Evidence map›Paper›PMID 14657234›Full record

ArticleThe Journal of cell biology2003

ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments.

Vitold E Galkin, Albina Orlova, Margaret S VanLoock, Alexander Shvetsov, Emil Reisler, Edward H Egelman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  3. Oncology letters · 2017
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Single-molecule imaging and kinetic analysis of cooperative cofilin-actin filament interactions.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Remodeling of actin filaments by ADF/cofilin proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  18. The interaction of cofilin with the actin filament.Journal of molecular biology · 2011
    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 2 institutions in 1 country.

Vitold E GalkinDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Jordan Hall, Charlottesville, VA 22908-0733, USA.
Albina Orlova
Margaret S VanLoock
Alexander Shvetsov
Emil Reisler
Edward H Egelman
University of Virginia · USUniversity of California, Los Angeles · US

Funding

Methods for the Analysis of Helical Macromolecular ComplexesR01EB001567 · NIBIB · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI EGELMAN, EDWARD H. · 2003 to 2014
$3.6M
DYNAMIC EVENTS IN MYOSIN DURING CONTRACTION OF MUSCLER01AR022031 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 1986 to 2004
$2.5M
NIAMS NIH HHS AR22031NIAMS NIH HHS AR424023NIAMS NIH HHS R01 AR022031NIBIB NIH HHS EB001567NIBIB NIH HHS R01 EB001567
6 · The paper itself

Abstract

Proteins in the ADF/cofilin (AC) family are essential for rapid rearrangements of cellular actin structures. They have been shown to be active in both the severing and depolymerization of actin filaments in vitro, but the detailed mechanism of action is not known. Under in vitro conditions, subunits in the actin filament can treadmill; with the hydrolysis of ATP driving the addition of subunits at one end of the filament and loss of subunits from the opposite end. We have used electron microscopy and image analysis to show that AC molecules effectively disrupt one of the longitudinal contacts between protomers within one helical strand of F-actin. We show that in the absence of any AC proteins, this same longitudinal contact between actin protomers is disrupted at the depolymerizing (pointed) end of actin filaments but is prominent at the polymerizing (barbed) end. We suggest that AC proteins use an intrinsic mechanism of F-actin's internal instability to depolymerize/sever actin filaments in the cell.

Indexed as

Protein Structure, QuaternaryActin Depolymerizing FactorsActinsAnimalsDestrinDisulfidesFungal ProteinsMacromolecular SubstancesMicrofilament ProteinsModels, MolecularMuscle, SkeletalRabbitsActin Depolymerizing FactorsActinsDestrinDisulfidesFungal ProteinsMacromolecular SubstancesMicrofilament Proteins

Identifiers

PMID14657234
PMCPMC2173606
OpenAlexW2125927252

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.