PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26657071-8 2015 Overall the results indicate that preventing N-glycosylation of hCES1 does not significantly affect the structure or activity of the enzyme. Nitrogen 45-46 carboxylesterase 1 Homo sapiens 64-69 33206527-10 2020 To investigate the regulatory effect of the N79 glycan on cellular growth, we mutated the single N-glycosylation site in CES1 from Asn to Gln (CES1-N79Q) via site-directed mutagenesis. Nitrogen 44-45 carboxylesterase 1 Homo sapiens 121-125 28112927-6 2017 A series of N-methylated amino derivatives, which are unable to undergo such tautomerism, were equal in potency to the phenoxy analogues and demonstrated selectivity for the liver enzyme hCE1. Nitrogen 12-13 carboxylesterase 1 Homo sapiens 187-191 25703794-2 2015 Our results suggest that an ionic S(N)2-Si outer-sphere pathway involving the heterolytic cleavage of the Si-H bond competes with the hydride pathway involving the C=N bond inserted into the Re-H bond for the rhenium hydride (1) catalyzed hydrosilylation of the less steric C=N functionalities (phenylmethanimine, PhCH=NH, and N-phenylbenzylideneimine, PhCH=NPh). Nitrogen 36-37 carboxylesterase 1 Homo sapiens 191-195 35500091-0 2022 Abatement of Nitrogen Oxides via Selective Catalytic Reduction over Ce1-W1 Atom-Pair Sites. Nitrogen 13-21 carboxylesterase 1 Homo sapiens 68-71