PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10888271-4 2000 We have shown that polyamines, hormones (including estrogen, testosterone and progesterone), antihormones (including tamoxifen and flutamide) and various antidepressants and antihistamines, all inhibit histamine binding to P450; we have postulated that, through binding to the heme moiety, intracellular histamine regulates cell function by modulating the catalytic activity of P450 enzymes, an action that may be perturbed by endogenous and exogenous substances. Progesterone 78-90 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 223-227 10403825-5 1999 This P450 exhibited 6beta-hydroxylation activity toward both testosterone and progesterone. Progesterone 78-90 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 5-9 8969926-6 1996 Incubation of the purified enzyme with steroid in a reaction vessel containing a platinum electrode and a Ag/AgCl electrode couple poised at -650 mV, together with the electromotively active redox mediator, cobalt sepulchrate, results in the 17 alpha-hydroxylation of progesterone at rates as high as 25 nmoles of progesterone hydroxylated/min/nmole of P450. Progesterone 268-280 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 353-357 9328296-1 1997 Roles of human cytochrome P450 (P450 or CYP) 2C9, 2C19, and 3A4 in the oxidation of progesterone and testosterone were studied in recombinant P450 enzymes and in human liver microsomes. Progesterone 84-96 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 32-48 8969926-6 1996 Incubation of the purified enzyme with steroid in a reaction vessel containing a platinum electrode and a Ag/AgCl electrode couple poised at -650 mV, together with the electromotively active redox mediator, cobalt sepulchrate, results in the 17 alpha-hydroxylation of progesterone at rates as high as 25 nmoles of progesterone hydroxylated/min/nmole of P450. Progesterone 314-326 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 353-357 8632407-10 1996 P450 17: K(m)progesterone = 7 microM, K(i)16 = 9 microM, K(i)20 = 80 nM). Progesterone 13-25 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 0-4 31339834-1 2019 PURPOSE: Hydroxylation activity at the 6beta-position of steroid hormones (testosterone, progesterone, and cortisol) by human cytochromes P450 (P450 or CYP) 3A4 and CYP3A5 and their molecular docking energy values were compared to understand the catalytic properties of the major forms of human CYP3A, namely, CYP3A4 and CYP3A5. Progesterone 89-101 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 126-160 22837389-0 2013 Isoform-specific regulation of cytochromes P450 expression by estradiol and progesterone. Progesterone 76-88 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 43-47 22837389-4 2013 The results showed that estradiol enhances CYP2A6, CYP2B6, and CYP3A4 expression, whereas progesterone induces CYP2A6, CYP2B6, CYP2C8, CYP3A4, and CYP3A5 expression. Progesterone 90-102 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 119-125 3502608-3 1987 The levels of mRNAs for the rate-limiting enzymes in the conversion of cholesterol into progesterone, namely cholesterol side-chain cleavage cytochrome P-450 and its electron donor, adrenodoxin, were higher in corpora lutea than in follicles. Progesterone 88-100 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 152-157 3502608-4 1987 Conversely the levels of mRNA specific for the key regulatory enzyme in the conversion of pregnenolone or progesterone to androgen, namely 17 alpha-hydroxylase cytochrome P-450, were high in all antral follicles examined but were low in young corpora lutea and undetectable in more mature corpora lutea. Progesterone 106-118 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 171-176 3795953-3 1986 Progesterone and 17 alpha-hydroxyprogesterone, the enzyme"s substrates, bound stoichiometrically to microsomal P-450 with unusually high affinity (Kd = 23-51 nM). Progesterone 0-12 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 111-116