Evidence map›Paper›PMID 20368459›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Actin filament remodeling by actin depolymerization factor/cofilin.

Jim Pfaendtner, Enrique M De La Cruz, Gregory A Voth

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

67 citing papers in PubMed, 111 citations in OpenAlex.

  1. mLife · 2025
    Article
  2. Article
  3. Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Discovery of Two Novel Immunoepitopes and Development of a Peptide-based Sarcoidosis Immunoassay.American journal of respiratory and critical care medicine · 2024
    Article
  5. Article
  6. Mechanism of phosphate release from actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Mechanism of Phosphate Release from Actin Filaments.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
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  12. Review
  13. Article
  14. Structure and activity of a thermally stable mutant of Acanthamoeba actophorin.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
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  16. Article
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  18. Article
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  20. Article

7 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 at 3 institutions in 1 country.

Jim PfaendtnerDepartment of Chemical Engineering, University of Washington, Box 351750, Seattle, WA 98195-1750, USA.
Enrique M De La Cruz
Gregory A Voth
University of Chicago · USUniversity of Utah · USWhitney Museum of American Art · US

Funding

Functional diversity of myosin VIIR01GM071688 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2007 to 2010
$1.2M
NIGMS NIH HHS GM071688NIGMS NIH HHS R01 GM071688
6 · The paper itself

Abstract

We investigate, using molecular dynamics, how the severing protein, actin depolymerization factor (ADF)/cofilin, modulates the structure, conformational dynamics, and mechanical properties of actin filaments. The actin and cofilactin filament bending stiffness and corresponding persistence lengths obtained from all-atom simulations are comparable to values obtained from analysis of thermal fluctuations in filament shape. Filament flexibility is strongly affected by the nucleotide-linked conformation of the actin subdomain 2 DNase-I binding loop and the filament radial mass density distribution. ADF/cofilin binding between subdomains 1 and 3 of a filament subunit triggers reorganization of subdomain 2 of the neighboring subunit such that the DNase-I binding loop (DB-loop) moves radially away from the filament. Repositioning of the neighboring subunit DB-loop significantly weakens subunit interactions along the long-pitch helix and lowers the filament bending rigidity. Lateral filament contacts between the hydrophobic loop and neighboring short-pitch helix monomers in native filaments are also compromised with cofilin binding. These works provide a molecular interpretation of biochemical solution studies documenting the disruption of filament subunit interactions and also reveal the molecular basis of actin filament allostery and its linkage to ADF/cofilin binding.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsActinsAnimalsBiochemistryBiopolymersCattleCofilin 1Computer SimulationCytoskeletonDeoxyribonuclease IHot TemperatureModels, MolecularModels, StatisticalMolecular ConformationProtein BindingActin Depolymerizing FactorsActinsBiopolymersCofilin 1Deoxyribonuclease I

Identifiers

PMID20368459
PMCPMC2867716
OpenAlexW2134099534

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.