PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30111624-4	2018	In this study, we expressed recombinant human UGT1A10 in human embryonic kidney (HEK)293 and Chinese hamster ovary (CHO) cells to examine its oligomeric states and characterize its enzymatic activities against two therapeutically interesting substrates, morphine and entacapone, including determination of the catalytic rate constant (kcat) values for the first time.	entacapone	267-277	UDP glucuronosyltransferase family 1 member A10	Homo sapiens	46-53	
30111624-6	2018	Owing to the formation of the covalently crosslinked higher-order oligomers, the UGT1A10 protein expressed in HEK293 cells had much lower catalytic activity (particularly the catalytic rate constant kcat) against both morphine and entacapone, compared with the UGT1A10 protein form expressed in CHO cells against the same substrates.	entacapone	231-241	UDP glucuronosyltransferase family 1 member A10	Homo sapiens	81-88	
25301937-5	2015	For example, similarly to the human UGT1A10, dUGT1A11 exhibited high glucuronidation activity toward the 3-OH of 17-beta-estradiol, 17-alpha-estradiol, and ethinylestradiol, and also conjugated the drug entacapone.	entacapone	203-213	UDP glucuronosyltransferase family 1 member A10	Homo sapiens	36-43	
27089846-4	2016	The results demonstrated that both tolcapone and entacapone exhibited inhibitory effects on UGT1A1, UGT1A7, UGT1A9 and UGT1A10.	entacapone	49-59	UDP glucuronosyltransferase family 1 member A10	Homo sapiens	119-126