Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Comparison of enzyme kinetic parameters obtained in vitro for reactions mediated by human CYP2C enzymes including major CYP2C9 variants.

Current drug metabolism - 1 Feb 2010

Rokitta D, Fuhr U

Abstract excerpt

Cytochrome P450 (CYP) 2C enzymes contribute to the metabolism of about 30% of all drugs. Known polymorphisms of the respective enzymes and drug-drug interactions have a major impact on the efficacy and safety of some CYP2C substrate drugs. In vivo - in vitro correlations including prediction of t...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aryl Hydrocarbon Hydroxylases
Share to Cytochrome P-450 CYP2C9
Share to Drug Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Variation

Share to Mixed Function Oxygenases

Share to Polymorphism, Genetic

Share to Substrate Specificity

Share to Vitamin K Epoxide Reductases

Source

Identifiers

PMID: 20359285
DOI: 10.2174/138920010791110872

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20359285-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Comparison of enzyme kinetic parameters obtained in vitro for reactions mediated by human CYP2C enzymes including major CYP2C9 variants.PMID 20359285Read ↗

Genetic Polymorphisms and in Vitro Functional Characterization of CYP2C8, CYP2C9, and CYP2C19 Allelic Variants.Semantic proximity Read ↗

Cytochrome P450 2C8: Substrates, inhibitors, pharmacogenetics, and clinical relevanceSemantic proximity Read ↗

Cytochrome P450 2C19 enzyme, Cytochrome P450 2C9 enzyme, and Cytochrome P450 2D6 enzyme allelic variants and its possible effect on drug metabolism: A retrospective study.Semantic proximity Read ↗

Comparison of cytochrome P450 2D6 and variants in terms of drug oxidation rates and substrate inhibition.Semantic proximity Read ↗

Impact of Genetic Polymorphisms in CYP2C9 and CYP2C19 on the Pharmacokinetics of Clinically Used DrugsSemantic proximity Read ↗

Cytochrome P450 2C9 polymorphisms: a comprehensive review of the in-vitro and human data.Semantic proximity Read ↗

Human Drug Metabolism and the Cytochromes P450: Application and Relevance of In Vitro ModelsSemantic proximity Read ↗

Inter-phenotypic differences in CYP2C9 and CYP2C19 metabolism: Bayesian meta-regression of human population variability in kinetics and application in chemical risk assessment.Semantic proximity Read ↗

Gene polymorphisms and contents of cytochrome P450s have only limited effects on metabolic activities in human liver microsomes.Semantic proximity Read ↗

In Vitro Functional Characterisation of Cytochrome P450 (CYP) 2C19 Allelic Variants CYP2C19*23 and CYP2C19*24.Semantic proximity Read ↗

Cytochrome P450 2C9-CYP2C9.Semantic proximity Read ↗

Prediction of the effects of genetic polymorphism on the pharmacokinetics of CYP2C9 substrates from in vitro data.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.