Evidence map›Paper›PMID 19111664›Full record

ArticleMolecular cell2008

Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.

Jianghai Zhu, Bing-Hao Luo, Tsan Xiao, Chengzhong Zhang, Noritaka Nishida, Timothy A Springer

Abstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 274 papers.

0numbers the graph read from it
0cells of the map it votes in
274citing 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

274 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. ΔJournal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. All-atom simulations reveal distinct pathways for αCellular and molecular life sciences : CMLS · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Functional unfolding of the integrin αX transmembrane helix.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Review
  20. Article

214 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

6 authors.

Jianghai ZhuThe Immune Disease Institute and Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Bing-Hao Luo
Tsan Xiao
Chengzhong Zhang
Noritaka Nishida
Timothy A Springer

Funding

STRUCTURE OF INTEGRINS AND YWTD BETA PROPELLER DOMAINSP01HL048675 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 1992 to 2009
$20.9M
Structural Studies of Pattern Recognition ReceptorsZIAAI000960 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI XIAO, TSAN · 2009 to 2014
$6.1M
NHLBI NIH HHS HL-48675NHLBI NIH HHS P01 HL048675
6 · The paper itself

Abstract

The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand. Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding. Electrophilicity of the ligand-binding Mg ion is increased in the open conformation. The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension. Different integrin molecules in crystals and EM reveal breathing that appears on pathway to extension. Tensile force applied to the extended ligand-receptor complex stabilizes the closed, low-affinity conformation. By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation. This mechanism propagates allostery over long distances and couples cytoskeleton attachment of integrins to their high-affinity state.

Indexed as

Binding SitesBiomechanical PhenomenaCell AdhesionCell MovementCrystallography, X-RayLigandsMetalsMicroscopy, ElectronModels, MolecularPlatelet Glycoprotein GPIIb-IIIa ComplexPliabilityProtein Structure, SecondaryProtein Structure, TertiaryX-Ray DiffractionLigandsMetalsPlatelet Glycoprotein GPIIb-IIIa Complex

Identifiers

PMID19111664
PMCPMC2758073

What OpenQuestion holds

Textmetadata
LicenceTDM
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.