Evidence map›Paper›PMID 19762919›Full record

ArticleThe Journal of biological chemistry2009

Integrin activation dynamics between the RGD-binding site and the headpiece hinge.

Eileen Puklin-Faucher, Viola Vogel

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Review
  2. Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024
    Article
  3. Multiscale models of integrins and cellular adhesions.Current opinion in structural biology · 2023
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. When Stiffness Matters: Mechanosensing in Heart Development and Disease.Frontiers in cell and developmental biology · 2020
    Review
  11. Integrins as biomechanical sensors of the microenvironment.Nature reviews. Molecular cell biology · 2019
    Review
  12. The human platelet antigen-1b (ProThe Journal of biological chemistry · 2018
    Article
  13. Receptor-mediated cell mechanosensing.Molecular biology of the cell · 2017
    Review
  14. Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study.Protein science : a publication of the Protein Society · 2017
    Article
  15. Theranostics · 2017
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Mechanical regulation of T-cell functions.Immunological reviews · 2013
    Review
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.

Eileen Puklin-FaucherDepartment of Materials, Laboratory of Biologically Oriented Materials, ETH, Zurich CH-8049, Switzerland.
Viola VogelDepartment of Materials, Laboratory of Biologically Oriented Materials, ETH, Zurich CH-8049, Switzerland. Electronic address: viola.vogel@mat.ethz.ch.

Funding

Nanomedicine development center for mechanobiologyPN2EY016586 · NEI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DUSTIN, MICHAEL LORAN · 2005 to 2014
$23.0M
NEI NIH HHS PN2 EY016586
6 · The paper itself

Abstract

Integrins form mechanical links between the extracellular matrix and the cytoskeleton. Although integrin activation is known to be regulated by an allosteric conformational change, which can be induced from the extracellular or intracellular end of the molecule, little is known regarding the sequence of structural events by which signals propagate between distant sites. Here, we reveal with molecular dynamics simulations of the FnIII(10)-bound alpha(V)beta(3) integrin headpiece how the binding pocket and interdomain betaA/hybrid domain hinge on the distal end of the betaA domain are allosterically linked via a hydrophobic T-junction between the middle of the alpha1 helix and top of the alpha7 helix. The key results of this study are: 1) that this T-junction is induced by ligand binding and hinge opening, and thus displays bidirectionality; 2) that formation of this junction can be accelerated by ligand-mediated force; and 3) how formation of this junction is inhibited by Ca(2+) in place of Mg(2+) at the site adjacent to the metal ion-dependent adhesion site ("ADMIDAS"). Together with recent experimental evidence that integrin complexes can form catch bonds (i.e. become strengthened under force), as well as earlier evidence that Ca(2+) at the ADMIDAS results in lower binding affinity, these simulations provide a common structural model for the dynamic process by which integrins become activated.

Indexed as

Computer SimulationModels, MolecularAnimalsBinding SitesHumansIntegrin alphaVbeta3OligopeptidesProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, Tertiaryarginyl-glycyl-aspartic acidIntegrin alphaVbeta3Oligopeptides

Identifiers

PMID19762919
PMCPMC2794771

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.