Evidence map›Paper›PMID 22404683›Full record

ReviewAnnual review of biophysics2012

Filamins in mechanosensing and signaling.

Ziba Razinia, Toni Mäkelä, Jari Ylänne, David A Calderwood

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed
8.3field-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

151 citing papers in PubMed, 255 citations in OpenAlex.

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91 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

4 authors at 3 institutions in 3 countries.

Ziba RaziniaDepartment of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Toni Mäkelä
Jari Ylänne
David A Calderwood
University of Jyväskylä · FIInstitute of Cell Biology · UAYale University · US

Funding

Integrin-Filamin Interactions in Migration and SignalingR01GM068600 · NIGMS · YALE UNIVERSITY · PI CALDERWOOD, DAVID A · 2003 to 2016
$4.4M
NIGMS NIH HHS R01 GM-068600NIGMS NIH HHS R01 GM068600
6 · The paper itself

Abstract

Filamins are essential, evolutionarily conserved, modular, multidomain, actin-binding proteins that organize the actin cytoskeleton and maintain extracellular matrix connections by anchoring actin filaments to transmembrane receptors. By cross-linking and anchoring actin filaments, filamins stabilize the plasma membrane, provide cellular cortical rigidity, and contribute to the mechanical stability of the plasma membrane and the cell cortex. In addition to binding actin, filamins interact with more than 90 other binding partners including intracellular signaling molecules, receptors, ion channels, transcription factors, and cytoskeletal and adhesion proteins. Thus, filamins scaffold a wide range of signaling pathways and are implicated in the regulation of a diverse array of cellular functions including motility, maintenance of cell shape, and differentiation. Here, we review emerging structural and functional evidence that filamins are mechanosensors and/or mechanotransducers playing essential roles in helping cells detect and respond to physical forces in their local environment.

Indexed as

Cell MovementMechanotransduction, CellularSignal TransductionAnimalsCell MembraneCell ShapeContractile ProteinsCytoskeletonFilaminsHumansMicrofilament ProteinsProtein BindingProtein Structure, TertiaryContractile ProteinsFilaminsMicrofilament Proteins

Identifiers

PMID22404683
PMCPMC5508560
OpenAlexW2124053776

What OpenQuestion holds

Textmetadata
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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.