Evidence map›Paper›PMID 15556978›Full record

ArticleBiophysical journal2005

Force history dependence of receptor-ligand dissociation.

Bryan T Marshall, Krishna K Sarangapani, Jizhong Lou, Rodger P McEver, Cheng Zhu

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.8field-weighted citation impact, top 2% of its field
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

52 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. Review
  3. Receptor-Ligand Binding: Effect of Mechanical Factors.International journal of molecular sciences · 2023
    Review
  4. Review
  5. Review
  6. Article
  7. Dynamic bonds and their roles in mechanosensing.Current opinion in chemical biology · 2019
    Review
  8. Single-molecule investigations of T-cell activation.Current opinion in biomedical engineering · 2019
    Article
  9. Article
  10. Article
  11. Stiff substrates enhance monocytic cell capture through E-selectin but not P-selectin.Integrative biology : quantitative biosciences from nano to macro · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Stochastic simulation of single-molecule pulling experiments.The European physical journal. E, Soft matter · 2014
    Article
  17. Review
  18. Article
  19. Rupture of multiple catch-slip bonds: Two-state two-pathway catch-slip bonds.The European physical journal. E, Soft matter · 2013
    Article
  20. Article
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

5 authors at 2 institutions in 1 country.

Bryan T MarshallWoodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Krishna K Sarangapani
Jizhong Lou
Rodger P McEver
Cheng Zhu
Georgia Institute of Technology · USOklahoma Medical Research Foundation · US

Funding

Visualizing Single Integrin Conformational Changes on Living CellsR01AI044902 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 2000 to 2016
$5.8M
MOLECULAR BASIS OF SELECTIN INTERACTIONS WITH LEUKOCYTESR01HL065631 · NHLBI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI MCEVER, RODGER PAUL · 2000 to 2004
$3.0M
KINETIC PROPERTIES OF SELECTINSR21AI044902 · NIAID · GEORGIA INSTITUTE OF TECHNOLOGY · PI ZHU, CHENG · 2000 to 2000
$71k
NHLBI NIH HHS HL65631NHLBI NIH HHS R01 HL065631NIAID NIH HHS AI44902NIAID NIH HHS R01 AI044902NIAID NIH HHS R21 AI044902
6 · The paper itself

Abstract

Receptor-ligand bonds that mediate cell adhesion are often subjected to forces that regulate their dissociation via modulating off-rates. Off-rates control how long receptor-ligand bonds last and how much force they withstand. One should therefore be able to determine off-rates from either bond lifetime or unbinding force measurements. However, substantial discrepancies exist between the force dependence of off-rates derived from the two types of measurements even for the same interactions, e.g., selectins dissociating from their ligands, which mediate the tethering and rolling of leukocytes on vascular surfaces during inflammation and immune surveillance. We used atomic force microscopy to measure survival times of P-selectin dissociating from P-selectin glycoprotein ligand 1 or from an antibody in both bond lifetime and unbinding force experiments. By a new method of data analysis, we showed that the discrepancies resulted from the assumption that off-rates were functions of force only. The off-rates derived from forced dissociation data depended not only on force but also on the history of force application. This finding provides a new paradigm for understanding how force regulates receptor-ligand interactions.

Indexed as

Models, ChemicalAlgorithmsComputer SimulationElasticityImage Interpretation, Computer-AssistedKineticsMembrane GlycoproteinsMicromanipulationMultiprotein ComplexesProtein BindingP-SelectinStress, MechanicalMembrane GlycoproteinsMultiprotein ComplexesP-SelectinP-selectin ligand protein

Identifiers

PMID15556978
PMCPMC1305147
OpenAlexW2077081627

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.