PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2095353-5	1990	Thus, after 3 beta-HSD-catalyzed formation from pregnenolone, progesterone was efficiently converted to 5 alpha-pregnan-3,20-dione (5 alpha-dihydroprogesterone) and subsequent metabolism to the corresponding 17 alpha-hydroxylated derivative and 5 alpha-androstan-3,17-dione in a reaction catalyzed by P-450(17) alpha.	Progesterone	62-74	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	301-316	
9070288-2	1997	In microsomal membranes from rat testes, the maximal type I optical difference spectrum induced by the physiological CYP17 substrate, progesterone, as a measure of spin state transition due to hydrophobic ligand-protein interaction is enhanced by 24% within 15 minutes in the presence of MgATP; the dissociation constant decreases from 71 to 43 nM.	Progesterone	134-146	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	117-122	
9257124-1	1997	This study uses microsomal membranes from rat testis tissue, including the cytochrome P450c17 (steroid 17 alpha-monooxygenase/17 alpha-hydroxyprogesterone aldolase, catalyzing the conversion of progesterone to androstenedione), to decipher the possible relation of NADPH-induced (no exogenous iron added) lipid peroxidation and cytochrome P450 inactivation and the protective effect of certain steroids.	Progesterone	142-154	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	75-93	
8525490-12	1995	The negative effect of lead on testosterone and progesterone production was correlated with the lower expression of the enzymes cytochromes P450scc (CYP11A1) and P450c17 (CYP17) and 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) involved in steroid hormone biosynthesis, as shown by immunohistochemistry.	Progesterone	48-60	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	162-169	
8525490-12	1995	The negative effect of lead on testosterone and progesterone production was correlated with the lower expression of the enzymes cytochromes P450scc (CYP11A1) and P450c17 (CYP17) and 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) involved in steroid hormone biosynthesis, as shown by immunohistochemistry.	Progesterone	48-60	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	171-176	
8119304-3	1993	Progesterone binding to CYP17 is competitively inhibited, with Ki = 2.6 microM norharman, whereas harman, tetrahydronorharman and tetrahydroharman are nearly ineffective.	Progesterone	0-12	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	24-29	
29729232-9	2019	CONCLUSIONS: These results showed that Hyperin and Icariin can promote the secretion of E2 and P through up-regulation of CYP17 and CYP19.	Progesterone	95-96	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	122-127	
34261222-4	2021	The results indicate that PFOS exposure significantly up-regulated the expressions of StAR, CYP11A1 and 3beta-HSD, while CYP17A1 and 17beta-HSD were down-regulated, thus contributing to the elevated progesterone and testosterone levels.	Progesterone	199-211	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	121-128	
35438966-3	2022	It was found that the serum levels of progesterone, testosterone, and estradiol were significantly increased after 0.015 and 0.15 mg/kg of PFOA exposure, and the expression of Star, a key rate-limiting gene, was up-regulated, while other steroidogenic genes Cyp11a1, Hsd3b, Cyp17a1, and Hsd17b were down-regulated.	Progesterone	38-50	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	274-281	
24451217-6	2014	The CYP17A1 enzyme is critical for androgen biosynthesis and catalyzes conversion of progesterone into androstenedione.	Progesterone	85-97	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	4-11	
24451217-11	2014	The mode of action of HPTE on CYP17A1 activity was determined to be uncompetitive with the substrate progesterone.	Progesterone	101-113	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	30-37	
9569017-6	1998	Upon enzymatic analysis utilizing microsomal fractions from livers, levels of 17alpha-hydroxylase and 17,20-lyase activity for pregnenolone and progesterone increased by 3 weeks and dramatically reduced at 7 weeks, which is consistent with the expression level of P450c17.	Progesterone	144-156	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	264-271	
22800812-2	2012	However, the presence of the cytochrome P450 17alpha-hydroxylase/C(17,20)-lyase (P450C(17)), an enzyme that converts pregnenolone and progesterone into dehydroepiandrosterone and androstenedione, in specific areas of the cerebellum such as the deep cerebellar nuclei, remains virtually unexplored.	Progesterone	134-146	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	86-90	
21925253-8	2011	The IC(50)s for human and rat CYP17A1 (1 muM progesterone) were 18.99+-3.75 and 64.67+-4.04 muM, respectively.	Progesterone	45-57	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	30-37	
21388459-3	2011	The cytochrome P450 17alpha-hydroxylase/C(17,20)-lyase (P450C(17) ) plays a pivotal role in the synthesis of DHEA from pregnenolone and progesterone.	Progesterone	136-148	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	61-65	
12693981-4	2003	Highly purified cytochromes P45017alpha were used for determination of enzyme activity and specificity in relation to progesterone, pregnenolone, 17alpha-hydroxyprogesterone, and 17alpha-hydroxypregnenolone with registration of the kinetics of reaction product formation using HPLC.	Progesterone	118-130	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	28-39	
17369198-7	2007	These results suggest that PCZ inhibits the conversion of progesterone to testosterone through the inhibition of CYP17.	Progesterone	58-70	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	113-118	
12668680-5	2003	In a low but physiological concentration of NADPH-cytochrome P-450 reductase and excess amount of progesterone, outer mitochondrial membrane cytochrome b5 stimulated the cytochrome P-45017alpha-catalyzed reactions, 17alpha-hydroxylation and C17-C20 bond cleavage.	Progesterone	98-110	cytochrome P450, family 17, subfamily a, polypeptide 1	Rattus norvegicus	181-193