Evidence map›Paper›PMID 27595492›Full record

ReviewTrends in cell biology2017

The Diverse Family of Arp2/3 Complexes.

Javier Pizarro-Cerdá, Dror Shlomo Chorev, Benjamin Geiger, Pascale Cossart

Open access · greenAbstract readReview
In one paragraph

Review in Trends in cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

70 citing papers in PubMed, 129 citations in OpenAlex.

  1. Review
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  10. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
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  16. Clinical Presentations and Nosocomial Infections of Neurolisteriosis.The Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

10 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

4 authors at 3 institutions in 3 countries.

Javier Pizarro-CerdáInstitut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France; INSERM, U604, Paris F-75015, France; INRA, USC2020, Paris F-75015, France. Electronic address: javier.pizarro-cerda@pasteur.fr.
Dror Shlomo ChorevThe Weizmann Institute of Science, Department of Molecular Cell Biology, Rehovot 761001, Israel; Department of Chemistry, University of Oxford, Physical and Theoretical Chemistry Laboratory, Oxford OX1 3QZ, UK.
Benjamin GeigerThe Weizmann Institute of Science, Department of Molecular Cell Biology, Rehovot 761001, Israel.
Pascale CossartInstitut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France; INSERM, U604, Paris F-75015, France; INRA, USC2020, Paris F-75015, France. Electronic address: pascale.cossart@pasteur.fr.
Institut Pasteur · FRUniversity of Oxford · GBWeizmann Institute of Science · IL

Funding

European Research Council 670823
6 · The paper itself

Abstract

The Arp2/3 complex has so far been considered to be a single seven-subunit protein complex required for actin nucleation and actin filament polymerization in diverse critical cellular functions including phagocytosis, vesicular trafficking and lamellipodia extension. The Arp2/3 complex is also exploited by bacterial pathogens and viruses during cellular infectious processes. Recent studies suggest that some subunits of the complex are dispensable in specific cellular contexts, pointing to the existence of alternative 'hybrid Arp2/3 complexes' containing other components such as vinculin or α-actinin, as well as different isoforms or phosphorylation variants of canonical Arp2/3 subunits. Therefore, this diversity should be now considered when assigning specific Arp2/3 assemblies to different actin-dependent cellular processes.

Indexed as

Multigene FamilyActin-Related Protein 2-3 ComplexAnimalsHumansModels, BiologicalActin-Related Protein 2-3 Complexactin polymerizationArp2/3focal adhesionsListeria monocytogenesvaccinia virus

Identifiers

PMID27595492
PMCPMC7098815
OpenAlexW2513252283

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.