Evidence map›Paper›PMID 24136164›Full record

ArticleBlood2013

Three-dimensional reconstruction of intact human integrin αIIbβ3: new implications for activation-dependent ligand binding.

Won-Seok Choi, William J Rice, David L Stokes, Barry S Coller

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Family-wide analysis of integrin structures predicted by AlphaFold2.bioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Review
  9. Family-wide analysis of integrin structures predicted by AlphaFold2.Computational and structural biotechnology journal · 2023
    Article
  10. Structural analysis of receptors and actin polarity in platelet protrusions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Cryo-Electron Microscopy Structure of the αIIbβ3-Abciximab Complex.Arteriosclerosis, thrombosis, and vascular biology · 2020
    Article
  13. Article
  14. Autonomous conformational regulation of βProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Force regulated conformational change of integrin αMatrix biology : journal of the International Society for Matrix Biology · 2017
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Won-Seok ChoiLaboratory of Blood and Vascular Biology, Rockefeller University, New York, NY;
William J Rice
David L Stokes
Barry S Coller
New York Structural Biology Center · USOsong Medical Innovation Foundation · KRRockefeller University · US

Funding

Platelet Integrin AlphaIIbBeta3 Structure, Activation, and Ligand Binding: Fibrinogen, Fibrin, D-dimer, and von Willebrand FactorR01HL019278 · NHLBI · STATE UNIVERSITY NEW YORK STONY BROOK · PI Claudia Lorena Buitrago, Barry Coller · 1985 to 2026
$17.6M
RES FACIL CONSTRUCTION: HALLUCINOGENSC06RR017528 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI COWBURN, DAVID · 2002 to 2002
$2.0M
BIOCHEMISTRY/PHYSIOLOGY OF PLATELET MEMBRANE RECEPTORSR37HL019278 · NHLBI · STATE UNIVERSITY NEW YORK STONY BROOK · PI COLLER, BARRY · 1989 to 1998
–
NCRR NIH HHS C06 RR017528NCRR NIH HHS C06RR017528-01NHLBI NIH HHS HL19278NHLBI NIH HHS R01 HL019278PHS HHS ULRR024143
6 · The paper itself

Abstract

Integrin αIIbβ3 plays a central role in hemostasis and thrombosis. We provide the first 3-dimensional reconstruction of intact purified αIIbβ3 in a nanodisc lipid bilayer. Unlike previous models, it shows that the ligand-binding head domain is on top, pointing away from the membrane. Moreover, unlike the crystal structure of the recombinant ectodomain, the lower legs are not parallel, straight, and adjacent. Rather, the αIIb lower leg is bent between the calf-1 and calf-2 domains and the β3 Integrin-Epidermal Growth Factor (I-EGF) 2 to 4 domains are freely coiled rather than in a cleft between the β3 headpiece and the αIIb lower leg. Our data indicate an important role for the region that links the distal calf-2 and β-tail domains to their respective transmembrane (TM) domains in transmitting the conformational changes in the TM domains associated with inside-out activation.

Indexed as

Imaging, Three-DimensionalModels, ChemicalCrystallography, X-RayHumansLigandsLipid BilayersMicroscopy, ElectronNanostructuresPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein Structure, TertiaryStructure-Activity RelationshipLigandsLipid BilayersPlatelet Glycoprotein GPIIb-IIIa Complex

Identifiers

PMID24136164
PMCPMC3868924
OpenAlexW2031577325

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.