ReviewArchives of biochemistry and biophysics2012
A novel type of allosteric regulation: functional cooperativity in monomeric proteins.
Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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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.
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Who cites it
38 citing papers in PubMed, 64 citations in OpenAlex.
- Lipid Dependence of CYP3A4 Activity in Nanodiscs.Biology · 2026Article
- Binding equations for the lipid composition dependence of peripheral membrane-binding proteins.Biophysical journal · 2024Article
- Equilibrium landscape of ingress/egress channels and gating residues of the Cytochrome P450 3A4.PloS one · 2024Article
- Article
- Structural characterization of the homotropic cooperative binding of azamulin to human cytochrome P450 3A5.The Journal of biological chemistry · 2022Article
- The role of protein acetylation in carcinogenesis and targeted drug discovery.Frontiers in endocrinology · 2022Review
- How Tim proteins differentially exploit membrane features to attain robust target sensitivity.Biophysical journal · 2021Article
- Monolignol acyltransferase for lignin p-hydroxybenzoylation in Populus.Nature plants · 2021Article
- Structural Dynamics of Cytochrome P450 3A4 in the Presence of Substrates and Cytochrome P450 Reductase.Biochemistry · 2021Article
- Homotropic Cooperativity of Midazolam Metabolism by Cytochrome P450 3A4: Insight from Computational Studies.Journal of chemical information and modeling · 2021Article
- Dynamics underlying hydroxylation selectivity of cytochrome P450cam.Biophysical journal · 2021Article
- Effects of alcohol-induced increase in CYP2E1 content in human liver microsomes on the activity and cooperativity of CYP3A4.Archives of biochemistry and biophysics · 2021Article
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Numerical Methods for Modeling Enzyme Kinetics.Methods in molecular biology (Clifton, N.J.) · 2021Article
- G-Protein coupled receptors: structure and function in drug discovery.RSC advances · 2020Review
- Metabolic Reprogramming and Signaling to Chromatin Modifications in Tumorigenesis.Advances in experimental medicine and biology · 2020Review
- Functional impact of cytochrome P450 3A (CYP3A) missense variants in cattle.Scientific reports · 2019Article
- Impact of Lipid Partitioning on the Design, Analysis, and Interpretation of Microsomal Time-Dependent Inactivation.Drug metabolism and disposition: the biological fate of chemicals · 2019Article
- T cell stemness and dysfunction in tumors are triggered by a common mechanism.Science (New York, N.Y.) · 2019Article
- Nanoscale Ion Emitters in Native Mass Spectrometry for Measuring Ligand-Protein Binding Affinities.ACS central science · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cooperative functional properties and allosteric regulation in cytochromes P450 play an important role in xenobiotic metabolism and define one of the main mechanisms of drug-drug interactions. Recent experimental results suggest that ability to bind simultaneously two or more small organic molecules can be the essential feature of cytochrome P450 fold, and often results in rich and complex pattern of allosteric behavior. Manifestations of non-Michaelis kinetics include homotropic and heterotropic activation and inhibition effects depending on the stoichiometric ratios of substrate and effector, changes in the regio- and stereospecificity of catalytic transformations, and often give rise to the clinically important drug-drug interactions. In addition, functional response of P450 systems is modulated by the presence of specific and non-specific effector molecules, metal ions, membrane incorporation, formation of homo- and hetero-oligomers, and interactions with the protein redox partners. In this article we briefly overview the main factors contributing to the allosteric effects in cytochromes P450 with the main focus on the sources of cooperative behavior in xenobiotic metabolizing monomeric heme enzymes with their conformational flexibility and extremely broad substrate specificity. The novel mechanism of functional cooperativity in P450 enzymes does not require substantial binding cooperativity, rather it implies the presence of one or more binding sites with higher affinity than the single catalytically active site in the vicinity of the heme iron.
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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.