PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6530334-1 1984 Boc-L-Asu-L-Ala-Gly-OMe crystallizes in the monoclinic space group P2(1) with cell dimensions a = 14.315 (3) A, b = 9.280 (2) A, c = 14.358(3) A, beta = 103.63(1) A, V= 1853.4 (9) A3, with two molecules in the asymmetric unit. Boc-L-Asu-L-Ala-Gly-OMe 0-23 cyclin dependent kinase inhibitor 1A Homo sapiens 67-72 20203109-9 2010 Finally, Simcyp was used to predict the in vivo magnitude of CYP3A4 DDIs caused by AMG 458 using midazolam, sildenafil, simvastatin, and testosterone as probe substrates. Testosterone 137-149 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 61-67 19480428-1 2009 Testosterone hydroxylation is a prototypical reaction of human cytochrome P450 3A4, which metabolizes about 50% of oral drugs on the market. Testosterone 0-12 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 63-82 19414624-5 2009 Marked increase in 6beta-hydroxylation of testosterone by CYP3A4 was also observed in the 6-day 1,25(OH)(2)D(3)-treated (100 nM) cell lysate. Testosterone 42-54 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 58-64 19020497-4 2009 In vitro functional analyses indicate that CYP3A4*18 is a gain-of-function mutation in sex steroid metabolism, resulting in rapid oxidation of estrogens and testosterone; in vivo pharmacokinetics using midazolam (MDZ) verify the altered activity of the CYP3A4*18, showing lower metabolic turnover in the mutant than in the wild type. Testosterone 157-169 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 43-49 18647599-7 2008 Flutamide and haloperidol were further demonstrated to cause CYP3A4 induction in human cryopreserved hepatocytes based on testosterone 6beta-hydroxylation activity. Testosterone 122-134 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 61-67 18431572-8 2008 In human liver microsomal preparations, eribulin suppressed the activities of CYP3A4-mediated testosterone and midazolam hydroxylation with an apparent K (i) of approximately 20 microM. Testosterone 94-106 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 78-84 18803184-1 2008 An electrophoretically mediated microanalysis method for the determination of CYP3A4 activity using testosterone and nifedipine as substrates was developed. Testosterone 100-112 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 78-84 18803184-7 2008 Using the Lineweaver-Burk equation, the Michaelis constants (K(m)) for the oxidation of testosterone and nifedipine by CYP3A4 were calculated to be 58.6+/-8.3 and 19.1+/-2.4 microM, respectively, which are consistent with off-line assay and previously reported values. Testosterone 88-100 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 119-125 21218106-4 2008 The aim of this study was to evaluate the efficiency of different in vitro systems containing individual enzymes of the mixed-function monooxygenase system to oxidize two model substrates of CYP3A enzymes, exogenous and endogenous compounds, alpha-naphtoflavone (alpha-NF) and testosterone, respectively. Testosterone 277-289 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 191-196 21218106-7 2008 The results presented in this study demonstrate the suitability of the supersomal CYP3A4 systems for studies investigating oxidation of testosterone and alpha-NF in vitro. Testosterone 136-148 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 82-88 18395506-7 2008 In addition, the red spectral component, with an apparent K(D)=2.2muM, is selectively eliminated by titration with the known allosteric effectors of CYP3A4, alpha-napthoflavone and testosterone. Testosterone 181-193 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 149-155 18819885-3 2008 After 15 min of culture, the substrates (testosterone for CYP3A4 and phenacetin for CYP1A2) were added and incubated for another 20 min. Testosterone 41-53 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 58-64 18322939-11 2008 Fipronil can inhibit testosterone metabolism by CYP3A4 and is an effective inducer of CYP isoforms in human hepatocytes. Testosterone 21-33 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 48-54 17650504-3 2007 To understand the overall kinetic processes operating in CYP3A4, we documented the kinetics of autoxidation of the oxy-ferrous intermediate of CYP3A4 as a function of testosterone concentration. Testosterone 167-179 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 57-63 18380401-3 2008 Initial velocity of testosterone 6beta-oxidation using human liver microsomes was determined as an indicator of the CYP3A activities. Testosterone 20-32 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 116-121 17826359-6 2008 Using erythromycin and testosterone as substrates, we demonstrated that CYP3A catalysis exhibited non-Michaelis-Menten kinetics in GCL cells, and that V(max)/K(m) values were significantly increased due to rifampicin-treatment. Testosterone 23-35 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 72-77 19326769-5 2008 Chlorpyrifos and DEET also mediated the expression of CYP isoforms, particularly CYP3A4, CYP2B6 and CYP1A1, as shown by CYP3A4-specific protein expression, testosterone metabolism and CYP1Al-specific activity assays. Testosterone 156-168 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 81-87 18328680-8 2008 Enzyme activity of CYP3A4, measured by testosterone metabolism, was increased after 24h by RIF. Testosterone 39-51 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 19-25 17650504-3 2007 To understand the overall kinetic processes operating in CYP3A4, we documented the kinetics of autoxidation of the oxy-ferrous intermediate of CYP3A4 as a function of testosterone concentration. Testosterone 167-179 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 143-149 17650504-6 2007 In contrast, the slow phase in the kinetics of cyanide binding to the ferric CYP3A4 correlated with a shift of the heme iron spin state, which is only caused by the association of a second molecule of testosterone. Testosterone 201-213 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 77-83 17914095-2 2007 Cytochrome P450 3A (CYP3A) enzymes hydroxylate testosterone and dehydroepiandrosterone to less active metabolites, which might be the basis for the association between CYP3A polymorphisms and prostate cancer. Testosterone 47-59 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 0-18 17914095-2 2007 Cytochrome P450 3A (CYP3A) enzymes hydroxylate testosterone and dehydroepiandrosterone to less active metabolites, which might be the basis for the association between CYP3A polymorphisms and prostate cancer. Testosterone 47-59 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 20-25 17914095-2 2007 Cytochrome P450 3A (CYP3A) enzymes hydroxylate testosterone and dehydroepiandrosterone to less active metabolites, which might be the basis for the association between CYP3A polymorphisms and prostate cancer. Testosterone 47-59 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 168-173 17526062-4 2007 We show that CYP3A4 tolerates only small amounts (<15 %) of water-miscible organic cosolvents or ionic liquids before its activity toward testosterone drops below detection. Testosterone 141-153 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 13-19 17526062-6 2007 CYP3A4 activity in the absence of buffer was only >or=10 % in solvents of the alkane series, with a minimum of 0.85 % water, and with the addition of sucrose and testosterone before enzyme lyophilization. Testosterone 165-177 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 0-6 17084830-7 2006 Similar increases and decreases were observed in CYP3A4-specific activity levels as measured using 6beta-hydroxytestosterone formation following incubation with testosterone. Testosterone 112-124 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 49-55 17555301-7 2007 Surprisingly, at high concentrations of allosteric substrates, the amplitude of the spin shift in both CYP3A4 in solution and Nanodiscs was very low, demonstrating that hydrostatic pressure induces neither substrate dissociation nor an increase in the heme pocket hydration in the complexes of the pressure-promoted conformation of CYP3A4 with 1-PB or testosterone. Testosterone 352-364 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 103-109 17555301-8 2007 These findings suggest that the mechanisms of interactions of CYP3A4 with 1-PB and testosterone involve an effector-induced transition that displaces a system of conformational equilibria in the enzyme toward the state(s) with decreased solvent accessibility of the active site so that the flux of water into the heme pocket is impeded and the high-spin state of the heme iron is stabilized. Testosterone 83-95 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 62-68