PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25451576-0	2014	Demethylation of neferine in human liver microsomes and formation of quinone methide metabolites mediated by CYP3A4 accentuates its cytotoxicity.	quinone	69-76	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	109-115	
32184040-6	2020	Outside of this compound, the other synthesized compounds, which could avoid the generation of a reactive quinone-methide intermediate, inhibited CYP3A4 equal to or stronger than NVP.	quinone	106-113	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	146-152	
20507089-9	2010	Characterization of the GSH conjugate structures allowed insight(s) into the bioactivation pathway, which involved CYP3A4-mediated phenol ring oxidation to the catechol, followed by further oxidation to the electrophilic ortho-quinone species.	quinone	227-234	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	115-121	
22517972-0	2012	Sequential metabolism of AMG 487, a novel CXCR3 antagonist, results in formation of quinone reactive metabolites that covalently modify CYP3A4 Cys239 and cause time-dependent inhibition of the enzyme.	quinone	84-91	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	136-142	
19364830-8	2009	In addition, the quinone methide reactive metabolite was a mechanism-based inactivator of CYP3A4, with inactivation parameters K(I) = 31 microM and k(inact) = 0.029 min(-1), respectively.	quinone	17-24	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	90-96	
19358519-12	2009	These studies suggest that the CYP3A4 mediated quinone methide formation was associated with dauricine bioactivation.	quinone	47-54	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	31-37	
10534310-6	1999	The results suggest that in human liver both CYP2C8 and CYP3A4 have major roles in quinone-type metabolite formation and that the hepatic contents of these two P-450 forms determine which P-450 enzymes play major roles in individual humans.	quinone	83-90	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	56-62	
10534310-7	1999	CYP3A4 may be expected to play a role in formation of quinone-type metabolite from troglitazone even at a low concentration in humans.	quinone	54-61	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	0-6	
10534310-2	1999	Of fourteen cDNA-expressed human P-450 enzymes examined, CYP1A1, CYP2C8, CYP2C19, and CYP3A4 were active in catalyzing formation of a quinone-type metabolite at a concentration of 10 microM troglitazone, whereas CYP3A4 had the highest catalytic activity at 100 microM substrate.	quinone	134-141	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	86-92	
10534310-2	1999	Of fourteen cDNA-expressed human P-450 enzymes examined, CYP1A1, CYP2C8, CYP2C19, and CYP3A4 were active in catalyzing formation of a quinone-type metabolite at a concentration of 10 microM troglitazone, whereas CYP3A4 had the highest catalytic activity at 100 microM substrate.	quinone	134-141	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	212-218	
9789061-3	1998	CYP3A metabolism generates epipodophyllotoxin catechol and quinone metabolites, which could damage DNA.	quinone	59-66	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	0-5