PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25346527-6 2015 To identify the enzyme(s) responsible for the amide hydrolysis, incubations with recombinant carboxylesterases and human serum, as well as inhibition studies in HLM and human pulmonary microsomes (HPM) were performed. Amides 46-51 carboxylesterase 1 Homo sapiens 93-110 26900660-1 2016 Human carboxylesterase 2 (hCE2), one of the major carboxylesterases in the human intestine and various tumour tissues, plays important roles in the oral bioavailability and treatment outcomes of ester- or amide-containing drugs or prodrugs, such as anticancer agents CPT-11 (irinotecan) and LY2334737 (gemcitabine). Amides 205-210 carboxylesterase 1 Homo sapiens 50-67 29407485-2 2018 Carboxylesterases (CESs) are enzymes catalyzing the hydrolysis of many structurally different ester, amide and carbamate chemicals, including prodrugs. Amides 101-106 carboxylesterase 1 Homo sapiens 0-17 29054529-0 2017 Development of amide-based fluorescent probes for selective measurement of carboxylesterase 1 activity in tissue extracts. Amides 15-20 carboxylesterase 1 Homo sapiens 75-93 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. Amides 105-110 carboxylesterase 1 Homo sapiens 10-27 26825642-1 2016 Human hepatic carboxylesterase 1 and 2 (CES1 and CES2) are important for the disposition of ester- and amide-bond-containing pharmaceuticals and environmental chemicals. Amides 103-108 carboxylesterase 1 Homo sapiens 14-32 26825642-1 2016 Human hepatic carboxylesterase 1 and 2 (CES1 and CES2) are important for the disposition of ester- and amide-bond-containing pharmaceuticals and environmental chemicals. Amides 103-108 carboxylesterase 1 Homo sapiens 40-44 25346527-7 2015 Carboxylesterase 1 (CES1) was identified as the major human hepatic and pulmonary enzyme responsible for the amide hydrolysis.We employed similar studies to identify the esterase(s) involved in the previously described hydrolytic metabolism of two quinolineindole synthetic cannabinoids, PB-22 and 5F-PB-22, as well as the closely related compound, BB-22. Amides 109-114 carboxylesterase 1 Homo sapiens 0-18 25346527-7 2015 Carboxylesterase 1 (CES1) was identified as the major human hepatic and pulmonary enzyme responsible for the amide hydrolysis.We employed similar studies to identify the esterase(s) involved in the previously described hydrolytic metabolism of two quinolineindole synthetic cannabinoids, PB-22 and 5F-PB-22, as well as the closely related compound, BB-22. Amides 109-114 carboxylesterase 1 Homo sapiens 20-24 21918037-1 2011 The carboxylesterases (CESs) are a family of serine hydrolases that hydrolyze compounds containing an ester, amide, or thioester. Amides 109-114 carboxylesterase 1 Homo sapiens 4-21 24988246-1 2014 Human carboxylesterase 1 (CES1) and carboxylesterase 2 (CES2) are serine esterases responsible for the hydrolysis of ester and amide bonds present in a number of pharmaceutical products. Amides 127-132 carboxylesterase 1 Homo sapiens 6-24 24988246-1 2014 Human carboxylesterase 1 (CES1) and carboxylesterase 2 (CES2) are serine esterases responsible for the hydrolysis of ester and amide bonds present in a number of pharmaceutical products. Amides 127-132 carboxylesterase 1 Homo sapiens 26-30 23386599-1 2013 Carboxylesterases are a multigene family of mammalian enzymes widely distributed throughout the body that catalyze the hydrolysis of esters, amides, thioesters, and carbamates. Amides 141-147 carboxylesterase 1 Homo sapiens 0-17 25462813-1 2015 Human liver carboxylesterase 1 (CES1) plays a critical role in the hydrolysis of various ester- and amide-containing molecules, including active metabolites, drugs and prodrugs. Amides 100-105 carboxylesterase 1 Homo sapiens 6-30 25462813-1 2015 Human liver carboxylesterase 1 (CES1) plays a critical role in the hydrolysis of various ester- and amide-containing molecules, including active metabolites, drugs and prodrugs. Amides 100-105 carboxylesterase 1 Homo sapiens 32-36 23386702-1 2013 UNLABELLED: Carboxylesterases hydrolyze esters, amides, and thioesters to produce carboxylic acids and resulting alcohols, amines, and thiols, respectively. Amides 48-54 carboxylesterase 1 Homo sapiens 12-29 23647544-1 2013 Human carboxylesterase I (hCES 1) plays an important role in the metabolism and activation of prodrugs, such as, the hydrolysis of a variety of drugs of prodrugs featuring an ester, amide or carbamate function. Amides 182-187 carboxylesterase 1 Homo sapiens 26-32 22100607-5 2012 Carboxylesterases (CES, EC 3.1.1.1) metabolize a number of xenobiotic and endobiotic compounds containing ester, amide, and thioester bonds and are important in the metabolism of many pharmaceuticals. Amides 113-118 carboxylesterase 1 Homo sapiens 0-17 18983829-1 2009 Carboxylesterases hydrolyze chemicals containing such functional groups as a carboxylic acid ester, amide and thioester. Amides 100-105 carboxylesterase 1 Homo sapiens 0-17 8496932-2 1993 Modification of fatty acid anilide ACAT inhibitors: bioisosteric replacement of the amide bond. Amides 84-89 carboxylesterase 1 Homo sapiens 35-39 18305428-1 2008 Mammalian carboxylesterases (CESs) comprise a multigene family whose gene products play important roles in biotransformation of ester- or amide-type prodrugs. Amides 138-143 carboxylesterase 1 Homo sapiens 10-27 15908471-9 2005 Since the substrate specificity of hCE-1 differs from that of hCE-2, it is suggested that the prediction of human intestinal absorption using Caco-2 cell monolayers should be performed carefully in the case of ester- and amide-containing drugs such as prodrugs. Amides 221-226 carboxylesterase 1 Homo sapiens 35-40 8496932-3 1993 In order to further define the structural features necessary for potent inhibition of acyl-coenzyme A:cholesterol acyltransferase (ACAT) in vitro and cholesterol lowering in vivo, systematic study of bioisosteric replacements for the amide bond in our previously identified series of fatty acid anilide ACAT inhibitors was undertaken. Amides 234-239 carboxylesterase 1 Homo sapiens 131-135 8496932-4 1993 Only replacement of amide bonds with isosterases having both hydrogen bond donor and acceptor functionalities yielded compounds retaining ACAT inhibitory activity. Amides 20-25 carboxylesterase 1 Homo sapiens 138-142 8496932-5 1993 Replacement of the amide bond with the urea bioisostere yielded compounds that were potent ACAT inhibitors in vitro and efficacious hypocholesterolemic agents in vivo. Amides 19-24 carboxylesterase 1 Homo sapiens 91-95 33864822-1 2021 AIMS: Human carboxylesterases (CESs) and arylacetamide deacetylase (AADAC) are serine-esterase enzymes catalyzing the hydrolysis of many compounds containing esters, amides, thioesters, or acetyl groups. Amides 166-172 carboxylesterase 1 Homo sapiens 12-29