PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19062296-1 2009 Carboxylesterases are enzymes that hydrolyze a broad suite of endogenous and exogenous ester-containing compounds to the corresponding alcohol and carboxylic acid. Alcohols 135-142 carboxylesterase 1 Homo sapiens 0-17 19062296-12 2009 This finding was successfully applied to examine substrate selectivity, demonstrating that the relative volumes of the alcohol and acid moieties of ester-containing substrates were predictive for whether hydrolysis was preferred by hiCE or hCE1. Alcohols 119-126 carboxylesterase 1 Homo sapiens 240-244 18305428-5 2008 The CES1 isozyme mainly hydrolyzes a substrate with as mall alcohol group and large acyl group, but its wide active pocket sometimes allows it to act on structurally distinct compounds of either a large or small alcohol moiety. Alcohols 60-67 carboxylesterase 1 Homo sapiens 4-8 18305428-5 2008 The CES1 isozyme mainly hydrolyzes a substrate with as mall alcohol group and large acyl group, but its wide active pocket sometimes allows it to act on structurally distinct compounds of either a large or small alcohol moiety. Alcohols 212-219 carboxylesterase 1 Homo sapiens 4-8 17936933-1 2007 Carboxylesterases (CEs) are traditionally regarded as xenobiotic metabolizing enzymes that hydrolyze esterified xenobiotics to alcohol and carboxylic acid products. Alcohols 127-134 carboxylesterase 1 Homo sapiens 0-17 17651701-8 2007 Phenylvalerate as a non-specific carboxylesterase substrate was hydrolysed mainly by hCE1 in human livers and there was good correlation with small alcohol leaving group parabens, suggesting hCE1 involvement. Alcohols 148-155 carboxylesterase 1 Homo sapiens 33-49 17651701-8 2007 Phenylvalerate as a non-specific carboxylesterase substrate was hydrolysed mainly by hCE1 in human livers and there was good correlation with small alcohol leaving group parabens, suggesting hCE1 involvement. Alcohols 148-155 carboxylesterase 1 Homo sapiens 85-89 16837570-7 2006 The hydrolytic activity of hCE-2 increased with increasing alcohol chain length in benzoic acid derivative substrates, whereas hCE-1 preferentially catalyzed the hydrolysis of substrates with short alcohol chains. Alcohols 198-205 carboxylesterase 1 Homo sapiens 127-132 16837570-9 2006 Furthermore, the addition of hydrophobic alcohols to the reaction mixture with p-aminobenzoic acid propyl ester induced high and low levels of transesterification by hCE-1 and hCE-2, respectively. Alcohols 41-49 carboxylesterase 1 Homo sapiens 166-171 31039046-3 2020 The purpose of this study is to determine the effects of the known CES1 inhibitor alcohol on clopidogrel metabolism: (1) in vitro in human recombinant CES1 and human liver S9 (HLS9) fractions and (2) in a plasma carboxylesterase deficient mouse (Es1e) strain administered 25 mg/kg oral clopidogrel alone and with 3 g/kg alcohol. Alcohols 82-89 carboxylesterase 1 Homo sapiens 67-71 33626394-6 2021 SIGNIFICANCE: Short-term standard alcohol consumption would significantly enhance suppression of ADP-induced platelet aggregation and activation by clopidogrel through significant inhibition of Nrf2/Ces1 signaling pathway and induction of Cyp2c, suggesting that alcohol may interact with drugs that are predominantly metabolized by CES1 or CYP2C in patient care, including clopidogrel. Alcohols 34-41 carboxylesterase 1 Homo sapiens 199-203 33626394-6 2021 SIGNIFICANCE: Short-term standard alcohol consumption would significantly enhance suppression of ADP-induced platelet aggregation and activation by clopidogrel through significant inhibition of Nrf2/Ces1 signaling pathway and induction of Cyp2c, suggesting that alcohol may interact with drugs that are predominantly metabolized by CES1 or CYP2C in patient care, including clopidogrel. Alcohols 34-41 carboxylesterase 1 Homo sapiens 332-336 33626394-6 2021 SIGNIFICANCE: Short-term standard alcohol consumption would significantly enhance suppression of ADP-induced platelet aggregation and activation by clopidogrel through significant inhibition of Nrf2/Ces1 signaling pathway and induction of Cyp2c, suggesting that alcohol may interact with drugs that are predominantly metabolized by CES1 or CYP2C in patient care, including clopidogrel. Alcohols 262-269 carboxylesterase 1 Homo sapiens 332-336 16858120-4 2006 hCE-1 mainly hydrolyzes a substrate with a small alcohol group and large acyl group, but its wide active pocket sometimes allows it to act on structurally distinct compounds of either large or small alcohol moiety. Alcohols 49-56 carboxylesterase 1 Homo sapiens 0-5 16858120-4 2006 hCE-1 mainly hydrolyzes a substrate with a small alcohol group and large acyl group, but its wide active pocket sometimes allows it to act on structurally distinct compounds of either large or small alcohol moiety. Alcohols 199-206 carboxylesterase 1 Homo sapiens 0-5 16858120-6 2006 Furthermore, hCE-1 shows high transesterification activity, especially with hydrophobic alcohol, but negligible for hCE-2. Alcohols 88-95 carboxylesterase 1 Homo sapiens 13-18 16858120-7 2006 Transesterification may be a reason for the substrate specificity of hCE-1 that hardly hydrolyzes a substrate with hydrophobic alcohol group, because transesterification can progress at the same time when a compound is hydrolyzed by hCE-1. Alcohols 127-134 carboxylesterase 1 Homo sapiens 69-74 16858120-7 2006 Transesterification may be a reason for the substrate specificity of hCE-1 that hardly hydrolyzes a substrate with hydrophobic alcohol group, because transesterification can progress at the same time when a compound is hydrolyzed by hCE-1. Alcohols 127-134 carboxylesterase 1 Homo sapiens 233-238 7980644-0 1994 Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine. Alcohols 164-171 carboxylesterase 1 Homo sapiens 51-75 31039046-3 2020 The purpose of this study is to determine the effects of the known CES1 inhibitor alcohol on clopidogrel metabolism: (1) in vitro in human recombinant CES1 and human liver S9 (HLS9) fractions and (2) in a plasma carboxylesterase deficient mouse (Es1e) strain administered 25 mg/kg oral clopidogrel alone and with 3 g/kg alcohol. Alcohols 320-327 carboxylesterase 1 Homo sapiens 67-71 31693270-2 2020 In this study, elucidation of the chiral recognition ability of hCES1 was attempted using indomethacin esters in which various chiral alcohols were introduced. Alcohols 134-142 carboxylesterase 1 Homo sapiens 64-69 32258948-3 2020 Hepatocyte-specific expression of human CES1 prevented Western diet or alcohol-induced steatohepatitis and hyperlipidemia. Alcohols 71-78 carboxylesterase 1 Homo sapiens 40-44 27075303-0 2016 Carboxylesterase 1 Is Regulated by Hepatocyte Nuclear Factor 4alpha and Protects Against Alcohol- and MCD diet-induced Liver Injury. Alcohols 89-96 carboxylesterase 1 Homo sapiens 0-18 27075303-6 2016 Alcohol repressed both HNF4alpha and CES1 expression in primary hepatocytes. Alcohols 0-7 carboxylesterase 1 Homo sapiens 37-41 27075303-8 2016 Global inactivation of CES1 aggravated alcohol- or MCD diet-induced liver inflammation and liver injury, likely as a result of increased production of acetaldehyde and reactive oxygen species and mitochondrial dysfunctions. Alcohols 39-46 carboxylesterase 1 Homo sapiens 23-27 27075303-10 2016 These data indicate that CES1 plays a crucial role in protection against alcohol- or MCD diet-induced liver injury. Alcohols 73-80 carboxylesterase 1 Homo sapiens 25-29 25103325-2 2014 Ethanol (alcohol)-mediated inhibition of CES1 and loss-of-function polymorphisms in the CES1 gene can markedly reduce this enzyme"s function. Alcohols 9-16 carboxylesterase 1 Homo sapiens 41-45 25103325-2 2014 Ethanol (alcohol)-mediated inhibition of CES1 and loss-of-function polymorphisms in the CES1 gene can markedly reduce this enzyme"s function. Alcohols 9-16 carboxylesterase 1 Homo sapiens 88-92 24512105-10 2014 The enzyme encoded by CES1 is a major liver enzyme that typically catalyzes the decomposition of ester into alcohol and carboxylic acid and is involved in drug or xenobiotics, fatty acid, and cholesterol metabolisms. Alcohols 108-115 carboxylesterase 1 Homo sapiens 22-26 23386702-1 2013 UNLABELLED: Carboxylesterases hydrolyze esters, amides, and thioesters to produce carboxylic acids and resulting alcohols, amines, and thiols, respectively. Alcohols 113-121 carboxylesterase 1 Homo sapiens 12-29 28126414-1 2017 Mammalian carboxylesterases (CEs) are important serine hydrolases catalyzing the hydrolysis of ester- or amide-containing compounds into the corresponding alcohols and carboxylic acids. Alcohols 155-163 carboxylesterase 1 Homo sapiens 10-27 29911769-5 2017 Our results clearly demonstrated that the substrate specificity of these ester substrates towards hCE1 would be improved with the decrease of the alcohol group on BODIPY-8-carboxylesters, while BODIPY-8-carboxylesters with small alcohol groups including methyl (BCM) and ethyl (BCE) esters could serve as the ideal probe substrates for hCE1. Alcohols 146-153 carboxylesterase 1 Homo sapiens 98-102 29911769-5 2017 Our results clearly demonstrated that the substrate specificity of these ester substrates towards hCE1 would be improved with the decrease of the alcohol group on BODIPY-8-carboxylesters, while BODIPY-8-carboxylesters with small alcohol groups including methyl (BCM) and ethyl (BCE) esters could serve as the ideal probe substrates for hCE1. Alcohols 146-153 carboxylesterase 1 Homo sapiens 336-340 29911769-5 2017 Our results clearly demonstrated that the substrate specificity of these ester substrates towards hCE1 would be improved with the decrease of the alcohol group on BODIPY-8-carboxylesters, while BODIPY-8-carboxylesters with small alcohol groups including methyl (BCM) and ethyl (BCE) esters could serve as the ideal probe substrates for hCE1. Alcohols 229-236 carboxylesterase 1 Homo sapiens 98-102 26164127-3 2015 It is generally recognized that CES1 prefers compounds with a large acyl moiety and a small alcohol or amine moiety as substrates, whereas CES2 prefers compounds with a small acyl moiety and a large alcohol or amine moiety. Alcohols 92-99 carboxylesterase 1 Homo sapiens 32-36 26164127-3 2015 It is generally recognized that CES1 prefers compounds with a large acyl moiety and a small alcohol or amine moiety as substrates, whereas CES2 prefers compounds with a small acyl moiety and a large alcohol or amine moiety. Alcohols 199-206 carboxylesterase 1 Homo sapiens 32-36 25511794-3 2015 The aim of this study was to determine the impact of alcohol on the metabolism of specific probes for CES1 (oseltamivir) and CES2 (aspirin). Alcohols 53-60 carboxylesterase 1 Homo sapiens 102-106 25511794-4 2015 METHODS: The effect of alcohol on CES1- and CES2-mediated probe drug hydrolysis was determined in vitro using recombinant human carboxylesterase. Alcohols 23-30 carboxylesterase 1 Homo sapiens 34-38 25511794-6 2015 RESULTS: Alcohol significantly inhibited oseltamivir hydrolysis by CES1 in vitro but did not affect aspirin metabolism by CES2. Alcohols 9-16 carboxylesterase 1 Homo sapiens 67-71 25511794-9 2015 CONCLUSIONS: Alcohol significantly inhibited the hydrolysis of oseltamivir by CES1 both in vitro and in humans, but did not affect the hydrolysis of aspirin to salicylic acid by CES2. Alcohols 13-20 carboxylesterase 1 Homo sapiens 78-82 25511794-10 2015 These results suggest that alcohol"s inhibition of CES1 could potentially result in clinically significant drug interactions with other CES1-substrate drugs, but it is unlikely to significantly affect CES2-substrate drug hydrolysis. Alcohols 27-34 carboxylesterase 1 Homo sapiens 51-55 25511794-10 2015 These results suggest that alcohol"s inhibition of CES1 could potentially result in clinically significant drug interactions with other CES1-substrate drugs, but it is unlikely to significantly affect CES2-substrate drug hydrolysis. Alcohols 27-34 carboxylesterase 1 Homo sapiens 136-140 25445008-7 2015 Compounds bearing a small alcohol part and a larger acyl part showed higher affinity to hCES1 while those with a large alcohol part showed higher affinity to hCES2. Alcohols 26-33 carboxylesterase 1 Homo sapiens 88-93