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4088371","PMID:31748497","PMC3627608","PMC7435460","PMID:12947150"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9970728040000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"It is interesting that the levels of IL-6 and VEGF in the ascitic fluid of our patient were markedly higher than the levels in his serum and plasma.|PMC4088371|However, his serum level of vascular endothelial growth factor(VEGF)was elevated to 1,520 pg/mL, and IgA-l type M protein was detected.|PMID:31748497|However, his serum level of vascular endothelial growth factor(VEGF)was elevated to 1,520 pg/mL, and IgA-l type M protein was detected.|PMID:31748497|We hypothesised that his effusion would have increased levels of eosinophil cytokines that promote oedema, and found a marked increase in pleural vascular endothelial growth factor (VEGF) and smaller increases in interleukins IL-5, IL-6, and IL-8.|PMID:12947150|We hypothesised that his effusion would have increased levels of eosinophil cytokines that promote oedema, and found a marked increase in pleural vascular endothelial growth factor (VEGF) and smaller increases in interleukins IL-5, IL-6, and IL-8.|PMID:12947150","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:28125684f2a3a70cd418fe313860d9bf7504a50d84af8b38b1d7a4b8817e01ce","tmkp:16a4b8edf025b114de27a39d4fa4bde8af4f345c4f8ddbd34720663caed206f4","tmkp:dfd6c53783d94f2aed9d01ee0356182e3664308980040ac5d1ad6bfe8f27eb8a","tmkp:641121d16e6ba4a96dd934b96389d0099c5b53391e952bcf0bba61eedbdb4871","tmkp:379320122de9723d278e4fba3953c2cf089b00a384030b9237e7732986f63ff9","tmkp:d45a2b5d165fda2afed0415be505e1791f6a648d51e6004afa366d5cf32f2ca7","tmkp:a0f5c7d6168bb4dd77688ba511a0e7ac819037b7809e5763ccd16619b3cb2642","tmkp:21f3552e6bf16b9349dc13c2372b9a8b685ad418ab7e4b419b33cdb041431ac8","tmkp:0b317679fa96edb85a7a90da736a94fe16783e6b449beb31dbced0bbd8ffcd46","tmkp:d19e5cddca25c1d092e7db444662e1dbea7edc4e052426ca07123e7631250082"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"129595912":{"subject":"PUBCHEM.COMPOUND:135398737","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:ea6878ade75678238bdca4614912952ead0f8868928b730d496e3d0d4d1bd1e0","tmkp:a3a9784b8bc0a7b7607723693280a653024fc4bf6c6d8f11590292de5518a298","tmkp:717b69ff0c356b7ef862b41814b6c5c86bb99d4319b54916f11cefe0b5fa5f15","tmkp:da661df3c73454ce3e1d8fbcf6a14763ba4f9e4631518d190af75dc61b2848b8","tmkp:3096a87df806d07ba21c4098dcf79bdc11b9e182f284b5e678c91a73508cb9e5","tmkp:a5004b54b32a5b52210536c633dd5107122fa780c9166349b913002ec65af433","tmkp:e7adcca8088f6635ff33dca7a774e7206d3eb2c916cb22ceb62712e96c58dfaf","tmkp:c54b4c55bbb91db59ac7c8969f4c5853e79adb82220102016c8c9f8a6629b1e6","tmkp:11b569691a67a58fab36f5a53e63c594dc1244a1621a703fe2e5802e4149b882","tmkp:53e8fe6ddec457b30c3463bfd5715edef4bc7e323e76e93f07d19a6e5600fdf5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Clozapine has also been shown to activate levels of ERK1/2 in the prefrontal cortex region, by interaction with the epidermal growth factor (EGF) receptor.|PMC3735488|The atypical antipsychotic clozapine also activated MAPK, albeit with lower potency and efficacy (pEC(50), 5.43 and 43%).|PMID:12110994|Chronic administration of the olanzapine and clozapine enhanced ERK1/2 activation in rat prefrontal cortex, whereas haloperidol does not produce any significant in ERK1/2 phosphorylation.|PMC4153869|In addition, clozapine, more than other second-generation antipsychotics, activates ERK1/2 (extracellular signal-regulated kinases), which may explain, in part, the therapeutic superiority of this drug on many aspects of mental disorders.|PMC6790347|Clozapine is the powerful drug activating ERK1/2 and part of this effect is due to the novel mechanism of 5-HT2A receptor activation.|PMC6790347","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC3735488","PMID:12871586","PMC6675791","PMC6790347","PMID:23771439","PMID:12110994","PMC2881214","PMC4153869"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9902225362857143","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"58292029":{"subject":"PUBCHEM.COMPOUND:6047","object":"NCBIGene:355","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9996544166666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The proportion of CD95/CD3 increases significantly in the lymphocytes from PD patients, but decreases significantly after L-dopa treatment.|PMC5002148|After treatment with L-DOPA, both the CD95/CD3 ratio, assumed to represent an antigen marker characteristic of apoptotic cells, and the number of cells dead due to apoptotic processes were found to be decreased.|PMID:23821384|Moreover, the ratio of CD95/CD3 increases in the lymphocytes of PD patients; however, after L-dopa treatment, it decreases 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GCH1 mRNA levels increased in response to Arg treatment.|PMID:21293034|Arg increases expression of GTP cyclohydrolase 1 (GCH1) and IFNT mRNAs while Arg and Gluc increase ornithine decarboxylase, nitric oxide synthase 2, and GCH1 mRNAs and proteins by Tr cells.|PMID:22738901|Arg increases expression of GTP cyclohydrolase 1 (GCH1) and IFNT mRNAs while Arg and Gluc increase ornithine decarboxylase, nitric oxide synthase 2, and GCH1 mRNAs and proteins by Tr cells.|PMID:22738901|In day-16 ovine conceptus explant cultures Arg increases GTP cyclohydrolase 1 (GCH1) mRNA; both Arg and glucose increase ornithine decarboxylase (ODC1), nitric oxide synthase 2 (NOS2), and GCH1 proteins; and Arg increases IFNT.|PMC3485747|Only conceptuses treated with Arg increased expression of GCH1 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could decrease the ratio of cleaved Caspase-3/Caspase-3 and the ratio of Bax/Bcl-2 in comparison with the histone group.|PMC7738632|In this article, the authors demonstrated that mice with cecal ligation and puncture- (CLP-) induced spetic acute kidney injury benefited from intraperitoneal heparin administration with improved survival, declined serum pro-inflammatory cytokines (namely tumor necrosis factor-a and interleukin-6) as well as kidney injury biomarkers (namely neutrophil gelatinase-associated lipocalin and kidney injury molecule-1), and decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP.|PMC8093565|Indeed, heparin treatment did not alter the levels of viral replication compared to control Vero cells, however, it significantly decreased the percentage of caspase-3+ cells, suggesting that heparin can also prevent ZIKV-induced 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was a significant decrease (p<0.01) in the expression of LC3, Bcl-2, BMP2, and Beclin-1 proteins in the tibia tissue of the prednisolone group compared to the control group.|PMC6338015|No change was found in the 22.5 mg/Kg nor 12.5 mg/Kg prednisolone treated groups when compared with the saline treated group, while a decrease in the Bcl-2/BAX ratio was found using the lower dose of prednisolone in liver and kidney (Bcl-2/BAX kidney: saline, 0.99 ± 0.30 and 5 mg/Kg prednisolone group; Bcl-2/BAX liver: saline, 0.09 ± 0.03 and 5 mg/Kg prednisolone group, 0.04 ± 0.01) (Figure 5).|PMC4452233|No change was found in the 22.5 mg/Kg nor 12.5 mg/Kg prednisolone treated groups when compared with the saline treated group, while a decrease in the Bcl-2/BAX ratio was found using the lower dose of prednisolone in liver and kidney (Bcl-2/BAX kidney: saline, 0.99 ± 0.30 and 5 mg/Kg prednisolone group; Bcl-2/BAX liver: saline, 0.09 ± 0.03 and 5 mg/Kg prednisolone group, 0.04 ± 0.01) (Figure 5).|PMC4452233|The apoptosis array results demonstrated that IR-prednisolone increased levels of cleaved caspase-3, Bax, tumor necrosis factor receptor 1, heme oxygenase-1, p21, phosphorylated-Rad17 and hypoxia inducible factor-1α, but decreased the expression levels of cellular inhibitor of apoptosis-1, Claspin, Survinin, Bcl-2, Bcl-x and p27 (Fig. 4A).|PMC8047763|High dose of prednisolone significantly up-regulated BAX expression and down-regulated BCL-2 in a time dependent manner.|PMC6171400","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:376cff9dbda216b1f47992e7ff9f1a1cee61a7e15e5225511551cf6ef241bc7f","tmkp:919cd25194eaf3d59344629592ba6d1cfd4a806790fc7444364e8af2c98b0fee","tmkp:990b263aa11a77b7bd25f04cc28882a6d4b55ab5891602aeca94b65119f2eb44","tmkp:5fb8f46ebd24f38957ba19ba94159451a206a570ae8022acbcb9372783a36a49","tmkp:5e9cb28cd9b15b31838b8a4b41893ff28197a48afc37d6453ac4a6a68eba6b21","tmkp:76a312da9314a916e05e911d2dc039e53f400096ec4e81946f07131a5afd935b","tmkp:67279ee3a4dc2053240429cec60a80abc3713ee5ef3f2a0bdc0f8a043cd4aafa","tmkp:3c7e1f52a6bfece0f6daad5a6d150191e9fffe98ee721178a31d4a6de594164d","tmkp:a04be90a3a8ebd61d8feaa1baea3e5a80dca8a45873610470b33757dda742e44","tmkp:aef84f9e6c5b555f69449e5f4a8757866e97d54c081e42d96dc516790384808a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6171400","PMID:15893350","PMC4452233","PMID:17997295","PMC8047763","PMC7467080","PMC6338015"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9993762413333334","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"34157570":{"subject":"PUBCHEM.COMPOUND:86287518","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMID:19757065","PMID:19634012","PMC6620293","PMC3987091","PMC6275909"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL) revealed that myocardial apoptosis was extensively present in SAP rats, and IMD infusion led to increased expression of the prosurvival factor Bcl-2, but decreased pro-apoptotic factors Bax and caspase-3.|PMC6275909|IMD(1-53) increased the mRNA and protein expression of Bcl-2 and ratio of Bcl-2 to Bax by 81 and 261%, respectively.|PMID:19757065|IMD(1-53) increased the mRNA and protein expression of Bcl-2 and ratio of Bcl-2 to Bax by 81 and 261%, 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L-DOPA treatment reduced the ERK1/2 response in the lesioned striatum to L-DOPA challenge (p=0.0083 for Treatment by three-way ANOVA).|PMC4464750|In comparison to wt littermates, AC5 KO mice treated with L-DOPA show a reduction of LID and a decrease in the phosphorylation of ERK1/2, MSK1, and histone H3.|PMC7926881|This suggests that ERK1/2 activity may be reduced as dopaminergic neurons die during chronic treatment with L-DOPA.|PMC6905327|There was no significant suppression in dopamine D1 receptor-related and ERK1/2 signaling in the DA-denervated striatum by β-Lapachone-cotreatment with L-DOPA.|PMC7845622|The behavioral protection of long-term treatment with L-DOPA in AC5-KO mice was preceded by a decrease in the phosphorylation levels of PKA substrates ERK (extracellular signal-regulated kinase) 1/2, MSK1 (mitogen- and stress-activated protein kinase 1), and histone H3, levels of which were all increased in the lesioned striatum of wild-type mice.|PMID:25164669","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC2760628","PMC4226453","PMID:25164669","PMC7845622","PMC5343040","PMC6905327","PMC7926881","PMID:17662258","PMC4464750"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7d0c9b259302fb7bdf3e59513938d6e36cc75fd49810391cbf466bcfd227585c","tmkp:50834623b756d96ffbecf89790d6ff3b232631a52cb2bce547752fdba69873eb","tmkp:1f2ce83807551e29f40fdd8db72b6c3a27725e9cdd9134516606c77c302365e2","tmkp:49d9db5dfc4ec3037105c4ee63368c58191e7dbf67f871486a7531932533c161","tmkp:a210aeaef6d19704dded48b00a01d366c3131fda855114036ffbd14d35fb6f65","tmkp:605034ddadb7daee09cc7f20644202a7c7c2329cbfb65fb4daf37010b9c2f907","tmkp:ad3c86eedd8c9be705a9016b97757aa880e02596cd3bbcda3d7e2dcfbc85c16b","tmkp:b144018dcc953c301bf988139f9f6c65edbc852f3f2f2110aaff0d4a95c17cd2","tmkp:c00e5f68b8704348ff606998c115b6afbbdee218421183f124a50ea65996c253","tmkp:8f21b429fd0365c70be8e6ba1d4d1dbaa8b65a90442d3887c6ce5c487aea2b79"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"58801865":{"subject":"PUBCHEM.COMPOUND:2244","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9969376","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Dual antiplatelet therapy with acetylsalicylic acid (ASA) and a P2Y12-receptor antagonist is often used to prevent thrombotic complications after placement of a Pipeline embolization device (PED) for cerebral aneurysm.|PMID:30626980|Dual antiplatelet therapy with acetylsalicylic acid (ASA) and a P2Y12-receptor antagonist is often used to prevent thrombotic complications after placement of a Pipeline embolization device (PED) for cerebral aneurysm.|PMID:30626980|In this case series describing the use of ticagrelor and ASA as dual antiplatelet therapy after PED placement for cerebral aneurysm, there was just one ischemic stroke, which occurred after the dual antiplatelet therapy had been discontinued.|PMID:30626980","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:30626980","PMID:30626980","PMID:30626980"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:65a641fd32017adc372282903bbd6a51bae93cc13ac7528b69c630a96a4faa65","tmkp:02137d6b8380d437f4d9ad99c78ae979252fd992527e1a1c12ca09cacba9fc0a","tmkp:eccdd452915ef92ec27011281587657f4164178dee141eaa9b0f9c2380f00682"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"84147092":{"subject":"PUBCHEM.COMPOUND:4649","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:18636191","PMC6051104","PMID:16679379","PMC7766935","PMID:16088182","PMID:28194878"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:d7dcb00fc24e3f135f2506ac944a6bdbbdf3de57c073a75a7e94c5eff522f114","tmkp:9f974b209495a56848c62a4062d2ac6cb9f794b77c0a57fada9dcfd7570a4c57","tmkp:58f8a9b623050d4f419e51fe7980130ac624307ff4fa492ad34ef433131840ca","tmkp:bcbfd0eeb2d9f56d76939a259666bcb8b385733f8a1d7ed4409f7992f662e3ec","tmkp:df7a847a0d542d00a86c79dd9245052ee6bdad6d419d57c667b0d2131cea4cf3","tmkp:5c37210690ef5a09de98970613e773d1d3659bd38abb38a7b65ed2f092f47aaf"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9997222","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The inhibitory effect of PAs on the expression of VEGF and hypoxia inducible factor 1 subunit alpha (HIF-1α) was also observed in cisplatin-resistant ovarian cancer cells.|PMC7766935","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"10369283":{"subject":"PUBCHEM.COMPOUND:135398744","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9991892","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In vivo, RhoA phosphorylation induced by PKG activation in the aortas of rats treated with sildenafil induced dissociation of Rac1 from GDIα and activation of the Rac1 signaling 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both VEGF and PDGF were significantly downregulated after completing a full CMP rush IgE desensitization.|PMC4065666|Both PDGF and VEGF were significantly downregulated (P < 0.05) 6 months after completion of the CMP desensitization process and remained significantly decreased 12 months 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L-DOPA treatment reduced the ERK1/2 response in the lesioned striatum to L-DOPA challenge (p=0.0083 for Treatment by three-way ANOVA).|PMC4464750|In comparison to wt littermates, AC5 KO mice treated with L-DOPA show a reduction of LID and a decrease in the phosphorylation of ERK1/2, MSK1, and histone H3.|PMC7926881|This suggests that ERK1/2 activity may be reduced as dopaminergic neurons die during chronic treatment with L-DOPA.|PMC6905327|There was no significant suppression in dopamine D1 receptor-related and ERK1/2 signaling in the DA-denervated striatum by β-Lapachone-cotreatment with L-DOPA.|PMC7845622|However, administration of Shudipingchan granule with levodopa reduced expression of phosphorylated extracellular signal-regulated kinase 1/2 and Bax, increased tyrosine hydroxylase and Bcl-2, reduced apoptosis in the substantia nigra, and markedly improved 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prednisone therapy of the glucocorticoid sensitive asthmatics was associated with reductions in the percentages of BAL cells expressing mRNA encoding IL-4 and IL-5 and elevation of the percentages of cells expressing mRNA encoding IFN-γ, only a decrease in the percentages of cells expressing mRNA encoding γ was observed in association with prednisone therapy of the glucocorticoid resistant asthmatics.|PMC2376076|Prednisone treatment inhibited the appearance of mRNA, protein, or both for T(H)2 cytokines (IL-4 and IL-5), as well as for IL-2 and transforming growth factor alpha, but did not inhibit increases of immunoreactive GM-CSF in bronchoalveolar lavage fluid.|PMID:11447379|Furthermore, our recent data show that an injection of 300 mg of hydrocortisone (=60 mg prednisone) suppresses the expression of IL-4, LTBR, ADAM-33, and MMP-9 and the plasma concentration of MCP-1.|PMC4302348|Daily prednisone dose had an inverse association with lower serum IL-4, IL6, IL-17A, IL-17E, IL-22 and 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regulate NSC apoptosis by inhibiting the VEGF/PI3K/AKT pathway.|PMC6126114|Sevoflurane minimised bronchoconstriction and cell infiltration, and decreased tumour necrosis factor-α, transforming growth factor-β, vascular endothelial growth factor, sirtuin, catalase and glutathione peroxidase, while increasing nuclear factor erythroid-2-related factor 2 expression.|PMID:24666314|Together, our findings indicate that exposure to a high concentration of sevoflurane (3.5%) in mid-gestation decreases VEGF, PI3K and p-AKT protein levels and induces neural stem cell apoptosis, thereby causing learning and memory dysfunction in the offspring.|PMC6126114|The present study showed that in human neuronal SH-SY5Y cells, the expression of BDNF and VEGF decreased after LPS and sevoflurane exposure for the environmental induction of 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glomerular tuft area, glomerular volume, MVD, VEGF protein expression in glomeruli and VEGF mRNA expression in the renal cortex tissue were significantly increased in diabetic rats and finasteride-treated rats when compared with controls (P < 0.01, P < 0.05).|PMID:25789687|The glomerular tuft area, glomerular volume, MVD, VEGF protein expression in glomeruli and VEGF mRNA expression in the renal cortex tissue were significantly increased in diabetic rats and finasteride-treated rats when compared with controls (P < 0.01, P < 0.05).|PMID:25789687|MVD, VEGF, and HIF-1alpha values were significantly lower statistically (P <0.001) in group 1 compared with group 2. 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we found that increased expression of the mCherry-GLUT1 fusion protein by doxycycline also resulted in accumulation of both Nluc-GLUT1 and endogenous GLUT1 (Fig. 6b).|PMC4928127|(c) Corrected BRET ratios were plotted relative to the concentration of doxycycline used to induce mCherry-GLUT1 expression.|PMC4928127|After selection of stable polyclonal cell lines (293FT/doxGB1) with puromycin, we induced expression of mCherry-GLUT1 with a 2-fold serial dilution of doxycycline for 48 hours to determine the amount of drug required to saturate cells with Glut1.|PMC4928127|A: Rac1, PAK1, GLUT4, and GLUT1 protein expression in soleus and EDL muscles of Rac1 KO mice after doxycycline 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together, these observations suggest that ketamine may suppress the SP-induced activation (IL-6 and IL-8 production) of U373MG cells by inhibiting the phosphorylation of signaling molecules (namely ERK1/2, p38 MAPK and NF-κB), thereby exerting anti‑inflammatory effects.|PMID:28204809|Further study of the molecular mechanisms revealed that ketamine markedly inhibited extracellular signal-regulated kinase (ERK1/2) phosphorylation but not c-Jun N-terminal kinase or p38 mitogen-activated protein kinase stimulated by LPS in microglia.|PMID:19343193|Thus, ketamine may modulate SP-induced inflammatory responses by NK-1R‑expressing cells through the suppression of signaling molecules (such as ERK1/2, p38 MAPK and NF-κB).|PMID:28204809|NMDA induced a neuronal death in the CA1 subregion area of organotypic hippocampal slices and kainic acid in the CA3 region (Figure 2 and Figure 3); these effects were associated with a significant reduction of the hippocampal levels of p-Erk1/2 and p-Akt (Figure 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these findings demonstrated that ketamine attenuated the expression of VEGF and cell migration ability in colorectal cancer cells, probably via blockage of NMDA receptor.|PMID:30817910|NMDA pretreatment elevated the expression level of HIF1α, whereas it decreased the expression of VEGF-A.|PMID:24911952|In chronic ketamine abusers, peripheral blood serum vascular endothelial growth factor (VEGF) protein is reduced.|PMC8228861|compared with NMDA-induced rats (228 ± 18% of control), and VEGF was decreased (133 ± 14%, 133 ± 16%, and 127 ± 20% of control, resp.)|PMC5660823|In accordance, Figure 5(e) presented that the IVB (0.25, 2.5, and 25 mg/ml) treatment decreased the expression of VEGF in the retinas of rats treated with NMDA (168 ± 11%, 137 ± 11%, and 140 ± 18% of control, resp.)|PMC5660823","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"50189768":{"subject":"UMLS:C0024808","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9932803499999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:6dac89295b916e5b6d908d240b12c84cb9dc5cf697ccb12146736dac7e9f14cc","tmkp:435833fa4a710ce619bfcc8f4793f5bb19eebaaa7000847dec513231dcbc3e1f","tmkp:e4ceb6d5d3684071da98bedab3f92821fb406199039ba7bf1cd12f40c0edf773","tmkp:56c6e8b56aaf6d6cf107971f8dd8bb915e0fe26c35720b6c9ccefb9905e66f6c","tmkp:0deff21de24fea15e0acff6d95aaf82ce794ed7590066e56735d5b1ec97610ce","tmkp:cb8e34c57f1dca4875a888a5db4819838eee94b2a90d617a8c7fde142cbe7c12","tmkp:6cbed340531995e7736b0a1721faddd45dbc56b4f9d5409cf680623e751e0131","tmkp:8f883360c9f51255063873f54d7e82f01437a174be16ce47dab0a04d5b5db171","tmkp:ee7d2e713a015e91e1123e2cc6a1c97f21240073f6ede2df231f4b6995709a2c","tmkp:6df28f3a2045583da347882cf4a5c81b88e2ea084339eef2600496a121acfee6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Increased insulin secretion may reflect an augmented insulin response following cannabis use and suggests the potential role of CB1Rs in the gastrointestinal tract.|PMC7295553|Regular cannabis users had significantly greater insulin secretion (as defined by the insulinogenic index 60’) compared with never users, in both the unadjusted (P = 0.049) and all adjusted (P = 0.003; P = 0.004) analyses.|PMC7295553|Increased insulin secretion may reflect an augmented insulin response following cannabis use and suggests the potential role of CB1Rs in the gastrointestinal tract.|PMC7295553|We found cannabis use was significantly associated with the insulinogenic index 60’ (reflecting increased insulin secretion at 60 min following mixed meal) but no significant changes in insulin sensitivity.|PMC7295553|Second, regular cannabis users had significantly greater insulin secretion (as defined by the insulinogenic index 60’) when compared with never cannabis users, whereas insulin sensitivity was not significantly altered in cannabis users.|PMC7295553","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC7295553","PMC4470723","PMC5648282","PMID:23684393","PMC6467701","PMID:31367991"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"53995913":{"subject":"UMLS:C0024808","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.94909817","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2c7d681256bf29fff3194dbd3715ae987292b5686b9af5d0bed47eddfd104e17"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"All children aged <6 years admitted to a tertiary-level pediatric emergency department (PED) for proven cannabis intoxication (compatible symptoms and positive toxicological screening results) during the reference period were included.|PMID:28808073","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:28808073"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"97281453":{"subject":"UMLS:C4529301","object":"NCBIGene:7424","predicate":"biolink:related_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.0004783906666666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b3fb87c70fcfd5e0e4fdad8fd93f67a2ef0da52071f288005e62b142a0c81c87","tmkp:feb6cca464a32efa38cffb8969673096931f8ca837528746b7cfc0dd532ee692","tmkp:cf16674f2e2dca2f922ead3d0d4b72efb2707d026c038419c44dd30fa27bf9d4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6501144","PMC6710319","PMC6501144"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Strategies have been developed to inhibit the VEGF signaling pathway including anti-VEGF antibody therapy (e.g., bevacizumab), anti-VEGFR antibody therapy (e.g., ramucirumab), inhibitors of VEGFR-2 tyrosine kinases (e.g., apatinib), and inhibitors of angiogenic receptor tyrosine kinases (e.g., sunitinib, pazopanib, sorafenib, and regorafenib).|PMC6501144|The patient was restaged as T2N0M1 of lung adenocarcinoma, and chose 6 courses of systematic chemotherapy (pemetrexed combined with nedaplatin) plus bevacizumab, a monoclonal antibody targeting vascular endothelial growth factor at 3 weeks intervals.|PMC6710319|Based on successful phase III trials, antiangiogenic therapeutics, anti-VEGF agents in particular (e.g., sorafenib, bevacizumab, and sunitinib), have entered the clinical practice in the USA and elsewhere.|PMC6501144","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"41139010":{"subject":"UMLS:C4529301","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Bcl-2 inhibitor with bevacizumab is currently an effectively therapeutic strategy to treat B-cell NHL.|PMC7810534|Bevacizumab promotes apoptosis by promoting caspase-3, Bax, PTEN and inhibiting β-catenin, Bcl2, PI3K, Akt, NF-κB.|PMC7377050|Bevacizumab down-regulated the expression of B-cell lymphoma 2 protein (BCL-2), vascular endothelial growth factor (VEGF) and E-cadherin in MCF-7 and inhibited vasculogenesis.|PMID:28358700|Previous studies have demonstrated increased hypoxia following antiangiogenic therapy in human colon cancer xenografts in mice following bevacizumab treatment; also, bevacizumab has been shown to upregulate apoptosis executioner protein cleaved caspase-3 and to downregulate both antiapoptotic protein Bcl-2 and tumor cell proliferation marker p-Erk expressions in human squamous cell carcinoma xenografts in mice.|PMC5660665|Bevacizumab promotes cell apoptosis by promoting caspase-3, Bax, PTEN and inhibiting β-catenin, Bcl2, PI3K, Akt, 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further obtained evidence of the upregulation of the intracellular apoptotic signalling cascade, represented by bcl-2 and bax, the transcription factor p53 and the active form of caspase 3, after pretreatment with mitomycin C.|PMID:11585319|After exposure for 1-2 h to 1 microg/ml MMC, upregulation of COX-2 and Bcl-2 protein expression was noted.|PMID:10803922|After exposure for 24 h to MMC, the expression of COX-2 and Bcl-2 protein was up-regulated, COX-2 levels were down-regulated but Bcl-2 gene expression was not changed significantly in combined treatment group.|PMID:15793875|In the low-dose MMC treatment, the increased mitochondrial p53, Bcl-xL, and Bcl-2 could attenuate apoptosis.|PMID:20126473|α-MMC-HBP led to an upregulation of cleaved PARP and an increase in the Bax/Bcl-2 ratio.|PMID:28090686","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:10803922","PMID:28090686","PMID:11585319","PMC5436365","PMID:15793875","PMID:22895172","PMC2538491","PMC5615796","PMID:20126473"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"86333627":{"subject":"PUBCHEM.COMPOUND:174","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Western blot analysis showed that both H4-PEG and H4-PEG-PT dramatically reduced caspase-3 and caspase-9 protein levels, which further suggested that their photothermal effect was triggered by a mitochondria-induced apoptosis pathway.|PMC7713230|Western blot analysis showed that H4-PEG-PT dramatically reduced caspase-3 and caspase-9 protein levels of 143B cells under 808 nm irradiation (1 W cm−2, Fig. 8k).|PMC7713230|According with this assumption, not surprisingly, the CASP3 appeared downregulated after the treatment with CDs-PEG-BT/IT at their IC50 value (Figure 4b).|PMC7692354|Western blot analysis showed that both H4-PEG and H4-PEG-PT dramatically reduced caspase-3 and caspase-9 protein levels, which further suggested that their photothermal effect was triggered by a mitochondria-induced apoptosis pathway.|PMC7713230|Here we report that a similar application of PEG resulted in marked decreases in apoptotic cell death and caspase-3 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the same time, there was a significant increase in the proportion of cells that express Scgb1a1, a marker for the Club cell secretory lineage (29.9 ± 3.6% vs. 44.0|PMC4639861|Further, treatment of human fetal brain tissue HN cells with NPD1 repressed Aβ42 activation of pro-inflammatory genes and at the same time upregulated antiapoptotic genes encoding Bcl-2, Bcl-xl, and Bfl-1(A1), thus promoting cytoprotection.|PMC6678666|Strikingly, at the same time, these tumors also showed substantial up-regulation, both at the RNA and protein level, of two potent anti-apoptotic genes, Bcl2a1 and Mcl1.|PMC4152557|Hence, Wnt/β-catenin pathway activity likely acts in the same cells to increase expression of col12a1a/b after a 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with PPT showed no significant effect on PDGF-induced proliferation, whereas WAY interestingly suppressed proliferation via inhibition of ERK1/2, Akt, and p38 signaling.|PMC6120801|PPT or E2 also prevented T-H-mediated activation of MAPK in KC.|PMID:16904963|Because PPT administration after T-H was more effective in decreasing Kupffer cell cytokine production and MAPK activation than DPN, it seems that the salutary effects of E2 on Kupffer cell functions are mediated predominantly via ER-α and normalization of MAPK after T-H.|PMC2814122|Since PPT administration after T-H was more effective in decreasing KC cytokine production and MAPK activation than DPN, the salutary effects of E2 on KC functions are mediated predominantly via ER-alpha and normalization of MAPK following T-H.|PMID:16904963|Estradiol's or PPT's inhibition of the fluvoxamine-induced slowing of 5-HT clearance mediated by ERα, was blocked after inhibition of either MAPK/ERK1/2 or PI3K/Akt signaling pathways.|PMID:24423185","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2e0ffcaee704fa7dc43d4ee78af56d7b9610602fc8ebdb9a04555f33cd668adc","tmkp:6b1747c03c4697019bc326a703b135862d45f2300ac4a2a0b27c0b5ce9861aa7","tmkp:eaaa86aa724d05e413454825b0169b280520e6ed5b86edec23c98529e5a1c30b","tmkp:8b8d0c0d2fa1526613f99011aaaf778f666e35aecbdd990f9283a85df10a0608","tmkp:affe6a064c672f332c8af776795d8a761e18f903a6c23c1a9a976f069833ef53","tmkp:f078c265c66960b08aaa42f04a277c5dbd601af9093cab991a6903b075098d9e","tmkp:860e4b6cbc23888f8d17c1aedc28af4218681df553e580bcab437f1fdcde37bc","tmkp:d1df1e779fbf72b39964ea507ea54e72232ca3ce85d13cb8fa3e44172b372408","tmkp:f743cb01d64d5b0db6045c566e3b9ded88af055202e48f7282cbc29849510166","tmkp:18abb5daef12eade4b66330499e0bb43ffa13413db7a6a72ddec92c97f409c2b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"90705597":{"subject":"PUBCHEM.COMPOUND:2554","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC5291934","PMC5291934","PMC7272308","PMC5291934"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f741f5148b96edd53c96e5e27e79d8cd06915c5a37aec8f8997a9991fb223ea8","tmkp:7b7dd9d94b7a072e0ef8c80900b823aec8de3affbfc65e4a031ca25dc02e46a8","tmkp:48601efd4da70f1887e6f8cede9b83ce826f4021d7134c1d776027ac0a9a17f9","tmkp:35835793a83ba31814b277df004e378820ce1cb3eb06a9101ed991c422ce2cd5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"VPA and CBZ treatments caused a decrease in β-Catenin and VEGF levels in SW480 colon cancer cell lines.|PMC5291934|We have shown here that VPA and CBZ decreased the hypoxia-mediated induction of VEGF secretion in the SW480 cell lines.|PMC5291934|CBZ is a small molecule that targets MET, AXL, and VEGF receptors and has recently been approved for treating advanced RCC patients.|PMC7272308|Treatment of SW480 cells with 5 μM of CBZ and 2.5 mM of VPA decreased the VEGF protein levels by 53.07%|PMC5291934","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996381875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"31247442":{"subject":"PUBCHEM.COMPOUND:4649","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:1acd56b8a8c25417ab117adbc4452f1d3bda04f43e0ba4cc217c8ccc0bce075a","tmkp:d5a6366fef45b9e285a282979fbfd29f599c38e29ef8efedb4ea0db8fdf2e62d","tmkp:d9b0d09dd4cbfd06eb9f8338eb6c8d7fbb0666bf75e407d351ba37503b71064b","tmkp:f0d957b49ba3f23a53de917044b4c89d7ac962ea3c6b6bb2da9c07825fe6364c","tmkp:0a9256918abe83a4b91d80752d18ae472738a54736fcf9e7e55b661ce4f6a458","tmkp:98f21445dac424fa26b1cde09818bdf3b7979cec3049f4179604598f6c6b504d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:16928445","PMC2771380","PMC7696651","PMC6015670","PMC2195770","PMID:10397301"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99941397","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"mRNA expression of plasminogen activator inhibitor-1 was increased in PAs of mice with recurrent PE after repetitive thrombin injections and to a lesser extent in DVT mice.|PMC6015670","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"115987908":{"subject":"PUBCHEM.COMPOUND:4946","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The relative expression of Vascular Endothelial Growth Factor (VEGF) in the propranolol group was significantly higher than that in the control group on the 2nd day (p<0.05),|PMID:31173327|The largest increase in expression was evident after 48 hours of treatment with 100 μM of propranolol (approximately 3.5-fold increase in HIF1α, approximately 15-fold increase in VEGF expression, and approximately 15-fold increase in GLUT1 expression; p < 0.0001).|PMC7265978|Propranolol induces HIF-1α, VEGF-A, and GLUT1 mRNA levels at 24 (E) and 48 (F) hours, which has been observed previously in propranolol-treated IHs (n = 3, for each data point).|PMC7265978|Propranolol leads to a discordant increase in VEGF mRNA expression while also reducing intracellular VEGF protein expression due to interference with VEGF mRNA translation.|PMC7265978|Similar to prior reports in infantile hemangiomas, propranolol induced apoptosis and paradoxically increased VEGF-A mRNA expression in patient-derived VHL-HBs and 786-O 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the same condition decreased the levels of PARP-1 and pro-caspase-3, accelerating apoptosis.|PMID:27633352|Consistent with these findings, treating cells with same concentrations of flavonoids resulted in decrease in the expression of PARP1 and increase in levels of cleaved caspase-3 (Figs 4C, S4A).|PMC6062549|The same group also found that PARP-1 inhibition can potentiate the DNA-damaging effects of chemotherapy in EWS-FLI1 or EWS-ERG driven Ewing sarcoma cells.|PMC3823674|Our results showed that AdoMet caused a downregulation of PARP-1 associated to the cleavage of pro-caspase 3, which was specifically mediated by caspase 9.|PMC7795960|However, 4 genes (Cxcl9, Set, Pim1, and Sfrs2) were regulated positively by PARP-1 in response to CD3 stimulation alone, but the same genes were regulated negatively by PARP-1 in the presence of co-stimulation through CD28.|PMC2375913","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a246d2a71bf56fdfecdd264a6fa98b5e29aa69d8a696c5ffcfcf8a77249fd00b","tmkp:adce6d6938647c9d846bdfb5e0c673f41cbbdb8857ad8a5a9d64650675a47ec6","tmkp:248ca0c7548f235c551f53f514d4ecb23f9fafcff82f878b0058621230834e17","tmkp:974443a3f0b0c1c092b7b96f85ae03c38066a77f3f9b1938ea31e6132b035948","tmkp:de9500bf9cf04106b38ac8c5522460080e216b999361cfac8db824363b352255","tmkp:37ceeb17d295dcdfec6f7bcbef8f8f6e49091327e2dedac16490b8d5d32f1066","tmkp:c29356e91d48dafbc45ec7ca2ed64b35c38161028e0640b0daebc2d8d78e7169","tmkp:754540176e307c2dd4458d93299dafeaa3c8facd9a892c128dacea610466bbcd","tmkp:dab4273f9f4762fc381eb4a2aa42f5c5dfd014bd6b8170415185645fc033838b","tmkp:08ce57e6e76a86aaeecf2d932f4bf7aeda14ae49905f94f83b67527a35c3552f"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"37489517":{"subject":"PUBCHEM.COMPOUND:6131","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3586600","PMC8120237","PMC8017502"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"The reduced inflammatory response in CMP treated mice was associated with a reduced production of TNFα and IL-4 in MLNs [Figure 3D].|PMC3586600|These results correlated significantly with the reduced secretion of the type 2 cytokines IL-4 and IL-5 by CMP-stimulated spleen cells in Ti-treated mice (p<0.0001).|PMC8120237|Overexpression of the proinflammatory factors, IL-1β, TNF-α, IL-6, and IL-8, and down-regulation of the anti-inflammatory factors IL-4 and IL-10 play an important role in CMP .|PMC8017502","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:93f55c27baf7025bef26f40164981f09d19df6c0ac2cef503130326b6a3fcd33","tmkp:187b74a0f96b911db9f8975a8da5ba7720e4830620f8042827a930f7aa4ba8cc","tmkp:2149a315d996caaf53b7b6158ab6f156ae151108da7b858e925726d4b8e749bc"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9995054099999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"96986006":{"subject":"PUBCHEM.COMPOUND:977","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6008318","PMC7568562","PMC7031416","PMC3682829","PMC6262377","PMID:20795759","PMC2815002","PMC4281343","PMC7352796"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7e9f3de6390250ec245ba619a57af8507769a217c5612e57d715b7ac51269a00","tmkp:ab9b759ed10ad3ba163e9cae538d7af68668a5c08735f5e50236849eec437e06","tmkp:7b4df18a7cacefeee640dbb4e29184be613bac3e386327eb67a28e90eb55d4a2","tmkp:9632a0182283bf00851fa20b0baaffb6e5dabbf38e7f65418ea4a4ec0a2e481e","tmkp:a1bff519419312eb6eb3b1e6965b09532c0c2efcaf775a145d25b8bc9002b27f","tmkp:404c2df1f12f89cc217f6955fdff3b49f5a96592c3798e0aabb74b1ae9dcbe6e","tmkp:82f90fff780b6f8dec2ba9e8506243f785475097c0eaac4261aa4a82ed573e2d","tmkp:56e9052514c388d8e2e09c2381d58cec1b3835acdaf565cbb8c7c90006680d4d","tmkp:97b1d83b31782759defe8ca5e0368b0f6d86bb2e8f9b97c9ea123279c4e9fbe0","tmkp:96585e1ed876ccdedb46559f61ba12a78c147ac07dbc2d188d91b309e7a9effd"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Hyperbaric oxygen exposure resulted in increased levels of VEGF, MMP-2 and MMP-9, and when mice were treated with sulodexide, a dose-dependent reduction in VEGF, MMP-2 and MMP-9 levels was observed.|PMC4281343|After 6 h in culture, levels of the CNS-specific transcripts B1B4 and B5E2 as well as VEGF transcripts were increased in cultures exposed to 1% oxygen in comparison to cells cultured in 20% O2.|PMC7031416|The expression of VEGF and IGF-1 was up-regulated in ASC cultured at 1% oxygen for 13 days compared with 4 days.|PMID:20795759|As expected, oxygen-exposed rats experienced a 4-fold increase in retinal VEGF compared to room air controls (Figure 5).|PMC2815002|At p14, VEGF expression may be increased as a result of previous exposure to 10% oxygen.|PMC3682829","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.995005150386598","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"83394073":{"subject":"PUBCHEM.COMPOUND:439501","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:28905075","PMC8085498"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:186f302e3b2d113b04dcd70cc54a1f6e03ad5091ab3ea5e23464b4f8cb12fd55","tmkp:d602510fd2d3bdc5f233ad3be29b5f5ca5b8519c077397c57435deac3c516458"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Furthermore, treatment with ouabain decreased IL-4 and IL-13 levels on BALF.|PMID:28905075|Furthermore, in a model of airway allergic inflammation, ouabain decreased the levels of IL-13 and IL-4 in bronchoalveolar lavage fluid, cell migration into peribronchiolar and perivascular areas, and mucus production in bronchioles.|PMC8085498","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99969845","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"56893039":{"subject":"PUBCHEM.COMPOUND:2803","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:361801499cbbc4bae587a7971475fe7485d5c1d9b6ee184ede8f063930e9c756","tmkp:fd9a39a8fbe6dec4ab5b639e8a87084992d40234b9b428c1a835ee0fcd54189c","tmkp:331780b588927819ffcaa09b83b9a82c989544a5f680fc8a1dbd712e49158209"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Clonidine enhances PED in young rats (p<0.001) but decreases it in old rats (p=0.038).|PMID:22653903|Rauwolscine (P = 0.803) and ARC239 (P = 0.236) abolished clonidine-induced PED improvement.|PMID:20523216|In a previous study, we showed that clonidine, an ??-adrenoceptor agonist, administered prior to hypoxia improves post-hypoxic contractility (PC) and endothelium-dependent dilatation (PED) in isolated young rat aortas.|PMID:22653903","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9918755166666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:22653903","PMID:20523216","PMID:22653903"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"128853726":{"subject":"UNII:15C2VL427D","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9892816261904762","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In addition, one eye developed a retinal hemorrhage and a recurrent PED just after the third injection of aflibercept.|PMC3935506|In addition, one eye developed a retinal hemorrhage and a recurrent PED just after the third injection of aflibercept.|PMID:24591809|One day after the third monthly injection of aflibercept, a subretinal hemorrhage and recurrent PED were observed.|PMC3935506|After three monthly injections of aflibercept, a recurrent large PED with SRF can be seen.|PMC3935506|All cases had received intravitreal aflibercept injection due to the presence of intraretinal/subretinal fluid and pigment epithelial detachment (PED), as detected by optical coherence tomography (OCT), despite having received intravitreal ranibizumab.|PMC4407797","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC3935506","PMID:24591809","PMC3935506","PMC3935506","PMC4407797"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:72a4f1491e57c917ab9caae7309822759b90463fbffb7d70ec8e004f70bfdfac","tmkp:eafc54e32514766edd023510aaffeff66ef5a5fd09b000fff7e078bad1527eda","tmkp:d79be8293e8aa461a19321ff81675db0caaa72e316d3ed2931a70957afa6e70c","tmkp:50152b476ed12833e34d84acb3dc688246bb631c84ba6ff469447acaf11f0716","tmkp:243a45f191c6e306e772746a12fba36ef25a3bb96878bff90bfb4f26a124884e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"18970189":{"subject":"PUBCHEM.COMPOUND:3033","object":"MONDO:0012805","predicate":"biolink:contributes_to","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99896216","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Association between the use of diclofenac sodium (DfNa) eyedrops and the development of a postkeratoplasty persistent epithelial defect (PED) of the cornea were studied.|PMID:8575187","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:8575187"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:09dd59a22f6ab5ca3c3ea21562c81c533bb1b3b9a651413fb01352e78693ff2a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"9879049":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Finkelman et al. have previously reported that IL-4 treatment significantly increased the number of MMC in both WT and STAT6−/− mice and that a much larger increase was observed in the latter, indicating that signaling through STAT6 seems to suppress IL-4 induction of MMC.|PMC2212862|Hogan and colleagues have recently demonstrated that IL-4, signaling via IL-4Rα induces MMC9 in a BATF-dependent mechanism, nicely linking the observed roles of IL-9 and IL-4 in mast cell homeostasis.|PMC7759531","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e8b584abb2cca4de69b126acaba799fa56f074e8b705d54ab146989f1144a89e","tmkp:5d481cd74214d2a3668168e1eca656d2011f673fe2a5a389c36444be6b772753","tmkp:da02ecd3ff43eba507e0f7b9cb4af963b25bc885e7a25a9a2008a628b318170f","tmkp:0f1c044a90358b549e12f1df46642dccb336b3776f8c0c46baac82b0b722f8de","tmkp:058f6441c08bbca9c3422d767e6b6f6c6c202dbce625d52bf407f0d257edcfaa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2212862","PMC2249738","PMC7759531","PMC6859295"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99816281","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"66008478":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"During MMC treatment, targeting of CCN2 improved cytotoxicity of MMC and promoted MMC-induced apoptosis, probably by inhibiting activation of proliferation-related Erk1/2 and survival-related Akt pathways.|PMC5630414|Compared to a single agent alone, MMC combined with minocycline resulted in cytotoxicity and cell growth inhibition synergistically in NSCLC cells, accompanied with reduced activation of phospho-ERK1/2, and reduced Rad51 protein levels.|PMID:26212550|A decrease in thymidine phosphorylase, ERCC1 and RAD51 can also be observed with this combination and with mitomycin C and curcumin, which is due to the inhibition of ERK1/2 activity and an increase in their ubiquitin-mediated 26S proteasome degradation.|PMC7710985|When treated with mitomycin C (MMC), CCN2-scilencing UBC cells showed lower survival and higher apoptotic rates and these effects were probably mediated via inactivation of Akt and Erk 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agreement with the essential role of solute carrier family 2 member 1(Glut 1/Slc2a1) phosphoglycerate kinase 1 (Pgk1) and multi-drug resistance protein 1 (MDR1) in maintaining epithelial integrity after toxic stimuli, we validated that hydrogen-water treatment dramatically increased the expression levels of Glut1, Pgk1 and MDR1 in the small intestine tissues of TAI-treated mice (Figures 2e–g).|PMC5799803|Additionally, in the presence of water-soluble cinnamon extract, the expression of genes coding glucose transporter (GLUT) increased 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contrast, treatment before hemorrhage with the beta-adrenergic receptor antagonist propranolol was associated with increases in mRNA levels for IL-1beta, TNF-alpha, and TGF-beta1, which were greater than those present in untreated hemorrhaged mice, and did not prevent hemorrhage-associated increases in lung IL-1beta 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experiments of ROS level and caspase-3 activity further confirmed the results of flow cytometry, PUE@TPP/PEG-PE micelles reduced the ROS level and Caspase-3 activity more significantly when compared to the PUE@PEG-PE micelles and free PUE (Figure 7C and D).|PMC6814317|As shown in Fig. 6g–j, the I/R injury induced the expression of Caspase-3 and BAX, and reduced the expression of Bcl-2 in the Vehicle group, and the DATS@MION-PEG-LF exhibited decreased levels of Caspase-3 and BAX, and increased levels of Bcl-2, respectively.|PMC7866762|When H/R injured H9c2 cells were cultured with CsA, CsA@PLGA-PEG and CsA@PLGA-PEG-SS31, the cleaved caspase-3 level in H/R injured H9c2 cells was decreased.|PMC6346555|When H/R injured H9c2 cells were cultured with CsA, CsA@PLGA-PEG and CsA@PLGA-PEG-SS31, the cleaved caspase-3 level in H/R injured H9c2 cells was decreased.|PMC6346555","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"30493123":{"subject":"PUBCHEM.COMPOUND:5280934","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The results revealed that ALA pretreatment significantly decreased the ulcer index, the gastric levels of MDA, TNF-α, PAI-1, and iNOS protein expression while increased the gastric levels of TAC as well as improved the histopathological appearance of gastric tissues.|PMID:29486337|We also found that ALA attenuated TGF-beta-stimulated PAI-1 mRNA expression, and inhibited PAI-1 promoter activity in liver cells; this effect was mediated by Smads and the JNK and ERK pathways.|PMID:20153726|We also found that ALA attenuated TGF-beta-stimulated PAI-1 mRNA expression, and inhibited PAI-1 promoter activity in liver cells; this effect was mediated by Smads and the JNK and ERK pathways.|PMID:20153726|We found that ALA markedly inhibited BDL-induced hepatic fibrosis and PAI-1 expression.|PMID:20153726|In a rat model of bile duct ligation (BDL)-induced liver fibrosis ALA downregulated the hepatic inhibitor-1 of the plasminogen activator inhibitor-1 (PAI-1) expression by inhibiting the TGF-β signaling mediators, like Smad3, activator protein-1 (AP1), and specificity protein 1 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administration increased albuminuria, renal matrix accumulation, TGF-beta 1, fibronectin, PAI-1, blood L-arginine, L-citrulline, BUN and blood and urine NOx levels, while protein restriction reduced these parameters.|PMID:12631354|In addition, the CsA-induced up-regulated expression of TGF-beta1, PAI-1, and the matrix proteins biglycan, fibronectin, and collagen I was significantly increased with L-NAME and strikingly improved with L-Arg.|PMID:10972680|Relative kidney weight, collagen content, fibronectin, macrophage infiltrate, CTGF, Col I, MMP2, TNF-α, CD68, Arg2, and SGK-1 were increased (p<0.05) in aldosterone + salt–treated rats, being reduced by spironolactone (p<0.05).|PMC4701403","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:10972680","PMC4701403","PMID:10720952","PMID:12631354","PMID:3242846","PMC4959021","PMID:3009364"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9920860333333333","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"26232903":{"subject":"PUBCHEM.COMPOUND:36314","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"It was shown that paclitaxel treatment induces microglia dysregulation in the dorsal horn of the spinal cord and increases the expression of cannabinoid type 2 receptor (CB2), and of the chemokines, CCL2 and interleukin (IL-6, IL-4 and IL-10).|PMC6993945|Paclitaxel also activates the ceramide-sphingosine 1- phosphate pathway, blocks sphingosine 1-phosphate receptor subtype 1 (S1PR1), ameliorated paclitaxel-induced CIPN, and decreased TNF-α and IL-1β production while increasing IL-4 and IL-10 release in the spinal cord.|PMC6627296|In addition, up-regulated T-bet/GATA-3 together with significantly increased mRNA expression of IL-4, IL-10, IFN-gamma and IL-12 by splenocytes, as well as the proliferative responses of splenocytes to Con A, LPS and OVA were observed in paclitaxel-adjuvanted 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promoted cell death due to apoptosis ((A), p < 0.05 vs. control) and inhibited the expression of B-cell lymphoma 2 (BCL-2), Cyclin D1 (CCND1) and Proto-Oncogene C-Myc (c-Myc) genes in HTB-35 cells (B).|PMC6073805|MET treatment also increased the proportion of apoptotic drug‐sensitive and drug‐resistant breast cancer cells, induced cleavage of caspase‐3, increased BAX expression and decreased BCL2 expression (Figure 2).|PMC7214175|The pro-apoptotic proteins such as cleaved caspase-3, cleaved caspase-9, Bak, Bax, and Cyto-C were up-regulated, whereas the anti-apoptotic protein (Bcl-2) was down-regulated in a concentration-dependent manner in MET-treated cells compared with the controls (Figure 2F).|PMC7171495|MET + PTX-treated cells exhibited decreased expression of Bcl-2 protein, and increased expression of caspase-3/9, Bax, PARP, Cyto-C and P53 proteins.|PMC6444335|In addition, MET increased the activity of caspase-3, increased the expression of Bax protein and decreased that of Bcl-2 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proteins are controlling the activity of Rho GTPases locally by activating or inhibiting RhoA and Rac1, resulting in cells migrating away from each other upon collision (Figure 1; Sebbagh and Borg,).|PMC6361784|Recently, it has been reported that Wnt/PCP signaling promotes RhoA activity and inhibits Rac1 in neural crest and human GNS-3314 glioblastoma cells.|PMC2824771|In this process, PCP-mediated RhoA activity inhibits Rac1 in order to regulate directional 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effect of betaine on pathologic retinal neovascularization via suppression of reactive oxygen species mediated vascular endothelial growth factor signaling|PMC8124599|Antiangiogenic effect of betaine on pathologic retinal neovascularization via suppression of reactive oxygen species mediated vascular endothelial growth factor signaling.|PMID:27473515|Our data suggest that betaine has an anti-angiogenic effect on pathologic retinal neovascularization via suppression of ROS mediated VEGF signaling.|PMID:27473515|In addition, betaine treatment alleviated diabetes-induced vascularization by suppressing VEGF and HIF-1α expression via downregulation of pAkt expression in the retina of the STZ-induced diabetic rats.|PMC4464397|A lower dose of betaine exerted a more potent inhibitory effect on the number VEGF-positive cells (Fig. 1, lower panel).|PMC4464397","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:0a01d41b9599c681bd26c8fef05ae0ff2a700b5b4be0b46725ba703f6fab2ce7","tmkp:25ca10cc24c957c4acd7964932c2ba7fbc6d3f4b674becd7f0088de98993e9f3","tmkp:e906656dcd6f87882decd005f90b63c326227360eb0d9bbe9102aa71289887a5","tmkp:e91f274624aa858aac3eb74fd26af9e47883bc965c2287405640618386b94e73","tmkp:d8281542f557f23f86ab3faba7caf7097695305e33f4a6fda5ab71826ea671fa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC8124599","PMID:27473515","PMID:27473515","PMC4464397","PMC4464397"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9984926407692308","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"55239091":{"subject":"PUBCHEM.COMPOUND:2244","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9992924","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"D. HT29 cells (1×106) were cultured with platelets (1×108) in the presence of vehicle (DMSO) or EP4 antagonist (L-161,982, 10 μM) for 40h; the migratory capacity was assessed by Boyden chamber, as described in the legend to Figure 2. E. In HT29 cells cultured alone (1×106) or cocultured with platelets pre-treated with vehicle (DMSO) or aspirin (300μM), the fold induction of RAC1 mRNA was assessed by qPCR.|PMC5078026","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5078026"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7a787abe0641496ab62b3434f5fa50d0de0fee22080242f9c3b14bccaf688a69","tmkp:07c13b919d135aa9d7d25b1943a319b55650d921ad1c1f53517aa9c3159c3577"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"88795531":{"subject":"PUBCHEM.COMPOUND:253602","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dff738cff8d95d52e3c2a9480013dc1fff866160b267382b4941c4a762d97496","tmkp:d90252484c15d05efe79bf908f410ec686baafe51bad9bb756ea66d41559a281","tmkp:71daa7343ead94917a3bff2b6f1213380a2fbedae6699abcdf87b7bcd40229c2","tmkp:48494a98ef2ae13148ea7a825566daccf89cf620c771a51548643b85725b56d7","tmkp:2b6e68ad86fa6d1c2d131a99917dfbb76c76b063c38ce4ffd98dad5e58b8c9b5","tmkp:963e58e4f1679eb94a9b87cded82c4985efea05492d93c3dfffcda8c80c85374"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Upon inhibition of RNA synthesis by actinomycin D, GLUT1 mRNA content decreased with a half-life of 1.9 +/- 0.4 h in control cells, while in contrast, GLUT1 mRNA half-life was 4.6 +/- 0.8 h in cells exposed to 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of the milk proteins β- and γ-casein were also markedly reduced in Rac1−/− mammary alveoli, confirming that pups died from severe malnourishment (Figures 2D, 2E, and S3).|PMC5022528","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"18690278":{"subject":"PUBCHEM.COMPOUND:253602","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"(I, L, O, R) Anisomycin treatment at E14.5 suppresses cell death (caspase 3, red) in P0 ric8a single (L) and s1pr1/ric8a compound mutant (O) striata, to levels similar to wildtype (I).|PMC5492999|In our experiment, we found that the upregulated levels of P-JNK and cleaved caspase-3 that had been induced by Dox were downregulated by the overexpression of sFRP1, but these effects were diminished by anisomycin (50 μM) treatment 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factors assessment, following treatment revealed the mRNA expression level of BDNF, GDNF and VEGF could be significantly up- regulated at various time points, mainly by 1 mM VPA.|PMID:30904572|VPA enhances postischemic angiogenesis via upregulation of HIF-1α and the downstream pro-angiogenic factors VEGF and MMP-2/9.|PMC6248271|In addition to enhancing HDAC inhibition, VPA potentiated MCAO-induced HIF-1α accumulation and upregulated VEGF protein levels and MMP-2/9 activities in the ipsilateral cortex on days 7 and 14 post-MCAO.|PMC3429729|The transcription factor hypoxia-inducible factor-1α and its downstream proangiogenic factors, vascular endothelial growth factor and matrix metalloproteinase-2/9, were upregulated after middle cerebral artery occlusion and significantly potentiated by VPA in the ipsilateral cortex.|PMID:22811460|As shown in Fig. 2a, the expression levels of 6 secreted proteins (GCSF, GM-CSF, M-CSF, PDGF Rα, PDGF Rβ, and PDGF-AA) were decreased and those of 4 secreted proteins (AR, EGFR, TGF-β2, and VEGF) were increased in VPA-treated cells, compared with the 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17β-oestradiol, PPT and insulin increased sGC α1 protein expression and inhibited β1, whereas co-incubation of 17β-oestradiol/insulin or PPT/insulin induced increases of the two isoforms α1 and β1.|PMID:20887556|At 4 weeks after PIT, mice treated with E2, 17α-E2, PPT, DPN or G1 showed protection of islet-graft beta cell mass (Fig. 2a, b) associated with a rise in human serum insulin concentrations compared with vehicle-treated PIT mice (Fig. 2c).|PMC3536964|In addition, increment of pancreatic insulin content by PPT, E2 and BPA was blocked by the ERK1/2 inhibitor PD98059.|PMC2323613|Remarkably, the increase in insulin content by PPT mimicked the inverted-U dose response described for E2.|PMC2323613|Increasing brain insulin concentrations using intranasal insulin administration increased PPT in PCOS sheep without any effects on blood glucose 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independent experimental models of HCC showed that the antitumoral properties of Sorafenib were related to a decrease in Trx1 expression, SNO-CD95 and caspase-8 activity (Fig. 5 and Supplementary Fig. 4).|PMC7210585|In the present studies i.e., Figure 1, we have found that sorafenib and sildenafil interact to kill both CD95 null HuH7 cells and hepatoma cells that express CD95 (HEPG2, HEP3B), though drug‐combination killing appears to be more efficient in HEPG2 and HEP3B cells.|PMC4835179|Sorafenib, a broad-spectrum kinase inhibitor targeting the RAF–MEK–ERK pathway, enhanced sensitization to TRAIL- or FAS-mediated apoptosis by downregulation of cFLIP in endometrial carcinoma cell lines that are resistant to TRAIL or 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barrier.|PMID:18387950","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"127559588":{"subject":"UMLS:C2740652","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:95827aad3ffd1049222f1d0f3cc60e993c4605366c427daa227669826abde619","tmkp:de49dad2eac073293d0fb432702e0426ed095efd3bdf4e34cd5cebd95ba2884c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.999701765","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6393461","PMC6393461"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Cytokine levels of IL-4, IL-5, IL-10, IL-13 and IFN-γ were significantly decreased in groups treated with onion extract.|PMC6393461|Oliveira et al. have reported that oral administration of onion extract can reduce the production of inflammatory cytokines such as IL-4, IL-5, and IL-13 in a murine allergic 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was a significant upregulation in Akt expression in L6 myotubes on quercetin pretreatment.|PMC5462925|Quercetin attenuates cell apoptosis in focal cerebral ischemia rat brain via activation of BDNF-TrkB-PI3K/Akt signaling pathway|PMC3706611|Quercetin attenuates cell apoptosis in focal cerebral ischemia rat brain via activation of BDNF-TrkB-PI3K/Akt signaling pathway|PMC5223001|Quercetin Attenuates Cell Apoptosis in Focal Cerebral Ischemia Rat Brain via Activation of BDNF-TrkB-PI3K/Akt Signaling Pathway|PMC8111446|Quercetin attenuates cell apoptosis in focal cerebral ischemia rat brain via activation of BDNF-TrkB-PI3K/Akt signaling 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expression, being accompanied by the delayed ulcer healing.|PMID:9073148|Indomethacin reduced TGF-beta 1 levels over time, but the surface roughness effect was still evident at 4 days.|PMID:11168271|Maximal IL-8 release was achieved with 10 ng/ml of TGF-beta1 after 16 h of incubation, which was inhibited by the transcription inhibitor actinomycin D and the corticosteroid dexamethasone but was not affected by the nonselective COX inhibitor indomethacin and the selective COX-2 inhibitor NS-398 despite their inhibition on TGF-beta1-induced PGE(2) release.|PMID:10893219|Inhibition of prostaglandin synthesis by indomethacin blocks surface-roughness-dependent decreases in cell proliferation and increases in alkaline phosphatase activity and the production of osteocalcin and TGF-beta1.|PMID:11255188|Indomethacin (1 microM), flurbiprofen (1 microM), and meclofenamic acid (1 microM) completely abolished the stimulatory effect of TGF-beta 1 on PGE2 and 6-keto-PGF 1 alpha formation without 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report that amiodarone promoted cell proliferation and collagen Ⅰ secretion, induced α-SMA and vimentin protein and mRNA expression accompanied by increased phosphorylation of ERK1/2 and p38 MAPK, and furthermore, PD98059 and SB203580 remarkably reduced the proliferative response of HELFs compared with amiodarone group and greatly attenuated α-SMA, vimentin and collagen Ⅰ protein production induced by 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upregulation of TGF-beta1 implies a role for this ligand as an effector of apoptosis induction in response to alpha1-blockade or finasteride therapy of BPH patients.|PMID:11170131|Expression of the angiogenesis pathway genes transforming growth factor beta 1 (TGFB1), endothelin (EDN1), TGFalpha (TGFA), and VEGFR1 was upregulated in LNCaP cells, and at least 7 out of 21 genes were upregulated in PC3 cells treated with finasteride (25 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Quercetin and baicalein reduced MCT-induced increased liver malondialdehyde (MDA) amount and enhanced the nuclear translocation of nuclear factor erythroid 2-related factor 2 (Nrf2).|PMID:27979702|The polyphenols catechin and quercetin transcriptionally repress PAI-1 gene expression in cultured HCAEC; the 251-bp fragment that maps to nt −800 and −549 in the PAI-1 promoter likely mediates Quer-initiated PAI-1 repression.|PMC3521593|A recent study conducted in cultured human coronary artery endothelial cells has also demonstrated a beneficial effect of polyphenols (ie, catechin and quercetin) on the expression of the plasminogen activator inhibitor-1 gene, potentially providing a further biological explanation to the cardiovascular protective role of these 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activates MAPK/ERK pathway associated with autophagy impairment a Representative western blot of p-ERK and ERK after PPA treatment.|PMC7268420|PPA also interferes with the neuroinflammatory response, oxidative stress and alters the mitogen-activated protein kinase (MAPK) signaling pathways, and increases the level of the extracellular signal-regulated kinase (ERK).|PMC7996534|PPA1 and PPB1 display powerful biologic activities including activation of mitogen-activated protein kinase (MAPK) and induction of glutathione-S-transferase (GST), defense genes, and phytoalexins.|PMID:12713542|Consistent with this report, our results showed that the MAPK/ERK pathway is activated during autophagy maturation impairment in PPA-induced cells.|PMC7268420|This effect inhibits PPA2‐mediated dephosphorylation of ERK1/2, resulting in prolonged activation of ERK1/2 and activation of survival proteins, such as protein kinase B (Akt) 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of TMPRSS4-overexpressing DU145 cells in suspension with KRT1853 and IMD-0354 at 5~10 μM resulted in increased anoikis in a dose-dependent manner (Fig. 4C), which was accompanied by an induction of cleaved caspase-3 and PARP as well as reduction of bcl-2 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interest, a peculiar metabolism seems to be associated with the resistance to PI3K/mTOR axis inhibitors: a metabolomic study carried out on 30 primary samples exposed to 4 molecular inhibitors (rapamycin, GDC-0941, human insulin, indomethacin), targeting this pathway with different selectivity, identified the proline/glutamine and the arachidonic acid metabolism as markers of AML cell resistance to these agents.|PMC7072383|Administration of indomethacin to patients with type 2 diabetes mellitus stimulates endogenous glucose production and inhibits insulin secretion.|PMID:11733868|Both indomethacin and L-NMMA inhibited insulin-induced vasodilation, while propranolol had no effect.|PMID:9217894|We conclude that indomethacin stimulates endogenous glucose production in patients with type 2 diabetes mellitus by inhibition of insulin secretion.|PMID:11733868|3. 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anticancer drugs, such as methotrexate, docetaxel, and doxorubicin, can also activate the Akt/CDK2 (cyclin dependent kinase) pathway to promote, rather than suppress, cell death.|PMC2838407|To assess the role of PI3K/Akt/mTOR signaling pathway in MTX-induced renal injury and the effect of GB on this pathway, we checked the phosphorylation levels of PI3K, Akt, mTOR in the renal tissue of all experimental groups as presented in Figure 3. MTX induced a significant activation in the phosphorylation of PI3K (A) by 4.9-fold with the activation of the p-Akt (B), and p-mTOR (C) proteins by 3.4-fold and 3-fold, respectively, when compared to the NC group.|PMC6920877|Furthermore, our results revealed a significant upregulation of the PI3K/Akt/mTOR pathway in MTX-treated rats and this may be explained by what was reported about the capability TGF-β in activating the PI3K/Akt/mTOR pathway.|PMC6920877|Moreover, the MTX-mediated upregulation of phospho-Akt in eWAT and liver was blocked in KO mice (Figure 4E).|PMC7840179|MTX potentiates AICAr-induced AMPK activation, mTOR inhibition and Akt activation in ALL cell lines (C).|PMC3053424","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"5431880":{"subject":"PUBCHEM.COMPOUND:2083","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7215681"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:44ec27df1dbc9b1981580b415d6ed04cf784f1ea70ee4eadfe20104e8b2638f2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Indeed, β2AR activation with salbutamol completely blocked Aldo-induced PAI-1 mRNA expression in ARVMs (Figure 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OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|However, OPC31260 and Tolvaptan significantly reduced vascular endothelial growth factor (VEGF) protein levels, an important angiogenic growth factor in the tumors compared to vehicle treatment (Fig-5E, F), while dDAVP did not affect VEGF levels.|PMC7007354|VEGF protein levels were unaffected in Caki-1 cells treated for 16h with dDAVP, but were significantly reduced by Tolvaptan and OPC31260 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protein content was reduced 65% in soleus and 90% in EDL from doxycycline-treated inducible muscle-specific Rac1 KO mice compared with WT control mice (Fig. 6A).|PMC3609592|Using this system, we demonstrate that doxycycline and cumate addition suppress Rac1-dependent motility in a subpopulation-specific and temporally-controlled manner.|PMC3954980|After doxycycline treatment of inducible muscle-specific Rac1 KO mice, Rac1 protein content was decreased by 85 and 90% in soleus and EDL, respectively, compared with control (untreated WT) mice (Fig. 3A).|PMC3661612|When the tumor size reached ~150 mm3, mice were injected with DDP intraperitoneally (4 mg/kg weekly), and fed with doxycycline (doxy) (2 mg/ml) to induce Rac1 knockdown (indicated by the arrow).|PMC7081201|Rac1 inhibitor and Y-27632 were purchased from Wako (Osaka, Japan), AG1478 from Merck (Darmstadt, Germany), and doxycycline (Dox) from Clontech (Mountain View, CA).|PMC3661186","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:23fb18ed1541efbbcee6a03f6309afd6fde23e736c984643387babba3050a994","tmkp:2bdb2cb6c9decba9a6b78cf3f5a1b6528983875aa20ffc02fa624a4b08296360","tmkp:73f91b69a75e066626f976d144532318d94e4bfe7a504a5a0c13732317595bac","tmkp:cf5000a18fe0679c2c0ed21c1e3b30741d1172d7b8c371a772e0c43dd39d90e7","tmkp:67a31d0fd12de6b5d6ba09730468a49ed250ed740c427d4cfb956b21d13832ae","tmkp:7dabc5d1501388d4232bd1dfea0a852af2ea92b4f529dc2b4295bc5908a9ecb8","tmkp:24258d1d5083766b25f2d99c3b48fb7814b36de20992e16c260cc87e86e7ce9d","tmkp:5f8e7cc2ed429f529c3e1db706a0240c47448b1f180581179adc09622c41624c","tmkp:92e1302ef66d37f8ed97a7aceeb4bff7b2effae30a05efd0a99fb4da35e5a432","tmkp:ece1b99d9b563f2f13bc14549f7a9c953217ace0548122751ff000fffe4a1fbb"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"22528383":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:7424","predicate":"biolink:related_to","attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.00028815","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6697704"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:24f859d3378a05a40f915c4c635ab595a8f62ea6528ca914acb1a4ba11feb7aa"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Approval of sorafenib (multi-kinase inhibitor of vascular endothelial growth factor (VEGF), platelet-derived growth factor (PDGF), and Raf kinases) was the first systemic therapy to conclusively demonstrate an improvement in overall survival in patients with advanced HCC.|PMC6697704","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"45022127":{"subject":"PUBCHEM.COMPOUND:2803","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:29463871","PMID:26632178","PMID:24055020","PMC5559446","PMID:15505117"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"At 21 days, clonidine withdrawal triggered rebound 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remarkable effect of quercetin was the intensive reduction of PCOS-IR and significant induction of uterine GLUT4 and ERα gene expression; it could thus be a possible effective treatment for PCOS and its complications, IR and infertility.|PMID:30103849|Pretreatment of quercetin, at 100 μM showed a 14-fold increase in GLUT4 mRNA levels relative to control.|PMC5462925|Also, it was revealed that quercetin as a flavonoid compound improved the utilization of glucose through the increase Glut-4 gene expression and glycogen synthesis in myotubes.|PMC6079346|In addition, hepatic mRNA expressions of both INSR and GLUT4 significantly increased in 1% OPE or quercetin administration compared with the diabetic control (P < 0.05, Figure 6).|PMC3074560|Herein we found that quercetin pretreatment caused a significant up regulation of both mRNA and protein levels of GLUT4 in L6 myotubes.|PMC5462925","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6035882","PMC6079346","PMC8073144","PMC3526129","PMC5462925","PMID:30103849","PMC8125960","PMC3074560","PMID:24343960"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9921112526666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:dcdbc220cd94859d0b4ad9c92a36bd5bd14bd751a973b5caccd4a28d560cb106","tmkp:1a0bf0aec2d1f36d7cc61b65dd3b71e2dc35bc20d4bccf6425268332e968ccfc","tmkp:e68786c707c2470ef697d91d7e9d33e83c8df52212cce84f9a71de2617cd9674","tmkp:3932ea2cb732698f5f91aeb4e59de0dbb58d3b61d0c715628eb284f11471875b","tmkp:35028512c376664a3728ac477b4c8ba5014db26f3fb791f655491f6a24299b19","tmkp:dc97376bf8b2ed71781c715a8e3641303b78c6bf10d7983d6f462f624955aab5","tmkp:b2f6b6609c367d476a303908c6964d7a36d6c1c8766c650b7c7fd18d1b8d546d","tmkp:faf38e559c72e9f5f10a869e7f3e093c969438534002e7468b93d9a367bc917e","tmkp:b4cc9b97bc4106ed97c3ca5966866c361a4c1e8850e9af1e445b68a10d94bbc8","tmkp:3a67ffde8472e209bac66817f7f6d2a15360125db93199a2bdddfbe5b01f3405"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"113207998":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:13f0ad47adfcdcf8767f6e639f80d1b4d2eb4e6230dfa3a2ad6b8869442a5555","tmkp:fdc0a5b3bde954f8d5b5d2a16bfa77cbd92ff384b99a61a7dd6348801a75025a","tmkp:3a73497e2728be1fc51905f3bf164572070b724051d01a8c53838b55b9daf747","tmkp:f556744d744ebd43e52802c8a82c16ab01c60e2d9ef1cfb2682a1d7ed72f81f0","tmkp:8811022a41ede75506540f21d64a48d5b3be6227b788d65517d4a282f827d16a","tmkp:477690fbaef3860da745f0707de52e5ae95232e7224e6844d25e1402de875739","tmkp:8d68f73f638955011a9f55c75359e838bdaedc66e5940bba6d0e5d62ab97d47a","tmkp:22e2d9adf9d24e10092830d7e0547e5af4f886ec7a007b337b4fc0950527d9e2","tmkp:3397a27afa741aebb4051f66af7e1aee519728536ea566ddc19104158eff57d6","tmkp:102590b8af15b639b50178f3bedc8651a9f785ba24aaa9cc6bd0ba1f7bdd5726"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.994898748","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:24984066","PMC6241369","PMC6384979","PMC3942917","PMC5040020","PMC4653342","PMID:22526928"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"M1 water treatment increased the mRNA and protein levels of glucose regulation protein 78 (GRP78) and C/EBP homologous protein (CHOP), and decreased the mRNA levels of B-cell lymphoma 2 (Bcl-2).|PMID:22526928|The hot-water extract of AB fruiting body preparations inhibited cell growth through apoptosis via the downregulation of Bcl-2, caspase-3 activation, and PARP cleavage in the human leukemic U937 cell (Jin et al., 2007).|PMC3942917|Ethanol and water extracts significantly modulated Bax and Bcl-2 mRNA expression levels in MCF-7 cells in a concentration-dependent manner, with Bax expression being significantly upregulated (p = 0.001) and Bcl-2 significantly down-regulated (p = 0.002).|PMC6384979|In the present study, the mRNA expression levels of bax and caspase-3 were significantly up-regulated (P < 0.05) after exposure of DU145 and PC-3 cells to the methanol and water extracts, whereas the expression of bcl-2 was down-regulated (P < 0.05).|PMC4653342|In our study, we observed that hydrogen-rich water exhibited anti-apoptotic effects by directly inducing Bcl-2 expression and indirectly downregulating the Bax/Bcl-2 ratio.|PMC5040020","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"14960369":{"subject":"PUBCHEM.COMPOUND:216239","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9972906286440678","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:12c2639af163b3ff29fa1e74a0150fc6bff35e2b7784978790f5114e614e12e6","tmkp:b6ffe2ec9061ff53a1461072ac82df34c2d134b4e58375b9bc298f5d97974124","tmkp:84cbc956f1e3912b72eb926e562fd6164b09d77bffa7efdd15327f48667b90ad","tmkp:ff23988324cbce6acb225e630eeb946853b4b6136c76367adb9d8e47cf13b01c","tmkp:afbcea5d66e67747bd8a7ecbe7bcc39fdb3ee162853649f6fb5d09af47749c86","tmkp:9990aa17adcc330c28fa1090e915edd19026cd25679c8db315e05c51472f5952","tmkp:2ab96c05360f17486a07a969e54600b496dd9442fac7ef47c8bfe8ad3c2d858f","tmkp:fee927756dcdd48e71ae5f266c410d7da7842a4b8bd0db32c90836e2445002e2","tmkp:ba13735f0189ac5277adc6372c2504aadd4ccad47fc46e5bd8223e1469d7ac76","tmkp:268390ae7c5118c2d0dcdcae534c38fbd63bde5dc8c5e39d2112343ee8d1abc3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Sorafenib did not detectably affect the expression of the other Bcl-2 family members BCL-xL, BAK, and BAX but significantly suppressed the expression of Bcl-2.|PMC4547411|ATRA and Sorafenib can be developed as a novel drug combination therapy for AML patients because this drug combination augments apoptosis by inhibiting Bcl-2 and Mcl-1.|PMC4775303|These findings suggest that combining sorafenib with agents that inhibit Mcl-1 and Bcl-2/Bcl-xL such as obatoclax may represent a novel and potentially effective strategy in AML.|PMID:22446485|In LM3 cells, capsaicin and sorafenib combination treatment achieved a markedly stronger induction of apoptosis by increasing caspase-3, Bax and poly(ADP-ribose) polymerase activity and inhibiting Bcl-2, and induction of autophagy by upregulating the levels of beclin-1 and LC3A/B II, enhancing P62 degradation.|PMC6196646|Notably, Tiam1 siRNA or sorafenib alone obviously increased p27 level, but reduced Mcl-1 and bcl-2 levels in xenografted nude mice, and their combinations reached the best effect.|PMID:24852430","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4775303","PMID:22446485","PMID:24852430","PMC3342476","PMC6196646","PMC4547411","PMC5095038","PMC3388571","PMC6520777","PMC3573056"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"99695383":{"subject":"UNII:ZL1R02VT79","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Also, in the HARBOR study, a greater reduction of PED height was found for patients receiving the largest dose of ranibizumab (2.0 mg), with a trend for more injections being necessary for PEDs increasing in height.|PMC6250287|There was a trend for greater PED resolution in eyes treated with the 2?mg dose of ranibizumab.|PMC7708599|To our knowledge, this is the first case presenting with complete resolution of PED after a single ranibizumab injection.|PMID:21373383|To our knowledge, this is the first case presenting with complete resolution of PED after a single ranibizumab injection.|PMC3047744|To describe the management of a large PED secondary to RAP with bimonthly, half-dose ranibizumab.|PMC3680079","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6250287","PMC7708599","PMID:21373383","PMC3047744","PMC3680079"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.995501385","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:eadf2c1a31f8792c6a47b9b4e906b227a5daaf9f9fa662b412b42136e1a0b6b3","tmkp:9dc8f3a9ca19c9ca8c711f51a26ce111637b7fa0a695ccac4962695dcf55b282","tmkp:0c0942ad86ee1586dd3ddd596bc857d163f29896a7c1188a0edd617a3a4c36aa","tmkp:444633636b89b7b9f9aa7b75ced25eb270ae5aedf9c38c5f3755f5bbe77c15a2","tmkp:a23806318fe6b9d110df991a2961a7a197c4a6da805ce7ad39ffc8210b90c148"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"127491895":{"subject":"PUBCHEM.COMPOUND:3345","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Fentanyl (400 µg/kg) administered intraperitoneally to mice increased brain glucose transporter 1 (GLUT-1) and VEGF mRNA levels and concomitant use of naloxone (2.0 mg/kg) suppressed this induction within 12 h.|PMC8128984|We found that fentanyl increased the expression of key molecules (p-GSK-3β, β-catenin) and target genes (Cyclin D1, CD44, VEGF, and c-Jun) in Wnt/β-catenin signaling pathway (Figure 5A).|PMC5526971|Fentanyl augments NO concentration in wounds, which triggers VEGF synthesis in keratinocytes.|PMC5421968","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.9953375000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3eb6eb46f97489c7ab25402f8e17818649e6480400662246e88c7a3e9f991e6d","tmkp:21bd22a8b4cc79d7d3024dbf4057216c3001c9cc5868e917eed17587b7eaa173","tmkp:ffd64fc68c2492b15a1e6d9646dca47ab70d71c89654d28b6e561b86f80a5209","tmkp:0893cf3da80b303ea1eac8966c5eda13a63d063a1dc73d311d25f138ad05365a","tmkp:02a7acc89958c91f596f4e38a4aa7be932a55b52e6cd54698f3a9be88851a94f","tmkp:93acdea267f53d7b537e1a3f56bf7e98d1172ce0b2135f23298c660022564d34","tmkp:aa994b5ccd7a96a8ed4a8c3d3cc03352309a81d46d869cafd51786352a0cd6b2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:24807396","PMC7652233","PMC5526971","PMC5421968","PMC8128984"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"116940406":{"subject":"PUBCHEM.COMPOUND:135398748","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:900eb7b0dd1133c4d37c4919ca9089c9619c756d8c1f6100a00264c12ba9b628","tmkp:f6485807042d886924533d282845d0c2eb912c3c657f7108efc488440b95433c","tmkp:9b8379ca69b37cfaed932a2e189794864e260130ac6b97603454f00301fa486c","tmkp:6a72e4aa27332cc8a37b21dda6fba007f859fc12890e88f718722009801d876b","tmkp:d49784153ef464c1b1c7300a08362afdad649ddb56de661268a78c1e83d7c0c1","tmkp:f882d7c53f633757703d36c503116ee14c66b7b322e1e15b45d60c650c82fbac","tmkp:fcb5a5d4fef4ed744445a53681b493cbd054c5e116d6823660328ba8d3b0bdd5","tmkp:38a77423a9fe6f57113042efec9445f62f499b600d7cd92331ea863939c157d6","tmkp:77c4290800dd7f776b7f22684b3570e8f43422a8bfd24d8115aee0265f6b4a1b","tmkp:685ed56208b19402544d67cf0ddb425b3cfaa1981095a2e4418675f87d6fee9a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.999296083846154","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Compared with lymphocytes incubated with PCV2 alone, those incubated with PCV2 and BAY11-7082 showed increased levels of IL-4 (from 12 h to 48 h) and decreased levels of IL-12 (from 6 h to 24 h), indicating that the changes in IL-4 and IL-12 expression were regulated via the NF-κB signal pathway.|PMC4026386|The levels of IL-4 after 12, 24 and 48 h in the group coincubated with PCV2 and BAY11-7082 were higher than in the PCV2 group, and the levels of IL-12 after 6, 12 and 24 h in the PCV2 and BAY11-7082 coincubation group were lower than in the control group (P<0.05) (Fig. 2B).|PMC4026386|Data also indicate that IL-5-producing cells are poorly represented in naive mice splenocytes stimulated with PMA/ionomycin, whereas the number of Th2 cells, represented by the higher frequency of cells producing IL-5 and IL-4, was consistently increased in splenocytes from mice immunized with PCV13 at either booster doses.|PMC8239470|In our analyses of serum cytokine profiles, IL-4 level in PHA-stimulated cultures was higher in PCV and nAMD patients than that in healthy controls.|PMC4895798|We found that PRV causes upregulation of IL-4, IL-12p40, and IFN-γ mRNA expression, while PCV2 causes mRNA upregulation of IL-4, IL-10, and IL-12p40.|PMID:24668628","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:14645926","PMC4026386","PMID:24668628","PMC4895798","PMC8239470","PMC6410029","PMID:31176418"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"39160283":{"subject":"UNII:15C2VL427D","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:3a34556ff094ea3e95af5fab70b018b3a3a6652e51e0d45cd8d44d804a208123","tmkp:079513dd68e4ac6c520246eca8607da669df9ce774bee259b323a97cbc6d0a05"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC8069662"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Aflibercept 1×-treated ARPE-19 cells showed upregulation of VEGF-A (1.12-fold, p = 0.67), HIF-1α (1.03-fold, p = 0.63), GPX3A (1.13-fold, p = 0.49), BCL2L13 (1.26-fold, p = 0.05), CASPASE-3 (1.21-fold, p = 0.04), CASPASE-9 (1.32-fold, p = 0.003) and IL-1β (1.38-fold, p = 0.22); and downregulation of SOD2 (0.76-fold, p = 0.14) and IL-18 (0.95-fold, p = 0.051), compared to untreated cells (Table 2, Figure 2).|PMC8069662","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99950314","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"87572552":{"subject":"PUBCHEM.COMPOUND:54729367","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Treatment with doxycycline in drinking water will drive an increase in the expression of VEGF that results in severe vascular leakage and exudative retinal detachment within 4–5 days.|PMC6939309|VEGF-C expression was activated in the respiratory tract of double transgenic CCSP-rtTA/tetO-VEGF-C mice at ages ranging from late gestation to adult by administration of doxycycline.|PMC3969887|The mRNA expression levels of CRT, VEGF, and GAP43 were confirmed by real-time PCR and were increased after doxycycline treatment.|PMC5593816|VEGF levels were higher after the injection of TGF-beta(2) than after administration of talc or doxycycline.|PMID:11779736|Upregulation of FGF-2 synthesis by addition of doxycycline resulted in a dramatic increase in VEGF expression.|PMC2132998","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4154507cdea318de65cc63edaa157bf970d31428b3d8dff82174748f91ad6520","tmkp:cf0a197f01e7ac28b9a97064d26e2ec2745604fcffa1ea25cbadf8dc6f25cf93","tmkp:e7c3845d03c03ce8eb4a169bc5a2d47d17ab6ace1eb73bbaa16a000e164c8ad2","tmkp:37517bb9f020d18467b36b3e4804b28d9d34afc835040fe054568f82b00d8396","tmkp:fded26e3f19923742699703a60ef6306707974e93633e18ade3d7c98757857a0","tmkp:ef9124dd80cf71b9543eddf6e80befbd6b94c438af5db00713ae847b7764b8ce","tmkp:719ba05286d9d67f355261f423c97df8898433871c82134cab9fdafcd2c5cf2a","tmkp:4b00aa0b0af5ca62a27da59eedc72e49981e1932ff6700f1181048e2f99b15b5","tmkp:1b2accc85e20ecaabfc8ac5e2d793759c04671284e447f2823196ba452f028f7","tmkp:27c62e705a24479f60bc10736b4734887f1f7bf0f0fcf0ab2bbb87a0322be2a7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC3881588","PMID:25268699","PMC6276763","PMC6939309","PMC3969887","PMID:11779736","PMC8105415","PMC5593816","PMC2132998"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9912667585074627","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"45420482":{"subject":"PUBCHEM.COMPOUND:135398748","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC4470199","PMID:23664208","PMC6895252","PMID:29924037","PMC7904418","PMC5111116","PMC4076260","PMC7705396"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"The mean cumulative number of anti-VEGF injections was significantly lower in PCV group (4.51 for AMD-CNV, 3.43 for PCV, p = 0.021).|PMC4076260|This theory is supported by previous findings that aqueous levels of VEGF are lower in PCV than in CNV-AMD.|PMC4470199|Intravitreal corticosteroids may therefore be useful in the treatment of PCV as they show a mild blocking of VEGF and a strong anti-inflammatory effect.|PMC5111116|Decreased levels of VEGF detected 1 week after PDT for PCV seems to reflect acute damage of vascular endothelial cells, one of the VEGF expression sites in PCV.|PMID:23664208|The rates of retreatment from 12 to 23 months were significantly higher in eyes with SRD at 6 and 12 months than in those without SRD (P = .004 and P < .001).In conclusion, during 24 months of antivascular endothelial growth factor (VEGF) therapy using ranibizumab for PCV, BCVA was maintained in those with good visual acuity at baseline.|PMID:29924037","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9936451139999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:193ca6663efe6b8a5a0b2eb6fad615859068986764e9f32beee938d63fbe9af8","tmkp:3beef66030bdd717b6a02ad8e2a00d2e5c69e9e551ad52c2eb819f1f6a717ca3","tmkp:27eda9f9f0131d63b8800b1ca96535dd70ef36aea7479a2beb73099275cace4a","tmkp:0f8d6ea6bfc13a47bea9cb8ce162bd91255fb27495d6ed14e4f2fd63831aac3c","tmkp:70ff37e1afd847603b9453900ea2628b05dae5ab3be5b81bd9e9b45c96054cb5","tmkp:e1d0a087a23993ab819fbd693d162bfe6806030aef9952c048077671d94ee37a","tmkp:394934ec7db0b383eff5290aca94e039287b84c603d31725c49e264274f2d9b0","tmkp:c85097fe179f2cecb14946404f67ef4a5bda291b3244933d3af84d630f93bc72","tmkp:7fa7b769670cb4704b118fe589ab89bac2fea5b6fb5b71a7b2f5691888ae4a79","tmkp:65bef9d1c31092b29c9e98f51ab0234ae17047e30648ca006d79dfc848ace21c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"30203352":{"subject":"PUBCHEM.COMPOUND:2803","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"However, after 1 day's withdrawal of clonidine, the rise in the serum insulin level induced by glucose was approximately 2-fold larger in clonidine-treated rats as compared to that in control rats.|PMID:3885047|These results indicate that the enhancement of serum insulin response to glucose following clonidine treatment is mainly attributable to the hyper-responsiveness developed in the pancreatic B-cells.|PMID:3885047|Increase in insulin response to glucose in the rat chronically treated with clonidine.|PMID:3885047|Pancreatic insulin and liver glycogen contents were significantly higher in the clonidine-treated than in the untreated diabetic rats.|PMID:1814806|Insulin content per islet of the clonidine-treated rat was slightly larger than that of control 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of PARP1 expression was achieved by Doxycycline treatment (1000ng/ml).|PMC7408484|The increase of cleavage of PARP1 was detected in shHP1γ-infected R-U937 cells and shHP1γ-infected R-HL-60 cells treated with doxycycline, while the presence of doxycycline did not affect on the PARP1 cleavage in shHP1γ-infected U937 cells and shHP1γ-infected HL-60 cells (Figure 3B).|PMC6198088|Generation of doxycycline-inducible HA-PARP1 cell line|PMC7408484|H9 cells treated with doxycycline demonstrated decreased levels of procaspase-3 and increased cleavage of PARP-1 in a dose dependent manner (Figure 5A), suggesting a potential role for 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6E).|PMC3394761","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"61512426":{"subject":"UMLS:C5242471","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Considering that macrophages are important players in the inflammatory response, we proposed that the high PAR level found in milk with high SCC could be connected to PARP-1 activation in the increased proportion of the macrophages 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of 3T3-L1-derived adipocytes with prednisone decreased insulin-stimulated glucose uptake (Fig. 3a), phosphorylation of Akt (Fig. 3b), and the expression of IRS-1 (Fig. 3c), GLUT4 (Fig. 3d), and adiponectin (Fig. 3e).|PMC5107914","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"71208507":{"subject":"PUBCHEM.COMPOUND:135398744","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:30721701","PMID:21220057","PMC3548048","PMC5337856","PMC4077707","PMC3914480","PMC6818210","PMID:21948520","PMC6240424","PMID:23140764"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ff9ee7c018a8235cd8bc742eef5360c76ac029b90669646db7097baa5f5243f5","tmkp:b573c3f2724e8a3440e4e0c3d21590ccac3235cd3e8425f16aa94021b380cb90","tmkp:aadde6ac6633462ed52c6eafe41cbb5454d9837b33c5f12a8d122a9c3432c1cd","tmkp:3a481017fd609625d89e450af6e3ccbe8db6fa41416e7580a175fad259aeac73","tmkp:594c93d0253d0566b97e9245d6f129f9e26a9ded68984b3f1c2ae95d5f8f8c40","tmkp:a5b3dd402a74b386120ea0d0553d29e4c30b3242eed2745c34a2de50d27e84d6","tmkp:a490ebbe852e7480376b0b3351f605c06c881c3450e6d4cec538a4671da9e4d7","tmkp:b17ccfb73ab1a4b539a984ada73bf0f73565144e6e42ba4fa809454f03f44cb9","tmkp:14e157d849ec379640c70cf5c9c0f77ea36bc30879ab86a6212a510f11e086c0","tmkp:29af114aeb7b43b144bf9bc1f97703c1a6b82e1bd899823031249a7695c5871a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"In the subacute LVH group, both KMUP-1 and sildenafil administered for 10 days attenuated the LVH in SHRs, with enhanced eNOS/cGMP/PKG and suppressed iNOS/calcineurin A/ERK1/2 expression in the left ventricle.|PMID:23140764|Zhao et al. showed that sildenafil exerts anti-inflammatory effects in vitro in LPS-activated microglial cells by blocking the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) and Mitogen Activated Protein Kinase (MAPK) activation.|PMC5337856|Sildenafil attenuates LPS-induced pro-inflammatory responses through down-regulation of intracellular ROS-related MAPK/NF-қB signaling pathways in N9 microglia |PMC6240424|Sildenafil also blocked IκBα phosphorylation and degradation, inhibited the phosphorylation of mitogen-activated protein kinases (MAPKs), extracellular signal-regulated kinases 1 and 2 (ERK1/2), p38 MAPK, and c-Jun N-terminal kinase (JNK).|PMID:21220057|Sildenafil attenuates LPS-induced pro-inflammatory responses through down-regulation of intracellular ROS-related MAPK/NF-kappaB signaling pathways in N9 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was a comparable reduction to triamcinolone acetonide in cytokines IL1-β, IL-4, IL-6 and CCL17/TARC, a group of cytokines involved in the inflammation processes in the skin (Fig. 6).|PMC7945677|A rank order of potency of the steroids tested for inhibition of IL-4 protein was as follows: triamcinolone > dexamethasone > betamethasone > hydrocortisone.|PMID:9164967","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996818000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ed348bd69453033bbb67502f98ea396b49c3cb239f4f7e78e82104992f29872e","tmkp:076f5ae175c1edef1cfa7c4a098a8adf70c56bfba200b8fbf7391fcb86bae942"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"95557390":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:3565","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996996666666668","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5334174","PMC5723695","PMC7873955","PMC7267058","PMID:21507304","PMC6091064","PMID:25056526","PMID:27168818","PMID:17374136"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Administration of AMD3100 significantly attenuated the influx of inflammatory cells to the airway and reduced the levels of IL-4, IL-5, and IL-13 in an murine asthmatic model either in the lavage fluid and lung homogenate through attenuation of the Th17, cell population.|PMC7267058|The results of the present study demonstrated that administration of AMD3100 significantly decreased airway responsiveness to methacholine, attenuated the influx of inflammatory cells to the airway and reduced the levels of IL-4, IL-5 and IL-13 in the BALF.|PMID:27168818|Importantly, AMD reduced the concentrations of TNF-α, IL-1β, IL-4,IL-6 and IL-8 in the serum, compared to LPS-challenged mice.|PMC6091064|The levels of interleukin 4 and interleukin 5 in whole lung homogenates in the AMD3100 intervention group were lower than those in the untreated asthma group (P<0.05).|PMID:21507304|AMD3100 also reduced IL-4 and IL-10 production of plate-bound anti-CD3 and anti-CD28-stimulated 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found that a high fat and high sucrose diet led to a significant increase in the expression ratio of p-JNK1/JNK1 in the liver by 12 weeks (an index of JNK1 activation; p < 0.001; Figure 1.5A-1.5E),|PMC5348315|We found that a high fat and high sucrose diet led to a significant increase in the expression ratio of p-JNK1/JNK1 in the liver by 12 weeks (an index of JNK1 activation; p < 0.001; Figure 1.5A-1.5E),|PMC5348315|We found that a high fat and high sucrose diet led to a significant increase in the expression ratio of p-JNK1/JNK1 in the liver by 12 weeks (an index of JNK1 activation; p < 0.001; Figure 1.5A-1.5E),|PMC5348315","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"66008449":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:15388795","PMC3261359","PMID:14997384","PMC3071292","PMC4792287"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4099fb51c9084f72bd8f6175aefab85e7c7f03097174c29571e22ccbe0b1129b","tmkp:fd929260c0c3bdef4120d2e7aab8d703aa344c69287ce373575f010513dd1eea","tmkp:3ab01058fbfb5f1137af861cf7aed6892353e97ee931f97c927ba79fb3b94d88","tmkp:d05ef67d2d9849833a7bfdeced04ec767b65660af718be476128a7c6cbbb9649","tmkp:55d86f21ac02ea2dbd31f4a8c8b18f97fd1dc2e3db8890f05ff2e43407773705","tmkp:d3a1e43266bc3bf341a8ab24956f90f930312497d718461f8865af23512d0ab4","tmkp:07a2ed8baccf2a6abe68304c5b117928c8ecb3e5de1156968096264641ff08c5","tmkp:a49dd734fed0c7eb3434446cc97916262d518f26bb3e8d9a39ebb6573970907a"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9984079166666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Pretreatment of glioma cells with the antisense oligonucleotide (OGN) of JNK1 immediately prior to tamoxifen treatment suppressed the expression of phospho-specific JNK1 and the activity of caspase 3. The apoptosis fraction of glioma cells induced by 4-h treatment with 50 microM tamoxifen was decreased from 51% to 28% by pretreatment with the antisense OGN of JNK1 (P<0.003), and to 20% by pretreatment with caspase 3 inhibitor (DEVD-CHO) (P<0.0008).|PMID:14997384|We find that E2, as well as the antiestrogens tamoxifen (TAM) and ICI 182,780 (ICI), inhibit class II MHC expression through activation of the c-Jun N-terminal kinase (JNK) pathway.|PMID:15388795|Genotype analysis of genomic DNA prepared from mammary tissue and cultured epithelial cells demonstrated that tamoxifen caused ablation of the conditional Jnk1 gene (Figure 1A).|PMC3261359","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"103509143":{"subject":"PUBCHEM.COMPOUND:6137","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6886123","PMC3317821","PMC7280013","PMID:16604373"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9980576800000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Given that EGFR or MET activates PARP1 in response to ROS, we speculated that MET and EGFR may physically interact with PARP1.|PMC6886123|On the basis of the above findings, we speculated that EGFR interacts with MET to induce PARP1 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53.07%|PMC5291934","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9996381875","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f98bd82348410530ca020c38b23e58e099dd75473097ca83f85ec804ebdf59d3","tmkp:75212ed39fd63a26f726d75300a3133a5cf5be71af5ffc91e49837b8ee9cac7b","tmkp:191c35845d14d7cb6eb71b4e9df5a8ce3247315540deeb810109ac78872d6ea7","tmkp:4b23bff2e111dde87bfcf2853a247ade2229b39ccf64565c058595fcac1ce314"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"69250578":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:e064885f960e39b4e947646cf0e9bc069b03b5aa808fafaf84214156cf4b09db","tmkp:3b9b104c4620cd3f6cb8d2d9db39c44a85bf0848a365f0e671f19ea1bedb5b1d","tmkp:07ab5f404497bd443159376a78f649279b71e03e29b87e08b4f2e7a923b4ba53","tmkp:6825089f82139f9c8156f6df27152622326bdc32367681a6f9bd80e8e74c5cba","tmkp:3e36a47a0c945a2392d5293c7866c556473fec3941365ec357e322564a507dd2"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:25617811","PMC4436794","PMID:30536359"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"VEGF upregulation by pro-inflammatory stimuli, IFNγ, DNCB or formaldehyde is preceded by the production of IL-8, an acute inflammatory phase cytokine.|PMID:25617811|There was significant upregulation of IL-1α,IL-1β, IL-5, IL-17A, leptin, NGF, VEGF, CXC and CC chemokines (*p < 0.05, unpaired t test) in formalin injected prostate, while expression of BDNF, IFNγ, G-CSF, IL-2, IL-4, IL-10, IL-12p70, IL-13, TNFα remained unchanged between the groups.|PMC4436794","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.9994255000000001","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"55790775":{"subject":"PUBCHEM.COMPOUND:69286","object":"MONDO:0000188","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:4674e6cbbd11642fb58c6ce00da5acee111d108b02c661a0d61f3b3aa9825b39","tmkp:4e01c3bbdc85e13d89829c67dd45e0892be2168e5a836d5f37018e2b6ed5134b","tmkp:94e2321ffe390fb6d951db6a9a224a2f932e79d8ab7955c92470677e587d346c","tmkp:bcf487e4a32bd27849af944582558131be25b5fa03db2f8eb3dd7d2e325ed85a","tmkp:4133c61e1cbbe52422b2e20a00cb44f6b5fd60dbed80504a7a2a6bc30d10f688"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5625655","PMC6860903","PMC7279391","PMC7575481","PMID:30948626"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.999353221","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Fanny Mochel holds a patent on the use of triheptanoin in Huntington disease and GLUT1 deficiency syndrome.|PMC5625655|Long-term follow-up in an open-label trial of triheptanoin in GLUT1 deficiency syndrome: a sustained dramatic effect |PMC6860903|Long-term follow-up in an open-label trial of triheptanoin in GLUT1 deficiency syndrome: A sustained dramatic effect|PMC7279391|Long-term follow-up in an open-label trial of triheptanoin in GLUT1 deficiency syndrome: a sustained dramatic effect|PMC7575481|Long-term follow-up in an open-label trial of triheptanoin in GLUT1 deficiency syndrome: a sustained dramatic effect.|PMID:30948626","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"105334587":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:6890","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"While expression of 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activation of c-Met by fibronectin and a(5)b(1)-integrin regulates ovarian cancer invasion and metastasis|PMC3549019|Ligand-independent activation of c-Met by fibronectin and alpha(5)beta(1)-integrin regulates ovarian cancer invasion and metastasis.|PMC5311074|Ligand-independent activation of c-Met by fibronectin and alpha(5)beta(1)-integrin regulates ovarian cancer invasion and metastasis|PMC4126870|Ligand-independent activation of c-Met by fibronectin and alpha(5)beta(1)-integrin regulates ovarian cancer invasion and metastasis|PMC5601130|Ligand-independent activation of c-Met by fibronectin and alpha(5)beta(1)-integrin regulates ovarian cancer invasion and metastasis|PMC5294249","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"0.99860222","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:1466504","PMC5311074","PMC3549019","PMC5601130","PMID:1572284","PMC5312262","PMC5362815","PMC5294249","PMC4126870","PMC3852538"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:750989779c280285daaa5692686b005e6e2ce1237f319226098c325a7566ed22","tmkp:ed1c6e45d069a1fb942a0209092ccf05c0a30b3438de554ec1a7c7c7d2062f69","tmkp:105712cfd298ce168a467422383e82561aad6ca22a5670c3bf86866966309992","tmkp:1a2f0b2a6a02e89ba940af9d2b28bd7c458d8b98e126af3868a9773238f56038","tmkp:1a61ca878be7c1fd71c4ba9aac35a198e48af8060483587fc12ba20fb4310a1b","tmkp:6f751686fbdc6edc087624c1555def302190eefc4597ee8e75936a1c8ecb651c","tmkp:8611f126374ca54ea67b00d70234f8f5cdd7b2084fa1083161309d3a3e3af352","tmkp:2725689af37fe7df6c9779fe3975744f2b1afee1aa6f040da3051c0556c74924","tmkp:0e11764ff13a5972fbd88b32e16fdeb9eff3c47d0337df8423121c3a5235d5ca","tmkp:27a008d325d2d40f60ae33c35044d800183fb58b1bc6b923e4cf7337d83e84b4"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"91349876":{"subject":"PUBCHEM.COMPOUND:38853","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3704138","PMC3079714","PMID:29485043","PMID:30048978","PMID:18516776","PMC2858240","PMID:19997926","PMC7956652","PMC6280338","PMC5618675"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"At baseline, the aqueous humor levels of sVEGFR-1, sVEGFR-2, VEGF, and PlGF were significantly higher in the AMD group than in the control group.|PMC6280338|Several studies demonstrate an up regulation of VEGF in the fibro-vascular membranes associated with AMD and also in RPE of the patients with AMD.|PMC2858240|Aqueous humor levels of vascular endothelial growth factor, soluble vascular endothelial growth factor receptor (sVEGFR)-1, sVEGFR-2, and inflammatory factors (monocyte chemotactic protein (MCP)-1, interleukin (IL)-6, and IL-8) were significantly higher in the AMD group than in the cataract group (all p < 0.05).|PMID:30048978|In the less common but more aggressive form, wet AMD, hypoxia and inflammation lead to an up-regulation of different growth factors such as VEGF resulting in formation of choroidal neovascularisation.|PMID:18516776|Another pro‐angiogenic factor, VEGF, was also increased in the ischaemic tissue of both P2G and AMD3100‐treated groups at 1 week and 2 weeks after administration and then regressed to the basal level at 3 weeks (Fig. 3C and D).|PMC5618675","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:7886a6ceec7b01744e11ec941ecb7e14fe45d7a15d6cd91e203aa16dbea7f1c3","tmkp:d8e491fac01bb9f39437d5186435979b7872297b621c209882add88f82d2faac","tmkp:1915f8df9a222ed5c0c3236840d9f0eceae9fe6f634a4a0017ef847274920089","tmkp:58d7252188af6a9c20af888ccc4d2a14ffaa0baa80309b47f5e2e7ed95d2b1b4","tmkp:382bdb97909f638890559ab3bcdf5d1753edb58ffce66609441d18f8ab4f3c2f","tmkp:7fddd4a150f110db767f02da651ea6c79a63dbd46623da91da08fe0a891a4733","tmkp:afdcc4c2330896d15ed3945b0b3482bd3000ba179e3db0f1c783911219c50de6","tmkp:d1685002aedb538963af66e1fbb85ad932eeee91b71656e5dad1e01861856379","tmkp:74f0dd759ac035e0b1908bdf823555cc3da42a1fca08b3505ab05ea24ec3c32b","tmkp:b3372ec33e7f418855309461aeea4838f8eddb44aa075ace117e72f7344ffed5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9956428839869281","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"49224177":{"subject":"UMLS:C5242471","object":"NCBIGene:7040","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:a0c23b242d4a0637dd21cad00e8888f771b70109dda20edb7300e88adde0f902","tmkp:67da2f6f43e69b056200a5418053e457ba552c8a6dbdd059b7df8d8cd59cf5a8","tmkp:8fbb26143ebd9ca269e4f69cb4e70c2c9cea56b461a7d79b79af95215999e3d2","tmkp:268b7f4d1d50beb47a09ae6e4c8eeaaba43257d00bbc77978b76264d8bd13ff3","tmkp:1629744376366f6489b722f5a14913ee33be42aefd2016a96a9a27b84a3f5a1f","tmkp:688e8edb11072f8d538eb2da3056ea0c47368515b3e59b9e94bedf4c14d5f75b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In the reference mothers, a significant decrease in TGF-beta1 concentrations was observed between colostrum (650, range 0-8000 pg/ml) and mature milk (250, range 0-8000 pg/ml) (p < 0.05).|PMID:20718928","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:22956078","PMC7216940","PMID:20718928","PMC7538670"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.999716","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"32802145":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:5803fef8b77f329ffb3cb1eefc26f11569a04aac1ac685987d0fc59c66e4d773","tmkp:c041471280439f1d20c8f26e08d51e9c3873b4c99312558d718b9c0d260b8808","tmkp:bef3991af177c9d6f647a7b150f7eefd47154de53e9395cc11b1167c0cef7469","tmkp:4e2f40a2fbe7a1d0bfaf2359fe98064d8eff5aa6b43c31c625133020411c4b16","tmkp:66f80c61a08a301c2625bfd523f44c575a1ae8b93d08add8bf3aa7a51497e82b","tmkp:76f1cc726063cb664c0e16a533e6faedc25f66d6456980210ba51c00ae41f940","tmkp:1724ea20a71644241b8babc88378702fb9334f2bb074ec95e579efd812cd8c55","tmkp:6a13531b64d1f58570e1a9a39055f425f685e99040eecee9a068ece591c798b9","tmkp:9ae82e6c465b88e8eb38b195d368a0ab16609d4c411917c5a46c1c718d2e6940","tmkp:d8d36bbecef69813bf25a7fde5eb901fedefb636838ad18b7386b90fcacbe5c3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC5485940","PMC2823990","PMC3202644","PMC2975514","PMC4216621","PMC4425041","PMC4215528","PMC5513690","PMC5458189","PMC5381968"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In response to acute ethanol treatment, there was an increased Akt activation resulting in decreased nuclear FoxO3a retention and FoxO3a-mediated expression of autophagy genes in FXR KO mice.|PMC4215528|Nevertheless, the levels of phosphorylated Akt and Erk (pAkt and pErk), which are downstream of the receptor tyrosine kinase cascade, were increased in the alcohol group, despite the mixed expression profile at the receptor level.|PMC4425041|Ethanol markedly enhanced arsenic-induced tumor angiogenesis which was attributed to intracellular ROS generation, NADPH oxidase activation, and activation of PI3K/Akt and hypoxia-inducible factor 1 alpha (HIF-1α).|PMC5485940|The hemodynamic effects of ethanol (reductions in BP, CO, and SV) were associated with significant increases in myocardial NOx and myocardial p-nNOS and p-Akt expressions while myocardial p-eNOS remained unchanged.|PMC2975514|Ethanol treatment activated both Flk-1 and Flt-1 as indicated by their phosphorylation, and subsequent stimulation of Akt.|PMC4216621","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9929163088405797","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"32920539":{"subject":"PUBCHEM.COMPOUND:5755","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.983786425","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC6309783","PMC7968946","PMID:20186670","PMID:11197800","PMID:24739614","PMC3756949","PMID:11481854"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a2790b93cbb407863ae78bc9d296ba5969f9f4fdc1bb5420de764a2e057ab9ab","tmkp:880ff7695d02d2419de51ba21ff2a025b56f21f7fec8e1e75854b73470fdead2","tmkp:6e8f0cc790f7e3a976b121ac2ed22b581ee69faccc2a9d9052a12c832d1f8011","tmkp:856c43f7e45588c32c68450f85c38e848b92148995559dbda25e2a727c767d74","tmkp:ff258ca45328bc1a3270b080998c09bb17633d51c3af649db69d39f26fa0a181","tmkp:9ea582ef6e306db4fd8d36eb180d7f1cab4f4e75c30dbc6810b714170efe3560","tmkp:ebbb37dc1df3a7f39e218f77af5ca0ff83914b3480fb10064b0d78b8114a90b3","tmkp:c9e57f49598e3e616818abfc855b6297baa572987142e57e9f8ad5069427fd97","tmkp:1cfde7da26016f2fe101d9e0d8fc8e6a8c5cfe677d17b47b8d2f32c251c0ca95"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"However, VEGF signal was still detected higher in the prednisolone group compared with the sham group (Table 3).|PMC7968946|He presented with a high level of serum vascular endothelial growth factor (VEGF) and RS3PE syndrome-like pitting edema in the extremities, which improved following treatment with low-dose prednisolone.|PMID:24739614|Combination of PDGF-BB and prednisolone ameliorated changes in VEGF and VEGFR2, but decreased angiostatin, PDGFR-β, and Ezh2 (Fig 9C).|PMC6309783|He presented with a high level of serum vascular endothelial growth factor (VEGF) and RS3PE syndrome-like pitting edema in the extremities, which improved following treatment with low-dose prednisolone.|PMID:24739614","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"34535072":{"subject":"PUBCHEM.COMPOUND:2733526","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"We observed that CBX (20 μM) in T47D cells decreases Cx43, BAX, caspase 3 and increases cyclin D1 expression while combination of tamoxifen and CBX decreased caspase 3 and cyclin D1 expression at 72 hr (Figure 8A).|PMC4378591|†P < 0.05, decreased protein levels of cleaved caspase-3 after treatment with tamoxifen plus sulfasalazine vs tamoxifen only.|PMC7262513|Histological analysis confirmed that caspase-3 activation induced by TRA-8 was significantly decreased when tamoxifen was used in combination.|PMID:25084100|In keeping with published data, tamoxifen reduced the percentage of apoptotic cells expressing cleaved caspase-3 (p = 0.02, Poisson regression analysis).|PMID:22048005|†P < 0.05, decreased protein levels of cleaved caspase-3 after treatment with tamoxifen plus sulfasalazine vs tamoxifen 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expression was 0.65- and 0.54-fold lower (p ˂ 0.05) in the HG-Lr and HG-Met groups, respectively, than in HG-Ctrl.|PMC8018548|Conversely, both Cγ and metformin treatments significantly downregulated Jnk1, expression compared to that in the HG-Ctrl group, with this reduction being slightly more pronounced in the group treated with Cγ (0.65- and 0.54-fold in HG-Lr and HG-Met, respectively; p ˂ 0.05) (Figure 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the ability of these cytokines to modulate the expression of PED/PEA-15 has not been explored before, this behavior seems to typically characterize undifferentiated neural cells because the same cytokines down-regulate PED/PEA-15 protein levels in NT2/D1-derived neurons.|PMC2211918|IHC confirmed that PEA-15 protein was downregulated in the breast tumor tissue (T) compared with the paired adjacent normal breast epithelium (N) from the same patient.|PMC4571276|Expression of PEA-15 is downregulated in breast tumor tissues compared with adjacent morphologically normal breast epithelial tissues from the same patient.|PMC4571276","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2211918","PMC4571276","PMC4571276"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99916474","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"57525795":{"subject":"PUBCHEM.COMPOUND:3821","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:f746d351aa841175f0b493a473144f8dd81a1609324f85317a087e2ab305ae86","tmkp:b4c4eb17719a7df77d4126a45fe31387e31ffdc9770b429331d5b1f59e61b16a","tmkp:53a2cc7903ce27c0a8c79664d8ce240174462efc2a726e0fa387b7f09202a6e8","tmkp:1114e891cdd5e20518767c69216851947ac8e71e44c7c52775cd1be0f4d858c3","tmkp:822e86b456c4f12f443cb5719a80f9f00006e42e29726f9b365debd7e069c7b9","tmkp:efff20ba81fbefd8e8bf2ba33e035043b1b05b3d9017fbad48d7f6f56584adb4","tmkp:69c2e9d903b75ba20f52ff0eb88465ad3f2bd1c5366c8d3643ea62f63fbe42dc","tmkp:5d847221ec7bf5686fb27bdbcb59aab10ded717d09662dab60a25603e424df1b","tmkp:6ac88bf595cf71f57d660cf3132af111c67ac8d9e209257d5d99bc2e769fc05f","tmkp:d7abc91f63bbabaef24009a382e5e89a3e528f5bf59d9714bce07463d845556e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Collectively, these findings demonstrated that ketamine attenuated the expression of VEGF and cell migration ability in colorectal cancer cells, probably via blockage of NMDA receptor.|PMID:30817910|In chronic ketamine abusers, peripheral blood serum vascular endothelial growth factor (VEGF) protein is reduced.|PMC8228861|compared with NMDA-induced rats (228 ± 18% of control), and VEGF was decreased (133 ± 14%, 133 ± 16%, and 127 ± 20% of control, resp.)|PMC5660823|In accordance, Figure 5(e) presented that the IVB (0.25, 2.5, and 25 mg/ml) treatment decreased the expression of VEGF in the retinas of rats treated with NMDA (168 ± 11%, 137 ± 11%, and 140 ± 18% of control, resp.)|PMC5660823|In chronic ketamine abusers, peripheral blood serum vascular endothelial growth factor (VEGF) protein is 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milk levels of VEGF, IGF-I and b-FGF were significantly higher (p<0.001).|PMID:20202860|We found that bLF purified from milk increased the mRNA expression of vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF2) in murine osteoblast-like MC3T3-E1 cells and primary murine osteoblasts in a time- and dose-dependent manner.|PMID:21404021|We found that bLF purified from milk increased the mRNA expression of vascular endothelial growth factor (VEGF) and fibroblast growth factor-2 (FGF2) in murine osteoblast-like MC3T3-E1 cells and primary murine osteoblasts in a time- and dose-dependent manner.|PMID:21404021|Bovine milk lactoferrin induces synthesis of the angiogenic factors VEGF and FGF2 in osteoblasts via the p44/p42 MAP kinase pathway.|PMID:21404021|Bovine milk lactoferrin induces synthesis of the angiogenic factors VEGF and FGF2 in osteoblasts via the p44/p42 MAP kinase 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was the trend in VHL-HBs, propranolol led to 1.9- and 1.4-fold increases in GLUT1 and HIF mRNA, respectively (p < 0.05, Fig. 2C).|PMC7265978|Propranolol Induces HIF, VEGF, and GLUT-1 mRNA Expression in VHL-HB Cells|PMC7265978|The largest increase in expression was evident after 48 hours of treatment with 100 μM of propranolol (approximately 3.5-fold increase in HIF1α, approximately 15-fold increase in VEGF expression, and approximately 15-fold increase in GLUT1 expression; p < 0.0001).|PMC7265978|Propranolol induces HIF-1α, VEGF-A, and GLUT1 mRNA levels at 24 (E) and 48 (F) hours, which has been observed previously in propranolol-treated IHs (n = 3, for each data point).|PMC7265978|On treatment with propranolol (50 μM and 100 μM) for 24 or 48 hours, HIF1α, VEGF-A, and GLUT1 mRNA were overexpressed (Fig. 1E and 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potent hepatoprotective effects of PCP on t-BHP-induced injury in human hepatic L02 cells were mainly mediated by mediating ROS clearance and upregulating the expression of B-cell lymphoma 2 protein (Bcl-2) and Bcl 2-associated X (Bax) and downregulating the caspase cleavage products caspase-7, caspase-9, and PARP to attenuate t-BHP-induced hepatocyte apoptosis.|PMC7519454|The potent hepatoprotective effects of PCP on t-BHP-induced injury in human hepatic L02 cells were mainly mediated by mediating ROS clearance and upregulating the expression of B-cell lymphoma 2 protein (Bcl-2) and Bcl 2-associated X (Bax) and downregulating the caspase cleavage products caspase-7, caspase-9, and PARP to attenuate t-BHP-induced hepatocyte 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liposomes loaded with paclitaxel and imatinib have shown effectiveness in promoting cell death and suppressing vascular endothelial growth factor (VEGF) expression in folate-receptor-overexpressing cancer cell lines.|PMC8001342|FR-targeted liposomes loaded with paclitaxel and imatinib have shown effectiveness in promoting cell death and suppressing vascular endothelial growth factor (VEGF) expression in folate-receptor-overexpressing cancer cell lines.|PMC8001342|In murine studies, paclitaxel was able to reduce new vessel formation at low, noncytotoxic doses (0.3 and 6 mg/kg per day in mice) by suppressing VEGF expression.|PMC4475536|Paclitaxel inhibits radiation induced VEGF secretion and enhances radiosensitizing effects in human colon cancer cell HT29|PMC4145830|Paclitaxel inhibits radiation induced VEGF secretion and enhances radiosensitizing effects in human colon cancer cell 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at 200 to approximately 400 micromol significantly inhibited the proliferation of HL-60 cells and induced the cell apoptosis in a time- or concentration-dependent manner; caspase-9, caspase-3, and PARP were cleaved and activated in undergoing apoptotic cells; and the expressions of MEK4, P-JNK, and P-C-Jun were upregulated with the increase of indomethacin concentration.|PMID:15804060|In an in vitro study, 6-OHDA-induced PC12 cells pretreated with celecoxib, indomethacin and ibuprofen for 24 h showed significantly increased cell viability, GSH content, and cytoplasmic level of NF-κB, as well as decreased levels of ROS and several apoptosis biomarkers, including cleaved caspase-3, Bax, P-SAPK/JNK and cleaved PARP.|PMC6877505|In the present study, pretreatment with celecoxib, indomethacin and ibuprofen (2.5 and 5 μM) in PC12 cells treated with 6-OHDA decreased caspase-3 (P<0.001),|PMC6556502|We found that indomethacin treatment blocked the AIE-induced increase of pNF-κB p65 in the 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4A).|PMC3465748","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"100519392":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99962723","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Consistently, decrease in tumor necrosis factor-α level, up-regulation of Bcl-2, and down-regulation of BAX and 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mechanistic study indicated that inhibition of c-Jun N-terminal kinase (JNK) protein phosphorylation, and activator protein (AP)-1 and nuclear factor (NF)-κB activation were involved in the anti-inflammatory actions of HIS in macrophages.|PMID:25128739|The appearance of phosphorylated form of p38 MAPKs and JNK1/2 was inhibited by the singlet oxygen scavenger l-histidine.|PMID:19496992","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"38893763":{"subject":"PUBCHEM.COMPOUND:948","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:04b909a578ac2d4a9fdd6ad0a944425b056074e21d65e276ecfdcf9af70a97a1","tmkp:0608303bfa68731df83e827d15cdbfbe06a75e0ad276cbaf9fc59e6858eb6149","tmkp:16b4972b4dea4a4595ca5cc343bf3ca37c7a35b55c5197102e6e68fdf0e410d9","tmkp:36162c844eb3ec594c5dc7d72e8d042db7b24dd54686f71c81f19d2bcc28591c","tmkp:dfcac4f7cb4498c34218667d62553f2954f61d5354f621c87397a97bf016861b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Collectively, these results illustrate that treatment with 70% nitrous oxide plus l% isoflurane for six hours can induce caspase-3 activation and increase TUNEL positive cells (apoptosis) in H4 naïve cells (without APP overload) and in primary neurons from naïve mice (healthy neurons), which suggest that the nitrous oxide plus isoflurane treatment can induce apoptosis in healthy neurons and independent of APP overexpressing.|PMC2797570|Caspase-3 immunoblotting showed visible increases in protein levels of caspase-3 fragment following treatment with 70% nitrous oxide plus l% isoflurane for six hours as compared to the control condition (Figure 1A).|PMC2797570|Quantification of the Western blot, by determining ratio of cleaved (activated) caspase-3 fragment (17 – 19 kDa) to FL-caspase-3 (35 – 40 kDa), revealed that treatment of nitrous oxide plus isoflurane led to a 264% increase in caspase-3 cleavage (activation) as compared to the control condition (Figure 1B) (P = 0.001).|PMC2797570|Exposure of 5-day-old piglet to the triple anesthesia combination (isoflurane, 0.55-vol% + N2O, 75-vol% + midazolam, 1 mg/kg, i.m.) caused significant caspase-3 activation.|PMC3629548|We were able to show that the treatment with 70% nitrous oxide plus l% isoflurane for six hours or staurosporine (the positive control in the experiments) induced caspase-3 activation as compared to control condition in H4 naïve cells (Figure 2A and 2B): 100% versus 172%, P = 0.0006, and primary neurons from naïve mice (Figure 3A and 3B): 100% versus 154%, P = 0.0357.|PMC2797570","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9987063916666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC2797570","PMC2797570","PMC2797570","PMC3629548","PMC2797570"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"85678483":{"subject":"PUBCHEM.COMPOUND:5743","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:6f94db3a6c3dc0701baee7af0a848be8170f57f162065af008c5ab7f9e0de930","tmkp:767e3d1dedca40e558a5fc6fd7164d2286879a56a034530f80265d1987877dcd","tmkp:b84f127a6e31bb1139b65b6d2001c66301a308843969e1119434918e76f68b06","tmkp:4b89bd4f76964b02042fe3336686bf503cd72bf86b3fbea7dd25febb9e1df193","tmkp:2bc818926c0e88036c318a8a957728688a6d52d2bf05362859c9685119b07ab8","tmkp:30a77f1fb43d6504d00f551a47db8b8cc0782b6e4641d8528fe8f441f1bea09b","tmkp:dfbc68bebbad32954d768da2a817c30fde7422cb4ec4d5723cfe3cdd8bb01ce1","tmkp:a56f1377669e56ae0a4250103bff876d56188faf7f500ac785cd906ede5cab09","tmkp:445e8c44c58aa31d8b12f577f4c8a089935adb2b7e5751d645ffee7a7bd151d1","tmkp:e8d9fb896c95a076cb1048a40a696d46aea7c5aef508d1fbdbad8cd216195047"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Immunostaining, Western, Northern and dot blot analyses showed that dexamethasone caused an increase in levels of fibronectin and collagen type IV in tissue-cultured TM cells.|PMID:9852235|A downregulation of tenascin-C mRNA and an upregulation of fibronectin mRNA expression by dexamethasone was noted.|PMID:7673336|Fibronectin expression was induced in HT1080 using 1uM dexamethasone before Cul3 knockdowns.|PMC3292188|Following dexamethasone treatment, three of the major ligands for αvβ3 integrin, fibronectin and thrombospondins-1 and −2 are upregulated.|PMC5612317|Dexamethasone, TNF-α, IL-1β and LPC treatment of TM cells also led to an increase in the levels of CTGF, fibronectin and collagen type 1 in an autotaxin dependent 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colon cancer, dexamethasone suppresses TGF-β1-induced migration via inhibition of AKT and extracellular signal-regulated kinase (ERK) phosphorylation.|PMC5288347|Again, NPe was as effective as dexamethasone in inhibiting ERK1/2 and NF-κB pathways (Figure 5D,E).|PMC6150367|While the literature on this topic is relatively sparse (and non-existent with respect to trigeminal neurons), there is evidence that a single pre-treatment with Dexamethasone inhibits neurite outgrowth in cultured PC12 cells treated with nerve growth factor, and that it does so by blocking phosphorylation of Akt and ERK1/2 in a glucocorticoid receptor-dependent manner.|PMC6443430|Hence, dexamethasone induced placental and embryonal developmental abnormalities could be associated with reduction of Akt and ERK1/2 activation.|PMID:21512721|Dexamethasone (DEX; 10(-12)-10(-4) M) reduced TNFalpha-induced phosphorylation of ERK-1/-2 and prevented TNFalpha-induced VEGF generation without differences between non-smokers, 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that study, tamoxifen use was associated with an increase in serum VEGF levels; a result consistent with higher platelet derived VEGF levels in tamoxifen users as compared to nonusers.19|PMC5350889|Tamoxifen 1 g and 3 g resulted in a dose-dependent increase in VEGF and endothelin 1 levels, and ovarian follicle reserves were significantly reduced in our experimental model.|PMID:25848212|Vascular endothelial growth factor (VEGF) mRNA and protein levels were higher in MCF7 breast cancer cells and orthotopic tumors after treatment with tamoxifen, as compared with treatment with estrogen.|PMID:11929808|Vascular endothelial growth factor (VEGF) mRNA and protein levels were higher in MCF7 breast cancer cells and orthotopic tumors after treatment with tamoxifen, as compared with treatment with estrogen.|PMID:11929808|Hormonal regulation of VEGF expression has been demonstrated, and some reports indicate that tamoxifen, a partial estrogen receptor agonist, increases VEGF mRNA in breast cancer 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C3, C4, and vascular endothelial growth factor (VEGF) decreased in a linear trend (P < 0.01) from baseline (control) to LAC and HAC.|PMID:27188987|Camel milk treatment attenuated the main components of the fibrovascular tissue, wet weight, vascularization (Hb content), macrophage recruitment (NAG activity), collagen deposition and the levels of vascular endothelial growth factor (VEGF), interleukin (IL)-1β, IL-6, IL-17, tumor necrosis factor-α, and transforming growth factor-β.|PMID:24320686|Cholesterol, C3, C4, and vascular endothelial growth factor (VEGF) decreased in a linear trend (P < 0.01) from baseline (control) to LAC and HAC.|PMID:27188987|Screening milk sialic oligosaccharides for their ability to inhibit VEGF-induced VEGFR-2 phosphorylation.|PMC6802645|Administration of camel milk and its exosomes led to significant downregulation in the expression of the angiogenesis-related gene, VEGF, in tumor tissues as compared to the tumor 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ethanol exposure also inhibited attachment to other substrata, including laminin, fibronectin and vitronectin.|PMID:8583506|Indeed, incubation of astrocytes with ethanol, at concentrations as low as 25 mM (corresponding to 0.115 mg/dl), in the presence of carbachol, followed by wash-out, inhibited the effects of carbachol on axonal length and on minor neurite length by inhibiting phospholipase D. By the same mechanism, ethanol also inhibited carbachol-induced increases in fibronectin and laminin-1 in the astrocyte lysate and in the medium.|PMC3205233|For instance, some components of the extracellular matrix like laminin, fibronectin, and plasminogen activator inhibitor-1 (PAI-1), that are secreted by astrocytes in response to carbachol, are reduced if these cells are exposed to ethanol.|PMC5471499|We had previously shown that ethanol (25, 50 or 100 mM) inhibited carbachol-induced, astrocyte-mediated neuritogenesis in hippocampal neurons in co-culture, as well as carbachol-induced expression and release of fibronectin and laminin-1 in astrocytes.|PMC3205233|We show here that an ethanol extract of HSM produces anti-fibrotic activities as shown by the inhibition of TGF-β1-induced myofibroblast differentiation and myofibroblast marker expression (α-SMA and fibronectin) in human MRC-5 lung fibroblast 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dexamethasone alone (Figure 6).|PMC3257180|Although there were no differences in the quantity of apoptosis between the fetuses of the multiple-course placebo and dexamethasone-treated ewes, the quantity of caspase-3 was lower in the fetuses after the exposure to the multiple dexamethasone courses (Fig. 3).|PMC2692887","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"34998366":{"subject":"UNII:ZL1R02VT79","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:066ed6306b60431eae20dc26648207a433131b9300e59d1116fde92a8edf56ed","tmkp:0818039cd2fc87a0797c94b03c5ab178ca97ee20dd76c84e5152d776e17aa117"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:publications","value":["PMC8069662","PMC8069662"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99971199","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Ranibizumab 2×-treated cells showed downregulation of VEGF-A (0.72-fold, p = 0.20), HIF-1α (0.76-fold, p = 0.008) and IL-1β (0.54-fold, p = 0.04), and upregulation of SOD2 (1.28-fold, p = 0.09), GPX3A (1.09-fold, p = 0.60), BCL2L13 (1.4-fold, p < 0.0001), CASPASE-3 (1.26-fold, p = 0.04), CASPASE-9 (2.82-fold, p < 0.0001) and IL-18 (1.32-fold, p = 0.002) (Table 2, Figure 2).|PMC8069662|ARPE-19 cells treated with ranibizumab 1× showed downregulation of VEGF-A (0.75-fold, p = 0.40), HIF-1α (0.85-fold, p = 0.05), GPX3A (0.96-fold, p = 0.89), and IL-1β (0.84-fold, p = 0.43) and upregulation of SOD2 (1.22-fold, p = 0.16), BCL2L13 (1.21-fold, p > 0.0001), CASPASE-3 (1.73-fold, p = 0.004), CASPASE-9 (1.61-fold, p < 0.0001) and IL-18 (1.67-fold, p < 0.0001) (Table 2, Figure 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there exists a significant increase in pro-inflammatory cytokines, such as IL-1β, IL-2, IL-4, IL-6, IFN-γ, NGF, and COX-2, in bladder tissue in ketamine-associated cystitis.|PMC6820961|Treatment with ketamine alone has also been shown to increase the ratios of Th1/Th2 and IFN-γ/IL-4.|PMC6732974|Gao et al have studied the effect of various concentrations of ketamine (0, 50, 100, 200 μmol/L) on the differenation of human T helper cells in vitro, and found that ketamine dose-dependently decreased TH1 and TH2 cell numbers, TFN-γ and IL-4 level, but increased the ratio of TH1/TH2 and TFN-γ/IL-4 in the presence of phorbol-12-myristate-13-acetate and ionomycin.|PMC5406080|Next, using the calcineurin inhibitor FK506, we implicated this phosphatase in activation of the nuclear factor of activated T-cells (NFAT; a transcription factor activated through calcineurin-mediated dephosphorylation) and propose that this pathway is involved in transcriptional upregulation of the IL-4 synthesis in NMDA-treated neurons.|PMID:30890073|Ketamine and MK-801 decreased TH1 cells, TH2 cells, IFN-γ and IL-4 levels but increased the ratio of TH1/TH2 and IFN-γ/IL-4 in the presence of PMA and 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conformational changes of PED/PEA-15 in ERK2 complex revealed by NMR backbone dynamics.|PMID:22820249|In conclusion, we show for the first time that PED and Rac1 interact and that this interaction modulates cell migration/invasion processes in cancer cells through ERK1/2 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clonidine reduced renal tumor necrosis factor-α (inflammatory marker) and caspase-3 (apoptotic marker) levels, while increased renal prostaglandine E2 and interleukin-10 levels (anti-inflammatory markers).|PMID:29452086|The present study tests the hypothesis that inhibiting nuclear Ca2+ -influx by pretreatment with clonidine, an inhibitor of high affinity Ca2+ -ATPase, will prevent the hypoxia-induced increase in caspase-9 and caspase-3 activity in the cerebral cortex of newborn piglets.|PMID:17268855|The data demonstrate that clonidine administration prior to hypoxia prevents the hypoxia-induced increase in the activity of caspase-9 and 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blot analysis showed that in U373 cells the content of PR isoforms (PR-A and PR-B), EGFR, VEGF and cyclin D1 increased after PPT treatment while in D54 cells only the content of EGFR was increased.|PMID:22142990|However, higher levels of myocardial VEGF were noted in the PPT-treated group compared with controls.|PMID:19628068|However, higher levels of myocardial VEGF were noted in the PPT treated group compared to control.|PMC2774782|In consonance with the more aggressive behaviour of RPt, we found the levels of IL-6, IL-8, and VEGF to be significantly higher than those observed in Pi and PPt.|PMC6875004|Interestingly, the PPT 10 nM group demonstrated significantly greater production of VEGF compared to control (185 ±11 pg/mg protein vs. 138±16 mg/mg protein), whereas DPN showed no effect (figure 7D).|PMC2774782","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:b8f4d26bd3a7f3e92ad8d7252e139eedb5bff00232e604c115b907fc2d865eb8","tmkp:5ef7ef929283ab8f6e0f46b6430d92666efefee0c24300fb92b13a04c553ee74","tmkp:1ab333dfbd674e5abb858f54b4c1463871ea4214c0b8caaf15c3100104a85234","tmkp:ade908ae0cf1c1568ca7c677bf1a66734e8047385bcc482637438399875cfcbf","tmkp:19cdc70a67624b22a8ace14ef5fa5fb29888a7b818d94fa995983f6f512fc0af","tmkp:0fff6d12646d91c58869fbd53cbd15549f4a20d5acf71422af550b560df8a25b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"20715489":{"subject":"PUBCHEM.COMPOUND:7814","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99940294","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f220f2d8bb99c9c2d29202f6a383f57b177165de9fce2232f3b314ad2fcab71d","tmkp:39cf40e66958665c73231a53780cb94fba753bcaf2a88be63b7bdc5eddee3b11","tmkp:c5412f9dbfb69c75afb2ee9b02cbc35c899cb42dff55d57c96f93e399fe6b236","tmkp:6aa90bc65dc181233f983f4ab5eef24ddc75e6a323080f0af34fcf612d83fb9d","tmkp:833f97aca0a4231dfa7dedd018ed25fbd54ce84a899f62549d0b08aa86410b70","tmkp:32322329bcc7ee7a0447991b1a66999e0069492ceda60cb6fbe0df88d4efa764","tmkp:f88ac769de32e86a4023b513a6d32a2511dcf38680af9f44604842a30aa65302","tmkp:199ac0bebf525219a01b9417790c60844d10a5a23c8c9c7aed0ecbd4e1dfe12d","tmkp:a2eb1077a82f2f1b4172bf4cc188966d3fc653d4f04508e37411de311d3bb084"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"The expression of p-mTOR, mTOR, HIF-1α, and VEGF were significantly reduced in 10.0 mg/kg C3C12PPD group compared with control (Figure 5B).|PMC6750213|Since mTOR is one of the targets of AKT, the p-mTOR and its downstream proteins HIF-1α, VEGF were also detected, and it was observed that they were downregulated by 100.0 µmol/L C3C12PPD (Figure 4B).|PMC6750213|Within the limitations of this study, it can be concluded that, rh-IGF-I+rh-VEGF treated sites resulted in greater improvement in PPD reduction, CAL gain as well as in osseous fill after 6 months when compared with rh-VEGF, rh-IGF-I and control sites.|PMID:27790578|Although PPD-type ginsenosides, Rb1 and Rk1, have been reported to inhibit vascular permeability induced by VEGF, lipopolysaccharide, thrombin, or histamine, it is not yet clear whether pro-angiogenic ginsenosides can induce vascular leakage similar to VEGF, or act as a leakage inhibitor, similar to ANG1, FGF and HGF.|PMC6418182","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6750213","PMC7471442","PMID:27790578","PMID:9390328","PMC6418182","PMC5668468"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"129203025":{"subject":"PUBCHEM.COMPOUND:702","object":"NCBIGene:5594","predicate":"biolink:affects","qualifiers":[{"qualifier_type_id":"biolink:object_aspect_qualifier","qualifier_value":"activity"},{"qualifier_type_id":"biolink:qualified_predicate","qualifier_value":"biolink:causes"},{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"decreased"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"10090","value_type_id":"EDAM:data_0006","original_attribute_name":"NCBITaxon"},{"attribute_type_id":"dct:description","value":"decreases 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mice given unsupplemented or PTS-supplemented drinking water had significantly reduced expression of beclin-1 and JNK1 compared to wild-type mice or Ubisol-Q10-treated mice.|PMC6942887|However, there was no significant difference in JNK1 expression between control and 24 μg/mL of Manilkara zapota leaf water extract (P > 0.05).|PMC6241369","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6241369","PMC6942887"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3a8d0abf47649e7424a684c36a2600320fd62e6120a95f63cbea603ccb984579","tmkp:3e044be02df444813d6300067586aaede92f3c42e22583f104c3d2ad943a099c","tmkp:ca00814a0d9f10afefa84a46c21d32bf7884de655aa7280b6b1fb83be3cde586","tmkp:449c8f5a99b87f1adafdd150a13bdf8e60448c7de106169bce381d9e2ab5dc1c","tmkp:ae509b81252fb632e49392077715bd79771400df4a76160140690bdd293fefe4","tmkp:749e7386b56f47a3428440c2b27064cde26ccc7636f4abed1cb6ab29c588cef5","tmkp:f0482546612d2d5babcada21574b63352ca8acaccd90d6a474df6154ebc5839d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"58654042":{"subject":"UMLS:C5242471","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9963057145454545","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Camel milk attenuates methotrexate-induced kidney injury via activation of PI3K/Akt/eNOS signaling and intervention with oxidative aberrations.|PMID:29667662|Camel milk attenuates methotrexate-induced kidney injury via activation of PI3K/Akt/eNOS signaling and intervention with oxidative aberrations|PMC8156492|Camel milk attenuates methotrexate-induced kidney injury via activation of PI3K/Akt/eNOS signaling and intervention with oxidative aberrations|PMC8020251|Camel milk attenuates methotrexate-induced kidney injury via activation of PI3K/Akt/eNOS signaling and intervention with oxidative aberrations|PMC7081586|Camel milk attenuates methotrexate-induced kidney injury via activation of PI3K/Akt/eNOS signaling and intervention with oxidative aberrations|PMC6920877","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:f0350623ea04f1ac7c19b243cadde4c4d6155b9cdd29019c2314eb2186a0fe01","tmkp:32254284bf3ff7fc5520b548cf860925250c9a0c6be17ea51410bddb9ebb0e38","tmkp:912e02fefe11024d33e4055165a6496426e93a81982487529a51233e213180cb","tmkp:94ff92de4c9fd6161c18ed1cff8b191392f9bef5f9811b859f8a9835a0359976","tmkp:afed6be8ab38763efc6bb4010b2efe8298b700ad58348c9a29f20a44ba9b6494","tmkp:9aae328fcbd3c79ade2675050f308c02abdf1bd03fee4994273537b6e27dd2d9","tmkp:ca7391605cb1b2075d17c2f91a7b67bacc844f048461e37422996a9172455128","tmkp:06593cded5ead38978dc9fb751e8fac44a1e9963eb34063f06ef63ecd2d747f9","tmkp:038dec0aca7f0041a458705e382312f969537b51336b6302283b368cc65fb49a","tmkp:3ddc0e00e6792446b54c104e4a6674eb88a7e27f96c55199e7ae0c73ce6561c9"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6920877","PMC5296740","PMC7081586","PMC8020251","PMC8156492","PMID:28176796","PMC5664280","PMID:29667662"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"1302793":{"subject":"PUBCHEM.COMPOUND:2244","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7665072","PMC6532785","PMC5573713","PMC6858356","PMID:26635114","PMID:21617849","PMID:27153943","PMC6323506","PMC5489459","PMC5341967"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:93681546846352783aae318ab87db304c2f8b4a953365212d62713f1790625c0","tmkp:9c2f78f958734a12296c95d25bfa0d1555464947a00b4058014d75b8ff3bd6dd","tmkp:d7eea7324e93e41d471d29e6957a66d64285c6beb02f9f6b9772d301ec944471","tmkp:0e963ede4126ab926be47e9dbc731792e3bc124ed5afb020d8fd514d2e14b5e3","tmkp:234dadbc156fa47382f1bd16d36568298a1c5d0a79b058742062bf98db122635","tmkp:8789e7dd2b69e89c311b23544b70febf3160830641c43ee12263bcd0175112a8","tmkp:f2feb362f362bb522d380b6a09d28c20e14923d826cf878052a5972ef798be85","tmkp:f70b70662d76ac132377582714b28d4d6697e2f205a0ed66e2304cfbcfa36b37","tmkp:5408c63902f0452fa2fd9149e326e5db92cb0df2994b86264fbb47ac0606d21e","tmkp:f9d8102e5b13af6025cdce8f58011214fe9019761c4a46a440d0cafef360eab1"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.9944261117567568","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Moreover, the Akt level in myocardial cells co-treated with GA and aspirin was significantly higher than in those treated with GA alone, and very close to the level in cells treated with aspirin alone.|PMC5489459|Oral treatment with a zinc complex of acetylsalicylic acid prevents diabetic cardiomyopathy in a rat model of type-2 diabetes: activation of the Akt pathway.|PMID:27153943|Oral treatment with a zinc complex of acetylsalicylic acid prevents diabetic cardiomyopathy in a rat model of type-2 diabetes: activation of the Akt pathway.|PMC5573713|Aspirin reduces the apoptotic effect of etoposide via Akt activation and up-regulation of p21(cip).|PMID:21617849|Therefore, we concluded that Akt and mTOR are being activated by SA and ASA, leading to the activation of eNOS which promotes NO-triggered ER stress.|PMC7665072","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"116985680":{"subject":"PUBCHEM.COMPOUND:5746","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"• VEGFR-2 mRNA and protein concentrations and urinary VEGF concentrations were increased in bladders of rats instilled with MMC.|PMID:20735383|It is nteresting to note that expression of angiogenic genes HGF, bFGF, and VEGF was induced at 24 h after Mitomycin C treatment.|PMC6150649|We have previously shown that VEGF111b expression is induced in SKOV3 cells after 100 μg/ml mitomycin C treatment, and VEGF111b protein was detected by our homemade VEGF111b polyclonal antibody.|PMC4480579|Our data showed that the number of fibroblast, capillary density and fibrotic tissue in the 0.5 and 0.7mg/ml MMC groups was significantly lower than the control, 0.1 and 0.3mg/ml MMC groups; while the expression of VEGF in control and 0.1mg/ml MMC groups was notably higher than 0.3, 0.5 and 0.7mg/ml MMC groups.|PMID:22056834|After culturing for 24 h, the VEGF levels in RPE cells in the BVZ and BVZ + 5-Fu groups were significantly lower than that in the control group, while the VEGF levels in the 5-Fu and MMC groups significantly increased (Figure 2).|PMC6151201","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9974846736363637","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ecf7a02959823b75c4160005aaa2b97b9b76c0232cb0ed5c20be679148faf1d7","tmkp:06e36d600c0362293f438e33c5087626e651b836dbb69427b89e465cd6bcc99c","tmkp:91fa71a856fba1d69123338b199e6e8352e29a1621100e8df419c47033f8e1ad","tmkp:10e712ca4e76b7b5c79a297be18b3648f9ea8a53580726f8a544e0727348cb5c","tmkp:3ee01de47f87b95758471c06ae3152271d45008ac48a1ea77e9932894b2495b1","tmkp:da05fd642d55abcc79ddea41db823d3e0095319e0ebda910dc09249e44d7131b","tmkp:e9da464eddadd20ada9919195767c335450fae4a3aedf2e96497acd1140d1ef6","tmkp:0191d9e27bd6ce79ec16adc87a6db1c490de37f2b085fc7af9a5327a1f377553","tmkp:243d63f6b0677429f1c5875cb6b91986478c0672b0ae43a2994969b86bc172d1","tmkp:b7fb040e079edae293923036cc5b47544e3a8d80f2e3968ca44b56e75b29bf0c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6925728","PMC6863018","PMC6151201","PMC6885197","PMID:20735383","PMC5444031","PMID:22056834","PMC7474357","PMC4480579","PMC6150649"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"60172723":{"subject":"PUBCHEM.COMPOUND:5280934","object":"NCBIGene:6513","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9976579","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:256e4df4b766383ba3288f81b33e3a60492dc3da316e9b3c0a3d6ea3ae259daf","tmkp:930fec4170170f9a9f3babba6ce5740c8eb8d9e6b3d72accef2301ab28a8207f","tmkp:afbce8e3bc201d2e7e483df4762cbcd173ec2345fee760373d5bd4ec9efced5b","tmkp:2e61345e0a1668814d278f628b168c0a2c33bc0cb49349c2f94caa27f26985a5","tmkp:19c2fe598b559090a923f52e3f14b1fde433dd59dc2ddf496ca5b7fef8d34b2c","tmkp:a3dcb8391b345b3ab32b2723f5a0e135a156e0f329baa3b523afd417385a1d12"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Three sequential injections with a neuroprotective dose of ALA increased neurogenesis and expression of key proteins involved in synaptic functions, namely, synaptophysin-1, VAMP-2, and SNAP-25, as well as proteins supporting glutamatergic neurotransmission, namely, V-GLUT1 and V-GLUT2.|PMID:19641487","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC1783864","PMC5641165","PMID:19641487"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"31388018":{"subject":"PUBCHEM.COMPOUND:5816","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Our findings that epinephrine, but not norepinephrine, suppressed VEGF-A expression in MIN6 cells, together with observations of differences in phenotypes between Adrb2 cKO and sympathectomized mice, suggest that epinephrine is the likely ligand responsible for Adrb2-mediated effects on VEGF-A levels and islet 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administration resulted in a significantly reduced hyaline cartilage volume (day 14), callus volume (day 42) and mineralized bone volume (day 42) and reduced expression of genes associated with endochondral ossification including collagen Type 1 alpha 1, collagen Type 2 alpha 1, vascular endothelial growth factor, Annexin A5, nitric oxide synthase 2, and mechanistic target of rapamycin.|PMC3704138|Furthermore, immunohistochemistry results revealed that expression levels of vascular endothelial growth factor, CXC chemokine ligand 12, CD68, CD3, and tumor necrosis factor α in the lesion area were significantly lower in treated (topotecan or AMD3100) brains versus control brains, while ionized calcium-binding adapter molecule 1 (Iba1) and HIF-1α expression was similar, though somewhat reduced.|PMID:29485043|In the AMD group, mean +/- standard deviation(SD) aqueous VEGF levels decreased from 68.0 +/- 32.1 pg/ml at baseline to 26.3 +/- 19.0 pg/ml after the first injection (p = 0.028) and to 25.2 +/- 12.8 pg/ml after the second injection (p = 0.005).|PMID:19997926|At the protein level, generally the flavonoids and methyldopa decreased the level of VEGF, and the administration of methyldopa with quercetin also showed a strong inhibitory effect in relation to the action of methyldopa alone.|PMC7956652|Until now, the main focus of drug target development for AMD was the inhibition of VEGF, due to its key role in 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densities of all TGF-beta1+ cell types in CMP were strongly increased in the connective tissue adjacent to the pocket epithelium, in the lamina propria and adjacent to the oral epithelium.|PMID:10382576","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"59201757":{"subject":"PUBCHEM.COMPOUND:6137","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9997099666666666","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The mRNA abundance levels of facilitative glucose transporters SLC2A1, SLC2A3, SLC2A4, and SLC2A10 in the placenta at E 17 decreased significantly in the 35% Met group compared with those in the control group (Figure 6B; Table S7), whereas substitution of 25% of Met with Met-Met enhanced these abundance levels to the control.|PMC6165284|Met treatment also increased the expression of these proteins, but the GLUT4 expression level in Met-treated cells was lower than that in all SP-treated cell groups.|PMC7072146|In this study, FJG, alone or in combination with Met, was found to significantly increase the suppressed mRNA and protein expression of IRS-1 and Glut4 in diabetic 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↑ upregulation ↓ downregulation 5-FU 5-fluorouracil ABC ATP-binding cassette transporter proteins ABCB1, ABCG1 isoforms of ATP-binding cassette transporter proteins ARE antioxidant response element ABT-263 small molecule that inhibits Bcl-2; 4-(4-{[2-(4-Chlorophenyl)-5,5-dimethyl-1-cyclohexen-1-yl]methyl}c-1-piperazinyl)-N-[(4-{[(2R)-4-(4-morpholinyl)-1-(phenylsulfanyl)-2-butanyl]amino}-3-[(trifluoromethyl)sulfonyl]phenyl)sulfonyl]benzamide ABT-737 small molecule that inhibits Bcl-2; 4-{4-[(4′-Chloro-2-biphenylyl)methyl]-1-piperazinyl}-N-[(4-{[(2R)-4-(dimethylamino)-1-(phenylsulfanyl)-2-butanyl]amino}-3-nitrophenyl)sulfonyl]benzamide AKT protein kinase B ALDH aldehyde dehydrogenase ALP autophagy lysosomes systems AMPK AMP-activated protein kinase APAF1 apoptotic protease activating factor 1 APR-246 drug that binds to p53 (restoring p53 function) and depletes glutathione; PRIMA-1, 2-hydroxymethyl-2-methoxymethyl-aza-bicyclo[2.2.2]octan-3-one AR androgen receptor ATR serine/threonine protein kinase Axl, Tyro3 receptors for tyrosine kinase BASE base excision repair Bax Bcl-2-associated X protein/Bcl-2-like protein 4 Bcl-2 B cell lymphoma 2 protein Bcl-XL B cell lymphoma extra-large protein BCRA1, 2 breast cancer susceptible genes BCRP breast cancer resistant protein BER base excision repair BH Bcl-2 homology domain BIM Bcl-2 like protein 11 BNDQ quercetin and doxorubicin co-encapsulated biotin receptor-targeting nanoparticles BPIS bound polyphenols of inner shell from foxtail millet bran BRAF serine/threonine-protein kinase B-Raf C catechin CAB carboplatin CAPE caffeic acid phenethyl ester CAR constitutive androstane receptor caspase-3, 8, 9 cysteine aspartic proteases-3, 8, 9 CBZ cabazitaxel CD44, 24, 133 cluster of differentiation 44, 24, 133 CDF difluorinated curcumin CDK 2,4,6 cyclin-dependent kinases 2,4,6 CDPP cisplatin 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blotting showed that the expression of PARP-1 in neuronal cells was significantly upregulated in both the cytoplasm and nucleus following 4% sevoflurane exposure for 6 h.|PMC7793874|(C–F) Western blotting and quantitative analysis showed that upregulation of cytoplasmic PAR polymer, PARP-1, and AIF both in cytoplasm and nucleus induced by 4 and 8% sevoflurane for 12 h were significantly inhibited when pretreated with 3AB in SH-SY5Y cells, HT22 cells, and hippocampal neurons.|PMC7793874|Our results found sevoflurane exposure induced neuronal cell death, which was accompanied by PARP-1 hyperactivation, cytoplasmic polymerized ADP-ribose (PAR) accumulation, mitochondrial depolarization, and apoptosis-inducing factor (AIF) nuclear translocation in the neuronal cells and hippocampi of rats.|PMC7793874|In contrast, pretreatment with PAPR-1 inhibitor 3AB not only significantly inhibited neonatal morphological changes caused by sevoflurane exposure and markedly increased the number of surviving pyramidal neurons in hippocampal CA1 region (Figures 9A,B), but also reversed sevoflurane-induced upregulation of PARP-1, PAR polymers, and nuclear AIF, indicating that 2.5% sevoflurane exposure for 6 h induced hippocampal neuronal Parthanatos in the developing brain (Figures 9G–J).|PMC7793874|(C–F) Western blotting and quantitative analysis showed that upregulation of cytoplasmic PAR polymer, PARP-1, and AIF both in the cytoplasm and nucleus induced by 8% sevoflurane exposure for 12 h were significantly inhibited when SH-SY5Y cells and HT22 cells were transfected with PARP-1 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et al. demonstrated a decrease of IL-4 and IL-10 in FEP patients who received risperidone over 10 weeks.|PMC8150759|A significant decrease in the production of IL-17a, IL-2, IL-4, and IL-13 occurred in MOG-stimulated splenocytes from risperidone-treated when compared to vehicle-treated mice during the peak of disease, whereas IFN-γ production was unaffected by risperidone treatment (Figure 2a-f).|PMC4130540|Thus, treatment with risperidone significantly decreased IL-4 and TNF-α in FEP patients with depressive symptoms and not in those without depressive symptoms.|PMC4360233|We found that treatment with risperidone significantly decreased IL-4 and TNF-α in FEP patients with depressive symptoms, but not in those without depressive symptoms.|PMC4360233|The broadest influence was observed for risperidone, which corresponded with a significant decrease in IL-1β, IL-2, IL-4, IL-6, IL-10, and increase in IL-12 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mice exposed to ISBN in air exhibited significant up-regulation of VEGF protein and mRNA in the liver, but not in the lung.|PMID:14521929|Retinal VEGF mRNA was increased 1.4-fold at day 10 in AIR, when compared with age-matched controls (p=0.03).|PMID:16500767|The immunofluorescence staining and RT-PCR analysis demonstrated that protein production and mRNA expression of VEGF and collagen III were significantly higher in TOE treatment group than vehicle alone and air control groups, while there was no significant difference in the level of collagen I.|PMID:25554261|On day 27, rats exposed to air displayed significant positive correlations between VEGF-IP-10, VEGF-KIM-1 and KIM-1-IP-10.|PMC7673239|On day 27, rats exposed to air displayed significant positive correlations between VEGF-IP-10, VEGF-KIM-1 and 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date indicated overexpressed HIF-1α could promote apoptosis by activating Bcl-2 and Bcl-Xl or enhancing the stability of p53.|PMC3359273","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"30981522":{"subject":"PUBCHEM.COMPOUND:5755","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"In this study, prednisolone improved the DMD pathologies by not up-regulation of utrophin protein but both up-regulation of laminin protein through the down-regulation of MMP-2 mRNA and promotion of cell survival such as inhibition of the expression of cleaved caspase 3 and up-regulation of p-Akt expression (Figures 4, 5A–C and Supplementary Figure 2).|PMC6287205|We found that the expression of cleaved caspase-3 in myotubes from the MyoD-transduced DMD fibroblasts treated with prednisolone significantly decreased compared with no treatment groups (Figure 4C).|PMC6287205|Results of our study reveal that the expression of Bcl-2 was significantly enhanced and the activity of caspase-3 was reduced in the fangchinoline-treated group compared to the prednisolone group in a dose-dependent 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staining revealed significantly increased Ki67, prolyl 4-hydroxylase, and vascular endothelial growth factor expression, and suppressed CD45 expression in the higher molecular weight hyaluronic acid plus povidone-iodine group when compared with the other groups.|PMID:30807498|Furthermore, it accelerated the wound-healing process by promoting angiogenesis in skin wounds with the hyaluronan oligosaccharide-mediated enhanced expression of vascular endothelial growth factor.|PMID:30519937|Hyaluronic acid stimulates the endogenous growth factor, epidermal growth factor, insulin growth factor, tumor necrosis factor, and vascular endothelial growth factor in a reported animal study.|PMC5127212|Indeed, hyaluronan with 6–10 residues has been described as: (i) promoting the proliferation of HUVEC, (ii) inducing angiogenesis in the chicken chorioallantoic membrane assay and (iii) increasing VEGF mRNA levels in HUVEC.|PMC3822652|In vitro, the treatment of Mo/MØ with lysates and conditioned media 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IPOC.|PMC3461004","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"29311664":{"subject":"PUBCHEM.COMPOUND:135398737","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC3735488","PMID:12871586","PMC6675791","PMC6790347","PMID:23771439","PMC2881214","PMC4153869"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9994072028571429","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"In PC-12 cells, U0126, Clozapine, and N-desmethylclozapine all attenuated the phosphorylation of ERK1 (p44), and Clozapine attenuated the phosphorylation of ERK2 (p42).|PMC2881214|(3) Clozapine also attenuated the ligand-dependent activation of Akt and Erk1/2 within its micromolar concentration ranges in culture.|PMC6675791|A clozapine-induced reduction in ERK1/2 phosphorylation was evident at both tyrosine and threonine residues, suggesting the involvement of dual specificity phosphatases (DUSPs; mitogen-activated protein kinase phosphatases [MKPs]).|PMID:23771439|In contrast, the atypical anti-psychotic clozapine reduced ERK1/2, CREB and Elk-1 phosphorylation.|PMID:12871586|In particular, while a single injection of haloperidol increased phosphorylations of ERK1/2 and Elk1 in mice dorsal striatum, these phosphorylations were decreased following clozapine 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together, the slight toxicity of PED appears to be neutralized by the conjugation of betaine to its backbone.|PMC5771809","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99618185","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"70185466":{"subject":"UMLS:C2740799","object":"NCBIGene:5337","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.999706","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c93a8f58eec3039ae3c00125581c1cfe7e7869ca3faff2aae0ee59d54281c726"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:20735042"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Here, we describe a matrix library strategy that afforded the most potent (PLD2 IC(50) = 20 nM) and selective (75-fold selective versus PLD1) PLD2 inhibitor to date, N-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide (22a), with an acceptable DMPK profile.|PMID:20735042","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"96153182":{"subject":"PUBCHEM.COMPOUND:6322","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"The present findings provide the molecular mechanisms by which insulin resistance and, by extension, reduced GLUT4 content in PM of muscles and WAT take place after chronic administration of Arg, and further suggest a putative role for GH in its genesis, considering its diabetogenic effect.|PMID:19106217|In addition, decreased expression of GLUT4 in adipose tissue of arginine-treated pigs is sufficient to impair glucose transport and fatty acid synthesis, suggesting that energy substrates are preferentially partitioned to skeletal muscle rather than white adipose tissue.|PMC3422877","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99712552","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:68220d75003c598973aae4aa435923ff0d9b1d02de312b1bed01de7aa395fed7","tmkp:457a66c197b111aa9a8a8874645c991207d9c05d0ec49f7f57f2ac5049850532","tmkp:0f1311c0f4ce0067bd661790e1d8c92fec4041546ad148c962ff567fc24fd357"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:22889511","PMC3422877","PMID:19106217"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"57382041":{"subject":"PUBCHEM.COMPOUND:247","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9984926407692308","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:27473515","PMC8124599","PMID:27473515","PMC4464397","PMC4464397"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Antiangiogenic effect of betaine on pathologic retinal neovascularization via suppression of reactive oxygen species mediated vascular endothelial growth factor signaling.|PMID:27473515|Antiangiogenic effect of betaine on pathologic retinal neovascularization via suppression of reactive oxygen species mediated vascular endothelial growth factor signaling|PMC8124599|Our data suggest that betaine has an anti-angiogenic effect on pathologic retinal neovascularization via suppression of ROS mediated VEGF signaling.|PMID:27473515|In addition, betaine treatment alleviated diabetes-induced vascularization by suppressing VEGF and HIF-1α expression via downregulation of pAkt expression in the retina of the STZ-induced diabetic rats.|PMC4464397|A lower dose of betaine exerted a more potent inhibitory effect on the number VEGF-positive cells (Fig. 1, lower panel).|PMC4464397","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:6c8281f11daa4cc1b807cc87d99de251410ece63a80b3f3d84d7f41a68bbc9cf","tmkp:93032582b1d5ee396f5b2bc623f3af6b6637339b79656de83c6d5eb19cd150d2","tmkp:7a86577c7b3aea5243eda3b675c3a828211bb0f3a72b97ed3dac0062a7d6afe0","tmkp:f1a769482d9bfd909c0cbbcebb1fa70d884534079ba27b9cf0ed894770399fb4","tmkp:af3d9df72fd11753bfcf8bd5189f4dad4b55a9ebd9e0a18da11ec86b6b061443"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"68362365":{"subject":"PUBCHEM.COMPOUND:5206","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC6916020","PMC5333720","PMC7180331","PMC5701644","PMID:27119513","PMC7295720","PMC4071288","PMC5364873","PMID:25753883","PMID:25971460"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:14efd916a8390aef578c865bf227daf9d4d751fdf54ba2f5824d0941c33dc45b","tmkp:fbc54f32c30feedaae18381c501a72c44c9c728d20b52db0f86d3cb23813cac6","tmkp:60737ce654e8426b6b8cfcd6fc8c1a164028b805f1bd1c7ba188b587cfac1fa2","tmkp:6a5148b2a7ac62d3a20ed3a9f1cc506dc45ceb06173f71c944f56722de922885","tmkp:e99b89778fa83ea8c7baa5300579cc70c4d1855653d1ea9dce98e7373a3150a3","tmkp:e800fb81d1896bb2b4834b0c1c2ab479549a5b427f97d02fa0c9e2e6e35a0369","tmkp:10d3953b6c833fef7a159960d4652c4e3bce2a074a9c3615f30ad55350894c1d","tmkp:b910cffa70d64ea2882eb9caa0cf1318e8791c8c2d00c28790faa55b3f638bcd","tmkp:e5afd153afc02ca47c22937498f49d50f4a099426fa0be8b499e3e35c6d95fde","tmkp:d8d3d07f8444b0645a7762688cc3870e74aba785acc3d39f12c1b880a33838d6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Sevoflurane exposure in neonatal rats was associated with increased expression of the pro-apoptotic proteins, BCL2 associated agonist of cell death (BAD) and BAX, and reduced expression of the anti-apoptotic proteins, Bcl-2 and Bcl-xL.|PMC7180331|Moreover, sevoflurane anaesthesia increased the number of TUNEL-positive cells and the levels of Bax, cleaved caspase 3 and cleaved PARP and reduced Bcl-2 levels in the hippocampus and temporal lobe.|PMC7295720|Here, we found that sevoflurane anesthesia can impair short-term cognitive function, which may be via down-regulating p-CREB1 and Bcl-2 expression and up-regulating Caspase-8 expression to reduce hippocampus neuronal apoptosis, and male rats suffered a more severe cognitive dysfunction than female rats.|PMID:25753883|Mechanistically, we also found that Sevoflurane treatment resulted in a reduced amount of the cytosolic anti-apoptotic protein Bcl-2 but an increased amount of Bax, which was exacerbated by knockdown of Sestrin-2.|PMID:25971460|Western blot analysis demonstrated that exposure to sevoflurane for 6 h induced a significant increase in p-p53, Bax and cleaved caspase-3 protein levels, and a significant decrease in Bcl-2 protein levels when compared with controls.|PMC5364873","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9978870067857143","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"66892901":{"subject":"PUBCHEM.COMPOUND:34755","object":"NCBIGene:5599","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"On the other hand the same treatment led to a more modest reduction in JNK1–/– cells (12–17%).|PMC3342290|The same concentrations of platonin significantly inhibited the phosphorylation of JNK1/2 but not ERK1/2 or AKT in VSMCs stimulated by PDGF-BB.|PMID:21892199|Similarly, the expression of phospho-JNK1/2, phospho-p38 MAPK, and NF-kappaB was decreased in the same culture system.|PMID:16342327|Consequently, the same fractions inhibited p38 and JNK1/2 activation induced by UVB or UVA radiation.|PMID:21405100|At the same time, phosphorylated JNK1 protein expression was reduced, while the mRNA and total protein levels of JNK1 were almost unchanged.|PMC6868062","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ec315e22cab89972281e645d12174c03561473d07aeab0f2414e255a4d9f8367","tmkp:071dbcad18010f63d3842ef33aa025af1a4f4fab259b663600aa5679e1152d1f","tmkp:40fc663ffa0b03eebe7021fd9d75a8c78e2da53215ec05e4a8dbde045a66b2df","tmkp:b3845288a57a5b7a2e3f3e8a1d4b0a7d0fa4262b4950440ed9212b6cb3edd5c6","tmkp:fed628b4da368d0c865dbb715434629082305bdf029b7f61965c128d02f6f8fa","tmkp:df4e8b9b2a1aa4a71d3369f93f69885028f0365aed1e862f3d16dc485d7ddcee","tmkp:035564600ba2787a18f4bb5d982bd9b576556f9ce1fd15210104973776865a6b","tmkp:267c68881b079b066b1b3ec5b1a605a5e9eb07f3f4ef437770443e1c8ded92e6","tmkp:4b1b45ce61d7396fcc8336169b4e0c8588cedd9593f5e55f19616e81e47ddb4e","tmkp:82909698b74d1844df74edd733ed7dba77365b33c1a69941d94729dbbc215eb8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.998664615","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:21892199","PMC3777698","PMID:16342327","PMC6868062","PMID:21405100","PMID:19122368","PMID:10467423","PMID:20206247","PMC3342290","PMC3135494"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"19780513":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:7423","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9967768333333332","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:78ecfe4dad6a7e66a8307cf6cf1e8206b718eaec0dc6322f99c104588c5ad43f","tmkp:e0e9cf9bcc36beb21993ef042f47c7d18ed816c41ff10fcaeac52221687ee2ac","tmkp:d0c53cc3f2008c601f268fe0845037f05a05bcaa6903020cb76ccace9b60d44d","tmkp:e3268b19b4c95f25393e4c6bc05d3bcbca7e23923a2a6052c03e0083980be24b","tmkp:44572058222a131cf4303c9a72cd74a5935a62fa8179d32f5dc8758ca89ec1ab","tmkp:121380402901869a69b7cf8952ccb72406105c8893c6997c2acdadf8ce71ccb0","tmkp:3e5e7d365e416502172bbaf7f4ff4709e31bfd7917c5f81a5a051455ee23c7f6","tmkp:bdb67b2f1b5b9bd6c916a5db50de748ff39e6e986208d383d467e0d82e19b428"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMID:20008399","PMC3107884","PMC6191968","PMID:19706677","PMC5532630","PMID:11329058","PMID:15240521","PMID:18470912"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Dopamine administration leads to increased VEGF-induced phosphorylation of SHP-2 and this increased phosphorylation parallels the increased phosphatase activity of SHP-2.|PMID:19706677|Activation of the dopamine (Dp)/dopamine receptor 2 (Dp-r2) pathway was involved in the VEGF/VEGFR-2 signaling process and can reduce neoangiogenesis.|PMC6191968|Dopamine stimulation slightly decreased the surface expression of vascular endothelial growth factor receptor-2 (VEGF-R2) but induced the phosphorylation of VEGF-R2 through Src in HUVEC.|PMID:18470912","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"44661761":{"subject":"PUBCHEM.COMPOUND:31307","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"We also confirmed that treatment with dexamethasone and triamcinolone acetonide reduced diabetes‐induced phosphorylation of AKT, ERK1/2, ATF2, c‐Fos and c‐Jun as well as galectin‐1 protein levels (Figure 5C).|PMC6787449","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.99967885","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:8844a935a167f4fb2135b2c33603bae2ac96253328c2f8727626c670b66bc20c","tmkp:742ece49a8174773e36ae73c4bebcbf31b32aad554f03d50906368e8b7a2a193"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC6787449","PMID:19234347"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"119894886":{"subject":"PUBCHEM.COMPOUND:5865","object":"NCBIGene:836","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9993991849999999","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:4049f691078a848a58360c8ed0957c218c5523de76ae6c6f3fdb48884152c809","tmkp:cd2158f425e774d463190ba8d4346fa95a09258c562ca129a02e512f274b5294","tmkp:0955bf85b16b56a415f80b51ffb3a20c8c9e4a2b94c8356d9b12aa7d7bd84545"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC5028770","PMC7568182","PMID:23486009"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The application of vincristine (1 ng/ml) or prednisone (0.5 μM) significantly (p < 0.01) increased the level of cytochrome c as well as activated caspase 9 and activated caspase 3 in both JurkatpRack1 and JurkatpEmp cell (Fig. 3c).|PMC5028770|We found that vincristine and prednisone showed upregulated BAD and BAX mRNA (pro-apoptotic) expression and chemotherapeutic drugs (vincristine and prednisone) exposure induces cell apoptosis by enhancing pro-apoptotic genes, BID, BAX, caspase-3 induction, and downregulation of BCL-2 expression in ALL cells.|PMC7568182","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"35989402":{"subject":"PUBCHEM.COMPOUND:135398744","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.9992299357142856","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC2681457","PMID:28974454","PMC3108059","PMID:28974454","PMC3108059"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Treatment with 100 mg/kg/day sildenafil resulted in a reduction in PAI-1 (by 26.8%; p < 0.05, Figure 5C) and amphiregulin (by 33.3%; p < 0.05, Figure 5D) mRNA expression, whereas sildenafil treatment showed only a tendency towards lower IL-6 and TF mRNA expression compared to oxygen-exposed controls.|PMC2681457|Hepatic content of tumor necrosis factor-α (TNF-α) and nuclear factor κB (NFκB) expression & content displayed significant reductions with sildenafil treatment, Furthermore, sildenafil caused marked reductions of transforming growth factor (TGF)-β content, expression of plasminogen activator inhibitor-1 (PAI-1), matrix metalloproteinase-9 (MMP-9), tissue inhibitor of metalloproteinase-1 (TIMP-1), α-smooth muscle actin (α-SMA), fibronectin, collagen I (α1) and hydroxyproline content.|PMID:28974454|Either sildenafil or simvastatin alone resulted in lower plasma t-PA and PAI-1 levels compared to the MCT-injected control group, indicating an endothelial protective effect.|PMC3108059|Hepatic content of tumor necrosis factor-α (TNF-α) and nuclear factor κB (NFκB) expression & content displayed significant reductions with sildenafil treatment, Furthermore, sildenafil caused marked reductions of transforming growth factor (TGF)-β content, expression of plasminogen activator inhibitor-1 (PAI-1), matrix metalloproteinase-9 (MMP-9), tissue inhibitor of metalloproteinase-1 (TIMP-1), α-smooth muscle actin (α-SMA), fibronectin, collagen I (α1) and hydroxyproline content.|PMID:28974454|The increase of plasma t-PA, PAI-1, MMP-2, and MMP-9 concentrations were attenuated significantly in the sildenafil, simvastatin and combination groups, but no difference was found among the three treatment groups (Table 1).|PMC3108059","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:96f39cdfbfa9ce649c77d2657d5f497ecd10d7e062239236e01f7638d4ea6f68","tmkp:2ca0737b2f0e2b3d34c7954c4f335061e83f2e294747aa70cb76af93b5927175","tmkp:68b7a09171aa5d4fe36488ee3d405fb5daa62386206850facb908dc77f39f375","tmkp:aac9fe23278f31bf546d87a49a1d071d36467b919ef5e7dee5e9b583b73520d8","tmkp:4001afb2d9977a4240cd2c2f9dc6c5d9deda673669519ea03af08f05c23b9510"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"75037202":{"subject":"PUBCHEM.COMPOUND:135398744","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5445371","PMID:25139994","PMID:28974454","PMC4346839","PMC7016856"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:fd34f835e1989d97d43b30d3ea9aa0e19042cee55f569349edbc67967d00b797","tmkp:d9bb66cb1e3637c3385c18c7dc8c853ad3d317bb12947944ddd699e04bcb78ee","tmkp:a7a229fe340280c9776f61fa38547708be61dc9c90097766ab50a51f5f71919d","tmkp:6316604daa758d9781a5830b8873ad0b15f73b5ffa9d7ca5e992c6e553609a4f","tmkp:46867312a0f1a23df1df6c86164ead848be672d6ab35d2f163f96557c1ea390c"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"In mdx mice, Sildenafil demonstrably increases specific force, reduces collagen I, fibronectin and TNFα infiltration, and improves sarcolemmal integrity of the diaphragm.|PMC5445371|However, sildenafil substantially blocked the increase in collagen I, fibronectin 1, TGFβ, and CTGF mRNA in Ctr but not in βRM hearts.|PMID:25139994|Hepatic content of tumor necrosis factor-α (TNF-α) and nuclear factor κB (NFκB) expression & content displayed significant reductions with sildenafil treatment, Furthermore, sildenafil caused marked reductions of transforming growth factor (TGF)-β content, expression of plasminogen activator inhibitor-1 (PAI-1), matrix metalloproteinase-9 (MMP-9), tissue inhibitor of metalloproteinase-1 (TIMP-1), α-smooth muscle actin (α-SMA), fibronectin, collagen I (α1) and hydroxyproline content.|PMID:28974454|In this experiment sildenafil reduced remodeling biomarkers, e.g., α-SMA and fibronectin, and thereby prevented progression of tubulointerstitial fibrosis and glomerulosclerosis.|PMC4346839|Finally, additional studies indicate that inhibition of PDE5 using sildenafil significantly reduces isoproterenol- and thoracic aortic constriction-induced expression of TGFβ, connective tissue growth factor (CTGF), collagen 1 and fibronectin 1 mRNAs in mouse hearts.|PMC7016856","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.999630436","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"94918358":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:2335","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99970576","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC3447896","PMC3165139"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:ab0e087f9a1e183700021c68b8f802f0d99db7cc53d66db31167273f287be48b","tmkp:9e7a60219f5c7a12d7df7bff5ebd0a633d6beb3d61ba02d23092c02db2de4f1e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Increased intrarenal dopamine also blunted increases in mesangial matrix and GBM thickening, as well as inhibiting expression of mediators (CTGF) and markers of fibrosis (collagen I, collagen IV, fibronectin, and FSP-1).|PMC3447896|By contrast, fibronectin and BCA (20 min hydrolysis) were associated with decreases in dopamine currents (Figs.|PMC3165139","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"42121366":{"subject":"PUBCHEM.COMPOUND:4649","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:77d26af59a783d0dfe306c813342222389b3d0fc9135885c2d0d4c3b4e3a05b2","tmkp:62eec9a337dd5b02d101a1f3b444dd0946ebd0edf5c280178fcd8ec2c55bee6c","tmkp:27f5b55ab078fac1dbf6623133cefddb0e8ad7e6a32b468eb223be98b1988548","tmkp:44c0ee8f9ed5c6181ed4974e63c586a2c98edfe68f497f903f386a42625849ca","tmkp:59c2cf63911a88b66a301619a56442d812b427f0065c947c570046becc6366a4","tmkp:35dc2eaefd6acf03f0602895d6ec71b8676f138be40e79818d375275062bfa6e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMID:18636191","PMC7786416","PMID:16679379","PMC7766935","PMID:16088182","PMID:28194878"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9997222","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"The inhibitory effect of PAs on the expression of VEGF and hypoxia inducible factor 1 subunit alpha (HIF-1α) was also observed in cisplatin-resistant ovarian cancer cells.|PMC7766935","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"12583356":{"subject":"PUBCHEM.COMPOUND:247","object":"NCBIGene:5054","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:c355bdca24d809e234ddeea48687ac1844db43a87277e795e36ca73ca3c9ec38","tmkp:bb3f3d37c40c3d0327c2e97f6ab7f46118172a408c4981159ff13c91a4fac923","tmkp:a98d9b148c49d0292401f492aa105e4dfa57cf55a1bce1d2887c753abead5b2d","tmkp:5c40d2b9f3af9a79ca8f40798a4ce11bed4e5321bbf687d248faac57ce7d576b"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Plasma plasminogen activator inhibitor 1 concentration increased in the betaine group (P = 0.028) and decreased in the control group (P = 0.006).|PMID:20978525|Plasma plasminogen activator inhibitor 1 (PAI‐1) concentration increased in the betaine group (from 7.19 ± 2.91 at week 0 to 8.85 ± 3.78 AU/mL at week 24; p = 0.028) and decreased in the control group, resulting in a statistically significantly higher concentration in the betaine group than in the control group at the end of the study (8.85 ± 3.78 vs 6.25 ± 2.38 AU/mL, p = 0.006).|PMC7009864|Plasma plasminogen activator inhibitor 1 (PAI‐1) concentration increased in the betaine group (from 7.19 ± 2.91 at week 0 to 8.85 ± 3.78 AU/mL at week 24; p = 0.028) and decreased in the control group, resulting in a statistically significantly higher concentration in the betaine group than in the control group at the end of the study (8.85 ± 3.78 vs 6.25 ± 2.38 AU/mL, 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HGF, VEGF and G-CSF levels were increased after heparin administration.|PMID:31738878|In addition, heparin significantly increases expression of a series of growth factors, including FGF14, FGF20, BDNF, IL6 and VEGF, but not FGF2 (Fig. 3C and data not shown) as well as the expression of a number of cell surface proteins, including ITGA6 (integrin α6) and NGFR, but not ITGA5 or ITGB3 (Fig. 3C and data not shown).|PMC5330685|The protein levels of VEGF were markedly increased only in the VEGF189-transfectants cultured in the presence of heparin.|PMID:12429975|VEGF mRNA expression was significantly inhibited by N-desulfated heparin and was higher in normal saline group than in N-desulfated heparin group (Ct value 19.51 +/- 1.01 vs 22.55 +/- 1.36, P < 0.05).|PMID:17230619|In the retina, VEGF paracrine signaling has been correlated with upregulation of the Heparin Binding EGF ligand (HB-EGF) after injury, which acts through 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have found that chlorpromazine destabilized and increased the autooxidation of hemoglobin, induced activation of caspase 3, increased phosphatase PTP-1B activity, and, markedly, influenced the ATP and reduced glutathione levels, with subsequent exposure of phosphatidylserine at the erythrocyte surface.|PMC5124449|The higher percentage of caspase-3 labeled cells in APC positive cells in CPZ group, however, resulted from a lower number of APC positive cells subsequent to continuous death of mature OLs.|PMC7296101|The percentage of caspase-3 labeled cells in the APC positive cells in CPZ group, however, was significantly higher than that in CNT group (Figure 7C).|PMC7296101|CPS and CPZ further induce caspase-3 activation and reduce tumor growth in vivo.|PMC6950741|Similarly, bafilomycin A1 abrogated the potentiation of bleomycin-induced caspase-3 activation by CPZ, FPZ or TFPZ (data not 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phospholipase C inhibitor U-73122 or protein kinase C inhibitor chelerythrine partially prevented the suppressive effect of clonidine on Con A-stimulated lymphocyte proliferation and IL-4 production.|PMID:18463421|Patients in the ropivacaine group (thoracic epidural block) had a significantly lower IFN-γ/IL-4 ratio at the end of surgery than those in the remifentanil group and clonidine group.|PMID:22429354|The inhibited lymphocyte proliferation and IFN-gamma and IL-4 production by clonidine were blocked by yohimbine, an alpha(2)-AR 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muscle immunohistochemistry demonstrated increased sarcolemmal expression of GLUT4 in both alcohol groups compared with HCC.|PMID:22938901|Skeletal muscle immunohistochemistry demonstrated increased sarcolemmal expression of GLUT4 in both alcohol groups compared to HCC. |PMC3435558|Qian et al demonstrated that alcohol extract of SZY can increase GLUT4 mRNA and its protein expression in T2DM rats through promoting proliferation of islet and increasing postprandial secretion of insulin and therefore accelerate glucose transport.|PMC6890936|Long-term moderate ethanol consumption restores insulin sensitivity in high-fat-fed rats by increasing SLC2A4 (GLUT4) in the adipose tissue by AMP-activated protein kinase activation.|PMID:18719073|Qian et al demonstrated that alcohol extract of SZY can accelerate glucose transport by promoting islet proliferation and increasing postprandial secretion of insulin, thereby increasing GLUT4 mRNA and protein expression in T2DM 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PPD and PPVII inhibit AKT, JNK1/2, and ERK1/2 expression, which further inhibit caspase-8, Bcl-2, and Bcl-xl while upregulating Bak and Bax, resulting in mitochondrial membrane permeability, allowing Cyt-c to translocate from the mitochondria into the 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long-term and low-dose of aspirin treatment in female mice re-sensitized the Insulin/Akt signaling via reducing phosphorylation at Ser1101 of IRS-1 and hyperphosphorylation at Thr308 of Akt, and increased the glucose homeostasis via enhanced expression of hepatic Glut4, Glut2, and hepatic PPAR-γ.|PMC6354253","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMC6354253"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:db04796bcb8fcf7c42b4cc4851b3022e9f1c0492ee4657adb04af2161471d88d"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"16903875":{"subject":"UNII:ZL1R02VT79","object":"NCBIGene:7424","predicate":"biolink:related_to","attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6681039"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"The treatment of this condition involves laser photocoagulation (panretinal, focal, and grid), intravitreal anti-VEGF agents (aflibercept and ranibizumab), corticosteroids (dexamethasone and fluocinolone acetonide intravitreal implants), and vitrectomy in the case of vitreous hemorrhage.|PMC6681039","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:1071610daccdd673d082d08b5f66974c741698b90da237940e6e6fbd8421576e"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"0.000122313","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"113726659":{"subject":"PUBCHEM.COMPOUND:2554","object":"NCBIGene:5595","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMID:22889231","PMID:12091467","PMC5426488","PMC4153869"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.99856165","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:67096608b60e6b33ee522133e664618b0016b763c4f4e61b7eb70939e7c2b253","tmkp:1c5c681baaa027e5e3a0dc277e1e443aa280778b85d2977939075b69ebea0abe","tmkp:9c66d06394aba43efe328655d43ac50801cf59e5397ecda78ee504e96bb60cf1","tmkp:6c42b255fbfb0609c85242a99de61dbb8427420ad8769617fa49008cbc7fef29"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"The effect of CBZ on adipogenesis involves activation of the ERK1/2 pathway.|PMID:22889231|In contrast to lithium, sodium valproate and lamotrigine did not affect BDNF-mediated signaling, whereas carbamazepine induced a rapid and prolonged phosphorylation of ERK1/2 and CREB in the absence or the presence of BDNF.|PMID:12091467|Carbamazepine was found to induce a rapid and prolonged phosphorylation of ERK1/2 and CREB in the absence or the presence of BDNF.|PMC5426488|In addition, carbamazepine has been reported to increase the phosphorylation of ERK1/2 in SH-SY5Y cells; however, this finding was not replicated using lamotrigine or carbamazepine in another study.|PMC4153869","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"55389943":{"subject":"PUBCHEM.COMPOUND:3821","object":"MONDO:0012805","predicate":"biolink:treats","attributes":[{"attribute_type_id":"biolink:Attribute","value":"Ketamine has been reviewed extensively and shown to be extremely safe for use in Pediatric Emergency Department (PED).|PMC4126119","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:2580231830f914005b1e7ae654814a8131dc622259c791aa6a5762d035aa57f3"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99948764","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC4126119"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"97283543":{"subject":"PUBCHEM.COMPOUND:253602","object":"NCBIGene:7424","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9873018866666667","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":"Here, we demonstrate that VEGF mRNA levels are increased by anisomycin, a strong activator of stress-activated protein kinases.|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 3'-UTR).|PMID:10849421|First, by using an in vitro mRNA degradation assay, the half-life of the VEGF mRNA 3'-UTR region transcript was found to be increased when incubated with extracts from anisomycin-treated cells; and second, the 3'-UTR was also sufficient to confer mRNA instability to the Nhe3 (Na(+)/H(+) exchanger 3) heterologous reporter gene, and anisomycin treatment stabilized the chimeric mRNA (Nhe3 fused to the VEGF mRNA 3'-UTR).|PMID:10849421","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:10849421","PMID:10849421","PMID:10849421"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:a457f68ec125b7dda88023fbb94318b3a5bd39d315a48a7ced4cb57f0b8e5791","tmkp:b3b4572622379dcfdb8b09d9c1712f24cca13ff38fb4fbcb12f3fb9849c2b727","tmkp:1260d8a9f25dadf813686e3ebddc3c95a2c4ba511a0ea8ab1a682fa262da1bd6"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"}]},"35695202":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:142","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:3ff6bb72671c0416c195e3f98a2ce2b22bee2796c22186bd2a362664f57ad875"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Consistently, dopamine activates the PARP1/CTCF-regulated transcriptional network to trigger morphological remodeling in astrocytes.|PMC7690980","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.99922824","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC7690980"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"39495738":{"subject":"CHEMBL.COMPOUND:CHEMBL2052016","object":"NCBIGene:5594","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"An anti-proliferative effect of verteporfin on human glioblastoma cells was also observed through activation of p38 MAPK, which has been implicated in the inhibition of tumor growth.|PMC5548915|Verteporfin (VP) activates p38 MAPK glioblastoma cells.|PMC5548915","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.999241925","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:5f9ec21d371a97494d94a76ccc46fe268853cba798f76e24156dc78567c4fda9","tmkp:6f84dc906e097a0e8b2cf44da48f199fb8752569f1097b8c83299de2e665041a","tmkp:4421dbb07b0fa183a89c791acafeb3b3fe5cc9aa1b74c99674dd25fe1eca86d6","tmkp:39db600bdda7fefc9336bad39a09f6643c8526512bae13089f90346f5d59d670"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:publications","value":["PMC5548915","PMC7483501"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"72394288":{"subject":"PUBCHEM.COMPOUND:712","object":"NCBIGene:596","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.99938997","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:e52b9d35e038732cff390d61ec24a09a4fc89ec8d8e085f5cb7e2ad71ed7c1f3","tmkp:f014c1601ccb8850ed188b6989aab122a2ef498e3405d6dda8b53f21e32f7eb8","tmkp:1b137c4afef02bd054cf7d693564576349031ec07bf08d1cea0734dabc1f647f","tmkp:2b3d77fafb424416c7b6c62a4bd4a9880dcc58cc9b9c81c179ac8c1bd777f5a4","tmkp:305f16f81c05f567ca5e8f9419eee59122d736feab12786eb0cf6936b4f2cea9","tmkp:ad1bcff6e3165fc4f2550ae2712cf9ca7bb09ffc504764a5ce1fe8a7c7be631a","tmkp:b8cf06ba6a5b875ad66958f857b9c9ee67be1c083e1639cb9c02f59ef7563790","tmkp:2086c9ffeb14e685e42877dfb06c11c36c4ff5f23f9406e4278a817dd3a11ce2","tmkp:ad2ac2c52a0efc3e803a2695b87fb1565c79fea2a4b8fb8499c2761a5ab39be0","tmkp:18bc979ff11b60705acda931e617bb8c11d585b9a6a13a5c4b8da3d1a65cd4b8"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:Attribute","value":"Additionally, relative to control mice, Bcl-2 expression increased and Bax expression decreased in the mice administered both formalin and L-carnitine.|PMC7482949|Another finding of this study was an increase in Bcl-2 expression and a decrease in Bax expression in mice administered both formalin and L-carnitine.|PMC7482949|Inhalation of low-level formaldehyde increases the Bcl-2/Bax expression ratio in the hippocampus of immunologically sensitized mice|PMC4146158|Inhalation of low-level formaldehyde increases the Bcl-2/Bax expression ratio in the hippocampus of immunologically sensitized mice|PMC7411409|Inhalation of low-level formaldehyde increases the Bcl-2/Bax expression ratio in the hippocampus of immunologically sensitized mice|PMC3818819","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC5127868","PMC7482949","PMC4146158","PMID:25040984","PMC7411409","PMC3702466","PMC3818819","PMC6112212"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"}]},"100661841":{"subject":"PUBCHEM.COMPOUND:681","object":"NCBIGene:3630","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:publications","value":["PMC7180501","PMC3402263","PMC6760484","PMID:1107123","PMC3735640","PMID:1860327","PMC4181516","PMID:6147289","PMID:16129680","PMID:18645345"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"0.9826018164227642","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:c418ec77abb25e0f324e8e5473e174d49be875722246147a877188ad7a9aeb34","tmkp:1545718d451cbdc71ae8599bf6b68b3c3fb66df5620ef34f46d776b743bb091d","tmkp:af1dbb55a66ca02f4ea1cab5518a4671fbba423c8ca2a8761bd8b88cc3c33241","tmkp:143fa0e7be7c17bf1857ee7efa0538f95e4a169bcae5e4c0bb2c6aba034f1088","tmkp:1f6fd5bbd2e4f2643403f9bc0f4f0dbbd40b6e28cebdaf0f66aa1d9d32c9a429","tmkp:899d01f259b942925ac6530240a56bcb4889d683b47308e400b188541beef051","tmkp:7277f17cfb071e1553121fd59e9cc7cd18e96bea643018978862ad1125316c6c","tmkp:1225b330e8d92888c7a58525cde4c15a829932f99d81a2c475745c00c5ae052c","tmkp:742bb5121e9fdfbde90d183a1bcab3b6337d37c671a169b4b5ed31a420398deb","tmkp:3baf52d43b52ac21443336db5056282e3fef145e990ff62d2e3707692459dffc","tmkp:4368c0ddc01d16e942e7c1838b0691d1496ced8d0f87015642ebe60385d1b8c5"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"Insulin plasma concentrations were significantly (p less than .05 to p less than 0.1) increased at the three dopamine infusion rates.|PMID:1860327|Studies in healthy volunteers revealed increased insulin levels after dopamine administration, but these studies were limited by small sample size.|PMC3402263|The total number of insulin+ cells was higher in dopamine-treated vs untreated explants (Fig. 6a, b) but, in agreement with our in vivo observations, we detected no change in the total number of glucagon-expressing cells (Fig. 6a, c).|PMC4181516|Dopamine infusion induced an increase in serum insulin, systolic blood pressure, and heart rate in healthy subjects but not in subjects with type 2 diabetes.|PMID:18645345|The dopamine concentration was higher in the diabetic control insulin group (group 5) than in diabetic main test group (group 7).|PMC6760484","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"5424635":{"subject":"PUBCHEM.COMPOUND:3121","object":"NCBIGene:7422","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":["tmkp:3bf248fac945f926fed7d3ef0aeb81f461336432bbcbd3cb9e570b3413dc7937","tmkp:9aa21b636eee3adb72430b64d1abb310e044738f95040ce1739c2a6cb220b2aa","tmkp:1c7fd576da067646d0715360cebdf670561d43300dd73c14d5a34e6946661ce4","tmkp:48825b5e1b1e1efb63ec171baa29d2584c85ecf5e6c2c1e76872f496a628d3a0","tmkp:816c0ee390ee9fd248273e04f3b6be35621dfc79631c71f771e6b8f7a69da627","tmkp:a936e3881e25042528cbbb7a79edd84eb9e5d7a48ea8ca075d5d8036aad8fb62","tmkp:8ee04007d0b348bfdc4eb3d1f0a36ddc89dec59551c104613a38d1b9062bb430","tmkp:b217cdcfd50c58bd2b0fa6025942d8522be35390b0ca3ce2c552e411693093c9","tmkp:526ae81357599555269014f4f4bf8815a7447f733ccf3cd1559dea0cf8af3911","tmkp:21f61b84a531ab0e2c41adabbcf3e04303d9851d13c78c531bd93c3020d68084"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:Attribute","value":"Trophic factors assessment, following treatment revealed the mRNA expression level of BDNF, GDNF and VEGF could be significantly up- regulated at various time points, mainly by 1 mM VPA.|PMID:30904572|VPA enhances postischemic angiogenesis via upregulation of HIF-1α and the downstream pro-angiogenic factors VEGF and MMP-2/9.|PMC6248271|In addition to enhancing HDAC inhibition, VPA potentiated MCAO-induced HIF-1α accumulation and upregulated VEGF protein levels and MMP-2/9 activities in the ipsilateral cortex on days 7 and 14 post-MCAO.|PMC3429729|The transcription factor hypoxia-inducible factor-1α and its downstream proangiogenic factors, vascular endothelial growth factor and matrix metalloproteinase-2/9, were upregulated after middle cerebral artery occlusion and significantly potentiated by VPA in the ipsilateral cortex.|PMID:22811460|As shown in Fig. 2a, the expression levels of 6 secreted proteins (GCSF, GM-CSF, M-CSF, PDGF Rα, PDGF Rβ, and PDGF-AA) were decreased and those of 4 secreted proteins (AR, EGFR, TGF-β2, and VEGF) were increased in VPA-treated cells, compared with the control.|PMC6670223","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:publications","value":["PMID:30904572","PMC3429729","PMC8147490","PMID:22811460","PMC6248271","PMC6123555","PMC4951598","PMC5327178","PMC6670223","PMID:26942921"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9942256437254903","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"}]},"70949738":{"subject":"PUBCHEM.COMPOUND:6468","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"0.986878025","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMID:18544676","PMC3492801","PMC2760688","PMC3479319","PMC5598403","PMC4726088","PMC7730291","PMC6098952","PMID:17637606"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"PCP-mediated inhibition of CK2 is accompanied by activation of AKT1 and suppression of NFκB/p65 signaling pathway |PMC5598403|The activation of the PCP pathway involves molecules such as Rac, RhoA, GTPases, and the JNK cascade.|PMC6098952|Indeed several PCP components and/or modulators have been shown to promote metastasis in different human cancer types, such as WNT5A in melanoma, gastric cancer, and breast cancer by activating Rac and JNK, FZD7 in hepatocellular carcinoma and colon cancer, FZD10 in synovial sarcoma or VANGL2, which promotes cellular migration and ECM invasion of fibrosarcoma tumour cells (Fig. 2H).|PMC3492801|Other G-protein mediated pathways are the PCP (planar-cell polarity) pathway (shown in blue) leading to the activation of Rac/Rho, JNK (c-Jun N-terminal kinase) and/or ROCK (Rho associated kinase).|PMC3479319|The PCP pathway, also referred as the Wnt/Jun-N-terminal kinase (JNK) pathway, activates small GTPases, including RhoA, Rac, Cdc42, and 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as shown in Figs. 3 (for FACS analysis examples, please, see additional file 1: Additional data #1.ppt), the expression of both TGFβ1-RII and ED-A fibronectin was lower in PP cultures than in non-PP 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there was no change in the phosphorylation of Akt after acute exercise in either muscle, phosphorylation of Akt in the soleus muscle increased after single-dose clenbuterol treatment, whereas that in the TA muscle remained unchanged.|PMC3633781|In the present study, we observed an increase in the phosphorylation of p38 MAPK after single-dose clenbuterol treatment and acute exercise in the soleus muscle (Fig. 1), and likewise an increase in the phosphorylation of Akt after single-dose clenbuterol treatment in the soleus muscle (Fig. 2a).|PMC3633781|Taken together, these results indicate that clenbuterol activates the PI3K/Akt pathway and increases the size of SBMA myotubes.|PMC5259768|Clenbuterol-treated cultures also showed elevated insulin-like growth factor I (IGF-1) mRNA and activation of the protein kinase Akt.|PMID:20577844|Kline et al. also observed an increase in the phosphorylation of Akt in rat fast-twitch muscles after single-dose and long-term (9 days) treatment with 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our previous study, the expression of GLUT1 and GLUT3 and the 18F-FDG uptake were significantly decreased in BHP 2-7 cells harboring RET/PTC rearrangement after redifferentiation therapy with either sorafenib or carbozatinib, indicating that monitoring efficacy of redifferentiation therapy using 18F-FDG PET is possible.|PMC5386727|Sorafenib decreased the expression of five glycolytic enzymes, including GLUT1, GPI, PFKL, PGAM1 and PKM2, in HepG2 cells.|PMC7293092|Moreover, the recruitment of glycolytic genes GLUT1, PFKL, PKM2 was decreased under sorafenib treatment, indicating that sorafenib inhibits the recruitment of glycolysis genes by ACTR (Figure 4E).|PMC7293092|Decreases of GLUT1 expression have been previously detected by our group when reinducing thyroid cancer iodine-uptake with multikinase inhibitors, sorafenib/cabozantinib, which also target the MAPK pathway.|PMC5386727|The combination of sorafenib and EF24, a curcumin analog, can overcome hypoxia-mediated sorafenib 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recent evidence has continued to demonstrate the neuroprotective effects of dexamethasone when given prior to a hypoxic-ischemic (HI) injury in the neonatal rat model through various biological mechanisms such as the up-regulation of vascular endothelial growth factor (VEGF) and Prostaglandin D2 (PGD2) synthesis via the glucocorticoid receptor (GR).|PMC5297652|At the same time, dexamethasone causes an increase in mRNA and protein levels of vascular endothelial growth factor A (VEGF), which has neurotrophic and neurogenesis enhancing effects.|PMC3513408|In vivo studies in neonatal rats have shown that dexamethasone treatment prior to hypoxia-ischemia increased VEGF protein, reducing brain injury, decreased caspase-3 activity and DNA fragments (Feng et al.,).|PMC3493883|However, recent evidence has continued to demonstrate the neuroprotective effects of dexamethasone when given prior to a hypoxic-ischemic (HI) injury in the neonatal rat model through various biological mechanisms such as the up-regulation of vascular endothelial growth factor (VEGF) and Prostaglandin D2 (PGD2) synthesis via the glucocorticoid receptor (GR).|PMC5297652|In addition, dexamethasone plays a neuroprotective role through the upregulation of the expression of neurotrophic factors and anti-apoptosis genes, such as nerve growth factor, basic fibroblast growth factor, and vascular endothelial growth 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combined with amlodipine can offer similar renoprotective effects on that of cilazapril and may be a potent therapy to attenuate renal injury by reducing renal protein levels of TGF-beta1 in diabetes with a hypertensive state.|PMID:12150723|ET-1 may be involved in the progression of renal interstitial fibrosis following unilateral ureter ligation and blockage of its receptors with bosentan attenuates the fibroticlesion to a certain extent by possibly inhibiting TGF-beta1 and TIMP-1.|PMID:12887768|The mRNA expressions of ColI, TGF-beta1 and TIMP-1 in renal tissue subjected to ureter ligation were significantly lower in the bosentan group then in the animal model group (all P < 0.05).|PMID:12887768|The positive staining areas of ColI, TGF-beta1 and TIMP-1 in the tubulointerstitium were significantly smaller in bosentan group than in the animal model group (all P < 0.05).|PMID:12887768|Treatment of allograft recipient rats with bosentan prevented upregulation of ED-B FN and 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compounds also significantly increased the ex vivo endotoxin-induced TNF-α release, but only propranolol normalized the IFN-γ/IL-4 ratio after Con A stimulation of whole blood cultures (Fig. 4 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patients with serous PED, 7 patients with PED associated with retinal angiomatous proliferation (RAP) exhibited insufficient stabilisation after initial treatment with pegaptanib (Macugen).|PMID:18951308|The first seven patients presenting with PED received intravitreal injections of commercially available pegaptanib sodium 0.3 mg (Macugen?; [OSI] Eyetech, Inc and Pfizer Inc, New York, USA).|PMC2861946|Intravitreal injections of pegaptanib or bevacizumab are both efficacious and safe treatments for PED associated with occult CNV secondary to AMD.|PMC2861946|Intravitreal injections of pegaptanib or bevacizumab are both efficacious and safe treatments for PED associated with occult CNV secondary to AMD.|PMID:20463807|The present pilot study examined the effectiveness of pegaptanib and bevacizumab in the treatment of PED associated with occult CNV secondary to 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that, several studies showed that acute exposure to AAPs (clozapine and risperidone) inhibited GLUT1- and GLUT3-mediated glucose uptake in PC12 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and Formoterol decreased SMA, fibronectin (FN) EDA, type I collagenA1, TGFβ1, and connective tissue growth factor (CCN2) gene expression by 24 to 49% and increased FGF2 gene expression by 1.2- and 2.1-fold, respectively, after 6 hours (Figure 2d).|PMC4263603|Compared with ZF lean rats, vehicle-treated ZDF showed an increased cardiac expression of collagen I/IV and fibronectin while salbutamol treatment significantly attenuated these changes (Figure 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is consistent with results from others showing that ibuprofen diminishes MDSC overall abundance and M2 associated cytokines (IL-4/IL-10) while facilitating IL-12 production.|PMC6167844|We have previously shown that ibuprofen started a day following inoculation decreases the range of Il-17 and Il-13 production with respect to interferon γ and IL-4.|PMC8191941","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"38428999":{"subject":"UMLS:C4529301","object":"NCBIGene:5879","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:de643f8b10a9972de8e761a2d546f8ad5f406570c8715fa5acc8618418f7c249","tmkp:c3819f2635f78feb8d4485ded31c5e5bbdf036036e197c0b90ae3c27d3e876b7"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:publications","value":["PMC6387347","PMC4791963"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"This study also provided evidence that bevacizumab or VEGFR-targeted therapy in prostate cancer is more efficacious if it is combined with targeted inhibition of the NRP2 effectors P-Rex1 and Rac1.|PMC6387347|Our data raise the exciting possibility that bevacizumab or VEGFR-targeted therapy in prostate cancer could be efficacious if it were combined with targeted inhibition of P-Rex1/Rac1.|PMC4791963","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:Attribute","value":"0.998402385","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"68604085":{"subject":"PUBCHEM.COMPOUND:5073","object":"NCBIGene:2277","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"As RT-PCR and Western blot revealed that the treatment effects of risperidone and haloperidol seemed to be mediated through activation of VEGF and MMP2.|PMID:19579000|The findings indicate a promoting effect of risperidone 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hyperosmolarity induced by sucrose and monodansyl-cadaverine blocked Erk activity induced by hop/STI-1, without affecting the high basal Akt activity typical of A172.|PMID:17498662|Reversible blocking of NT/neurotensin receptor (NTR) complex endocytosis by hyperosmolar sucrose totally abolished both the phosphorylation of the MAP kinases Erk1/2 and the [3H]-thymidine incorporation induced by the peptide.|PMID:16870305|Significant ERK1/2 phosphorylation was observed only in conditions in which opioids triggered endocytosis and was blocked by hypertonic sucrose, or dynasore, a dynamin inhibitor, and in enteric neurons transfected with a dominant negative K44E mutant dynamin, which prevent clathrin-dependent, dynamin-mediated 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clear, dose-dependent reduction of proteasomal activity was also seen in the presence of increasing doses of dopamine, which was accompanied by a slight dose-dependent increase of caspases activities and Bcl-2 levels.|PMID:17647258|We found that treatment with DPD, dopamine + NECA, dBu-cAMP, or 5IT (iodotubercidin), an adenosine kinase inhibitor, increased the expression level of an anti-apoptotic protein BCL2 (Figure 6A).|PMC4944721|In human neuroblastoma SH-SY5Y cells, excess dopamine-induced cell death could be inhibited by resveratrol through ameliorating intracellular oxidative stress and enhancing the activity of Bcl-2, thus disrupting the apoptotic 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line with mRNA regulation (Figure 2C), we found a decrease in the intracellular expression of the mature form of IL-4 in Vδ2 T-cells after treatment with 5 mM VPA (Figure 3A, middle panel).|PMC5323112|“Toxic” concentrations of VPA (5 mM) significantly induced expression of IL-4δ13 and decreased the expression of mature IL-4, but did not modulate IFN-γ cytokine.|PMC5323112|(D) Dose-dependent inhibition by VPA of plasma cell (B220loCD138+) differentiation (upper row) in B cells stimulated for 4 d with LPS plus IL-4, without alteration of plasma cell viability, as analyzed by 7-AAD staining (lower row, proportions of 7-AAD− viable cell among B220loCD138+ cells are indicated).|PMC4258531|Both preventive (from Day 0 to Day 18) and therapeutic (from Day 7 to Day 18 or from Day 9 to Day 19) VPA (500 mg/kg, intra-gastric) administration to EAE rats once daily greatly reduced the severity and duration of EAE, and suppressed mRNA levels of interferon-γ (IFN-γ), tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β) and IL-17, matrix metalloproteinase 9 (MMP9), inducible nitric oxide synthase (iNOS) and transcription factor T-bet, but increased levels of IL-4 mRNA in EAE spinal cords.|PMID:22800566|We found a significant reduction of IL-1 and IL-2 levels with all tested drugs other than lithium in the CD3/5C3-stimulated blood; VPA led to a decrease in IL-1β, IL-2, IL-4, IL-6, IL-17, and TNF-α production, which substantiates and adds knowledge to current hypotheses on VPA's anti-inflammatory properties.|PMID:24757498","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"}]},"61117073":{"subject":"PUBCHEM.COMPOUND:19649","object":"NCBIGene:6517","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"downregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":"Streptomycin reduced the increase seen in GLUT4 protein following CLFS 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cells.|PMID:25073960","value_type_id":"EDAM:data_0006","original_attribute_name":"sentences"},{"attribute_type_id":"biolink:aggregator_knowledge_source","value":["infores:automat-robokop"],"value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:aggregator_knowledge_source","attribute_source":"infores:automat-robokop"}]},"41567786":{"subject":"PUBCHEM.COMPOUND:962","object":"NCBIGene:207","predicate":"biolink:regulates","qualifiers":[{"qualifier_type_id":"biolink:object_direction_qualifier","qualifier_value":"upregulated"}],"attributes":[{"attribute_type_id":"biolink:Attribute","value":["tmkp:c28346d3c26ba81c9ed00ac8a520c0257b1011fd03837c55f2d6b33ef79b862c","tmkp:39910aa70ce0e4726e37142a3d123568fa5a7538d39a7d68ca8a5981d48ec9cc","tmkp:8e251e32cf7ea40d4026f1ba1176c7d1bd352b13c6a74969fbaf4de3e5dff319","tmkp:fd16bdf32d1f5c7f4478fbe876bbc4d162062f952a944f1e60d8edfd0fb3c344","tmkp:ab072cc37d7b8e6730203edf1fc29b7412bbe6af0d9f98c4fe34e8be24749d39","tmkp:6d1615cc943432a01b220892dcfce5a3dbf3677f9b24aa4ba56d872f65516298","tmkp:a651c2ecdad225720a8dccc0acdfb36b720ba2f42ba290667425638f7adaca5a","tmkp:3ffae576b7d70ae690f22c456ca46286cb7817a54a170ff5faf53abb12f84471","tmkp:30ef43fdeb3e122030b72f6afd4eda93c33b0819053f911fbea5f3ee98f45a05","tmkp:efdca80e1b2a6fa73feac9d1576bb2b195c47aa32398ad534c08bbbf26e23170"],"value_type_id":"EDAM:data_0006","original_attribute_name":"tmkp_ids"},{"attribute_type_id":"biolink:has_numeric_value","value":1,"value_type_id":"EDAM:data_1669","original_attribute_name":"weight"},{"attribute_type_id":"biolink:primary_knowledge_source","value":"infores:textminingkp","value_type_id":"biolink:InformationResource","original_attribute_name":"biolink:primary_knowledge_source","attribute_source":"infores:automat-robokop"},{"attribute_type_id":"biolink:Attribute","value":"0.9905182307692308","value_type_id":"EDAM:data_0006","original_attribute_name":"biolink:tmkp_confidence_score"},{"attribute_type_id":"biolink:publications","value":["PMC5555886","PMID:16339203","PMC6241369","PMC7833367","PMC6801723","PMID:21050718","PMID:31315738","PMC4286153","PMC6607866"],"value_type_id":"EDAM:data_0006","original_attribute_name":"publications"},{"attribute_type_id":"biolink:Attribute","value":"Hydrogen-rich water activates the PI3K/Akt pathway, thereby mediates mice astrocytes to exert the biological function of antioxidant.|PMID:31315738|Doxycycline was administered through the drinking water to all animals from weeks 9–12 of the experiment, which caused a muscle-specific Akt1 induction in the DTG mice but not in the single transgenic controls.|PMC4286153|In this study we demonstrated that local testicular heat treatment of adult monkey with water at 43 C for 30 min once daily for 2 consecutive days was capable of activating reexpression of ck-18 in Sertoli cells, which was coincident with activation of ERK1/2 and Akt kinases.|PMID:16339203|(2013) also reported that the phosphorylation of Akt‐mTOR signaling components Akt and p70S6K was significantly increased in soleus and plantaris muscles immediately after warm water immersion (41°C for 30 min).|PMC5555886|In the glucose plus WPH group, the levels of phosphorylated Akt were increased significantly compared to the group ingesting water 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show the utility of tele-presence in medicine, the scope of this pilot study included evaluating PTP as an alternative method to TNT in a PED.|PMC3972345|The objective of the study is to compare traditional nurse triage (TNT) in a pediatric emergency department (PED) with physician telepresence (PTP).|PMID:24445223|To compare traditional nurse triage (TNT) in a Pediatric Emergency Department (PED) to physician tele-presence 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porcine epidemic diarrhea virus (PEDV) strain CV777, an enveloped virus member of the Coronaviridae family, genus Alphacoronavirus, and etiological agent of porcine epidemic diarrhea (PED), was preliminary used to evaluate the water concentration protocol together with the mengovirus (MgV) vMC0 (CECT 100000), a non-enveloped member of the Picornaviridae designated in the standard method as process 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