Evidence map›Paper›PMID 19931282›Full record

ArticleJournal of molecular biology2010

Structure and dynamics of the actin filament.

Jim Pfaendtner, Edward Lyman, Thomas D Pollard, Gregory A Voth

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
13.0field-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

36 citing papers in PubMed, 97 citations in OpenAlex.

  1. Mechanism of phosphate release from actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Mechanism of Phosphate Release from Actin Filaments.bioRxiv : the preprint server for biology · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. KBTBD13 is an actin-binding protein that modulates muscle kinetics.The Journal of clinical investigation · 2020
    Article
  9. Article
  10. When Stiffness Matters: Mechanosensing in Heart Development and Disease.Frontiers in cell and developmental biology · 2020
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Coarse-Grained Directed Simulation.Journal of chemical theory and computation · 2017
    Article
  18. Article
  19. Article
  20. Actin Mechanics and Fragmentation.The Journal of biological chemistry · 2015
    Review
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

4 authors at 2 institutions in 1 country.

Jim PfaendtnerCenter for Biophysical Modeling and Simulation, University of Utah, Salt Lake City, UT 84112-0850, USA.
Edward Lyman
Thomas D Pollard
Gregory A Voth
University of Utah · USYale University · US

Funding

Structure and function of Arp 2/3 complex--Subproject 4P01GM066311 · NIGMS · YALE UNIVERSITY · PI LI, RONG · 2003 to 2013
$16.8M
NIGMS NIH HHS GM066311NIGMS NIH HHS P01 GM066311
6 · The paper itself

Abstract

We used all-atom molecular dynamics simulations to investigate the structure and properties of the actin filament, starting with either the recent Oda model or the older Holmes model. Simulations of monomeric and polymerized actin show that polymerization changes the nucleotide-binding cleft, bringing together the Q137 side chain and bound ATP in a way that may enhance the ATP hydrolysis rate in the filament. Simulations with different bound nucleotides and conformations of the DNase I binding loop show that the persistence length of the filament depends only on loop conformation. Computational modeling reveals how bound phalloidin stiffens actin filaments and inhibits the release of gamma-phosphate from ADP-P(i) actin.

Indexed as

Actin CytoskeletonActinsAnimalsComputer SimulationCrystallography, X-RayEukaryotic CellsHumansModels, MolecularMolecular Dynamics SimulationNucleotidesPhalloidineProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein MultimerizationStructure-Activity RelationshipActinsNucleotidesPhalloidine

Identifiers

PMID19931282
PMCPMC2815099
OpenAlexW1976295685

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.