Evidence map›Paper›PMID 29463680›Full record

ArticleThe Journal of biological chemistry2018

The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments.

Andrew Huehn, Wenxiang Cao, W Austin Elam, Xueqi Liu, Enrique M De La Cruz, Charles V Sindelar

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  12. Article
  13. Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Molecular and structural basis of actin filament severing by ADF/cofilin.Computational and structural biotechnology journal · 2022
    Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Andrew HuehnFrom the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520.
Wenxiang CaoFrom the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520.
W Austin ElamFrom the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520.
Xueqi LiuFrom the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520.
Enrique M De La CruzFrom the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520 enrique.delacruz@yale.edu.
Charles V SindelarFrom the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520 charles.sindelar@yale.edu.
Yale University · US

Funding

PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
Actin filament elasticity and actin-binding protein functionR01GM097348 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2011 to 2018
$3.1M
Structural basis of motility by dimeric kinesin motor proteinsR01GM110530 · NIGMS · YALE UNIVERSITY · PI SINDELAR, CHARLES VAUGHN · 2014 to 2023
$3.0M
NIGMS NIH HHS R01 GM097348NIGMS NIH HHS R01 GM110530NIGMS NIH HHS T32 GM008283
6 · The paper itself

Abstract

Cofilin/ADF proteins are actin-remodeling proteins, essential for actin disassembly in various cellular processes, including cell division, intracellular transport, and motility. Cofilins bind actin filaments cooperatively and sever them preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments. The cooperative binding to actin has been proposed to originate from conformational changes that propagate allosterically from clusters of bound cofilin to bare actin segments. Estimates of the lengths over which these cooperative conformational changes propagate vary dramatically, ranging from 2 to >100 subunits. Here, we present a general, structure-based method for detecting from cryo-EM micrographs small variations in filament geometry (

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsAnimalsCryoelectron MicroscopyProtein Structure, QuaternaryRabbitsActin Depolymerizing Factorsactincofilincooperativitycryo-electron microscopycytoskeletonsingle particle analysis

Identifiers

PMID29463680
PMCPMC5900768
OpenAlexW2788377804

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.