Evidence map›Paper›PMID 19124767›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Force amplification response of actin filaments under confined compression.

George W Greene, Travers H Anderson, Hongbo Zeng, Bruno Zappone, Jacob N Israelachvili

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. An Integrated Cytoskeletal Model of Neurite Outgrowth.Frontiers in cellular neuroscience · 2018
    Review
  6. Article
  7. Near-atomic resolution for one state of F-actin.Structure (London, England : 1993) · 2015
    Article
  8. Power transduction of actin filaments ratcheting in vitro against a load.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. A mechanical-biochemical feedback loop regulates remodeling in the actin cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Article
  11. Mathematical modeling of eukaryotic cell migration: insights beyond experiments.Annual review of cell and developmental biology · 2013
    Review
  12. Measuring forces at the leading edge: a force assay for cell motility.Integrative biology : quantitative biosciences from nano to macro · 2013
    Article
  13. Article
  14. Actin filaments as tension sensors.Current biology : CB · 2012
    Review
  15. Article
  16. 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

5 authors at 2 institutions in 2 countries.

George W GreeneMaterials Department and Department of Chemical Engineering, University of California, Santa Barbara, CA 93106, USA.
Travers H Anderson
Hongbo Zeng
Bruno Zappone
Jacob N Israelachvili
University of California, Santa Barbara · USUniversity of Calabria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin protein is a major component of the cell cytoskeleton, and its ability to respond to external forces and generate propulsive forces through the polymerization of filaments is central to many cellular processes. The mechanisms governing actin's abilities are still not fully understood because of the difficulty in observing these processes at a molecular level. Here, we describe a technique for studying actin-surface interactions by using a surface forces apparatus that is able to directly visualize and quantify the collective forces generated when layers of noninterconnected, end-tethered actin filaments are confined between 2 (mica) surfaces. We also identify a force-response mechanism in which filaments not only stiffen under compression, which increases the bending modulus, but more importantly generates opposing forces that are larger than the compressive force. This elastic stiffening mechanism appears to require the presence of confining surfaces, enabling actin filaments to both sense and respond to compressive forces without additional mediating proteins, providing insight into the potential role compressive forces play in many actin and other motor protein-based phenomena.

Indexed as

Biomechanical PhenomenaActin CytoskeletonAdsorptionAluminum SilicatesCompressive StrengthElasticityAluminum Silicatesmica

Identifiers

PMID19124767
PMCPMC2626722
OpenAlexW2135418046

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.