Evidence map›Paper›PMID 25533486›Full record

ArticleStructure (London, England : 1993)2015

Near-atomic resolution for one state of F-actin.

Vitold E Galkin, Albina Orlova, Matthijn R Vos, Gunnar F Schröder, Edward H Egelman

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 1 pooled it
11.7field-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

72 citing papers in PubMed, 1 synthesis or guideline pooled it, 144 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Myosin-5 varies its step length to carry cargo straight along the irregular F-actin track.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Myosin-5 varies its steps along the irregular F-actin track.bioRxiv : the preprint server for biology · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  18. Structural analysis of receptors and actin polarity in platelet protrusions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. Article

12 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

5 authors at 3 institutions in 2 countries.

Vitold E GalkinDepartment of Physiological Sciences, Eastern Virginia Medical School, Norfolk, VA 23507, USA. Electronic address: galkinve@evms.edu.
Albina OrlovaDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA.
Matthijn R VosFEI Company, Nanoport Europe, 5651 GG Eindhoven, the Netherlands.
Gunnar F SchröderInstitute of Complex Systems, Forschungszentrum Jülich, 52425 Jülich, Germany; Physics Department, University of Düsseldorf, 40225 Düsseldorf, Germany.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA. Electronic address: egelman@virginia.edu.
University of Virginia · USEastern Virginia Medical School · USForschungszentrum Jülich · DE

Funding

Structural Studies of ActinR01GM081303 · NIGMS · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2007 to 2016
$3.6M
NIGMS NIH HHS GM081303NIGMS NIH HHS R01 GM081303
6 · The paper itself

Abstract

Actin functions as a helical polymer, F-actin, but attempts to build an atomic model for this filament have been hampered by the fact that the filament cannot be crystallized and by structural heterogeneity. We have used a direct electron detector, cryo-electron microscopy, and the forces imposed on actin filaments in thin films to reconstruct one state of the filament at 4.7 Å resolution, which allows for building a reliable pseudo-atomic model of F-actin. We also report a different state of the filament where actin protomers adopt a conformation observed in the crystal structure of the G-actin-profilin complex with an open ATP-binding cleft. Comparison of the two structural states provides insights into ATP-hydrolysis and filament dynamics. The atomic model provides a framework for understanding why every buried residue in actin has been under intense selective pressure.

Indexed as

Actin CytoskeletonActinsAnimalsCryoelectron MicroscopyModels, MolecularNucleotidesPhosphatesProtein MultimerizationProtein Structure, QuaternaryRabbitsActinsNucleotidesPhosphates

Identifiers

PMID25533486
PMCPMC4286464
OpenAlexW2051173799

What OpenQuestion holds

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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.