Zobrazeno 1 - 10
of 44
pro vyhledávání: '"W F, Trager"'
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 29(5)
Human liver microsomes catalyze the oxidation of sulfinpyrazone sulfide (SPZS) to a variable mixture of sulfinpyrazone (SPZ) enantiomers and two minor phenolic metabolites. In one, the thiophenyl ring is hydroxylated, whereas in the second an N-pheny
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 27(12)
Nevirapine (NVP), a non-nucleoside inhibitor of HIV-1 reverse transcriptase, is concomitantly administered to patients with a variety of medications. To assess the potential for its involvement in drug interactions, cytochrome P-450 (CYP) reaction ph
Publikováno v:
Biochemistry. 38(11)
Previous modeling efforts have suggested that coumarin ligand binding to CYP2C9 is dictated by electrostatic and pi-stacking interactions with complementary amino acids of the protein. In this study, analysis of a combined CoMFA-homology model for th
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 26(7)
(R)-(+)-Menthofuran is a potent, mechanism-based inactivator of human liver cytochrome P450 (CYP or P450) 2A6. Menthofuran caused a time- and concentration-dependent loss of CYP2A6 activity. The inactivation of CYP2A6 was characterized by a Ki of 2.5
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 25(12)
The P450 2A6 catalyzed 7-hydroxylation of coumarin proceeded with a mean Km of 0.40 (+/-0.13) microM and Vmax of 6.34 nmol/nmol P450/min (36-fold variation) in microsomal preparations from a panel of 12 human livers. Substrate depletion was avoided d
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 24(9)
The effect of branch pathways on the observed intramolecular isotope effect and deuterium retention associated with 6- and 7-hydroxylation of selectively monodeuterated (R)- and (S)-warfarin with cytochrome P450 (CYP) 2C9 and CYP1A2 were studied. cDN
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 24(5)
Kinetic studies demonstrate that two forms of human liver cytochrome P450 are responsible for the formation of (R)-8-hydroxywarfarin: a low-affinity enzyme (KM approximately 1.5 mM), previously identified as P4501A2; and a high-affinity enzyme (KM =
Autor:
D J, Black, K L, Kunze, L C, Wienkers, B E, Gidal, T L, Seaton, N D, McDonnell, J S, Evans, J E, Bauwens, W F, Trager
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 24(4)
Consistent with expectations based on human in vitro microsomal experiments, administration of fluconazole (400 mg/day) for 6 days to six human volunteers significantly reduced the cytochrome P450 (P450)-dependent metabolic clearance of the warfarin
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 24(4)
The antifungal agent fluconazole was found to be a potent inhibitor of cytochrome P450 (P450) 2C9 (Ki = 7-8 microM), the principal enzyme responsible for the clearance (85%) of the more potent anticoagulant (S)-warfarin to the inactive (S)-7- and (S)
Autor:
K L, Kunze, W F, Trager
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 24(4)
The results of studies of the effect of fluconazole on cytochrome P450 (P450) 2C9 activity in vivo and in vitro are used to develop an approach to the safe management of the warfarin-fluconazole drug interaction. This approach begins with a determina