PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
20839931-9	2010	CsA but not the high-cholesterol diet induced significant elevation in MDA, protein carbonyl and CYP2E1 activities in the kidney.	Cyclosporine	0-3	cytochrome P450 2E1	Oryctolagus cuniculus	97-103
22422469-6	2012	CYP1A2, CYP3A4, but not CYP2E1, were significantly diminished by TQ treatment.	thymoquinone	65-67	cytochrome P450 2E1	Oryctolagus cuniculus	24-30
20839931-12	2010	CsA-enhanced rabbit kidney ROS and CYP2E1 activities.	Cyclosporine	0-3	cytochrome P450 2E1	Oryctolagus cuniculus	35-41
18638298-9	2008	Significant correlations were found between the rate of biotransformation of medetomidine and the activities of CYP2D and CYP2E, as well as between CYP450 enzyme activities and the anaesthetic response to medetomidine.	Medetomidine	77-89	cytochrome P450 2E1	Oryctolagus cuniculus	122-127
16601807-4	2005	Using purified CYP enzymes, reconstituted with NADPH: CYP reductase, rabbit CYP2E1 was the most efficient enzyme oxidizing o-anisidine, but the ability of CYP1A1, 1A2, 2B2, 2B4 and 3A6 to participate in o-anisidine oxidation was also proved.	NADP	47-52	cytochrome P450 2E1	Oryctolagus cuniculus	76-82
16601807-4	2005	Using purified CYP enzymes, reconstituted with NADPH: CYP reductase, rabbit CYP2E1 was the most efficient enzyme oxidizing o-anisidine, but the ability of CYP1A1, 1A2, 2B2, 2B4 and 3A6 to participate in o-anisidine oxidation was also proved.	2-anisidine	123-134	cytochrome P450 2E1	Oryctolagus cuniculus	76-82
16601807-4	2005	Using purified CYP enzymes, reconstituted with NADPH: CYP reductase, rabbit CYP2E1 was the most efficient enzyme oxidizing o-anisidine, but the ability of CYP1A1, 1A2, 2B2, 2B4 and 3A6 to participate in o-anisidine oxidation was also proved.	2-anisidine	203-214	cytochrome P450 2E1	Oryctolagus cuniculus	76-82
15815077-9	2004	Based on these data, we conclude that EtOH-inducible microsomal CYP isoforms (mainly CYP2E1) are responsible for binding and N-demethylation metabolism of both studied N-nitrosamines in rabbit liver microsomal system.	Ethanol	38-42	cytochrome P450 2E1	Oryctolagus cuniculus	85-91
15815077-9	2004	Based on these data, we conclude that EtOH-inducible microsomal CYP isoforms (mainly CYP2E1) are responsible for binding and N-demethylation metabolism of both studied N-nitrosamines in rabbit liver microsomal system.	Nitrogen	125-126	cytochrome P450 2E1	Oryctolagus cuniculus	85-91
15815077-9	2004	Based on these data, we conclude that EtOH-inducible microsomal CYP isoforms (mainly CYP2E1) are responsible for binding and N-demethylation metabolism of both studied N-nitrosamines in rabbit liver microsomal system.	n-nitrosamines	168-182	cytochrome P450 2E1	Oryctolagus cuniculus	85-91
15012901-11	2003	We suggest that although CYP2E1 is expressed in the tongue, it is rapidly degraded in this organ, and the nitrophenol hydroxylation and caffeine hydroxylation we observe is the result of activity of CYP1A1.	Nitrophenols	106-117	cytochrome P450 2E1	Oryctolagus cuniculus	25-31
14988423-0	2004	Novel reversible inactivation of cytochrome P450 2E1 T303A by tert-butyl acetylene: the role of threonine 303 in proton delivery to the active site of cytochrome P450 2E1.	3,3-Dimethyl-1-Butyne	62-82	cytochrome P450 2E1	Oryctolagus cuniculus	33-52
14988423-0	2004	Novel reversible inactivation of cytochrome P450 2E1 T303A by tert-butyl acetylene: the role of threonine 303 in proton delivery to the active site of cytochrome P450 2E1.	3,3-Dimethyl-1-Butyne	62-82	cytochrome P450 2E1	Oryctolagus cuniculus	151-170
14988423-0	2004	Novel reversible inactivation of cytochrome P450 2E1 T303A by tert-butyl acetylene: the role of threonine 303 in proton delivery to the active site of cytochrome P450 2E1.	Threonine	96-105	cytochrome P450 2E1	Oryctolagus cuniculus	33-52
14988423-0	2004	Novel reversible inactivation of cytochrome P450 2E1 T303A by tert-butyl acetylene: the role of threonine 303 in proton delivery to the active site of cytochrome P450 2E1.	Threonine	96-105	cytochrome P450 2E1	Oryctolagus cuniculus	151-170
14680963-8	2004	An improved purification procedure for the expressed CYP2E1 involving chromatography on diethylaminoethyl cellulose (DE52), Reactive Red-agarose (type 1000-CL), and hydroxyapatite is also reported.	DEAE-Cellulose	88-115	cytochrome P450 2E1	Oryctolagus cuniculus	53-59
14680963-8	2004	An improved purification procedure for the expressed CYP2E1 involving chromatography on diethylaminoethyl cellulose (DE52), Reactive Red-agarose (type 1000-CL), and hydroxyapatite is also reported.	reactive red-agarose	124-144	cytochrome P450 2E1	Oryctolagus cuniculus	53-59
14680963-8	2004	An improved purification procedure for the expressed CYP2E1 involving chromatography on diethylaminoethyl cellulose (DE52), Reactive Red-agarose (type 1000-CL), and hydroxyapatite is also reported.	1000-cl	151-158	cytochrome P450 2E1	Oryctolagus cuniculus	53-59
14680963-8	2004	An improved purification procedure for the expressed CYP2E1 involving chromatography on diethylaminoethyl cellulose (DE52), Reactive Red-agarose (type 1000-CL), and hydroxyapatite is also reported.	Durapatite	165-179	cytochrome P450 2E1	Oryctolagus cuniculus	53-59
14680963-9	2004	This procedure allowed recovery of 45% of the expressed protein and CYP2E1 with a specific content of 14 nmol/mg protein, which showed a single band on a polyacrylamide gel stained with Coomassie brilliant blue.	polyacrylamide	154-168	cytochrome P450 2E1	Oryctolagus cuniculus	68-74
14680963-9	2004	This procedure allowed recovery of 45% of the expressed protein and CYP2E1 with a specific content of 14 nmol/mg protein, which showed a single band on a polyacrylamide gel stained with Coomassie brilliant blue.	coomassie Brilliant Blue	186-210	cytochrome P450 2E1	Oryctolagus cuniculus	68-74
15012901-11	2003	We suggest that although CYP2E1 is expressed in the tongue, it is rapidly degraded in this organ, and the nitrophenol hydroxylation and caffeine hydroxylation we observe is the result of activity of CYP1A1.	Caffeine	136-144	cytochrome P450 2E1	Oryctolagus cuniculus	25-31
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	Chlorzoxazone	26-39	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	4-nitrophenol	41-54	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	Dimethylnitrosamine	56-78	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	Acetaminophen	80-93	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	Caffeine	95-103	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	Theophylline	105-117	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	Methoxyflurane	123-137	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12699383-4	2003	Autodock was used to dock chlorzoxazone, p-nitrophenol, N-nitrosodimethylamine, acetominophen, caffeine, theophylline, and methoxyflurane into the model CYP2E1 employing a model oxyferryl heme with charges based on density functional theoretical parametrization.	oxyferryl heme	178-192	cytochrome P450 2E1	Oryctolagus cuniculus	153-159
12464263-8	2003	The physical entity of the switch was identified by site-directed mutation as the phosphoryl acceptor Ser in the PKA recognition motif, which is Ser(138) in CYPs 2B (rat CYP2B1 and rabbit CYP2B4) and its homologous Ser(139) in CYP2E1.	Serine	102-105	cytochrome P450 2E1	Oryctolagus cuniculus	227-233
12464263-8	2003	The physical entity of the switch was identified by site-directed mutation as the phosphoryl acceptor Ser in the PKA recognition motif, which is Ser(138) in CYPs 2B (rat CYP2B1 and rabbit CYP2B4) and its homologous Ser(139) in CYP2E1.	Serine	145-148	cytochrome P450 2E1	Oryctolagus cuniculus	227-233
12464263-8	2003	The physical entity of the switch was identified by site-directed mutation as the phosphoryl acceptor Ser in the PKA recognition motif, which is Ser(138) in CYPs 2B (rat CYP2B1 and rabbit CYP2B4) and its homologous Ser(139) in CYP2E1.	Serine	145-148	cytochrome P450 2E1	Oryctolagus cuniculus	227-233
9635416-0	1998	Oxidation of 1,3-butadiene to (R)- and (S)-butadiene monoxide by purified recombinant cytochrome P450 2E1 from rabbit, rat and human.	1,3-butadiene	13-26	cytochrome P450 2E1	Oryctolagus cuniculus	86-105
11042099-4	2000	CYP1A2, CYP2E1, CYP2J2, CYP2J3, CYP2J5, and CYP2J9 metabolized linoleic acid at rates comparable to arachidonic acid and produced linoleic acid monoepoxides as major products.	Linoleic Acid	63-76	cytochrome P450 2E1	Oryctolagus cuniculus	8-14
11042099-4	2000	CYP1A2, CYP2E1, CYP2J2, CYP2J3, CYP2J5, and CYP2J9 metabolized linoleic acid at rates comparable to arachidonic acid and produced linoleic acid monoepoxides as major products.	linoleic acid monoepoxides	130-156	cytochrome P450 2E1	Oryctolagus cuniculus	8-14
10101151-0	1999	Tightly regulated and inducible expression of rabbit CYP2E1 using a tetracycline-controlled expression system.	Tetracycline	68-80	cytochrome P450 2E1	Oryctolagus cuniculus	53-59
10101151-4	1999	There was a time-dependent induction of CYP2E1 after removal of Tc.	Tetracycline	64-66	cytochrome P450 2E1	Oryctolagus cuniculus	40-46
10101151-5	1999	In the absence of Tc, the enzyme was induced more than 100-fold and expressed about 18 pmol of CYP2E1/mg microsomal protein.	Tetracycline	18-20	cytochrome P450 2E1	Oryctolagus cuniculus	95-101
10101151-9	1999	In contrast, menadione, a redox cycling toxicant, was less toxic to the cells after induction of CYP2E1 when compared with noninduced cells.	Vitamin K 3	13-22	cytochrome P450 2E1	Oryctolagus cuniculus	97-103
10101151-10	1999	Pulse-chase studies conducted 72 h after removal of Tc indicated a rapid turnover of CYP2E1 with a half-life of 3.9 h. Addition of the ligand, 4-methylpyrazole, and the suicide substrate, 1-aminobenzotrizole, decreased the degradation of CYP2E1.	Tetracycline	52-54	cytochrome P450 2E1	Oryctolagus cuniculus	85-91
10101151-10	1999	Pulse-chase studies conducted 72 h after removal of Tc indicated a rapid turnover of CYP2E1 with a half-life of 3.9 h. Addition of the ligand, 4-methylpyrazole, and the suicide substrate, 1-aminobenzotrizole, decreased the degradation of CYP2E1.	Fomepizole	143-159	cytochrome P450 2E1	Oryctolagus cuniculus	85-91
10101151-10	1999	Pulse-chase studies conducted 72 h after removal of Tc indicated a rapid turnover of CYP2E1 with a half-life of 3.9 h. Addition of the ligand, 4-methylpyrazole, and the suicide substrate, 1-aminobenzotrizole, decreased the degradation of CYP2E1.	1-aminobenzotrizole	188-207	cytochrome P450 2E1	Oryctolagus cuniculus	85-91
10101151-10	1999	Pulse-chase studies conducted 72 h after removal of Tc indicated a rapid turnover of CYP2E1 with a half-life of 3.9 h. Addition of the ligand, 4-methylpyrazole, and the suicide substrate, 1-aminobenzotrizole, decreased the degradation of CYP2E1.	1-aminobenzotrizole	188-207	cytochrome P450 2E1	Oryctolagus cuniculus	238-244
9809083-0	1998	A comparison of the inhibitory effects of four volatile anaesthetics on the metabolism of chlorzoxazone, a substrate for CYP2E1, in rabbits.	Chlorzoxazone	90-103	cytochrome P450 2E1	Oryctolagus cuniculus	121-127
9809083-1	1998	BACKGROUND: Halothane inhibits in vitro and in vivo activity of cytochrome P-450 (CYP) 2E1.	Halothane	12-21	cytochrome P450 2E1	Oryctolagus cuniculus	64-90
12482238-1	2002	The kinetics for the inactivation of cytochrome P450 2E1 and the mutant P450 2E1 T303A by tert-butyl acetylene (tBA) and tert-butyl 1-methyl-2-propynyl ether (tBMP) were investigated.	3,3-Dimethyl-1-Butyne	90-110	cytochrome P450 2E1	Oryctolagus cuniculus	37-56
12482238-1	2002	The kinetics for the inactivation of cytochrome P450 2E1 and the mutant P450 2E1 T303A by tert-butyl acetylene (tBA) and tert-butyl 1-methyl-2-propynyl ether (tBMP) were investigated.	tba	112-115	cytochrome P450 2E1	Oryctolagus cuniculus	37-56
12482238-1	2002	The kinetics for the inactivation of cytochrome P450 2E1 and the mutant P450 2E1 T303A by tert-butyl acetylene (tBA) and tert-butyl 1-methyl-2-propynyl ether (tBMP) were investigated.	tert-butyl 1-methyl-2-propynyl ether	121-157	cytochrome P450 2E1	Oryctolagus cuniculus	37-56
12482238-1	2002	The kinetics for the inactivation of cytochrome P450 2E1 and the mutant P450 2E1 T303A by tert-butyl acetylene (tBA) and tert-butyl 1-methyl-2-propynyl ether (tBMP) were investigated.	tert-butyl 1-methyl-2-propynyl ether	159-163	cytochrome P450 2E1	Oryctolagus cuniculus	37-56
9714300-6	1998	Diallyl sulfide (DAS), a known inhibitor of CYP2E1 and of CYP2A10/2A11 (the rabbit orthologue of mouse CYP2A5), completely eliminated olfactory toxicity of AP in both the Cyp1a2(-/-) and wild-type mouse olfactory mucosa.	allyl sulfide	0-15	cytochrome P450 2E1	Oryctolagus cuniculus	44-50
9714300-6	1998	Diallyl sulfide (DAS), a known inhibitor of CYP2E1 and of CYP2A10/2A11 (the rabbit orthologue of mouse CYP2A5), completely eliminated olfactory toxicity of AP in both the Cyp1a2(-/-) and wild-type mouse olfactory mucosa.	allyl sulfide	17-20	cytochrome P450 2E1	Oryctolagus cuniculus	44-50
9635416-0	1998	Oxidation of 1,3-butadiene to (R)- and (S)-butadiene monoxide by purified recombinant cytochrome P450 2E1 from rabbit, rat and human.	(r)- and (s)-butadiene monoxide	30-61	cytochrome P450 2E1	Oryctolagus cuniculus	86-105
8509425-0	1993	Formation of 19(S)-, 19(R)-, and 18(R)-hydroxyeicosatetraenoic acids by alcohol-inducible cytochrome P450 2E1.	Sulfur	15-19	cytochrome P450 2E1	Oryctolagus cuniculus	90-109
9212147-1	1997	We demonstrated the inhibitory effect of halothane (HAL) inhalation on the metabolism of chlorzoxazone (CZZ), a substrate for CYP2E1, in a bolus and a continuous injection study in rabbits receiving artificial ventilation.	Chlorzoxazone	104-107	cytochrome P450 2E1	Oryctolagus cuniculus	126-132
9212147-7	1997	These results suggest that general anesthesia obtained with HAL inhalation will affect the metabolism of drugs administered concomitantly when the drug is a substrate for CYP2E1.	Halothane	60-63	cytochrome P450 2E1	Oryctolagus cuniculus	171-177
7733676-1	1995	This laboratory previously expressed cDNAs encoding rabbit liver cytochrome P450 2E1 (the ethanol-inducible isoform) and the corresponding protein lacking amino acids 3-29, a proposed membrane anchor, in Escherichia coli.	Ethanol	90-97	cytochrome P450 2E1	Oryctolagus cuniculus	65-84
8180223-0	1994	Mutagenesis at a highly conserved phenylalanine in cytochrome P450 2E1 affects heme incorporation and catalytic activity.	Phenylalanine	34-47	cytochrome P450 2E1	Oryctolagus cuniculus	51-70
8180223-0	1994	Mutagenesis at a highly conserved phenylalanine in cytochrome P450 2E1 affects heme incorporation and catalytic activity.	Heme	79-83	cytochrome P450 2E1	Oryctolagus cuniculus	51-70
8180223-1	1994	The phenylalanine corresponding to Phe-429 of rabbit cytochrome P450 2E1 is 1 of approximately 10 highly conserved residues in this superfamily of over 200 sequenced enzymes.	Phenylalanine	4-17	cytochrome P450 2E1	Oryctolagus cuniculus	53-72
8180223-1	1994	The phenylalanine corresponding to Phe-429 of rabbit cytochrome P450 2E1 is 1 of approximately 10 highly conserved residues in this superfamily of over 200 sequenced enzymes.	Phenylalanine	35-38	cytochrome P450 2E1	Oryctolagus cuniculus	53-72
8509425-1	1993	When reconstituted with cytochrome b5 and NADPH cytochrome P450 oxidoreductase, cytochrome P450 2E1 metabolized lauric, stearic, oleic, linoleic, linolenic, and arachidonic acid to multiple metabolites.	oleic	129-134	cytochrome P450 2E1	Oryctolagus cuniculus	42-99
8509425-1	1993	When reconstituted with cytochrome b5 and NADPH cytochrome P450 oxidoreductase, cytochrome P450 2E1 metabolized lauric, stearic, oleic, linoleic, linolenic, and arachidonic acid to multiple metabolites.	Linoleic Acid	136-144	cytochrome P450 2E1	Oryctolagus cuniculus	42-99
8509425-1	1993	When reconstituted with cytochrome b5 and NADPH cytochrome P450 oxidoreductase, cytochrome P450 2E1 metabolized lauric, stearic, oleic, linoleic, linolenic, and arachidonic acid to multiple metabolites.	linolenic	146-155	cytochrome P450 2E1	Oryctolagus cuniculus	42-99
8509425-1	1993	When reconstituted with cytochrome b5 and NADPH cytochrome P450 oxidoreductase, cytochrome P450 2E1 metabolized lauric, stearic, oleic, linoleic, linolenic, and arachidonic acid to multiple metabolites.	Arachidonic Acid	161-177	cytochrome P450 2E1	Oryctolagus cuniculus	42-99
8509425-15	1993	Thus, under conditions where cytochrome P450 2E1 is induced, the enzyme could contribute significantly to the formation of the omega-1 and omega-2 hydroxylated metabolites of arachidonic acid.	omega-1	127-134	cytochrome P450 2E1	Oryctolagus cuniculus	29-48
9212147-0	1997	Halothane inhalation inhibits the metabolism of chlorzoxazone, a substrate for CYP2E1, in rabbits.	Halothane	0-9	cytochrome P450 2E1	Oryctolagus cuniculus	79-85
9212147-0	1997	Halothane inhalation inhibits the metabolism of chlorzoxazone, a substrate for CYP2E1, in rabbits.	Chlorzoxazone	48-61	cytochrome P450 2E1	Oryctolagus cuniculus	79-85
9212147-1	1997	We demonstrated the inhibitory effect of halothane (HAL) inhalation on the metabolism of chlorzoxazone (CZZ), a substrate for CYP2E1, in a bolus and a continuous injection study in rabbits receiving artificial ventilation.	Halothane	41-50	cytochrome P450 2E1	Oryctolagus cuniculus	126-132
9212147-1	1997	We demonstrated the inhibitory effect of halothane (HAL) inhalation on the metabolism of chlorzoxazone (CZZ), a substrate for CYP2E1, in a bolus and a continuous injection study in rabbits receiving artificial ventilation.	Halothane	52-55	cytochrome P450 2E1	Oryctolagus cuniculus	126-132
9212147-1	1997	We demonstrated the inhibitory effect of halothane (HAL) inhalation on the metabolism of chlorzoxazone (CZZ), a substrate for CYP2E1, in a bolus and a continuous injection study in rabbits receiving artificial ventilation.	Chlorzoxazone	89-102	cytochrome P450 2E1	Oryctolagus cuniculus	126-132
7654254-3	1995	One protein was detected by anti-CYP2E1 which was modestly inducible by imidazole.	imidazole	72-81	cytochrome P450 2E1	Oryctolagus cuniculus	33-39
8155832-4	1994	Addition of cytosol to purified rabbit liver cytochrome P450 2E1 in a reconstituted system consisting of NADPH-cytochrome P450 reductase, 2E1, and phospholipid produced an 18-fold increase in DNA alkylation over that observed with the reconstituted system alone.	Phospholipids	147-159	cytochrome P450 2E1	Oryctolagus cuniculus	45-64
8509425-15	1993	Thus, under conditions where cytochrome P450 2E1 is induced, the enzyme could contribute significantly to the formation of the omega-1 and omega-2 hydroxylated metabolites of arachidonic acid.	omega-2	139-146	cytochrome P450 2E1	Oryctolagus cuniculus	29-48
8509425-15	1993	Thus, under conditions where cytochrome P450 2E1 is induced, the enzyme could contribute significantly to the formation of the omega-1 and omega-2 hydroxylated metabolites of arachidonic acid.	Arachidonic Acid	175-191	cytochrome P450 2E1	Oryctolagus cuniculus	29-48
8509425-0	1993	Formation of 19(S)-, 19(R)-, and 18(R)-hydroxyeicosatetraenoic acids by alcohol-inducible cytochrome P450 2E1.	(R)-(2,3-Dimethoxyphenyl)-4-piperidinemethanol	23-27	cytochrome P450 2E1	Oryctolagus cuniculus	90-109
8509425-0	1993	Formation of 19(S)-, 19(R)-, and 18(R)-hydroxyeicosatetraenoic acids by alcohol-inducible cytochrome P450 2E1.	(r)-hydroxyeicosatetraenoic acids	35-68	cytochrome P450 2E1	Oryctolagus cuniculus	90-109
8509425-0	1993	Formation of 19(S)-, 19(R)-, and 18(R)-hydroxyeicosatetraenoic acids by alcohol-inducible cytochrome P450 2E1.	Alcohols	72-79	cytochrome P450 2E1	Oryctolagus cuniculus	90-109
8509425-1	1993	When reconstituted with cytochrome b5 and NADPH cytochrome P450 oxidoreductase, cytochrome P450 2E1 metabolized lauric, stearic, oleic, linoleic, linolenic, and arachidonic acid to multiple metabolites.	stearic	120-127	cytochrome P450 2E1	Oryctolagus cuniculus	42-99
3518633-0	1986	Evidence that isoniazid and ethanol induce the same microsomal cytochrome P-450 in rat liver, an isozyme homologous to rabbit liver cytochrome P-450 isozyme 3a.	Isoniazid	14-23	cytochrome P450 2E1	Oryctolagus cuniculus	132-159
1362928-1	1992	Cytochrome P-450 2E1 is induced in adult rabbits by treatment with alcohol, imidazole, and a variety of other agents, as shown earlier in this laboratory, but it is not known whether the highly homologous P-450 2E2 is similarly induced.	Alcohols	67-74	cytochrome P450 2E1	Oryctolagus cuniculus	0-20
1362928-1	1992	Cytochrome P-450 2E1 is induced in adult rabbits by treatment with alcohol, imidazole, and a variety of other agents, as shown earlier in this laboratory, but it is not known whether the highly homologous P-450 2E2 is similarly induced.	imidazole	76-85	cytochrome P450 2E1	Oryctolagus cuniculus	0-20
1906976-1	1991	The alcohol-inducible CYP2E subfamily in rabbits contains two genes; CYP2E1 encodes the cytochrome earlier termed P-450 3a, and CYP2E2 encodes a cytochrome that is 97% identical in amino acid sequence to cytochrome P-450 (P-450) 2E1.	Alcohols	4-11	cytochrome P450 2E1	Oryctolagus cuniculus	69-75
1981730-0	1990	Induction of cytochrome P-450 isozyme 3a (P-450IIE1) in rabbit olfactory mucosa by ethanol and acetone.	Ethanol	83-90	cytochrome P450 2E1	Oryctolagus cuniculus	13-40
1981730-0	1990	Induction of cytochrome P-450 isozyme 3a (P-450IIE1) in rabbit olfactory mucosa by ethanol and acetone.	Acetone	95-102	cytochrome P450 2E1	Oryctolagus cuniculus	13-40
1981730-1	1990	Cytochrome P-450 isozyme 3a, the alcohol-inducible form of cytochrome P-450 (P-450IIE1), was previously identified in rabbit nasal microsomes with the use of immunochemical techniques; the occurrence of this cytochrome in the nasal mucosa was subsequently confirmed through RNA hybridization experiments.	Alcohols	33-40	cytochrome P450 2E1	Oryctolagus cuniculus	0-27
3404442-12	1988	In conclusion, the oxidation of halothane to trifluoroacetic acid by cytochrome P-450 isozymes 3a and 2 is enhanced markedly by cytochrome b5.	Halothane	32-41	cytochrome P450 2E1	Oryctolagus cuniculus	69-103
3404442-12	1988	In conclusion, the oxidation of halothane to trifluoroacetic acid by cytochrome P-450 isozymes 3a and 2 is enhanced markedly by cytochrome b5.	Trifluoroacetic Acid	45-65	cytochrome P450 2E1	Oryctolagus cuniculus	69-103
3027695-0	1987	cDNA and derived amino acid sequence of ethanol-inducible rabbit liver cytochrome P-450 isozyme 3a (P-450ALC).	Ethanol	40-47	cytochrome P450 2E1	Oryctolagus cuniculus	71-98
3762523-1	1986	Polyclonal and monoclonal antibodies to rabbit liver microsomal alcohol-inducible cytochrome P-450 isozyme 3a (P-450ALC) were used to examine the tissue distribution of the cytochrome.	Alcohols	64-71	cytochrome P450 2E1	Oryctolagus cuniculus	82-109
8471070-13	1993	Since this increase in 2E1 synthesis stems, at least in part, from the acetone-mediated enhancement of hepatocyte 2E1 mRNA content and is inhibitable by alpha-amanitin, transcriptional activation of the rabbit CYP2E1 gene is apparently involved in the induction of 2E1 protein by acetone.	Acetone	71-78	cytochrome P450 2E1	Oryctolagus cuniculus	210-216
8471070-13	1993	Since this increase in 2E1 synthesis stems, at least in part, from the acetone-mediated enhancement of hepatocyte 2E1 mRNA content and is inhibitable by alpha-amanitin, transcriptional activation of the rabbit CYP2E1 gene is apparently involved in the induction of 2E1 protein by acetone.	Alpha-Amanitin	153-167	cytochrome P450 2E1	Oryctolagus cuniculus	210-216
8471070-13	1993	Since this increase in 2E1 synthesis stems, at least in part, from the acetone-mediated enhancement of hepatocyte 2E1 mRNA content and is inhibitable by alpha-amanitin, transcriptional activation of the rabbit CYP2E1 gene is apparently involved in the induction of 2E1 protein by acetone.	Acetone	280-287	cytochrome P450 2E1	Oryctolagus cuniculus	210-216
1358586-0	1992	Inhibition of rabbit microsomal cytochrome P-450 2E1-dependent p-nitrophenol hydroxylation by substituted benzene derivatives.	4-nitrophenol	63-76	cytochrome P450 2E1	Oryctolagus cuniculus	32-52
1358586-0	1992	Inhibition of rabbit microsomal cytochrome P-450 2E1-dependent p-nitrophenol hydroxylation by substituted benzene derivatives.	Benzene	106-113	cytochrome P450 2E1	Oryctolagus cuniculus	32-52
3395117-13	1988	Further, cytochrome P-450ALC appears to be responsible for about one-half of the increase in the rate of ethanol elimination in vivo after chronic treatment with ethanol.	Ethanol	105-112	cytochrome P450 2E1	Oryctolagus cuniculus	9-28
3395117-13	1988	Further, cytochrome P-450ALC appears to be responsible for about one-half of the increase in the rate of ethanol elimination in vivo after chronic treatment with ethanol.	Ethanol	162-169	cytochrome P450 2E1	Oryctolagus cuniculus	9-28
3518633-0	1986	Evidence that isoniazid and ethanol induce the same microsomal cytochrome P-450 in rat liver, an isozyme homologous to rabbit liver cytochrome P-450 isozyme 3a.	Ethanol	28-35	cytochrome P450 2E1	Oryctolagus cuniculus	132-159
3518633-12	1986	All of the evidence presented in this study indicates that the identical cytochrome P-450, P-450j, is induced in rat liver by either isoniazid or ethanol, and that this isozyme is closely related to rabbit cytochrome P-450 isozyme 3a.	Isoniazid	133-142	cytochrome P450 2E1	Oryctolagus cuniculus	206-233
3518633-12	1986	All of the evidence presented in this study indicates that the identical cytochrome P-450, P-450j, is induced in rat liver by either isoniazid or ethanol, and that this isozyme is closely related to rabbit cytochrome P-450 isozyme 3a.	Ethanol	146-153	cytochrome P450 2E1	Oryctolagus cuniculus	206-233
3702859-0	1986	Hydroxylation of p-nitrophenol by rabbit ethanol-inducible cytochrome P-450 isozyme 3a.	4-nitrophenol	17-30	cytochrome P450 2E1	Oryctolagus cuniculus	59-86
7142188-0	1982	Catalytic activity of cytochrome P-450 isozyme 3a isolated from liver microsomes of ethanol-treated rabbits.	Ethanol	84-91	cytochrome P450 2E1	Oryctolagus cuniculus	22-49
6497392-1	1984	Antibodies to cytochrome P-450 isozyme 3a, the ethanol-inducible isozyme in rabbit liver, were used to determine the role of this enzyme in the microsomal oxidation of alcohols and the p-hydroxylation of aniline.	Ethanol	47-54	cytochrome P450 2E1	Oryctolagus cuniculus	14-41
6497392-1	1984	Antibodies to cytochrome P-450 isozyme 3a, the ethanol-inducible isozyme in rabbit liver, were used to determine the role of this enzyme in the microsomal oxidation of alcohols and the p-hydroxylation of aniline.	Alcohols	168-176	cytochrome P450 2E1	Oryctolagus cuniculus	14-41
6497392-1	1984	Antibodies to cytochrome P-450 isozyme 3a, the ethanol-inducible isozyme in rabbit liver, were used to determine the role of this enzyme in the microsomal oxidation of alcohols and the p-hydroxylation of aniline.	aniline	204-211	cytochrome P450 2E1	Oryctolagus cuniculus	14-41
6427601-0	1984	Purification of liver microsomal cytochrome P-450 isozymes 3a and 6 from imidazole-treated rabbits.	imidazole	73-82	cytochrome P450 2E1	Oryctolagus cuniculus	33-67
7142188-2	1982	Cytochrome P-450 isozyme 3a, isolated from hepatic microsomes of rabbits treated chronically with ethanol, was found to have a unique substrate specificity when compared with isozymes 2, 3b, 3c, and 4.	Ethanol	98-105	cytochrome P450 2E1	Oryctolagus cuniculus	0-27