PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24733789-0	2014	Metabolic activation of the antibacterial agent triclocarban by cytochrome P450 1A1 yielding glutathione adducts.	Glutathione	93-104	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	64-83	
24733789-6	2014	Incubations containing CYP1A1, but not 1B1, led to formation of a single TCC-GSH adduct with a conversion rate of 1% of parent compound in 2 hours.	Glutathione	77-80	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	23-29	
21913247-8	2011	Incubation of sterigmatocystin with recombinant cytochrome P450 1A1 led to the formation of three metabolites identified as monohydroxysterigmatocystin, dihydroxysterigmatocystin and one glutathione adduct, the latter after the formation of a transient intermediate.	Glutathione	187-198	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	48-67	
15579657-4	2005	It has been demonstrated that the CYP1A1 metabolizes not only environmental chemicals but also estrogens, and glutathione-S-transferases (GSTs) are detoxification enzymes that protect cells from toxicants by conjugation with glutathione.	Glutathione	110-121	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	34-40	
20382753-9	2010	CYP1A1, CYP1A2, and CYP2D6 were not inactivated despite catalyzing the formation of ERL-GSH adducts.	Glutathione	88-91	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	0-6	
17570247-11	2007	These experiments demonstrated that CYP1A1, CYP1B1, and CYP3A4 are able to oxidize catechol estrogens to their respective quinones, which can further react with GSH, protein, and DNA, the last resulting in depurinating adducts that can lead to mutagenesis.	Glutathione	161-164	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	36-42	
16137656-4	2005	Oxidation of 2PT by recombinant, human cytochrome P4501A1, in the presence of NADPH and GSH, also led to these three kinds of metabolites.	Glutathione	88-91	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	39-57	
16274885-6	2005	When cellular GSH was depleted with buthionine-(S,R)-sulfoximine (BSO), Cyp1a1 mRNA expression was further potentiated whereas Cyp1a1 activity was further inhibited.	Glutathione	14-17	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	72-78	
16274885-6	2005	When cellular GSH was depleted with buthionine-(S,R)-sulfoximine (BSO), Cyp1a1 mRNA expression was further potentiated whereas Cyp1a1 activity was further inhibited.	Glutathione	14-17	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	127-133	
12519694-9	2003	Studies on the susceptibility of CYP1A1 to SeCys conjugates implicated a thiol-reactive intermediate, as evidenced by reduced inhibition levels in the presence of glutathione and N-acetyl cysteine.	Glutathione	163-174	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	33-39	
12569393-3	2003	2-(4-Amino-3-methylphenyl)benzothiazole-derived covalent binding to cytochrome P450 1A1 is reduced by glutathione, suggesting 1A1-dependent production of a reactive electrophilic species.	Glutathione	102-113	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	68-87	
35395335-8	2022	Finally, the intracellular levels of ROS, superoxide dismutase and reduced glutathione in C3A and HepG2-hCYP1A1 exposed to BPAF were all moderately increased, while unchanged in HepG2 cells.	Glutathione	75-86	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	104-111	
11016648-13	2000	The covalent binding of [14C]DF 203 to recombinant CYP1A1 enzyme was NADPH-dependent and reduced by 6-OH 203 and glutathione.	Glutathione	113-124	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	51-57	
10852673-11	2000	Glutathione and taurine in certain concentrations showed protective effects against loss of CYPIA1 activity (p < 0.05 and <0.01 respectively).	Glutathione	0-11	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	92-98	
9815579-5	1997	Confirming and extending the observations of others, levels of glutathione, a molecular determinant of cellular sensitivity to various DNA cross-linking agents including cyclophosphamide, and of DT-diaphorase, glutathione S-transferases, and cytochrome P450 1A1, each of which is known to catalyze the detoxification/toxification of one or more anticancer agents (although not of cyclophosphamide), also varied widely in primary and metastatic breast malignancies.	Glutathione	63-74	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	242-261	
29975444-0	2018	GSH/GSSG redox couple plays central role in aryl hydrocarbon receptor-dependent modulation of cytochrome P450 1A1.	Glutathione	0-3	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	94-113	
29975444-4	2018	A clear link between CYP1A1 transcription and enzyme activity and changes in the glutathione/oxidised glutathione (GSH/GSSG) redox couple was shown.	Glutathione	81-92	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	21-27	
29975444-4	2018	A clear link between CYP1A1 transcription and enzyme activity and changes in the glutathione/oxidised glutathione (GSH/GSSG) redox couple was shown.	Glutathione	102-113	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	21-27	
29975444-4	2018	A clear link between CYP1A1 transcription and enzyme activity and changes in the glutathione/oxidised glutathione (GSH/GSSG) redox couple was shown.	Glutathione	115-118	cytochrome P450 family 1 subfamily A member 1	Homo sapiens	21-27