Evidence map›Paper›PMID 11257131›Full record

ArticleThe Journal of cell biology2001

The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-interacting protein 1 required for organized assembly of muscle actin filaments.

S Ono

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

70 citing papers in PubMed, 102 citations in OpenAlex.

  1. Trial
  2. Caenorhabditis elegans small heat-shock protein HSP-12.6 has a highly specialized protective function towards muscle thick filaments in vivo.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Article
  3. Article
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  5. Overexpression of Lifeact in theFrontiers in cell and developmental biology · 2024
    Article
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  7. Article
  8. Article
  9. Imaging of Actin Cytoskeleton in the Nematode Caenorhabditis elegans.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. TwoThe Journal of biological chemistry · 2020
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  14. Article
  15. Mutations inF1000Research · 2019
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

S OnoDepartment of Pathology, Emory University, Atlanta, Georgia 30322, USA. sono@emory.edu
Emory University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembly and maintenance of myofibrils require dynamic regulation of the actin cytoskeleton. In Caenorhabditis elegans, UNC-60B, a muscle-specific actin depolymerizing factor (ADF)/cofilin isoform, is required for proper actin filament assembly in body wall muscle (Ono, S., D.L. Baillie, and G.M. Benian. 1999. J. Cell Biol. 145:491--502). Here, I show that UNC-78 is a homologue of actin-interacting protein 1 (AIP1) and functions as a novel regulator of actin organization in myofibrils. In unc-78 mutants, the striated organization of actin filaments is disrupted, and large actin aggregates are formed in the body wall muscle cells, resulting in defects in their motility. Point mutations in unc-78 alleles change conserved residues within different WD repeats of the UNC-78 protein and cause less severe phenotypes than a deletion allele, suggesting that these mutations partially impair the function of UNC-78. UNC-60B is normally localized in the diffuse cytoplasm and to the myofibrils in wild type but mislocalized to the actin aggregates in unc-78 mutants. Similar Unc-78 phenotypes are observed in both embryonic and adult muscles. Thus, AIP1 is an important regulator of actin filament organization and localization of ADF/cofilin during development of myofibrils.

Indexed as

Caenorhabditis elegans ProteinsActinsAmino Acid SequenceAnimalsCaenorhabditis elegansGenes, HelminthHelminth ProteinsMicrofilament ProteinsMicroscopy, FluorescenceMolecular Sequence DataMovementMutationMyofibrilsPhylogenySequence AlignmentActinsCaenorhabditis elegans ProteinsHelminth ProteinsMicrofilament ProteinsUNC-60 protein, C elegansunc-78 protein, C elegans

Identifiers

PMID11257131
PMCPMC2199200
OpenAlexW2121190186

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.