ReviewDrug metabolism and disposition: the biological fate of chemicals2016
Cytochrome P450 Organization and Function Are Modulated by Endoplasmic Reticulum Phospholipid Heterogeneity.
Review in Drug metabolism and disposition: the biological fate of chemicals, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
37 citing papers in PubMed, 64 citations in OpenAlex.
- Lipid Dependence of CYP3A4 Activity in Nanodiscs.Biology · 2026Article
- Enhancing cross-organelle coordination to advance plant cytochrome P450 functionality in yeast.Science advances · 2025Article
- InteracTor: Feature engineering and explainable AI for profiling protein structure-interaction-function relationships.PLoS computational biology · 2025Article
- Redox partner exchanges between spatially confined complexes control the coupling effect of cytochrome bScientific reports · 2025Article
- Coenzyme QMolecules (Basel, Switzerland) · 2025Article
- Biotechnological production of terpenoids using cell factories.Frontiers in pharmacology · 2025Review
- Uptake and Metabolic Conversion of Exogenous Phosphatidylcholines Depending on Their Acyl Chain Structure inInternational journal of molecular sciences · 2023Article
- Combinatorial optimization and spatial remodeling of CYPs to control product profile.Metabolic engineering · 2023Article
- The Dynamic Role of Endoplasmic Reticulum Stress in Chronic Liver Disease.The American journal of pathology · 2023Review
- A Comprehensive Genome-Wide Investigation of the Cytochrome 71 (Plants (Basel, Switzerland) · 2023Article
- Zonal expression of StARD1 and oxidative stress in alcoholic-related liver disease.Journal of lipid research · 2023Article
- Genome-based identification of the CYP75 gene family in Orchidaceae and its expression patterns inFrontiers in plant science · 2023Article
- The Combination of Electrochemistry and Microfluidic Technology in Drug Metabolism Studies.ChemistryOpen · 2022Review
- Engineering Saccharomyces cerevisiae for the production of dihydroquercetin from naringenin.Microbial cell factories · 2022Article
- Non-Ionic Inulin-Based Polymer Nanodiscs Enable Functional Reconstitution of a Redox Complex Composed of Oppositely Charged CYP450 and CPR in a Lipid Bilayer Membrane.Analytical chemistry · 2022Article
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
- Electron transfer between cytochrome c and microsomal monooxygenase generates reactive oxygen species that accelerates apoptosis.Redox biology · 2022Article
- Proteomic and Bioinformatics Analysis of Membrane Lipid Domains after Brij 98 Solubilization of Uninduced and Phenobarbital-Induced Rat Liver Microsomes: Defining the Membrane Localization of the P450 Enzyme System.Drug metabolism and disposition: the biological fate of chemicals · 2022Article
- Single-Cell Ribonucleic Acid Sequencing Clarifies Cold Tolerance Mechanisms in the Pacific White Shrimp (Frontiers in genetics · 2021Article
- Effects of Real-Ambient PMFrontiers in pharmacology · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome P450s (P450s) comprise a superfamily of proteins that catalyze numerous monooxygenase reactions in animals, plants, and bacteria. In eukaryotic organisms, these proteins not only carry out reactions necessary for the metabolism of endogenous compounds, but they are also important in the oxidation of exogenous drugs and other foreign compounds. Eukaryotic P450 system proteins generally reside in membranes, primarily the endoplasmic reticulum or the mitochondrial membrane. These membranes provide a scaffold for the P450 system proteins that facilitate interactions with their redox partners as well as other P450s. This review focuses on the ability of specific lipid components to influence P450 activities, as well as the role of the membrane in P450 function. These studies have shown that P450s and NADPH-cytochrome P450 reductase appear to selectively associate with specific phospholipids and that these lipid-protein interactions influence P450 activities. Finally, because of the heterogeneous nature of the endoplasmic reticulum as well as other biologic membranes, the phospholipids are not arranged randomly but associate to generate lipid microdomains. Together, these characteristics can affect P450 function by 1) altering the conformation of the proteins, 2) influencing the P450 interactions with their redox partners, and 3) affecting the localization of the proteins into specific membrane microdomains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.