Evidence map›Paper›PMID 9533689›Full record

ArticleBiophysical journal1998

Determination of the gelsolin binding site on F-actin: implications for severing and capping.

A McGough, W Chiu, M Way

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Mechanism of actin filament severing and capping by gelsolin.Nature structural & molecular biology · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Antioxidant and Wound Healing Property of Gelsolin in 3T3-L1 Cells.Oxidative medicine and cellular longevity · 2020
    Article
  7. The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics.International journal of molecular sciences · 2018
    Article
  8. My various thoughts on actin.Biophysics and physicobiology · 2018
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. The 3D structure of villin as an unusual F-Actin crosslinker.Structure (London, England : 1993) · 2008
    Article
  17. Actin filament severing by cofilin.Journal of molecular biology · 2007
    Article
  18. Article
  19. Article
  20. Transcriptional profiles associated with aging and middle age-onset caloric restriction in mouse hearts.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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

3 authors at 2 institutions in 2 countries.

A McGoughVerna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA. amcgough@bcm.tmc.edu
W Chiu
M Way
Baylor College of Medicine · USEuropean Molecular Biology Laboratory · DE

Funding

STRUCTURAL STUDIES OF CELLULAR ASSEMBLIES OF ACTINR01GM026357 · NIGMS · BRANDEIS UNIVERSITY · PI DEROSIER, DAVID J · 1985 to 2002
$791k
STRUCTURAL ANALYSIS OF DYSTROPHINF32AR008207 · NIAMS · BRANDEIS UNIVERSITY · PI MCGOUGH, AMY M · 1991 to 1994
–
NCRR NIH HHS RR02250NIAMS NIH HHS AR08207-03NIGMS NIH HHS GM26357
6 · The paper itself

Abstract

Gelsolin is a six-domain protein that regulates actin assembly by severing, capping, and nucleating filaments. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on F-actin. To obtain fully decorated filaments under severing conditions, we have studied a derivative (G2-6) that has a reduced severing efficiency compared to gelsolin. A three-dimensional reconstruction of G2-6:F-actin was obtained by electron cryomicroscopy and helical reconstruction. The structure shows that gelsolin bridges two longitudinally associated monomers when it binds the filament. The F-actin binding region of G2-6 is centered axially at subdomain 3 and radially between subdomains 1 and 3 of the upper actin monomer. Our results suggest that for severing to occur, both gelsolin and actin undergo large conformational changes.

Indexed as

Protein Structure, SecondaryActinsBinding SitesCloning, MolecularEscherichia coliFreezingGelsolinImage Processing, Computer-AssistedMicrofilament ProteinsMicroscopy, ElectronModels, MolecularRecombinant ProteinsActinsGelsolinMicrofilament ProteinsRecombinant Proteins

Identifiers

PMID9533689
PMCPMC1302557
OpenAlexW2091090390

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.