Evidence map›Paper›PMID 8761450›Full record

ArticleThe Biochemical journal1996

Focal adhesion kinase (pp125FAK) cleavage and regulation by calpain.

P Cooray, Y Yuan, S M Schoenwaelder, C A Mitchell, H H Salem, S P Jackson

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

47 citing papers in PubMed, 163 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

P CoorayDepartment of Medicine, Monash Medical School, Victoria, Australia.
Y Yuan
S M Schoenwaelder
C A Mitchell
H H Salem
S P Jackson
Box Hill Hospital · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Focal adhesion kinase (125 kDa form; pp125FAK) is a widely expressed non-receptor tyrosine kinase that is implicated in integrin-mediated signal transduction. We have identified a novel means of pp 125FAK regulation in human platelets, in which this kinase undergoes sequential proteolytic modification from the native 125 kDa form to 90, 45 and 40 kDa fragments in thrombin-, collagen- and ionophore A23187-stimulated platelets. The proteolysis of pp125FAK was prevented by pretreating platelets with the calpain inhibitors calpeptin or calpain inhibitor-1, and was reproduced in vitro by incubating immunoprecipitated pp125FAK with purified calpain. Proteolysis of pp125FAK resulted in a dramatic reduction in its autokinase activity and led to its dissociation from the cytoskeletal fraction of platelets. These studies define a novel signal-terminating role for calpain, wherein proteolytic modification of pp125FAK attenuates its autokinase activity and induces its subcellular relocation within the cell.

Indexed as

Blood PlateletsCalcimycinCalpainCell Adhesion MoleculesCysteine Proteinase InhibitorsCytoskeletonDipeptidesFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGlycoproteinsHumansImmunoblottingIonophoresMolecular WeightPeptide FragmentsPhosphorylationCalcimycinCalpaincalpain inhibitorscalpeptinCell Adhesion MoleculesCysteine Proteinase InhibitorsDipeptidesFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGlycoproteinsIonophoresPeptide FragmentsPhosphotyrosineProtein-Tyrosine KinasesPTK2 protein, humanThrombin

Identifiers

PMID8761450
PMCPMC1217586
OpenAlexW2162164344

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.