PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26066995-1 2015 We co-crystallized human cytochrome P450 3A4 (CYP3A4) with progesterone (PRG) under two different conditions, but the resulting complexes contained only one PRG molecule bound to the previously identified peripheral site. Progesterone 59-71 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 25-44 28949811-0 2017 Characterization of Maternal and Fetal CYP3A-Mediated Progesterone Metabolism. Progesterone 54-66 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 39-44 28339191-0 2017 Allosteric Activation of Cytochrome P450 3A4 via Progesterone Bioconjugation. Progesterone 49-61 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 25-44 28339191-6 2017 CYP3A4 mutants were created and covalently modified with various small molecules including progesterone. Progesterone 91-103 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 0-6 27995413-9 2017 Stromal cells isolated from ovarian endometriotic lesions expressed CYP3A4 and their exposure to luteal phase-mimicking hormones (estradiol + progesterone) reduced CYP3A4 mRNA in parallel with a diminished expression of the corresponding receptors, estrogen receptor alpha and progesterone receptor. Progesterone 142-154 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 68-74 27995413-9 2017 Stromal cells isolated from ovarian endometriotic lesions expressed CYP3A4 and their exposure to luteal phase-mimicking hormones (estradiol + progesterone) reduced CYP3A4 mRNA in parallel with a diminished expression of the corresponding receptors, estrogen receptor alpha and progesterone receptor. Progesterone 142-154 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 164-170 26066995-1 2015 We co-crystallized human cytochrome P450 3A4 (CYP3A4) with progesterone (PRG) under two different conditions, but the resulting complexes contained only one PRG molecule bound to the previously identified peripheral site. Progesterone 59-71 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 46-52 28221037-7 2017 Our results revealed that the binding mode of progesterone (PGS), a substrate of CYP3A4, in the crystal structure was not stable and underwent a significant conformational change. Progesterone 46-58 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 81-87 23223499-2 2013 Placental growth hormone (PGH), estrogens (primarily 17beta-estradiol), cortisol, and progesterone have the potential to modulate CYP3A activity. Progesterone 86-98 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 130-135 25678418-3 2015 6beta-Hydroxylation of many steroids, including cortisol, cortisone, progesterone and testosterone, was catalyzed primarily by CYP3A4. Progesterone 69-81 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 127-133 24256945-2 2014 Here, we show that b5 mutations E48G, E49G, D58G, and D65G have reduced capacity to stimulate CYP3A4-catalyzed progesterone and testosterone 6beta-hydroxylation or nifedipine oxidation. Progesterone 111-123 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 94-100 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 3 subfamily A member 4 Homo sapiens 135-141 19414330-6 2009 In progesterone-bound CYP3A4, four candidate ligand accessible regions were observed and progesterone could be bound by two selected ligand accessible regions. Progesterone 3-15 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 22-28 22194603-7 2012 It is located in the vicinity of residues 217-220, similar to the position of the progesterone molecule bound at the distal surface of the CYP3A4 in a prior x-ray crystal structure. Progesterone 82-94 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 139-145 19189363-3 2009 The results demonstrate that the apparent radical recombination rate in the CYP3A4 hydroxylation of beta-thujone is accelerated by the progesterone heterotropic cooperativity. Progesterone 135-147 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 76-82 18957504-8 2009 RESULTS: Compared to P450c21, the Vmax/Km for 21-hydroxylation of progesterone by CYP2C19 and CYP3A4 were 17 and 10%, respectively. Progesterone 66-78 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 94-100 16490811-8 2006 Higher CYP3A activity in women may be associated with higher endogenous progesterone concentrations. Progesterone 72-84 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 7-12 15256616-0 2004 Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Progesterone 72-84 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 28-47 16190729-8 2005 The structural and dynamic features of the CYP3A4-progesterone complex indicate that the oxidative degradation of progesterone occurs through hydroxylation at the C16 position by the reactive oxygen coordinated to the heme iron. Progesterone 50-62 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 43-49 16190729-8 2005 The structural and dynamic features of the CYP3A4-progesterone complex indicate that the oxidative degradation of progesterone occurs through hydroxylation at the C16 position by the reactive oxygen coordinated to the heme iron. Progesterone 114-126 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 43-49 15256616-4 2004 Here we report three crystal structures of CYP3A4: unliganded, bound to the inhibitor metyrapone, and bound to the substrate progesterone. Progesterone 125-137 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 43-49 34196520-4 2021 We have used hydrogen-deuterium exchange mass spectrometry to investigate the impact of binding of CPR and of three different substrates (7-benzyloxy-4-trifluoromethyl-coumarin, testosterone, and progesterone) on the conformational dynamics of CYP3A4. Progesterone 196-208 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 244-250 12893521-7 2003 Additionally, 7-benzyloxyresorufin O-debenzylation by recombinant CYP3A4 was increased by the addition of alpha-naphthoflavone, testosterone and progesterone but not by quinidine, whereas no chemicals tested could activate the O-debenzylation of 7-benzyloxyresorufin by CYP2B6. Progesterone 145-157 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 66-72 12893521-9 2003 The K(m) for nifedipine oxidation activity by CYP3A4 decreased by the addition of progesterone, whereas the V(max) remained constant. Progesterone 82-94 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 46-52 9667077-5 1998 6 beta-Hydroxylation of progesterone was catalysed most efficiently by CYP3A4, followed by CYP2D6. Progesterone 24-36 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 71-77 9667077-6 1998 CYP3A4 showed the highest progesterone 16 alpha-hydroxylation activity, followed by CYP1A1 and CYP2D6. Progesterone 26-38 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 0-6 9667077-10 1998 Addition of nifedipine, a typical substrate of CYP3A4, inhibited the 6 beta- and 16 alpha-hydroxylation of progesterone by CYP3A4. Progesterone 107-119 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 47-53 9667077-10 1998 Addition of nifedipine, a typical substrate of CYP3A4, inhibited the 6 beta- and 16 alpha-hydroxylation of progesterone by CYP3A4. Progesterone 107-119 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 123-129 8010982-5 1994 Results of the study showed that: (1) purified CYP3A4 catalyzed 10,11-epoxidation; (2) cDNA-expressed CYP3A4 catalyzed 10,11-epoxidation (Vmax = 1730 pmol/min/nmol P450, Km = 442 microM); (3) the rate of 10,11-epoxidation correlated with CYP3A4 content in microsomes from sixteen human livers (r2 = 0.57, P < 0.001); (4) triacetyloleandomycin and anti-CYP3A4 IgG reduced 10,11-epoxidation to 31 +/- 6% (sixteen livers) and 43 +/- 2% (four livers) of control rates, respectively; and (5) microsomal 10,11-epoxidation but not phenol formation was activated 2- to 3-fold by alpha-naphthoflavone and progesterone and by carbamazepine itself (substrate activation). Progesterone 599-611 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 47-53 8010982-5 1994 Results of the study showed that: (1) purified CYP3A4 catalyzed 10,11-epoxidation; (2) cDNA-expressed CYP3A4 catalyzed 10,11-epoxidation (Vmax = 1730 pmol/min/nmol P450, Km = 442 microM); (3) the rate of 10,11-epoxidation correlated with CYP3A4 content in microsomes from sixteen human livers (r2 = 0.57, P < 0.001); (4) triacetyloleandomycin and anti-CYP3A4 IgG reduced 10,11-epoxidation to 31 +/- 6% (sixteen livers) and 43 +/- 2% (four livers) of control rates, respectively; and (5) microsomal 10,11-epoxidation but not phenol formation was activated 2- to 3-fold by alpha-naphthoflavone and progesterone and by carbamazepine itself (substrate activation). Progesterone 599-611 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 102-108 8010982-5 1994 Results of the study showed that: (1) purified CYP3A4 catalyzed 10,11-epoxidation; (2) cDNA-expressed CYP3A4 catalyzed 10,11-epoxidation (Vmax = 1730 pmol/min/nmol P450, Km = 442 microM); (3) the rate of 10,11-epoxidation correlated with CYP3A4 content in microsomes from sixteen human livers (r2 = 0.57, P < 0.001); (4) triacetyloleandomycin and anti-CYP3A4 IgG reduced 10,11-epoxidation to 31 +/- 6% (sixteen livers) and 43 +/- 2% (four livers) of control rates, respectively; and (5) microsomal 10,11-epoxidation but not phenol formation was activated 2- to 3-fold by alpha-naphthoflavone and progesterone and by carbamazepine itself (substrate activation). Progesterone 599-611 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 102-108 8010982-5 1994 Results of the study showed that: (1) purified CYP3A4 catalyzed 10,11-epoxidation; (2) cDNA-expressed CYP3A4 catalyzed 10,11-epoxidation (Vmax = 1730 pmol/min/nmol P450, Km = 442 microM); (3) the rate of 10,11-epoxidation correlated with CYP3A4 content in microsomes from sixteen human livers (r2 = 0.57, P < 0.001); (4) triacetyloleandomycin and anti-CYP3A4 IgG reduced 10,11-epoxidation to 31 +/- 6% (sixteen livers) and 43 +/- 2% (four livers) of control rates, respectively; and (5) microsomal 10,11-epoxidation but not phenol formation was activated 2- to 3-fold by alpha-naphthoflavone and progesterone and by carbamazepine itself (substrate activation). Progesterone 599-611 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 102-108 12781333-5 2003 Addition of CYP3A4 substrates (verapamil, midazolam, quinidine, and progesterone) to the oxygenated solution caused a concentration-dependent increase in the reduction current in cyclic voltammetric and amperometric experiments. Progesterone 68-80 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 12-18 12464250-2 2003 Unlike CYP3A4, it is a very poor testosterone 6beta- and 2beta-hydroxylase, but a relatively better catalyst of progesterone monohydroxylation largely at 6beta, 16alpha, and 21 positions with negligible 6beta, 21-dihydroxylation. Progesterone 112-124 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 7-13 10773032-1 2000 The structural basis of cooperativity of progesterone hydroxylation catalyzed by human cytochrome P450 3A4 has been investigated. Progesterone 41-53 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 87-106 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 3 subfamily A member 4 Homo sapiens 165-170 31829451-10 2019 In conclusion, the progesterone metabolites formed via CYP3A cause inhibitory effects on hERG channels and predict QTcI intervals in healthy women pretreated with progesterone. Progesterone 19-31 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 55-60 31829451-10 2019 In conclusion, the progesterone metabolites formed via CYP3A cause inhibitory effects on hERG channels and predict QTcI intervals in healthy women pretreated with progesterone. Progesterone 163-175 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 55-60 31339834-2 2019 METHODS: Testosterone, progesterone, and cortisol 6beta-hydroxylation activities of recombinant CYP3A4 and CYP3A5 were determined by liquid chromatography. Progesterone 23-35 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 96-102 31339834-4 2019 RESULTS: Michaelis constants (Km) for CYP3A5- mediated 6beta-hydroxylation of testosterone and progesterone were approximately twice those for CYP3A4, whereas the value for cortisol 6beta-hydroxylation mediated by CYP3A5 was similar to the value for that by CYP3A4. Progesterone 95-107 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 258-264 33790108-1 2021 The inhibitory and stimulatory effects of steroid hormones and related compounds on the hydroxylation activity at the 6beta-position of two steroid hormones, progesterone and testosterone, by CYP3A4, polymorphically expressed CYP3A5, and fetal CYP3A7 were compared to clarify the catalytic properties of the predominant forms of the human CYP3A subfamily. Progesterone 158-170 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 192-198 33790108-2 2021 Hydroxylation activities of progesterone and testosterone by CYP3A4, CYP3A5, and CYP3A7 were estimated using HPLC. Progesterone 28-40 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 61-67 33790108-3 2021 The Michaelis constants (Km) for progesterone 6beta-hydroxylation by CYP3A5 were markedly decreased in the presence of dehydroepiandrosterone (DHEA) and alpha-naphthoflavone (ANF), whereas progesterone and DHEA competitively inhibited testosterone 6beta-hydroxylation mediated by CYP3A4, and progesterone competitively inhibited CYP3A5-mediated activity, which was weaker than that for CYP3A4. Progesterone 33-45 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 280-286 33790108-3 2021 The Michaelis constants (Km) for progesterone 6beta-hydroxylation by CYP3A5 were markedly decreased in the presence of dehydroepiandrosterone (DHEA) and alpha-naphthoflavone (ANF), whereas progesterone and DHEA competitively inhibited testosterone 6beta-hydroxylation mediated by CYP3A4, and progesterone competitively inhibited CYP3A5-mediated activity, which was weaker than that for CYP3A4. Progesterone 33-45 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 386-392 32001245-1 2020 Hydroxylation activity at the 6beta-position of steroid hormones (testosterone, progesterone, and cortisol) by human cytochromes P450 (CYP) 3A4, polymorphic CYP3A5, and fetal CYP3A7 were compared to understand the catalytic properties of the major forms of human CYP3A subfamily. Progesterone 80-92 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 117-143 32001245-2 2020 Testosterone, progesterone, and cortisol 6beta-hydroxylation activities of recombinant CYP3A4, CYP3A5, and CYP3A7 were determined by liquid chromatography. Progesterone 14-26 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 87-93 32001245-5 2020 A decrease in Km values for progesterone 6beta-hydroxylation by CYP3A4, CYP3A5, and CYP3A7 in the presence of testosterone was observed, and the kcat values for CYP3A5 gradually increased with increasing testosterone. Progesterone 28-40 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 64-70 32001245-7 2020 However, progesterone inhibited testosterone 6beta-hydroxylation mediated by CYP3A4, CYP3A5, and CYP3A7. Progesterone 9-21 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 77-83 31083930-0 2019 A Covalently Attached Progesterone Molecule Outcompetes the Binding of Free Progesterone at an Allosteric Site of Cytochrome P450 3A4. Progesterone 22-34 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 114-133 31083930-0 2019 A Covalently Attached Progesterone Molecule Outcompetes the Binding of Free Progesterone at an Allosteric Site of Cytochrome P450 3A4. Progesterone 76-88 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 114-133 31083930-4 2019 Progesterone (PRG) is a known allosteric activator of CYP3A4-catalyzed 7-benzyloxy-4-trifluoromethylcoumarin (BFC) debenzylation. Progesterone 0-12 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 54-60 31083930-4 2019 Progesterone (PRG) is a known allosteric activator of CYP3A4-catalyzed 7-benzyloxy-4-trifluoromethylcoumarin (BFC) debenzylation. Progesterone 14-17 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 54-60 30785734-1 2019 The role of Phe213 in the allosteric mechanism of human cytochrome P450 CYP3A4 was studied using a combination of progesterone (PGS) and carbamazepine (CBZ) as probe substrates. Progesterone 114-126 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 72-78 30785734-1 2019 The role of Phe213 in the allosteric mechanism of human cytochrome P450 CYP3A4 was studied using a combination of progesterone (PGS) and carbamazepine (CBZ) as probe substrates. Progesterone 128-131 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 72-78 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 3 subfamily A member 4 Homo sapiens 310-316 30125880-6 2018 Furthermore, the constructed CYP3A4/PNGF-1 nanoreactor is successfully applied to the metabolism of three steroid hormones (testosterone, estrone and progesterone), and the order of the calculated Kmapp values is consistent with literature. Progesterone 150-162 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 29-35