Evidence map›Paper›PMID 24559982›Full record

ArticleBiophysical journal2014

Mechanism of calponin stabilization of cross-linked actin networks.

Mikkel Herholdt Jensen, Eliza J Morris, Cynthia M Gallant, Kathleen G Morgan, David A Weitz, Jeffrey R Moore

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Combined control of the fibroblast contractile program by YAP and TAZ.American journal of physiology. Lung cellular and molecular physiology · 2022
    Article
  7. TwoThe Journal of biological chemistry · 2020
    Article
  8. Article
  9. Downregulation of calponin 2 contributes to the quiescence of lung macrophages.American journal of physiology. Cell physiology · 2019
    Article
  10. Review
  11. Article
  12. Article
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 2 institutions in 1 country.

Mikkel Herholdt JensenDepartment of Physiology and Biophysics, Boston University, Boston, Massachusetts; School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts.
Eliza J MorrisSchool of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts.
Cynthia M GallantDepartment of Health Sciences, Boston University, Boston, Massachusetts.
Kathleen G MorganDepartment of Health Sciences, Boston University, Boston, Massachusetts.
David A WeitzSchool of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts.
Jeffrey R MooreDepartment of Physiology and Biophysics, Boston University, Boston, Massachusetts. Electronic address: jxmoore@bu.edu.
Boston University · USHarvard University · US

Funding

Structure-Function of the CytoskeletonP01HL086655 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2007 to 2011
$8.8M
Thin Filaments and Muscle RegulationR37HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 2008 to 2017
$4.1M
NHLBI NIH HHS HL86655NHLBI NIH HHS P01 HL086655NHLBI NIH HHS R37 HL036153
6 · The paper itself

Abstract

The actin-binding protein calponin has been previously implicated in actin cytoskeletal regulation and is thought to act as an actin stabilizer, but the mechanism of its function is poorly understood. To investigate this underlying physical mechanism, we studied an in vitro model system of cross-linked actin using bulk rheology. Networks with basic calponin exhibited a delayed onset of strain stiffening (10.0% without calponin, 14.9% with calponin) and were able to withstand a higher maximal strain before failing (35% without calponin, 56% with calponin). Using fluorescence microscopy to study the mechanics of single actin filaments, we found that calponin increased the flexibility of actin filaments, evident as a decrease in persistence length from 17.6 μm without to 7.7 μm with calponin. Our data are consistent with current models of affine strain behavior in semiflexible polymer networks, and suggest that calponin stabilization of actin networks can be explained purely by changes in single-filament mechanics. We propose a model in which calponin stabilizes actin networks against shear through a reduction of persistence length of individual filaments.

Indexed as

Models, BiologicalActin CytoskeletonAnimalsCalcium-Binding ProteinsCalponinsElasticityHumansMicrofilament ProteinsProtein StabilityRabbitsCalcium-Binding ProteinsCalponinsMicrofilament Proteins

Identifiers

PMID24559982
PMCPMC3944828
OpenAlexW2153643491

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.