The DOI matches its Crossref record; 119 of the 124 references it cites were found in a registry or an index.
Cytochrome P450 Enzymes and Drug Metabolism in Humans
Open accessAbstract
Human cytochrome P450 (CYP) enzymes, as membrane-bound hemoproteins, play important roles in the detoxification of drugs, cellular metabolism, and homeostasis. In humans, almost 80% of oxidative metabolism and approximately 50% of the overall elimination of common clinical drugs can be attributed to one or more of the various CYPs, from the CYP families 1–3. In addition to the basic metabolic effects for elimination, CYPs are also capable of affecting drug responses by influencing drug action, safety, bioavailability, and drug resistance through metabolism, in both metabolic organs and local sites of action. Structures of CYPs have recently provided new insights into both understanding the mechanisms of drug metabolism and exploiting CYPs as drug targets. Genetic polymorphisms and epigenetic changes in CYP genes and environmental factors may be responsible for interethnic and interindividual variations in the therapeutic efficacy of drugs. In this review, we summarize and highlight the structural knowledge about CYPs and the major CYPs in drug metabolism. Additionally, genetic and epigenetic factors, as well as several intrinsic and extrinsic factors that contribute to interindividual variation in drug response are also reviewed, to reveal the multifarious and important roles of CYP-mediated metabolism and elimination in drug therapy.
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“These enzymes are responsible for metabolizing 70% of clinically prescribed drugs22,23, establishing this timepoint as pivotal for investigating drug metabolism, interactions, and toxicity.”
From Temporal proteomic profiling of iPSC-derived human liver organoids reveals optimal maturation for drug metabolism and toxicology (2026) · cites this paper as [22]
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Predicting in vivo drug interactions from in vitro drug discovery data
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Cytochrome P450 Structure, Function and Clinical Significance: A Review
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Inhibition and Induction of Cytochrome P450 and the Clinical Implications
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Metadata
- Authors
- Zhao, M., Ma, J., Li, M., Zhang, Y., Jiang, B., Zhao, X., Huai, C., Shen, L., Zhang, N., He, L., & Qin, S.
- Affiliations
- Shanghai Jiao Tong University (CN)
- Institutes for Shanghai Pudong Decoding Life, Shanghai 200135, China
- Corresponding author
- Qin, Shengying
- ORCID
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2021-11-26
- Volume
- 22
- Issue
- 23
- Pages
- 12808
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC8657965
- OpenAlex
- W3216238012
- Cited by
- 1,070
- References
- 124
- Citations by year
- 2026: 255 · 2025: 349 · 2024: 301 · 2023: 134 · 2022: 30
- FWCI
- 20.56
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Nature Science Foundation of China (81773818, 81273596, 30900799, 81671326)
- National key research and development program (2016YFC0905000, 2016YFC0905002, 2016YFC1200200, 2016YFC0906400)
- 111 project, Shanghai Pujiang Program (17PJD020)
- Shanghai Key Laboratory of Psychotic Disorders (13dz2260500)
- Shanghai Science and Technology Innovation Fund (20DZ2202000, 21002411100)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- cytochrome P450, drug metabolism, human drug metabolism, CYP1A2, CYP2C9, CYP2C19, CYP3A4, CYP2D6, CYP2B6, CYP2A6, CYP2E1, CYP1B1, CYP1A1
- MeSH terms
- Animals, Cytochrome P-450 Enzyme System, Pharmaceutical Preparations, Humans, Metabolic Clearance Rate, Inactivation, Metabolic, Polymorphism, Genetic, Xenobiotics
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