Evidence map›Paper›PMID 37228182›Full record

ArticleScience (New York, N.Y.)2023

Structures of the free and capped ends of the actin filament.

Peter J Carman, Kyle R Barrie, Grzegorz Rebowski, Roberto Dominguez

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
14.2field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  12. Review
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  15. Article
  16. ATP-dependent actin barbed-end fluctuations at steady state.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Review
  18. Proteomic Analysis of Low-Temperature Stress Response in Maize (Current issues in molecular biology · 2025
    Article
  19. Nucleation limited assembly and polarized growth of abioRxiv : the preprint server for biology · 2025
    Article
  20. Microscopic and structural observations of actin filament capping and severing by cytochalasin D.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

4 authors at 1 institution in 1 country.

Peter J Carman *Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-6120-5507
Kyle R Barrie *Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0003-0860-1639
Grzegorz RebowskiDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-0766-6302
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0003-3186-5229
University of Pennsylvania · US

Funding

Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
Computational Resource for Structural Biology and Molecular BiophysicsS10OD023592 · OD · UNIVERSITY OF PENNSYLVANIA · PI SHARP, KIM A · 2017 to 2017
$402k
Unadulterated expression of tropomyosin isoforms and their interactions with F-actin, tropomodulin and leiomodinF31HL156431 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI CARMAN, PETER J · 2021 to 2021
$33k
NHLBI NIH HHS F31 HL156431NIGMS NIH HHS R01 GM073791NIH HHS S10 OD023592
6 · The paper itself

Abstract

The barbed and pointed ends of the actin filament (F-actin) are the sites of growth and shrinkage and the targets of capping proteins that block subunit exchange, including CapZ at the barbed end and tropomodulin at the pointed end. We describe cryo-electron microscopy structures of the free and capped ends of F-actin. Terminal subunits at the free barbed end adopt a "flat" F-actin conformation. CapZ binds with minor changes to the barbed end but with major changes to itself. By contrast, subunits at the free pointed end adopt a "twisted" monomeric actin (G-actin) conformation. Tropomodulin binding forces the second subunit into an F-actin conformation. The structures reveal how the ends differ from the middle in F-actin and how these differences control subunit addition, dissociation, capping, and interactions with end-binding proteins.

Indexed as

ActinsCapZ Actin Capping ProteinActin CytoskeletonCryoelectron MicroscopyProtein BindingProtein ConformationSingle Molecule ImagingTropomodulinActinsCapZ Actin Capping ProteinTropomodulin

Identifiers

PMID37228182
PMCPMC10880383
OpenAlexW4378194817

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.