Evidence map›Paper›PMID 17142266›Full record

ArticleBiophysical journal2007

A structure-based sliding-rebinding mechanism for catch bonds.

Jizhong Lou, Cheng Zhu

Abstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

67 citing papers in PubMed.

  1. Trial
  2. Article
  3. Engineering tunable catch bonds with DNA.Nature communications · 2024
    Article
  4. A physiologic roll for cell surface GlycoRNAs.Journal of leukocyte biology · 2024
    Article
  5. Review
  6. Article
  7. Topology of molecular deformations induces triphasic catch bonding in selectin-ligand bonds.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Receptor-Ligand Binding: Effect of Mechanical Factors.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Single-molecule studies of classical and desmosomal cadherin adhesion.Current opinion in biomedical engineering · 2019
    Article
  20. Article

7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Jizhong LouInstitute for Bioengineering and Bioscience, Coulter Department of Biomedical Engineering, and Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia, USA.
Cheng Zhu

Funding

Visualizing Single Integrin Conformational Changes on Living CellsR01AI044902 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 2000 to 2016
$5.8M
KINETIC PROPERTIES OF SELECTINSR21AI044902 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 2000 to 2000
$71k
NIAID NIH HHS AI44902NIAID NIH HHS R01 AI044902NIAID NIH HHS R21 AI044902
6 · The paper itself

Abstract

Catch bonds, whose lifetimes are prolonged by force, have been observed in selectin-ligand interactions and other systems. Several biophysical models have been proposed to explain this counterintuitive phenomenon, but none was based on the structure of the interacting molecules and the noncovalent interactions at the binding interface. Here we used molecular dynamics simulations to study changes in structure and atomic-level interactions during forced unbinding of P-selectin from P-selectin glycoprotein ligand-1. A mechanistic model for catch bonds was developed based on these observations. In the model, "catch" results from forced opening of an interdomain hinge that tilts the binding interface to allow two sides of the contact to slide against each other. Sliding promotes formation of new interactions and even rebinding to the original state, thereby slowing dissociation and prolonging bond lifetimes. Properties of this sliding-rebinding mechanism were explored using a pseudoatom representation and Monte Carlo simulations. The model has been supported by its ability to fit experimental data and can be related to previously proposed two-pathway models.

Indexed as

Models, BiologicalModels, MolecularComputer SimulationEpidermal Growth FactorLectinsMembrane GlycoproteinsMonte Carlo MethodProtein BindingProtein Structure, TertiaryP-SelectinEpidermal Growth FactorLectinsMembrane GlycoproteinsP-SelectinP-selectin ligand protein

Identifiers

PMID17142266
PMCPMC1796828

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.