Evidence map›Paper›PMID 18805923›Full record

ArticleBiophysical journal2008

Molecular dynamics simulation and coarse-grained analysis of the Arp2/3 complex.

Jim Pfaendtner, Gregory A Voth

Abstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. 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
  2. Review
  3. Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Actin filament remodeling by actin depolymerization factor/cofilin.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  9. Structure and dynamics of the actin filament.Journal of molecular biology · 2010
    Article
  10. Article
  11. Nucleotide-dependent conformational states of actin.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  12. 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

2 authors.

Jim PfaendtnerDepartment of Chemistry, Center for Biophysical Modeling and Simulation, University of Utah, Salt Lake City, Utah 84112-0850, USA.
Gregory A Voth

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A molecular dynamics investigation and coarse-grained analysis of inactivated actin-related protein (Arp) 2/3 complex is presented. It was found that the nucleotide binding site within Arp3 remained in a closed position with bound ATP or ADP, but opened when simulation with no nucleotide was performed. In contrast, simulation of the isolated Arp3 subunit with bound ATP, showed a fast opening of the nucleotide binding cleft. A homology model for the missing subdomains 1 and 2 of Arp2 was constructed, and it was also found that the Arp2 binding cleft remained closed with bound nucleotide. Within the nucleotide binding cleft a distinct opening and closing period of 10 ns was observed in many of the simulations of Arp2/3 as well as isolated Arp3. Substitution studies were employed, and several alanine substitutions were found to induce a partial opening of the ATP binding cleft in Arp3 and Arp2, whereas only a single substitution was found to induce opening of the ADP binding cleft. It was also found that the nucleotide type did not cause a substantial change on interfacial contacts between Arp3 and the ArpC2, ArpC3 and ArpC4 subunits. Nucleotide-free Arp3 had generally less stable contacts, but the overall contact architecture was constant. Finally, nucleotide-dependent coarse-grained models for Arp3 are developed that serve to further highlight the structural differences induced in Arp3 by nucleotide hydrolysis.

Indexed as

Models, MolecularActin-Related Protein 2-3 ComplexAdenosine DiphosphateAdenosine TriphosphateMutationProtein ConformationProtein Structure, TertiarySequence Homology, Amino AcidTime FactorsActin-Related Protein 2-3 ComplexAdenosine DiphosphateAdenosine Triphosphate

Identifiers

PMID18805923
PMCPMC2586551

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.