PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3336347-1	1988	The steroid androstenedione has been shown to be a valuable tool for the study of the selective inactivation of cytochrome P-450 isozymes in intact rat liver microsomes.	Steroids	4-11	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	112-128	
3200857-1	1988	Results of studies of hypophysectomized rats suggest that growth hormone serves as a final common mediator through which gonadal steroids and other modifiers of pituitary function alter the expression of gender-specific liver genes such as the sexually dimorphic pair of cytochrome P-450 isozymes, male-specific P-450h and female-specific P-450i.	Steroids	129-137	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	271-287	
3378384-3	1988	An antiserum raised against a steroid-inducible rat cytochrome P-450 (P-450 PCN) strongly inhibited the formation of these metabolites.	Steroids	30-37	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	52-68	
3444117-8	1987	All these results indicate that neonatal androgen imprinting on sex-dependent cytochrome P-450 and drug and steroid metabolizing activities in rat liver microsomes is not a permanent programming process and is modified by the presence and absence of sex-steroid hormones.	Steroids	254-261	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	78-94	
3820857-0	1986	Effects of hypophysectomy and growth hormone treatment on sex-specific forms of cytochrome P-450 in relation to drug and steroid metabolisms in rat liver microsomes.	Steroids	121-128	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	80-96	
3119986-0	1987	Monoclonal antibodies inhibitory to rat hepatic cytochromes P-450: P-450 form specificities and use as probes for cytochrome P-450-dependent steroid hydroxylations.	Steroids	141-148	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	114-130	
2820696-0	1987	Steroid synthesis-dependent, oxygen-mediated damage of mitochondrial and microsomal cytochrome P-450 enzymes in rat Leydig cell cultures.	Steroids	0-7	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	84-100	
2880590-10	1987	These data suggest that factors yet to be identified strongly influence the steroid-induced pattern of cytochrome P-450 gene expression.	Steroids	76-83	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	103-119	
3707617-1	1986	The contraceptive steroid norethindrone caused a rapid time and dose-dependent loss of cytochrome P-450 from rat hepatocytes in suspension cultures.	Steroids	18-25	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	87-103	
3017365-2	1986	In the mitochondria, 1 day after Cu2+ treatment, when the concentration of the metal ion was increased by 2- to 3-fold over the control value, a significant increase in cytochrome P-450-dependent steroid 11 beta-hydroxylase activity was observed.	Steroids	196-203	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	169-185	
3840669-7	1985	Both preparations consisted of the same isozyme which was previously characterized as a developmentally regulated, male-specific cytochrome P-450 active in the 16 alpha-hydroxylation of steroids.	Steroids	186-194	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	129-145	
4084542-0	1985	Multiple sites of steroid hydroxylation by the liver microsomal cytochrome P-450 system: primary and secondary metabolism of androstenedione.	Steroids	18-25	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	64-80	
24277281-1	1984	Compounds containing a terminal carbon-carbon triple bond, ranging in structure from the 17alpha-ethynyl substituted contraceptive steroids to acetylene gas, when administered to rats cause a selective and rapid time dependent loss of up to 50% of hepatic cytochrome P-450.	Steroids	131-139	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	256-272	
3875783-1	1985	We have recently demonstrated that P-450p, a form of rat liver cytochrome P-450 inducible by steroids such as dexamethasone and pregnenolone-16 alpha-carbonitrile, by the macrolide antibiotic triacetyloleandomycin, and by phenobarbital, is immunochemically related to and shares 73% NH2-terminal amino acid sequence homology with rabbit cytochrome LM3c.	Steroids	93-101	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	63-79	
6723583-7	1984	It is concluded that the prostatic 5 alpha-androstane-3 beta,17 beta-diol hydroxylase activities represent a constitutive cytochrome P-450 form in the rat ventral prostate with a high steroid substrate specificity.	Steroids	184-191	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	122-138	
6196179-6	1983	When the cytochrome P-450 obtained from the PMSG-treated rats was subjected to spectrometric analysis of binding with progesterone and 17 alpha-hydroxy-progesterone, type I spectra were obtained for both steroids, indicating that the steroids bound to the cytochrome as substrate.	Steroids	204-212	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	9-25	
6420703-1	1984	The cytochrome P450-containing mixed function oxidases metabolize a variety of endogenous and exogenous compounds including drugs, carcinogens, fatty acids and steroids.	Steroids	160-168	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	4-19	
6697240-3	1984	In the liver, energy from Type I H is used for cytochrome P-450-dependent oxidation of steroids, as well as xenobiotics.	Steroids	87-95	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	47-63	
6196179-6	1983	When the cytochrome P-450 obtained from the PMSG-treated rats was subjected to spectrometric analysis of binding with progesterone and 17 alpha-hydroxy-progesterone, type I spectra were obtained for both steroids, indicating that the steroids bound to the cytochrome as substrate.	Steroids	234-242	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	9-25	
6863312-0	1983	Regio- and stereoselective metabolism of two C19 steroids by five highly purified and reconstituted rat hepatic cytochrome P-450 isozymes.	Steroids	49-57	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	112-128	
6620170-2	1983	Studies were conducted to evaluate the effects of beta-NF administration on several extrahepatic cytochrome P-450-dependent enzymes responsible for steroid biosynthesis in the ovary.	Steroids	148-155	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	97-113	
6863312-8	1983	These results indicate that certain cytochrome P-450 isozymes show marked positional specificity in the metabolism of both testosterone and androstenedione, and that the rate as well as stereoselectivity of the oxidative reactions can be markedly dependent on subtle differences in the structure of the steroid substrate.	Steroids	303-310	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	36-52	
6291900-4	1982	A direct relationship between rates of steroid synthesis in the presence of 25-OH-cholesterol and mitochondrial cytochrome P-450 levels was found.	Steroids	39-46	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	112-128	
6304056-0	1983	25-hydroxylation of C27-steroids and vitamin D3 by a constitutive cytochrome P-450 from rat liver microsomes.	Steroids	24-32	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	66-82	
6304056-4	1983	The cytochrome P-450 showed no detectable 25-hydroxylase activity towards vitamin D2 and was inactive in cholesterol 7 alpha-hydroxylation as well as in 12 alpha- and 26-hydroxylations of C27-steroids.	Steroids	192-200	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	4-20	
6304056-8	1983	The possibility that 25-hydroxylation of C27-steroids and vitamin D3 is catalyzed by the same species of cytochrome P-450 is discussed.	Steroids	45-53	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	105-121	
6834827-0	1983	Comparison of trans-stilbene oxide, phenobarbital and 3-methylcholanthrene as inducers of steroid metabolism by the rat liver microsomal cytochrome P-450 system.	Steroids	90-97	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	137-153	
7318823-0	1981	Ontogenic development of steroid 16 alpha-hydroxylase as a tool for the study of the multiplicity of cytochrome P-450.	Steroids	25-32	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	101-117	
6800653-8	1982	Among androgens and estrogens, estradiol proved to be the most inhibitory steroid, suggesting a role of the hydrocarbon-metabolizing cytochrome P-450 in estrogen biosynthesis.	Steroids	74-81	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	133-149	
7318823-8	1981	In the adult rat liver, steroid 16 alpha-hydroxylase is supported by two forms of cytochrome P-450 (form I and form II), which differ in their relative affinities for the various steroid substrates, and by their relative proportions in male and female rat livers.	Steroids	24-31	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	82-98	
420819-0	1979	Iodosylbenzene derivatives as oxygen donors in cytochrome P-450 catalyzed steroid hydroxylations.	Steroids	74-81	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	47-63	
6450647-0	1981	Competition between benzo[a]pyrene and various steroids for cytochrome P-450-dependent rat liver monooxygenases.	Steroids	47-55	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	60-76	
6261833-3	1981	At the same time, mitochondrial cytochrome P-450 exhibited a 10-fold increase in concentration, reflecting the ability of the gland to synthesize steroids.	Steroids	146-154	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	32-48	
7282239-0	1981	Changes in the matabolism of steroid hormones by the rat liver cytochrome P-450 system after induction with trans-stilbene oxide.	Steroids	29-36	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	63-79	
6773745-0	1980	Reconstitution of steroid 17,20-lyase activity after separation and purification of cytochrome P-450 and its reductase from rat testis microsomes.	Steroids	18-25	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	84-100	
420819-5	1979	The capacity of the oxidation agents to serve as oxygen donors in cytochrome P-450 dependent steroid hydroxylation is probably dependent upon several factors such as the tendency of iodosyl compounds to associate, which decreases coordination with the heme iron, the presence of bulky substituents in the 2 position (decreases association), and the presence of electron-withdrawing substituents (tends to decrease coordination with the heme iron).	Steroids	93-100	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	66-82	
420819-1	1979	The mechanism of cytochrome P-450 catalyzed steroid hydroxylations in rat liver microsomes has been investigated by employing derivatives of iodosylbenzene as oxygen donors.	Steroids	44-51	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	17-33	
173555-0	1976	The involvement of cytochrome P-450 in hepatic microsomal steroid hydroxylation reactions supported by sodium periodate, sodium chlorite, and organic hydroperoxides.	Steroids	58-65	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	19-35	
953300-3	1976	A reduction of the hydroxylation rate of steroid hormones by rat hepatic microsomes under the effect of total gamma-irradiation apparently depended on the qualitative changes of cytochrome P-450.	Steroids	41-48	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	178-194	
570494-1	1978	The distribution of cytochrome P-450 (C-P450), an essential component of the oxidative enzyme system involved in the hydroxylation of steroids, was measured by quantitative cytochemistry in cryostat sections of preovulatory follicles obtained from rats in proestrous.	Steroids	134-142	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	20-44	
1262348-1	1976	Cytochrome P-450 appears to be a component of the steroid-coverting enzymes, 17alpha-hydroxylase and 17,20-lyase, which catalyze sequential steps in sex hormone synthesis.	Steroids	50-57	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	0-16	
1262348-2	1976	Further evidence indicates that the steroid substrates of these enzymes bind to cytochrome P-450 during catalysis.	Steroids	36-43	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	80-96	
819263-13	1976	It is concluded that rat liver microsomes contain multiple forms of cytochrome P-450 active on steroid hormones.	Steroids	95-111	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	68-84	
173555-13	1976	It is proposed that NaIO4, NaClO2, and organic hydroperoxides promote steroid hydroxylation by forming a transient ferryl ion (compound I) of cytochrome P-450 which may be the common intermediate hydroxylating species involved in hydroxylations catalyzed by cytochrome P-450.	Steroids	70-77	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	142-158	
173555-13	1976	It is proposed that NaIO4, NaClO2, and organic hydroperoxides promote steroid hydroxylation by forming a transient ferryl ion (compound I) of cytochrome P-450 which may be the common intermediate hydroxylating species involved in hydroxylations catalyzed by cytochrome P-450.	Steroids	70-77	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	258-274	
1102797-0	1975	Sources of reducing equivalents for cytochrome P-450 mitochondrial steroid hydroxylations in rat adrenal cortex cells.	Steroids	67-74	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	36-52	
10565810-6	1999	Microsomal androst-4-ene-3,17-dione hydroxylation activities mediated by CYP2C11 (16alpha-hydroxylation) and CYP3A2 (6beta-hydroxylation) were decreased in liver from OA-fed rats for only 5 days, whereas CYP2A1/2-mediated steroid 7alpha-hydroxylation was decreased after 10 days; these observations were complemented by immunoblot analysis that demonstrated the impaired expression of the corresponding CYP proteins.	Steroids	222-229	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	73-76	
30362088-1	2018	Cytochrome P450 (P450) enzymes are involved in the metabolism of carcinogens, as well as drugs, steroids, vitamins, and other classes of chemicals.	Steroids	96-104	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	0-21	
17691922-9	2007	Hence stimulation or inhibition of the brain dopaminergic system (e.g. by dopamine receptor-blocking neuroleptics) may cause changes in CYP activity of physiological, pharmacological and toxicological significance, since CYP isoforms that are regulated by the dopaminergic system catalyze the metabolism of endogenous substances (e.g. steroids), clinically important drugs (e.g. psychotropics, calcium channel antagonists, antibiotics) and toxins.	Steroids	335-343	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	136-139	
17691922-9	2007	Hence stimulation or inhibition of the brain dopaminergic system (e.g. by dopamine receptor-blocking neuroleptics) may cause changes in CYP activity of physiological, pharmacological and toxicological significance, since CYP isoforms that are regulated by the dopaminergic system catalyze the metabolism of endogenous substances (e.g. steroids), clinically important drugs (e.g. psychotropics, calcium channel antagonists, antibiotics) and toxins.	Steroids	335-343	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	221-224	
14574442-12	2003	The data on CYP activities indicated that high metabolic rates of steroids, fatty acids, and xenobiotics may occur in male wild ruminants.	Steroids	66-74	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	12-15	
11403911-5	2001	These effects suggest the possibility of DDE-caused induction of aromatase, a member of CYP family that catalyzes the conversion of C19 steroids to estrogens.	Steroids	136-144	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	88-91	
10653987-0	2000	Interactive binding at cytochrome P-450 of cell growth regulatory bioamines, steroid hormones, antihormones, and drugs.	Steroids	77-93	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	23-39	
10653987-5	2000	We now show that several classes of steroid hormones, antiestrogens, and antiandrogens, as well as various arylalkylamine drugs, all potently inhibit (3)H-histamine binding to cytochrome P-450 (K(i) values: testosterone 0.28 microM, progesterone 0.56 microM, flutamide 1.7 microM, tamoxifen 9.0 microM).	Steroids	36-43	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	176-192	
30044725-2	2019	The CO-binding pigment (cytochrome P450) had been discovered a few years earlier and was subsequently found to be involved in steroid hydroxylation in adrenal cortex microsomes.	Steroids	126-133	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	24-39	
28935656-2	2017	The aim of our present research was to determine the effect of the novel atypical neuroleptic drug with antidepressant properties lurasidone, on the expression (mRNA and protein level) and activity of liver CYP isoforms involved in the metabolism of drugs and endogenous steroids, in the chronic mild stress (CMS) model of depression.	Steroids	271-279	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	207-210	
28935656-6	2017	Based on the obtained results, it can be suggested that the metabolism of endogenous substrates (e.g., steroids) and drugs, catalyzed by the isoforms CYP2B, CYP2C11, or CYP3A, may proceed at a different rate in the two groups of animals (nonstressed and stressed) in the rat CMS model.	Steroids	103-111	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	150-155	
7797018-4	1995	METHODS: Microsomal steroid hydroxylation was used to indicate the activities of specific CYPs after TNF-alpha treatment and immunoblotting to correlate CYP activities with protein contents.	Steroids	20-27	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	90-93	
10406934-3	1999	The expression of CYP enzymes is regulated by steroid hormones, which, in turn, are inactivated in the liver by CYP-catalyzed hydroxylations and subsequent conjugations.	Steroids	46-53	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	18-21	
10406934-3	1999	The expression of CYP enzymes is regulated by steroid hormones, which, in turn, are inactivated in the liver by CYP-catalyzed hydroxylations and subsequent conjugations.	Steroids	46-53	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	112-115	
9405271-2	1998	Cytochrome P-450 (CYP) enzymes are expressed mainly in the liver and are active in mono-oxygenation and hydroxylation of various xenobiotics, including drugs and alcohols, as well as that of endogenous compounds such as steroids, bile acids, prostaglandins, leukotrienes and biogenic amines.	Steroids	220-228	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	0-16	
9405271-2	1998	Cytochrome P-450 (CYP) enzymes are expressed mainly in the liver and are active in mono-oxygenation and hydroxylation of various xenobiotics, including drugs and alcohols, as well as that of endogenous compounds such as steroids, bile acids, prostaglandins, leukotrienes and biogenic amines.	Steroids	220-228	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	18-21	
9452186-1	1997	The cytochrome P-450 (P-450) monooxygenase system can catalyze the oxidation of a wide variety of endogenous and exogenous compounds, including steroid hormones, fatty acids, drugs and pollutants.	Steroids	144-160	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	4-20	
9310395-0	1997	Regulation of expression of cytochrome P-450 2D mRNA in rat brain with steroid hormones.	Steroids	71-87	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	28-44	
9174981-5	1997	At the same time, resolution of 15 different steroid metabolites catalyzed by the cytochrome P-450 enzymes are readily separated in rat or mouse liver microsomes.	Steroids	45-52	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	82-98	
9273729-2	1996	The obtained results show the increase in catalytic activities of main forms of cytochrome P-450, participating in steroid hydroxylation, as well as the decrease in total content of cytochrome P-450 in hepatic microsomal fraction and the lowering of its demethylase activity.	Steroids	115-122	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	80-96	
7880321-6	1994	Analysis of cytochrome P450 isozymes in diabetic rats is helpful in elucidating the impaired metabolism of some endogenous substrates catalyzed by the cytochrome P450, such as steroid hormones and fatty acids, in diabetes.	Steroids	176-192	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	12-27	
7880321-6	1994	Analysis of cytochrome P450 isozymes in diabetic rats is helpful in elucidating the impaired metabolism of some endogenous substrates catalyzed by the cytochrome P450, such as steroid hormones and fatty acids, in diabetes.	Steroids	176-192	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	151-166	
8350704-5	1993	The levels of cytochrome P-450 and cytochrome b5 were markedly decreased by the anabolic-androgenic steroid treatment in male rat microsomes, but neither the steroid administration nor exercise training induced significant changes in the cytochrome levels of female rat livers.	Steroids	100-107	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	14-48	
7518966-5	1994	This data supports our earlier observations that FK 506 metabolism is mediated predominantly by the steroid inducible cytochrome P-450 IIIA enzyme subfamily.	Steroids	100-107	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	118-134	
8298502-6	1993	The possibility that the NSAIDS may interfere with cytochrome P-450 is discussed, since several steroid-transforming enzymes, known to be dependent on this cytochrome for their activity, were markedly inhibited.	Steroids	96-103	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	51-67	
1732040-1	1992	Treatment of male rats with the anticancer drug cisplatin leads to feminization of the profile of cytochrome P-450 and other microsomal enzymes involved in steroid hormone and drug metabolism (G.A.	Steroids	156-171	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	98-114	
1495014-6	1992	These data indicate that the affinity of azoles for cytochrome P-450 enzymes involved in steroid synthesis is highly dependent on the stereochemistry of the entire molecule, whereas binding to drug metabolizing enzymes is a less selective process.	Steroids	89-96	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	52-68	
7681660-0	1993	Regulation of two members of the steroid-inducible cytochrome P450 subfamily (3A) in rats.	Steroids	33-40	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	51-66	
7681660-1	1993	Monoclonal antibodies have been successfully isolated which are isozyme-specific for cytochrome P450p (3A1) or P4501 (3A2), two members of the steroid-inducible cytochrome P450 subfamily exhibiting 89% amino acid sequence homology, and these antibodies show less than 5% cross-reaction with 11 other cytochromes P450 (P450a-P450k).	Steroids	143-150	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	85-101	
7681660-1	1993	Monoclonal antibodies have been successfully isolated which are isozyme-specific for cytochrome P450p (3A1) or P4501 (3A2), two members of the steroid-inducible cytochrome P450 subfamily exhibiting 89% amino acid sequence homology, and these antibodies show less than 5% cross-reaction with 11 other cytochromes P450 (P450a-P450k).	Steroids	143-150	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	85-100	
1999182-1	1991	The hepatic metabolism of steroid hormones and of xenobiotics frequently depends on the expression of the sex-specific isoforms of cytochrome P-450 and on differences in sex hormones.	Steroids	26-42	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	131-147	
1912073-6	1991	Cytochrome P-450 induction may play an important role in the triterpensaponine action on the organism, because this enzyme participates in the metabolism of such endogenous compounds as prostaglandins, steroid hormones, cholesterol, etc.	Steroids	202-218	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	0-16	
2018466-0	1991	Distinct forms of cytochrome P-450 are responsible for 6 beta-hydroxylation of bile acids and of neutral steroids.	Steroids	105-113	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	18-34	
2316635-1	1990	We found microsomal corticosterone 6 beta-hydroxylase (6 beta-OHase) from cultured A6 kidney epithelial cells to be a cytochrome P-450 enzyme with both similarities to and differences from the rat liver steroid 6 beta-OHase P-450p.	Steroids	203-210	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	118-134