Evidence map›Paper›PMID 26391523›Full record

ArticleThe Journal of biological chemistry2015

The Structure of a Full-length Membrane-embedded Integrin Bound to a Physiological Ligand.

Aguang Dai, Feng Ye, Dianne W Taylor, Guiqing Hu, Mark H Ginsberg, Kenneth A Taylor

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Beyond MIDAS: AnACS omega · 2026
    Article
  2. MnBiophysical journal · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  10. Roles of Membrane Domains in Integrin-Mediated Cell Adhesion.International journal of molecular sciences · 2020
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. 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

6 authors at 2 institutions in 1 country.

Aguang DaiInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4380 and.
Feng YeDepartment of Hematology and Oncology, University of California at San Diego, La Jolla, California 92093-0726.
Dianne W TaylorInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4380 and.
Guiqing HuInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4380 and.
Mark H GinsbergDepartment of Hematology and Oncology, University of California at San Diego, La Jolla, California 92093-0726.
Kenneth A TaylorInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306-4380 and. Electronic address: taylor@bio.fsu.edu.
Florida State University · USUniversity of California, San Diego · US

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
THROMBUS FORMATION IN BABOONSP01HL031950 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI GRIFFIN, JOHN H · 1985 to 2015
$29.4M
The Interaction of TPO and Integrins in Hematopoiesis CellsP01HL078784 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2005 to 2019
$28.3M
Composition and Functions of the Integrin Activation ComplexR01HL117807 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2014 to 2017
$1.5M
NHLBI NIH HHS HL 078784NHLBI NIH HHS HL 117807NHLBI NIH HHS HL 31950NHLBI NIH HHS P01 HL031950NHLBI NIH HHS P01 HL078784NHLBI NIH HHS R01 HL117807NIGMS NIH HHS GM 64346NIGMS NIH HHS U54 GM064346
6 · The paper itself

Abstract

Increased ligand binding to integrin ("activation") underpins many biological processes, such as leukocyte trafficking, cell migration, host-pathogen interaction, and hemostasis. Integrins exist in several conformations, ranging from compact and bent to extended and open. However, the exact conformation of membrane-embedded, full-length integrin bound to its physiological macromolecular ligand is still unclear. Integrin αIIbβ3, the most abundant integrin in platelets, has been a prototype for integrin activation studies. Using negative stain electron microscopy and nanodisc-embedding to provide a membrane-like environment, we visualized the conformation of full-length αIIbβ3 in both a Mn(2+)-activated, ligand-free state and a Mn(2+)-activated, fibrin-bound state. Activated but ligand-free integrins exist mainly in the compact conformation, whereas fibrin-bound αIIbβ3 predominantly exists in a fully extended, headpiece open conformation. Our results show that membrane-embedded, full-length integrin adopts an extended and open conformation when bound to its physiological macromolecular ligand.

Indexed as

Blood PlateletsFibrinHumansIn Vitro TechniquesLigandsManganeseMembrane LipidsMicroscopy, Electron, TransmissionModels, MolecularNanostructuresPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein ConformationFibrinLigandsManganeseMembrane LipidsPlatelet Glycoprotein GPIIb-IIIa Complexcell adhesionelectron microscopy (EM)fibrinnanodiscplateletsignal transductionαIIbβ3 integrin

Identifiers

PMID26391523
PMCPMC4646401
OpenAlexW2256940081

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.