ArticleProceedings of the National Academy of Sciences of the United States of America2024
Topology of molecular deformations induces triphasic catch bonding in selectin-ligand bonds.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 12 citations in OpenAlex.
- Models of Cellular Mechanosensation.Results and problems in cell differentiation · 2026Review
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Integrin force loading rate in mechanobiology: From model to molecular measurement.QRB discovery · 2025Review
- Should Artificial Intelligence Play a Durable Role in Biomedical Research and Practice?International journal of molecular sciences · 2024Review
- Engineering tunable catch bonds with DNA.Nature communications · 2024Article
- Theory and Examples of Catch Bonds.The journal of physical chemistry. B · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Among the long-standing efforts to elucidate the physical mechanisms of protein-ligand catch bonding, particular attention has been directed at the family of selectin proteins. Selectins exhibit slip, catch-slip, and slip-catch-slip bonding, with minor structural modifications causing major changes in selectins' response to force. How can a single structural mechanism allow interconversion between these various behaviors? We present a unifying theory of selectin-ligand catch bonding, using a structurally motivated free energy landscape to show how the topology of force-induced deformations of the molecular system produces the full range of observed behaviors. We find that the pathway of bond rupture deforms in non-trivial ways, such that unbinding dynamics depend sensitively on force. This implies a severe breakdown of Bell's theory-a paradigmatic theory used widely in catch bond modeling-raising questions about the suitability of Bell's theory in modeling other catch bonds. Our approach can be applied broadly to other protein-ligand systems.
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