ReviewBiophysical journal2010
Relationships between structural dynamics and functional kinetics in oligomeric membrane receptors.
Review in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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.
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Who cites it
11 citing papers in PubMed.
- Addressing the Binding Mechanism of the Meprin and TRAF-C Homology Domain of the Speckle-Type POZ Protein Using Protein Engineering.International journal of molecular sciences · 2023Article
- An intramolecular energetic network regulates ligand recognition in a SH2 domain.Protein science : a publication of the Protein Society · 2023Article
- Illumination of a progressive allosteric mechanism mediating the glycine receptor activation.Nature communications · 2023Article
- AlphaFold accurately predicts distinct conformations based on the oligomeric state of a de novo designed protein.Protein science : a publication of the Protein Society · 2022Article
- Modeling ion channels: past, present, and future.The Journal of general physiology · 2014Review
- Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Perspectives on: conformational coupling in ion channels: allosteric coupling in ligand-gated ion channels.The Journal of general physiology · 2012Article
- The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Medicinal chemistry for 2020.Future medicinal chemistry · 2011Article
- From the stochasticity of molecular processes to the variability of synaptic transmission.Nature reviews. Neuroscience · 2011Review
- Conformational selection or induced fit? 50 years of debate resolved.F1000 biology reports · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Recent efforts to broaden understanding of the molecular mechanisms of membrane receptors in signal transduction make use of rate-equilibrium free-energy relationships (REFERs), previously applied to chemical reactions, enzyme kinetics, and protein folding. For oligomeric membrane receptors, we distinguish between a), the Leffler parameter alpha(L), to characterize the global transition state for the interconversion between conformations; and b), the Fersht parameter, varphi(F), to assign the degree of progression of individual residue positions at the transition state. For both alpha(L) and varphi(F), insights are achieved by using harmonic energy profiles to reflect the dynamic nature of proteins, as illustrated with single-channel results reported for normal and mutant nicotinic receptors. We also describe new applications of alpha(L) based on published results. For large-conductance calcium-activated potassium channels, data are satisfactorily fit with an alpha(L) value of 0.65, in accord with REFERs. In contrast, results reported for the flip conformational state of glycine and nicotinic receptors are in disaccord with REFERs, since they yield alpha(L) values outside the usual limits of 0-1. Concerning published varphi(F) values underlying the conformational wave hypothesis for nicotinic receptors, we note that interpretations may be complicated by variations in the width of harmonic energy profiles.
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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.