Evidence map›Paper›PMID 11546839›Full record

ArticleScience (New York, N.Y.)2001

Crystal structure of the extracellular segment of integrin alpha Vbeta3.

J P Xiong, T Stehle, B Diefenbach, R Zhang, R Dunker, D L Scott, A Joachimiak, S L Goodman, M A Arnaout

Open access · bronzeAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 451 papers.

0numbers the graph read from it
0cells of the map it votes in
451citing papers in PubMed
31.1field-weighted citation impact, top 1% 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

451 citing papers in PubMed, 1,266 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  6. Article
  7. Review
  8. Review
  9. Article
  10. MnBiophysical journal · 2025
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Conformational response of αStructure (London, England : 1993) · 2025
    Article
  17. Review
  18. Article
  19. Review
  20. Article

391 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

J P XiongRenal Unit, Leukocyte Biology & Inflammation Program, Structural Biology Program, Massachusetts General Hospital and Harvard Medical School, 149 13th Street, Charlestown, MA 02129, USA.
T Stehle
B Diefenbach
R Zhang
R Dunker
D L Scott
A Joachimiak
S L Goodman
M A Arnaout
Argonne National Laboratory · USMassachusetts General Hospital · US

Funding

THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
Structure and Function of beta2 IntegrinR01DK048549 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI ARNAOUT, M. AMIN · 1994 to 2016
$6.0M
Transcriptional regulation of beta2 integrinsP01DK050305 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI ARNAOUT, M. AMIN · 1995 to 2004
$5.8M
MEASLES VIRUS AND ITS CELLULAR RECEPTOR CD46R01AI045716 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI STEHLE, THILO · 1999 to 2003
$976k
B2 INTEGRINS IN ISCHEMIA-REPERFUSION INJURYR01HL054227 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI ARNAOUT, M. AMIN · 1996 to 1999
–
NHLBI NIH HHS HL54227NIAID NIH HHS AI45716NIDDK NIH HHS DK48549NIDDK NIH HHS DK50305NIGMS NIH HHS P50 GM062414
6 · The paper itself

Abstract

Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands. We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution. Its 12 domains assemble into an ovoid "head" and two "tails." In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation. The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins. A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding SitesCalciumCrystallizationCrystallography, X-RayDimerizationHumansLigandsMetalsModels, MolecularMolecular Sequence DataMutationProtein ConformationProtein FoldingProtein Structure, QuaternaryCalciumLigandsMetalsProtein SubunitsReceptors, Vitronectin

Identifiers

PMID11546839
PMCPMC2885948
OpenAlexW1938388466

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.