Evidence map›Paper›PMID 12785102›Full record

ReviewJournal of muscle research and cell motility2002

Mechanical response of single filamin A (ABP-280) molecules and its role in the actin cytoskeleton.

Masahito Yamazaki, Shou Furuike, Tadanao Ito

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Mechanotransduction at the Plasma Membrane-Cytoskeleton Interface.International journal of molecular sciences · 2021
    Review
  3. Review
  4. Microtubules: Evolving roles and critical cellular interactions.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Filamins in mechanosensing and signaling.Annual review of biophysics · 2012
    Review
  13. Review
  14. Article
  15. Article
  16. Molecular origin of strain softening in cross-linked F-actin networks.Physical review. E, Statistical, nonlinear, and soft matter physics · 2010
    Article
  17. Article
  18. Measuring molecular rupture forces between single actin filaments and actin-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  19. Article
  20. Biological roles of filamin a in prostate cancer cells.International braz j urol : official journal of the Brazilian Society of Urology
    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

3 authors at 1 institution in 1 country.

Masahito YamazakiGraduate School of Science and Engineering, Department of Physics, Faculty of Science, Shizuoka University, Shizuoka 422-8529, Japan. spmyama@ipc.shizuoka.ac.jp
Shou Furuike
Tadanao Ito
Shizuoka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Filamin A produces isotropic cross-linked three-dimensional orthogonal networks with actin filaments in the cortex and at the leading edge of cells. Filamin A also links the actin cytoskeleton to the plasma membrane via its association with various kinds of membrane proteins. Recent new findings strongly support that filamin A plays important roles in the mechanical stability of plasma membrane and cortex, formation of cell shape, mechanical responses of cells, and cell locomotion. To elucidate the mechanical properties of the actin/filamin A network and the complex of membrane protein-filamin A-actin cytoskeleton, the mechanical properties of single human filamin A (hsFLNa) molecules in aqueous solution were investigated using atomic force microscopy. Ig-fold domains of filamin A can be unfolded by the critical external force (50-220 pN), and this unfolding is reversible, i.e., the refolding of the unfolded chain of the filamin A occurs when the external force is removed. Due to this reversible unfolding of Ig-fold domains, filamin A molecule can be stretched to several times the length of its native state. Based on this new feature of filamin A as the 'large-extensible linker', we describe our hypothesis for the mechanical role of filamin A in the actin cytoskeletons in cells and discuss its biological implications. In this review, function of filamin A in actin cytoskeleton, mechanical properties of single filamin A proteins, and the hypothesis for the mechanical role of filamin A in the actin cytoskeletons are discussed.

Indexed as

Computer SimulationActinsAnimalsCD18 AntigensCell MembraneContractile ProteinsCytoskeletonElasticityFilaminsHumansImmunoglobulinsMembrane ProteinsMicrofilament ProteinsMicroscopy, Atomic ForceMolecular ConformationProtein DenaturationActinsCD18 AntigensContractile ProteinsFilaminsImmunoglobulinsMembrane ProteinsMicrofilament ProteinsWater

Identifiers

PMID12785102
OpenAlexW2913157370

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.