Evidence map›Paper›PMID 27872252›Full record

ReviewThe Journal of cell biology2016

Integrin-mediated mechanotransduction.

Zhiqi Sun, Shengzhen S Guo, Reinhard Fässler

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 605 papers.

0numbers the graph read from it
0cells of the map it votes in
605citing papers in PubMed
44.0field-weighted citation impact, top 1% 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

605 citing papers in PubMed, 1,003 citations in OpenAlex.

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545 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 1 institution in 1 country.

Zhiqi SunMax Planck Institute of Biochemistry, 82152 Martinsried, Germany zsun@biochem.mpg.de.ORCID http://orcid.org/0000-0002-2792-2158
Shengzhen S GuoMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Reinhard FässlerMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Max Planck Institute of Biochemistry · DE

Funding

European Research Council 322652
6 · The paper itself

Abstract

Cells can detect and react to the biophysical properties of the extracellular environment through integrin-based adhesion sites and adapt to the extracellular milieu in a process called mechanotransduction. At these adhesion sites, integrins connect the extracellular matrix (ECM) with the F-actin cytoskeleton and transduce mechanical forces generated by the actin retrograde flow and myosin II to the ECM through mechanosensitive focal adhesion proteins that are collectively termed the "molecular clutch." The transmission of forces across integrin-based adhesions establishes a mechanical reciprocity between the viscoelasticity of the ECM and the cellular tension. During mechanotransduction, force allosterically alters the functions of mechanosensitive proteins within adhesions to elicit biochemical signals that regulate both rapid responses in cellular mechanics and long-term changes in gene expression. Integrin-mediated mechanotransduction plays important roles in development and tissue homeostasis, and its dysregulation is often associated with diseases.

Indexed as

Mechanotransduction, CellularAnimalsBiomechanical PhenomenaCell AdhesionHumansIntegrinsNeoplasmsTalinIntegrinsTalin

Identifiers

PMID27872252
PMCPMC5119943
OpenAlexW2549070824

What OpenQuestion holds

Textmetadata
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.