Evidence map›Paper›PMID 15557320›Full record

ArticleThe Journal of biological chemistry2005

Evidence that monoclonal antibodies directed against the integrin beta subunit plexin/semaphorin/integrin domain stimulate function by inducing receptor extension.

A Paul Mould, Mark A Travis, Stephanie J Barton, Jennifer A Hamilton, Janet A Askari, Susan E Craig, Philip R Macdonald, Richard A Kammerer, Patrick A Buckley, Martin J Humphries

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Visualization of integrin molecules by fluorescence imaging and techniques.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2021
    Article
  6. Low-affinity binding inMolecular biology of the cell · 2017
    Article
  7. Article
  8. Relating conformation to function in integrin α5β1.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Activation states of blood eosinophils in asthma.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2014
    Review
  10. Anti-IL-5 attenuates activation and surface density of β(2) -integrins on circulating eosinophils after segmental antigen challenge.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2013
    Article
  11. Article
  12. Review
  13. Platelet activation, P-selectin, and eosinophil β1-integrin activation in asthma.American journal of respiratory and critical care medicine · 2012
    Article
  14. Overview: assays for studying integrin-dependent cell adhesion.Methods in molecular biology (Clifton, N.J.) · 2012
    Review
  15. Activation of beta1 integrins on blood eosinophils by P-selectin.American journal of respiratory cell and molecular biology · 2011
    Article
  16. Article
  17. Article
  18. Focal adhesions are sites of integrin extension.The Journal of cell biology · 2010
    Article
  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

10 authors at 2 institutions in 1 country.

A Paul MouldWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom. paul.mould@manchester.ac.uk
Mark A Travis
Stephanie J Barton
Jennifer A Hamilton
Janet A Askari
Susan E Craig
Philip R Macdonald
Richard A Kammerer
Patrick A Buckley
Martin J Humphries
University of Manchester · GBWellcome Centre for Cell-Matrix Research · GB

Funding

Wellcome Trust 074941
6 · The paper itself

Abstract

The overall structure of integrins is that of a ligand-binding head connected to two long legs. The legs can exhibit a pronounced bend at the "knees," and it has been proposed that the legs undergo a dramatic straightening when integrins transit from a low affinity to a high affinity state. The knee region contains domains from both alpha and beta subunits, including the N-terminal plexin/semaphorin/integrin (PSI) domain of the beta subunit. The role played by the knee domains in the regulation of integrin-ligand binding is uncertain. Here we show that: (i) monoclonal antibodies (mAbs) N29 and 8E3 have epitopes in the beta(1) subunit PSI domain and stimulate ligand binding to alpha(5)beta(1); (ii) N29 and 8E3 cause long range conformational changes that alter the ligand binding activity of the head region; (iii) the stimulatory action of these mAbs is dependent on the calf-1 domain, which forms part of the alpha subunit knee; and (iv) the epitopes of 8E3 and N29 map close to the extreme N terminus of the PSI and are likely to lie on the side of this domain that faces the alpha subunit. Taken together, our data suggest that the binding of these mAbs results in a levering apart of the PSI and calf-1 domains, and thereby causes the alpha and beta subunit knees to separate. Several major inferences can be drawn from our findings. First, the PSI domain appears to form part of an interface with the alpha subunit that normally restrains the integrin in a bent state. Second, the PSI domain is important for the transduction of conformational changes from the knee to head. Third, unbending is likely to provide a general mechanism for control of integrin-ligand recognition.

Indexed as

AnimalsAntibodies, MonoclonalCell Adhesion MoleculesCHO CellsCricetinaeEnzyme-Linked Immunosorbent AssayEpitope MappingEpitopesGenetic VectorsHumansIntegrin alpha5beta1Integrin beta ChainsIntegrinsLigandsMutagenesis, Site-DirectedNerve Tissue ProteinsAntibodies, MonoclonalCell Adhesion MoleculesEpitopesIntegrin alpha5beta1Integrin beta ChainsIntegrinsLigandsNerve Tissue ProteinsplexinRecombinant ProteinsSemaphorins

Identifiers

PMID15557320
PMCPMC3328395
OpenAlexW2089701375

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.