Evidence map›Paper›PMID 8970156›Full record

ArticleMolecular biology of the cell1996

Trans-dominant inhibition of integrin function.

F Díaz-González, J Forsyth, B Steiner, M H Ginsberg

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 173 citations in OpenAlex.

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  15. Molecular architecture and function of matrix adhesions.Cold Spring Harbor perspectives in biology · 2011
    Review
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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

4 authors at 1 institution in 1 country.

F Díaz-GonzálezDepartment of Vascular Biology, Scripps Research Institute, La Jolla, California 92037, USA.
J Forsyth
B Steiner
M H Ginsberg
Scripps Research Institute · US

Funding

REGULATION OF SECOND MESSENGERS BY BETA3 INTEGRINS IN THE VASCULAR SYSTEMP01HL048728 · NHLBI · SCRIPPS RESEARCH INSTITUTE · PI GINSBERG, MARK HOWARD · 1992 to 2003
$7.4M
Regulation of Integrin Alpha4 BetalR01AR027214 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 1986 to 2010
$3.5M
PLATELETS IN RHEUMATIC DISEASER37AR027214 · NIAMS · SCRIPPS RESEARCH INSTITUTE · PI GINSBERG, MARK HOWARD · 1991 to 2000
$279k
NHLBI NIH HHS HL-48728NIAMS NIH HHS AR-27214
6 · The paper itself

Abstract

Occupancy of integrin adhesion receptors can alter the functions of other integrins and cause partition of the ligand-occupied integrin into focal adhesions. Ligand binding also changes the conformation of integrin extracellular domains. To explore the relationship between ligand-induced conformational change and integrin signaling, we examined the effect of ligands specific for integrin alpha IIb beta 3 on the functions of target integrins alpha 5 beta 1 and alpha 2 beta 1. We report that binding of integrin-specific ligands to a suppressive integrin can inhibit the function of other target integrins (trans-dominant inhibition). Trans-dominant inhibition is due to a blockade of integrin signaling. Furthermore, this inhibition involves both a conformational change in the extracellular domain and the presence of the beta cytoplasmic tail in the suppressive integrin. Similarly, ligand-induced recruitment of alpha IIb beta 3 to focal adhesions also involves a conformational rearrangement of its extracellular domain. These findings imply that the ligand-induced conformational changes can propagate from an integrin's extracellular to its intracellular face. Trans-dominant inhibition by integrin ligands may coordinate integrin signaling and can lead to unexpected biological effects of integrin-specific inhibitors.

Indexed as

AnimalsApoptosisCHO CellsCricetinaeCytoplasmHumansIntegrinsLigandsPlatelet Glycoprotein GPIIb-IIIa ComplexProtein ConformationRabbitsReceptors, CollagenReceptors, FibronectinSignal TransductionIntegrinsLigandsPlatelet Glycoprotein GPIIb-IIIa ComplexReceptors, CollagenReceptors, Fibronectin

Identifiers

PMID8970156
PMCPMC276041
OpenAlexW2142929443

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.