Cytochromes P450 (CYP) are a major source of variability in drug pharmacokinetics and
response. Of 57 putatively functional human CYPs only about a dozen enzymes, belonging …

Genetic polymorphisms in drug-metabolizing enzymes, transporters, receptors, and other
drug targets have been linked to interindividual differences in the efficacy and toxicity of …

Variation in the CYP3A enzymes, which act in drug metabolism, influences circulating
steroid levels and responses to half of all oxidatively metabolized drugs. CYP3A activity is …

Pharmacogenetics is the study of how interindividual variations in the DNA sequence of
specific genes affect drug response. This article highlights current pharmacogenetic …

Cytochrome P450s comprise a superfamily of heme-thiolate proteins named for the spectral
absorbance peak of their carbon-monoxide-bound species at 450 nm. Having been found in …

Abstract Cytochrome P450 3A4 (CYP3A4) metabolizes∼ 50% of all clinically used drugs.
Although CYP3A4 expression varies widely between individuals, the contribution of genetic …

The human CYP3A subfamily plays a dominant role in the metabolic elimination of more
drugs than any other biotransformation enzyme. CYP3A enzyme is localized in the liver and …

Human cytochrome P450 (CYP) 3A4 is the most abundant hepatic and intestinal phase I
enzyme that metabolizes approximately 50% marketed drugs. The crystal structure of bound …

Cytochrome P450 3A4 (CYP3A4) is involved in the metabolism of more drugs in clinical use
than any other foreign compound–metabolizing enzyme in humans. Recently, increasing …

We investigated the elimination routes for the 200 drugs that are sold most often by
prescription count in the United States. The majority (78%) of the hepatically cleared drugs …