Associated Papers
Multiple substrate-binding sites are retained in cytochrome P450 3A4 mutants with decreased cooperativity.
Fernando H et al.
Xenobiotica; the Fate of Foreign Compounds in Biological Systems, 2011
CYP3A4 is a vitamin D-24- and 25-hydroxylase: analysis of structure function by site-directed mutagenesis.
Gupta RP et al.
The Journal of Clinical Endocrinology and Metabolism, 2005
Phenylalanine and tryptophan scanning mutagenesis of CYP3A4 substrate recognition site residues and effect on substrate oxidation and cooperativity.
Domanski TL et al.
Biochemistry, 2001
Influence of P450 3A4 SRS-2 residues on cooperativity and/or regioselectivity of aflatoxin B(1) oxidation.
Xue L et al.
Chemical Research in Toxicology, 2001
Dual role of human cytochrome P450 3A4 residue Phe-304 in substrate specificity and cooperativity.
Domanski TL et al.
The Journal of Pharmacology and Experimental Therapeutics, 2000
Analysis of human cytochrome P450 3A4 cooperativity: construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics.
Harlow GR et al.
Proceedings of the National Academy of Sciences of the United States of America, 1998
Select a paper to view details