PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9311626-1 1997 Purified human liver carboxylesterase (hCE-1) catalyzes the hydrolysis of cocaine to form benzoylecgonine, the deacetylation of heroin to form 6-acetylmorphine, and the ethanol-dependent transesterification of cocaine to form cocaethylene. Ethanol 169-176 carboxylesterase 1 Homo sapiens 39-44 12773168-2 2003 hCE1 catalyses the hydrolysis of heroin and cocaine, and the transesterification of cocaine in the presence of ethanol to the toxic metabolite cocaethylene. Ethanol 111-118 carboxylesterase 1 Homo sapiens 0-4 10381793-5 1999 Meperidine was hydrolyzed to meperidinic acid and ethanol by hCE-1 but not hCE-2. Ethanol 50-57 carboxylesterase 1 Homo sapiens 61-66 7980644-4 1994 The carboxylesterase obeys simple Michaelis-Menten kinetics with Km values of 116 microM for cocaine and 43 mM for ethanol. Ethanol 115-122 carboxylesterase 1 Homo sapiens 4-20 27075303-9 2016 Knockdown of hepatic CES1 exacerbated ethanol-induced steatohepatitis. Ethanol 38-45 carboxylesterase 1 Homo sapiens 21-25 31871135-6 2020 Currently, the loss-of-function SNP G143E (rs71647871) is the only clinically significant CES1 variant identified to date, and alcohol is the only potent CES1 inhibitor that could alter the therapeutic outcomes of CES1 substrate medications. Ethanol 127-134 carboxylesterase 1 Homo sapiens 154-158 31871135-6 2020 Currently, the loss-of-function SNP G143E (rs71647871) is the only clinically significant CES1 variant identified to date, and alcohol is the only potent CES1 inhibitor that could alter the therapeutic outcomes of CES1 substrate medications. Ethanol 127-134 carboxylesterase 1 Homo sapiens 154-158 31871135-7 2020 However, G143E and alcohol can only explain a small portion of the interindividual variability in the CES1 function. Ethanol 19-26 carboxylesterase 1 Homo sapiens 102-106 31028056-9 2019 For example, (a) with transdermal dl-MPH delivery; (b) in cases of concomitant dl-MPH and a CES1 inhibitor, e.g., ethanol, which elevates l-MPH and d-MPH concentrations; (d) in forensic studies of intravenous or intranasal dl-MPH abuse; (e) were dl-MPH to be formulated as a free base sublingual product; or (f) as emerging advances in dl-MPH gene-dose effects warrant isomer correlations. Ethanol 114-121 carboxylesterase 1 Homo sapiens 92-96 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. Ethanol 0-7 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. Ethanol 0-7 carboxylesterase 1 Homo sapiens 88-92 25103325-4 2014 The aim of this study is to develop a physiologically based pharmacokinetic (PBPK) model to predict changes in CES1 substrate drug exposure in humans with CES1 activity impaired by ethanol or loss-of-function CES1 genetic polymorphisms. Ethanol 181-188 carboxylesterase 1 Homo sapiens 111-115 25103325-4 2014 The aim of this study is to develop a physiologically based pharmacokinetic (PBPK) model to predict changes in CES1 substrate drug exposure in humans with CES1 activity impaired by ethanol or loss-of-function CES1 genetic polymorphisms. Ethanol 181-188 carboxylesterase 1 Homo sapiens 155-159 25103325-4 2014 The aim of this study is to develop a physiologically based pharmacokinetic (PBPK) model to predict changes in CES1 substrate drug exposure in humans with CES1 activity impaired by ethanol or loss-of-function CES1 genetic polymorphisms. Ethanol 181-188 carboxylesterase 1 Homo sapiens 155-159 25103325-7 2014 Then the changes in oseltamivir and OSC exposure in humans with CES1 impaired by ethanol or polymorphisms were simulated using a PBPK model incorporating in vitro inhibition and enzyme kinetic data. Ethanol 81-88 carboxylesterase 1 Homo sapiens 64-68 25103325-10 2014 RESULTS: The simulated changes in oseltamivir and OSC exposures in humans with CES1 impaired by ethanol or polymorphism were similar to the observed data. Ethanol 96-103 carboxylesterase 1 Homo sapiens 79-83 23104969-2 2013 Coadministration of dl-MPH with ethanol results in elevated d-MPH plasma concentrations accompanied by CES1-mediated enantioselective transesterification of l-MPH to l-ethylphenidate (EPH). Ethanol 32-39 carboxylesterase 1 Homo sapiens 103-107 23104969-3 2013 The present study tested the hypothesis that administration of the pure isomer dexmethylphenidate (d-MPH) will overcome the influence of ethanol on d-MPH absorption by eliminating competitive CES1-mediated presystemic metabolism of l-MPH to l-EPH. Ethanol 137-144 carboxylesterase 1 Homo sapiens 192-196 21402502-1 2011 In humans, concomitant DL-methylphenidate (DL-MPH) and ethanol results in the carboxylesterase 1 (hCES1) mediated biotransformation of MPH to the transesterification metabolite DL-ethylphenidate (DL-EPH). Ethanol 55-62 carboxylesterase 1 Homo sapiens 78-96 21402502-1 2011 In humans, concomitant DL-methylphenidate (DL-MPH) and ethanol results in the carboxylesterase 1 (hCES1) mediated biotransformation of MPH to the transesterification metabolite DL-ethylphenidate (DL-EPH). Ethanol 55-62 carboxylesterase 1 Homo sapiens 98-103