Evidence map›Paper›PMID 22321312›Full record

ReviewCurrent biology : CB2012

Actin filaments as tension sensors.

Vitold E Galkin, Albina Orlova, Edward H Egelman

Abstract readReview
In one paragraph

Review in Current biology : CB, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
–field-weighted citation impact
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

91 citing papers in PubMed.

  1. Trial
  2. Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Myosin-5 varies its step length to carry cargo straight along the irregular F-actin track.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Myosin-5 varies its steps along the irregular F-actin track.bioRxiv : the preprint server for biology · 2023
    Article
  15. Article
  16. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article

31 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.

Vitold E GalkinDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA.
Albina Orlova
Edward H Egelman

Funding

Structural Studies of ActinR01GM081303 · NIGMS · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2007 to 2016
$3.6M
NIGMS NIH HHS R01 GM081303
6 · The paper itself

Abstract

The field of mechanobiology has witnessed an explosive growth over the past several years as interest has greatly increased in understanding how mechanical forces are transduced by cells and how cells migrate, adhere and generate traction. Actin, a highly abundant and anomalously conserved protein, plays a large role in forming the dynamic cytoskeleton that is so essential for cell form, motility and mechanosensitivity. While the actin filament (F-actin) has been viewed as dynamic in terms of polymerization and depolymerization, new results suggest that F-actin itself may function as a highly dynamic tension sensor. This property may help explain the unusual conservation of actin's sequence, as well as shed further light on actin's essential role in structures from sarcomeres to stress fibers.

Indexed as

Actin CytoskeletonActinsMechanotransduction, CellularModels, MolecularProtein Structure, TertiaryActins

Identifiers

PMID22321312
PMCPMC3277726

What OpenQuestion holds

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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.