The DOI matches its Crossref record; 51 of the 52 references it cites were found in a registry or an index.
Mammalian Microsomal Cytochrome P450 Monooxygenase
Open accessAbstract
Microsomal cytochrome P450s participate in xenobiotic detoxification, procarcinogen activation, and steroid hormone synthesis. The first structure of a mammalian microsomal P450 suggests that the association of P450s with the endoplasmic reticulum involves a hydrophobic surface of the protein formed by noncontiguous portions of the polypeptide chain. This interaction places the entrance of the putative substrate access channel in or near the membrane and orients the face of the protein proximal to the heme cofactor perpendicular to the plane of the membrane for interaction with the P450 reductase. This structure offers a template for modeling other mammalian P450s and should aid drug discovery and the prediction of drug-drug interactions.
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“There are low-circulating levels of plasma XO in baseline conditions that can increase in disease conditions by the release from damaged cells in liver or other tissues (1010).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1010]
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Mechanism of Oxidation Reactions Catalyzed by Cytochrome P450 Enzymes
Meunier, B., de Visser, S. P., & Shaik, S. S. (2004) · Chemical Reviews · doi:10.1021/cr020443g · Cited by 2,433
Structure and chemistry of cytochrome p450
Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005) · Chemical Reviews · doi:10.1021/cr0307143 · Cited by 2,106
Common and Uncommon Cytochrome P450 Reactions Related to Metabolism and Chemical Toxicity
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Cytochromes P450: a success story.
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Cytochromes P450 and metabolism of xenobiotics
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Metadata
- Authors
- Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- McRee, Duncan E.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-01
- Volume
- 5
- Issue
- 1
- Pages
- 121-131
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2051639214
- Cited by
- 696
- References
- 52
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 10 · 2023: 5 · 2022: 8 · 2021: 7 · 2020: 19 · 2019: 15 · 2018: 18 · 2017: 18 · 2016: 21 · 2015: 13 · 2014: 18 · 2013: 20 · 2012: 11
- FWCI
- 53.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p01gm048495-08)
- National Institute of General Medical Sciences (R01GM031001, GM-31001, GM-48495)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- cytochrome P450, endoplasmic reticulum, protein structure, NADPH-cytochrome P450 reductase, xenobiotic detoxification, procarcinogen activation, steroidogenesis, drug-drug interactions, drug discovery
- MeSH terms
- Cytochrome P450 Family 2, Amino Acid Sequence, Animals, Binding Sites, Cytochrome P-450 Enzyme System, Endoplasmic Reticulum, Heme, Mammals, Microsomes, Models, Molecular, Molecular Sequence Data, Steroid 21-Hydroxylase, Protein Structure, Secondary, Crystallography, X-Ray
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