Evidence map›Paper›PMID 20959098›Full record

ArticleBiophysical journal2010

Molecular dynamics simulations of Arp2/3 complex activation.

Paul Dalhaimer, Thomas D Pollard

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  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
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  10. 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
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  11. The Expression of Actin-Related Protein 2/3 Complex Subunit 5 (ARPC5) Expression in Multiple Myeloma and its Prognostic Significance.Medical science monitor : international medical journal of experimental and clinical research · 2018
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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 1 institution in 1 country.

Paul DalhaimerDepartments of Molecular Cellular and Developmental Biology, Yale University, New Haven, Connecticut, USA.
Thomas D Pollard
Yale University · US

Funding

Structure and function of Arp 2/3 complex--Subproject 4P01GM066311 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 2003 to 2013
$16.8M
MOLECULAR MECHANISMS OF CELLULAR MOTILITYR01GM026338 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2020
$9.8M
Bridge to the Baccalaureate: The Brooklyn BridgeR25GM066331 · NIGMS · KINGSBOROUGH COMMUNITY COLLEGE · PI ZEITLIN, ARTHUR · 2002 to 2004
$558k
Characterization of constitutively active Arp2/3F32GM074504 · NIGMS · YALE UNIVERSITY · PI DALHAIMER, PAUL · 2005 to 2007
$143k
NIGMS NIH HHS F32 GM074504NIGMS NIH HHS F32GM074504NIGMS NIH HHS GM-026338NIGMS NIH HHS GM-066331NIGMS NIH HHS P01 GM066311NIGMS NIH HHS R01 GM026338NIGMS NIH HHS R25 GM066331
6 · The paper itself

Abstract

Actin-related protein 2 and 3 (Arp2/3) complex forms a dendritic network of actin filaments during endocytosis and cellular locomotion by nucleating branches on the sides of preexisting actin filaments. Reconstructions of electron tomograms of branch junctions show how Arp2/3 complex anchors the branch, with Arp2 and Arp3 serving as the first two subunits of the branch. Our aim was to characterize the massive conformational change that moves Arp2 ∼30 Å from its position in crystal structures of inactive Arp2/3 complex to its position in branch junctions. Starting with the inactive crystal structure, we used atomistic-scale molecular dynamics simulations to drive Arp2 toward the position observed in branch junctions. When we applied forces to Arp2 while restraining Arp3, one block of structure (Arp2, subunit ARPC1, the globular domain of ARPC4 and ARPC5) rotated counterclockwise by 30° around a pivot point in an α-helix of ARPC4 (Glu⁸¹-Asn¹⁰⁰) to align Arp2 next to Arp3 in a second block of structure including ARPC3 and the globular domains of ARPC2. This active structure buried more surface area than the inactive conformation. The complex was stable in all simulations. In most simulations, collisions of subdomain 2 of Arp2 with Arp3 impeded the movement of Arp2.

Indexed as

Molecular Dynamics SimulationActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3MovementProtein StabilityProtein Structure, TertiaryProtein SubunitsActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3Protein Subunits

Identifiers

PMID20959098
PMCPMC2955496
OpenAlexW2020750626

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.