Evidence map›Paper›PMID 34014527›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2021

Mechanoregulation of PDZ Proteins, An Emerging Function.

Elsa Bazellières, André Le Bivic

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Review
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

2 authors at 2 institutions in 1 country.

Elsa BazellièresAix Marseille Université, CNRS, IBDM-UMR7288, Turing Centre for Living Systems, Marseille, France. elsa.BAZELLIERES@univ-amu.fr.
André Le BivicAix Marseille Université, CNRS, IBDM-UMR7288, Turing Centre for Living Systems, Marseille, France.
Aix-Marseille Université · FRInstitut de Biologie du Développement Marseille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mechanical forces have emerged as essential regulators of cell organization, proliferation, migration, and polarity to regulate cellular and tissue homeostasis. Changes in forces or loss of the cellular response to them can result in abnormal embryonic development and diseases. Over the past two decades, many efforts have been put in deciphering the molecular mechanisms that convert forces into biochemical signals, allowing for the identification of many mechanotransducer proteins. Here we discuss how PDZ proteins are emerging as new mechanotransducer proteins by altering their conformations or localizations upon force loads, leading to the formation of macromolecular modules tethering the cell membrane to the actin cytoskeleton.

Indexed as

Mechanotransduction, CellularPDZ DomainsActin CytoskeletonAnimalsCell MembraneHumansMultiprotein ComplexesProteinsMultiprotein ComplexesProteinsActomyosinAdherens junctionsForcesPDZ proteinsTight junctions

Identifiers

PMID34014527
OpenAlexW3163205659

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.