Probe Substrate Dependencies in CYP3A4 Allosteric Inhibition: A Novel Molecular Mechanism Involving F–F′ Loop Perturbations
Author:
Affiliation:
1. Bioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, 138671 Singapore
2. Department of Pharmacy, Faculty of Science, National University of Singapore, 18 Science Drive 4, 117543 Singapore
Funder
Ministry of Education - Singapore
National Research Foundation Singapore
Singapore Institute of Food and Biotechnology Innovation
Biomedical Research Council
National University of Singapore
Publisher
American Chemical Society (ACS)
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.3c01837
Reference30 articles.
1. Common and Uncommon Cytochrome P450 Reactions Related to Metabolism and Chemical Toxicity
2. Cytochrome P450 enzymes in drug metabolism: Regulation of gene expression, enzyme activities, and impact of genetic variation
3. Substrate Dependent Inhibition Profiles of Fourteen Drugs on CYP3A4 Activity Measured by A High Throughput LCMS/MS Method with Four Probe Drugs, Midazolam, Testosterone, Nifedipine and Terfenadine
4. IN VITRO METABOLISM OF MIDAZOLAM, TRIAZOLAM, NIFEDIPINE, AND TESTOSTERONE BY HUMAN LIVER MICROSOMES AND RECOMBINANT CYTOCHROMES P450: ROLE OF CYP3A4 AND CYP3A5
5. PBPK modeling and simulation in drug research and development
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