Evidence map›Paper›PMID 7906647›Full record

ArticleThe EMBO journal1994

Chaperone activity of alpha-crystallins modulates intermediate filament assembly.

I D Nicholl, R A Quinlan

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed, 1 pooled it
8.8field-weighted citation impact, top 1% 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

126 citing papers in PubMed, 1 synthesis or guideline pooled it, 415 citations in OpenAlex.

  1. Pooled it
  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
  4. Article
  5. Article
  6. Hypertrophic Cardiomyopathy-Associated CRYABInternational journal of molecular sciences · 2025
    Article
  7. Article
  8. Role of the Alpha-B-Crystallin Protein in Cardiomyopathic Disease.International journal of molecular sciences · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Mechanisms of Small Heat Shock Proteins.Cold Spring Harbor perspectives in biology · 2019
    Review

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

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

2 authors at 1 institution in 1 country.

I D NichollDepartment of Biochemistry, The University, Dundee, UK.
R A Quinlan
University of Dundee · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Intermediate filaments are generally regarded as one of the most insoluble and resilient cytoskeletal structures of eukaryotic cells. In extracts from the ocular lens, we noticed an unusually high level of vimentin in a soluble, non-filamentous form. Immunoprecipitation of this soluble vimentin resulted in the co-precipitation of alpha-crystallins. The alpha-crystallins are homologous to the small heat shock proteins (sHSPs) and have recently been identified as molecular chaperones, capable of preventing the heat-induced aggregation of proteins. We find that the alpha-crystallins dramatically inhibit the in vitro assembly of GFAP and vimentin in an ATP-independent manner. This inhibition is also independent of the phosphorylation state of the alpha-crystallin polypeptides and each one of the four polypeptides, either alpha A1-, alpha A2-, alpha B1- or alpha B2-crystallin, are equally effective in this inhibition. Furthermore, we show that alpha-crystallins can increase the soluble pool of GFAP when added to preformed filaments. Electron microscopy demonstrated that alpha-crystallin particles could bind to intermediate filaments in a regular fashion, the spacing coinciding with the molecular length of GFAP. This is the first report, as far as we are aware, of a chaperone being involved in intermediate filament assembly and implicates chaperones in the remodeling of intermediate filaments during development and cell differentiation.

Indexed as

Adenosine TriphosphateAnimalsCattleChaperoninsCrystallinsGlial Fibrillary Acidic ProteinIntermediate Filament ProteinsLens, CrystallineMicroscopy, ElectronProteinsVimentinAdenosine TriphosphateChaperoninsCrystallinsGlial Fibrillary Acidic ProteinIntermediate Filament ProteinsProteinsVimentin

Identifiers

PMID7906647
PMCPMC394896
OpenAlexW1755868117

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.