Evidence map›Paper›PMID 1331120›Full record

ArticleThe Journal of cell biology1992

Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping.

M Way, B Pope, A G Weeds

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

51 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Mechanism of actin filament severing and capping by gelsolin.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Article
  7. Novel inter-domain CaJournal of muscle research and cell motility · 2020
    Review
  8. Article
  9. The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics.International journal of molecular sciences · 2018
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. The role of MACF1 in nervous system development and maintenance.Seminars in cell & developmental biology · 2017
    Review
  15. Article
  16. Article
  17. Review
  18. 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

3 authors at 2 institutions in 1 country.

M WayMedical Research Council Laboratory of Molecular Biology, Cambridge, England.
B Pope
A G Weeds
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The F-actin binding domains of gelsolin and alpha-actinin compete for the same site on actin filaments with similar binding affinities. Both contain tandem repeats of approximately 125 amino acids, the first of which is shown to contain the actin-binding site. We have replaced the F-actin binding domain in the NH2-terminal half of gelsolin by that of alpha-actinin. The hybrid severs filaments almost as efficiently as does gelsolin or its NH2-terminal half, but unlike the latter, requires calcium ions. The hybrid binds two actin monomers and caps the barbed ends of filaments in the presence or absence of calcium. The cap produced by the hybrid binds with lower affinity than that of gelsolin and is not stable: It dissociates from filament ends with a half life of approximately 15 min. Although there is no extended sequence homology between these two different F-actin binding domains, our experiments show that they are functionally equivalent and provide new insights into the mechanism of microfilament severing.

Indexed as

ActininActinsAmino Acid SequenceBinding SitesCalcium-Binding ProteinsGelsolinMicrofilament ProteinsMolecular Sequence DataActininActinsCalcium-Binding ProteinsGelsolinMicrofilament Proteins

Identifiers

PMID1331120
PMCPMC2289707
OpenAlexW2116269882

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.