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Assessment of drug-drug interactions caused by metabolism-dependent cytochrome P450 inhibition
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“P450 (CYP) enzymes are the major enzymatic system responsible for elimination of many pharmaceutical agents (Lee et al., 2012).”
From Piperine Is a Mechanism-Based Inactivator of CYP3A (2020) · cites this paper as Lee et al., 2012
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Research works printed but not linked: 26
- VandenBrink, 2010, The role of metabolites in predicting drug–drug interactions: focus on irreversible cytochrome P450 inhibition, Curr. Opin. Drug Discov. Dev., 13, 66
- Parkinson, 2011, An evaluation of the dilution method for identifying metabolism-dependent inhibitors of cytochrome P450 enzymes, Drug Metab. Dispos., 39, 1370, 10.1124/dmd.111.038596 · DOI · Paper page
- Lee, 2011, Assessment of reactive metabolites in drug-induced liver injury, Arch. Pharm. Res., 34, 1879, 10.1007/s12272-011-1108-x · DOI
- Obach, 2007, Mechanism based inactivation of human cytochrome P450 enzymes and the prediction of drug–drug interactions, Drug Metab. Dispos., 35, 246, 10.1124/dmd.106.012633 · DOI
- Venkatakrishnan, 2007, Mechanism-based inactivation of human cytochrome P450 enzymes: strategies for diagnosis and drug–drug interaction risk assessment, Xenobiotica, 37, 1225, 10.1080/00498250701670945 · DOI
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- Lin, 1998, Inhibition and induction of cytochrome P450 and the clinical implications, Clin. Pharmacokinet., 35, 361, 10.2165/00003088-199835050-00003 · DOI · Paper page
- Polasek, 2007, In vitro approaches to investigate mechanism-based inactivation of CYP enzymes, Expert Opin. Drug Metab. Toxicol., 3, 321, 10.1517/17425255.3.3.321 · DOI
- Fowler, 2008, In vitro evaluation of reversible and irreversible cytochrome P450 inhibition: current status on methodologies and their utility for predicting drug–drug interactions, AAPS J., 10, 410, 10.1208/s12248-008-9042-7 · DOI
- Krippendorff, 2009, Mechanism-based inhibition: deriving KI and kinact directly from time-dependent IC50 values, J. Biomol. Screen., 14, 913, 10.1177/1087057109336751 · DOI
- Perloff, 2009, Validation of cytochrome P450 time-dependent inhibition assays: a two-time point IC50 shift approach facilitates kinact assay design, Xenobiotica, 39, 99, 10.1080/00498250802638155 · DOI
- Atkinson, 2005, Automated assessment of time-dependent inhibition of human cytochrome P450 enzymes using liquid chromatography–tandem mass spectrometry analysis, Drug Metab. Dispos., 33, 1637, 10.1124/dmd.105.005579 · DOI
- Lim, 2005, Automated screening with confirmation of mechanism-based inactivation of CYP3A4, CYP2C9, CYP2C19, CYP2D6, and CYP1A2 in pooled human liver microsomes, Drug Metab. Dispos., 33, 1211, 10.1124/dmd.104.003475 · DOI
- K.S. Lee, S.K. Kim, Direct and metabolism-dependent cytochrome P450 inhibition assays for evaluating drug–drug interactions, J. Appl. Toxicol., in press.
- Stresser, 2009, Differential time- and NADPH-dependent inhibition of CYP2C19 by enantiomers of fluoxetine, Drug Metab. Dispos., 37, 695, 10.1124/dmd.108.025726 · DOI
- Ring, 2001, Identification of the human cytochromes P450 responsible for the in vitro formation of R- and S-norfluoxetine, J. Pharmacol. Exp. Ther., 297, 1044, 10.1016/S0022-3565(24)29631-2 · DOI
- Foti, 2008, CYP2C19 inhibition: the impact of substrate probe selection on in vitro inhibition profiles, Drug Metab. Dispos., 36, 523, 10.1124/dmd.107.019265 · DOI
- Berry, 2008, An examination of IC50 and IC50-shift experiments in assessing time-dependent inhibition of CYP3A4, CYP2D6 and CYP2C9 in human liver microsomes, Drug Metab. Lett., 2, 51, 10.2174/187231208783478407 · DOI
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Cited by
Piperine Is a Mechanism-Based Inactivator of CYP3A
Cui, T., Wang, Q., Tian, X., Zhang, K., Peng, Y., & Zheng, J. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.119.088955 · Cited by 37
Quasi-Irreversible Inhibition of CYP2D6 by Berberine
Kim, H. G., Lee, H. S., Jeon, J. S., Choi, Y. J., Choi, Y. J., Yoo, S.-Y., Kim, E.-Y., Lee, K., Park, I., Na, M., et al. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12100916 · Cited by 21
Self-citation
Metadata
- Authors
- Lee, J.-Y., Lee, S. Y., Oh, S. J., Lee, K. H., Jung, Y. S., & Kim, S. K.
- Venue
- Chemico-Biological Interactions
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 198
- Issue
- 1-3
- Pages
- 49-56
- ISSN
- 0009-2797
- Cited by
- 38
- References
- 0
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.