ArticleBiophysical journal2011
The two-pathway model of the biological catch-bond as a limit of the allosteric model.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Trial
- Theory and Examples of Catch Bonds.The journal of physical chemistry. B · 2024Article
- Mechanical forces amplify TCR mechanotransduction in T cell activation and function.Applied physics reviews · 2024Review
- Cardiac desmosomal adhesion relies on ideal-, slip- and catch bonds.Scientific reports · 2024Article
- Molecular mechanisms of catch bonds and their implications for platelet hemostasis.Biophysical reviews · 2023Review
- High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion.Communications biology · 2023Article
- Assessing models of force-dependent unbinding rates via infrequent metadynamics.The Journal of chemical physics · 2022Article
- Molecular Paradigms for Biological Mechanosensing.The journal of physical chemistry. B · 2021Article
- Molecular design of the γδT cell receptor ectodomain encodes biologically fit ligand recognition in the absence of mechanosensing.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Targeting Neutrophil Adhesive Events to Address Vaso-Occlusive Crisis in Sickle Cell Patients.Frontiers in immunology · 2021Review
- The bioenergetics of integrin-based adhesion, from single molecule dynamics to stability of macromolecular complexes.Computational and structural biotechnology journal · 2020Review
- Dynamics of Mechanosensitive Nascent Adhesion Formation.Biophysical journal · 2019Article
- Exploring the Sulfatase 1 Catch Bond Free Energy Landscape using Jarzynski's Equality.Scientific reports · 2018Article
- Catch bond interaction between cell-surface sulfatase Sulf1 and glycosaminoglycans.Biophysical journal · 2015Article
- Asymmetric effect of mechanical stress on the forward and reverse reaction catalyzed by an enzyme.PloS one · 2014Article
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Authors and funding
3 authors.
Funding
Abstract
Catch-binding is a counterintuitive phenomenon in which the lifetime of a receptor/ligand bond increases when a force is applied to break the bond. Several mechanisms have been proposed to rationalize catch-binding. In the two-pathway model, the force drives the system away from its native dissociation pathway into an alternative pathway involving a higher energy barrier. Here, we analyze an allosteric model suggesting that a force applied to the complex alters the distribution of receptor conformations, and as a result, induces changes in the ligand-binding site. The model assumes explicitly that the allosteric transitions govern the properties of the ligand site. We demonstrate that the dynamics of the ligand is described by two relaxation times, one of which arises from the allosteric site. Therefore, we argue that one can characterize the allosteric transitions by studying the receptor/ligand binding. We show that the allosteric description reduces to the two-pathway model in the limit when the allosteric transitions are faster than the bond dissociation. The formal results are illustrated with two systems, P-selectin/PSGL-1 and FimH/mannose, subjected to both constant and time-dependent forces. The report advances our understanding of catch-binding by combining alternative physical models into a unified description and makes the problem more tractable for the bond mechanics community.
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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.