Evidence map›Paper›PMID 3536951›Full record

ArticleThe Journal of cell biology1986

Identification of a new protein localized at sites of cell-substrate adhesion.

M C Beckerle

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.1field-weighted citation impact, top 10% 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

49 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
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  7. TRIP6 functions in brain ciliogenesis.Nature communications · 2021
    Article
  8. Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis.Frontiers in cell and developmental biology · 2021
    Article
  9. Zyxin Mediates Vascular RepairFrontiers in physiology · 2021
    Article
  10. Zyxin (ZYX) promotes invasion and acts as a biomarker for aggressive phenotypes of human glioblastoma multiforme.Laboratory investigation; a journal of technical methods and pathology · 2020
    Article
  11. Article
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  17. The effect of oxide thickness on osteoblast attachment and survival on NiTi alloy.Journal of materials science. Materials in medicine · 2007
    Article
  18. Molecular characterization of the Caenorhabditis elegans ALP/Enigma gene alp-1.Developmental dynamics : an official publication of the American Association of Anatomists · 2006
    Article
  19. Article
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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

1 author.

M C Beckerle

Funding

STRUCTURE/FUNCTION OF FOCAL ADHESIONSR01GM029860 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BURRIDGE, KEITH · 1985 to 2018
$6.7M
THE ROLE OF ACTIN BINDING PROTEINS IN SECRETIONF32GM009516 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI BECKERLE, MARY C. · 1985 to 1986
–
NIGMS NIH HHS GM-09516NIGMS NIH HHS GM-29860
6 · The paper itself

Abstract

A new protein found at sites of cell-substrate adhesion has been identified by analysis of a nonimmune rabbit serum. By indirect immunofluorescence this serum stains focal contacts (adhesion plaques) and the associated termini of actin filament bundles in cultured chicken cells. Western immunoblot analysis of total chick embryo fibroblast protein demonstrated an 82-kD polypeptide to be the major protein recognized by the unfractionated serum. This 82-kD protein is immunologically distinct from other known adhesion plaque proteins such as vinculin, talin, alpha-actinin, and fimbrin. Antibody affinity-purified against the electrophoretically isolated, nitrocellulose-bound 82-kD protein retained the ability to stain the area of the adhesion plaque, which confirms that the 82-kD protein is indeed a constituent of the focal contact. The 82-kD polypeptide has a basic isoelectric point relative to actin and fibronectin, and it appears to be very low in abundance. The 82-kD protein is ubiquitous in chicken embryo tissues. However, it appears to be more abundant in fibroblasts and smooth muscle than in brain or liver. Intermediate levels of the protein were detected in skeletal and cardiac muscle. The subcellular distribution of the 82-kD protein raises the possibility that this polypeptide is involved in linking actin filaments to the plasma membrane at sites of substrate attachment or regulating these dynamic interactions.

Indexed as

Cell AdhesionActinsAnimalsCell MembraneCells, CulturedChick EmbryoFluorescent Antibody TechniqueMembrane ProteinsMolecular WeightTissue DistributionActinsMembrane Proteins

Identifiers

PMID3536951
PMCPMC2114371
OpenAlexW2171723086

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.