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	
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	
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