Evidence map›Paper›PMID 20446344›Full record

ReviewMolecules and cells2010

Regulation of actin cytoskeleton dynamics in cells.

Sung Haeng Lee, Roberto Dominguez

Abstract readReview
In one paragraph

Review in Molecules and cells, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 185 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
185citing papers in PubMed, 1 pooled it
7.6field-weighted citation impact, top 2% 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

185 citing papers in PubMed, 1 synthesis or guideline pooled it, 367 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Lasting effects of early-life oxytocin treatment on LTP and episodic memory in a mouse model of Fragile X syndrome.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2026
    Article
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  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Baraitser-Winter Cerebrofrontofacial Syndrome Recurrent R196H Variant in Cytoplasmic β-Actin Impairs Its Cellular Polymerization and Stability.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  14. Article
  15. Article
  16. Polyploidy and Senescence of Cancer Cells: Impact of Cell Fusion.Advances in experimental medicine and biology · 2026
    Review
  17. Article
  18. Review
  19. Article
  20. Effect of Retinal on Dictyostelium Cells During Development.Genes to cells : devoted to molecular & cellular mechanisms · 2025
    Article

125 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

2 authors at 2 institutions in 2 countries.

Sung Haeng LeeChosun University School of Medicine, Department of Cellular and Molecular Medicine, Gwangju 501-759, Korea. sunglee@chosun.ac.kr
Roberto Dominguez
Chosun University · KRUniversity of Pennsylvania · US

Funding

Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
NIGMS NIH HHS GM073791NIGMS NIH HHS R01 GM073791
6 · The paper itself

Abstract

The dynamic remolding of the actin cytoskeleton is a critical part of most cellular activities, and malfunction of cytoskeletal proteins results in various human diseases. The transition between two forms of actin, monomeric or G-actin and filamentous or F-actin, is tightly regulated in time and space by a large number of signaling, scaffolding and actin-binding proteins (ABPs). New ABPs are constantly being discovered in the post-genomic era. Most of these proteins are modular, integrating actin binding, protein-protein interaction, membrane-binding, and signaling domains. In response to extracellular signals, often mediated by Rho family GTPases, ABPs control different steps of actin cytoskeleton assembly, including filament nucleation, elongation, severing, capping, and depolymerization. This review summarizes structure-function relationships among ABPs in the regulation of actin cytoskeleton assembly.

Indexed as

ActinsAmino Acid SequenceAnimalsCytoskeletonHumansMicrofilament ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, TertiaryActinsMicrofilament Proteins

Identifiers

PMID20446344
PMCPMC3910092
OpenAlexW2011544204

What OpenQuestion holds

Textmetadata
LicenceTDM
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.