PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2192911-4	1990	Xenobiotics may lead to liver injury after biotransformation to highly reactive electrophilic metabolites (mainly cytochrome P-450 mediated), which easily conjugate with GSH, thus producing GSH depletion.	Glutathione	170-173	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	125-130	
2192911-4	1990	Xenobiotics may lead to liver injury after biotransformation to highly reactive electrophilic metabolites (mainly cytochrome P-450 mediated), which easily conjugate with GSH, thus producing GSH depletion.	Glutathione	190-193	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	125-130	
26335194-5	2015	Exogenous nucleophile glutathione (GSH) and catalase/superoxide dismutase showed limited protection of CYP2B6 from the inactivation.	Glutathione	22-33	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	103-109	
4292159-0	1967	Reconversion of detergent- and sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathione.	Glutathione	89-100	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	68-73	
26335194-5	2015	Exogenous nucleophile glutathione (GSH) and catalase/superoxide dismutase showed limited protection of CYP2B6 from the inactivation.	Glutathione	35-38	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	103-109	
24598282-11	2014	The formation of a glutathione conjugate of allitinib was independent of NADPH and P450 isoforms, but was catalyzed by glutathione-S-transferase.	Glutathione	19-30	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	83-87	
25634537-5	2015	In the model, we tested the hypothesis that metabolism responsibilities were shared by the p450 CYP2E1 and glutathione (GSH) conjugation.	Glutathione	120-123	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	91-95	
21930824-4	2011	Unlike CYP2B1 and CYP2B4, in addition to the formation of an apoprotein adduct and a glutathione conjugate, a small heme adduct was observed when CYP2B6 was incubated with BPA.	Glutathione	85-96	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	146-152	
23088752-2	2013	Multiple glutathione and beta-mercaptoethanol conjugates (a.k.a., adducts), derived from the trapping of quinone methide and quinone intermediates of capsaicin, its analogue nonivamide, and O-demethylated and aromatic hydroxylated metabolites thereof, were produced by human liver microsomes and individual recombinant human P450 enzymes.	Glutathione	9-20	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	325-329	
22859722-4	2012	Every P450 tested except CYP2E1 was capable of raloxifene bioactivation, based on glutathione adduct formation.	Glutathione	82-93	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	6-10	
12460909-2	2002	Attempts to additionally increase tumor cell kill by enhancing the intrinsic chemosensitivity of P450-expressing tumor cells by chemical means (depletion of cellular glutathione) or by coexpression of proapoptotic factors was shown to result in the desired increase in chemosensitivity, but with a decrease in net production of bystander cytotoxic drug metabolites because of accelerated death of the prodrug-activating tumor cells.	Glutathione	166-177	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	97-101	
8286335-8	1994	Moreover, a specific covalent binding of 0.9 mol of TA metabolite per mole of P450 2C10 was found to occur before the complete loss of enzyme activity (in incubations performed in the presence of glutathione).	Glutathione	196-207	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	78-82	
11240372-4	2001	The mercury chloride-treated P-420 form of nNOS could be reconverted to the P-450 form on incubation with reduced glutathione (GSH) or L-cysteine, and the nNOS activity was recovered.	Glutathione	114-125	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	76-81	
11240372-4	2001	The mercury chloride-treated P-420 form of nNOS could be reconverted to the P-450 form on incubation with reduced glutathione (GSH) or L-cysteine, and the nNOS activity was recovered.	Glutathione	127-130	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	76-81	
12228192-2	2002	The decrease in the activity followed time- and concentration-dependent kinetics, required oxidative metabolism, and was resistant to reduced glutathione, suggesting that diclofenac causes a mechanism-based inactivation of cytochrome p450 (p450) 3A4 (CYP3A4).	Glutathione	142-153	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	234-238