Evidence map›Paper›PMID 12604783›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand.

Bing-Hao Luo, Timothy A Springer, Junichi Takagi

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.8field-weighted citation impact, top 2% 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

67 citing papers in PubMed, 148 citations in OpenAlex.

  1. Review
  2. Glycosylation in Cancer.Handbook of experimental pharmacology · 2025
    Review
  3. Article
  4. Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024
    Article
  5. Local pH mapping in the cell adhesion nano-interfaces on a pH-responsive fluorescence-dye-immobilized substrate.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2023
    Article
  6. Review
  7. Review
  8. Article
  9. Site-specificiScience · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Autonomous conformational regulation of βProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. The importance of N-glycosylation on βScientific reports · 2017
    Article
  17. Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study.Protein science : a publication of the Protein Society · 2017
    Article
  18. Article
  19. Article
  20. Article

7 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

3 authors at 2 institutions in 1 country.

Bing-Hao LuoCenter for Blood Research and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
Timothy A Springer
Junichi Takagi
Harvard University · USDana-Farber/Boston Children's Cancer and Blood Disorders Center · US

Funding

STRUCTURE OF INTEGRINS AND YWTD BETA PROPELLER DOMAINSP01HL048675 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 1992 to 2009
$20.9M
NHLBI NIH HHS HL-48675NHLBI NIH HHS P01 HL048675
6 · The paper itself

Abstract

The affinity of the extracellular domain of integrins for ligand is regulated by conformational changes signaled from the cytoplasm. Alternative types of conformational movement in the ligand-binding headpiece have been proposed. In one study, electron micrograph image averages of the headpiece of integrin aV beta 3 show two different conformations. The open conformation of the headpiece is present when a ligand mimetic peptide is bound and differs from the closed conformation in the presence of an obtuse angle between the beta 3 subunit hybrid and I-like domains. We tested the hypothesis that opening of the hybrid-I-like domain interface increases ligand-binding affinity by mutationally introducing an N-glycosylation site into it. Both beta 3 and beta1 integrin glycan wedge mutants exhibit constitutively high affinity for physiological ligands. The data uniquely support one model of integrin activation and suggest that movement at the interface with the hybrid domain pulls down the C-terminal helix of the I-like domain and activates its metal ion-dependent adhesion site, analogously to activation of the integrin I domain.

Indexed as

AnimalsCell LineCHO CellsCricetinaeDNA, ComplementaryDose-Response Relationship, DrugFlow CytometryGenetic LinkageGlycosylationHumansIntegrin alphaVbeta3IntegrinsLigandsModels, MolecularMutationPhenotypeDNA, ComplementaryIntegrin alphaVbeta3IntegrinsLigandsPolysaccharides

Identifiers

PMID12604783
PMCPMC151353
OpenAlexW2102376680

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.