Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians
T. Shimada Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians J. Pharmacol. Exp. Ther. 270 1994 414 423
The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05 Å resolution
J.K. Yano The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05 Å resolution J. Biol. Chem. 279 2004 38091 38094
Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding
J. Cosme, and E.F. Johnson Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding J. Biol. Chem. 275 2000 2545 2553
Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 Å resolution: Evidence for an induced fit model of substrate binding
M.R. Wester Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 Å resolution: evidence for an induced fit model of substrate binding Biochemistry 42 2003 9335 9345
Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by α-naphthoflavone
G.E. Schwab Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by α-naphthoflavone Mol. Pharmacol. 33 1988 493 499
Multisite kinetic models for CYP3A4: Simultaneous activation and inhibition of diazepam and testosterone metabolism
K.E. Kenworthy Multisite kinetic models for CYP3A4: simultaneous activation and inhibition of diazepam and testosterone metabolism Drug Metab. Dispos. 29 2001 1644 1651
Analysis of homotropic and heterotropic cooperativity of diazepam oxidation by CYP3A4 using site-directed mutagenesis and kinetic modeling
Y.A. He Analysis of homotropic and heterotropic cooperativity of diazepam oxidation by CYP3A4 using site-directed mutagenesis and kinetic modeling Arch. Biochem. Biophys. 409 2003 92 101
Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 Å resolution: Evidence for multiple substrate binding modes
M.R. Wester Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 Å resolution: evidence for multiple substrate binding modes Biochemistry 42 2003 6370 6379
Analysis of human cytochrome P450 3A4 cooperativity: Construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics
G.R. Harlow, and J.R. Halpert Analysis of human cytochrome P450 3A4 cooperativity: construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics Proc. Natl. Acad. Sci. U. S. A. 95 1998 6636 6641