Evidence map›Paper›PMID 18256191›Full record

ArticleDevelopment (Cambridge, England)2008

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis.

Thomas A Hawkins, Anna-Pavlina Haramis, Christelle Etard, Chrisostomos Prodromou, Cara K Vaughan, Rachel Ashworth, Saikat Ray, Martine Behra, Nigel Holder, William S Talbot and 3 more

Open access · greenAbstract read
In one paragraph

Article in Development (Cambridge, England), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed, 90 citations in OpenAlex.

  1. Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
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  10. Defective sarcomere assembly inFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  11. Article
  12. Therapeutic potential of heat shock protein induction for muscular dystrophy and other muscle wasting conditions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  13. Impact ofFrontiers in physiology · 2018
    Article
  14. Review
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  19. Article
  20. Defects of the Glycinergic Synapse in Zebrafish.Frontiers in molecular neuroscience · 2016
    Review
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

13 authors at 3 institutions in 2 countries.

Thomas A HawkinsDepartment of Anatomy and Developmental Biology, UCL, London, UK.
Anna-Pavlina Haramis
Christelle Etard
Chrisostomos Prodromou
Cara K Vaughan
Rachel Ashworth
Saikat Ray
Martine Behra
Nigel Holder
William S Talbot
Laurence H Pearl
Uwe Strähle
Stephen W Wilson
University College London · GBInstitute of Cancer Research · GBStanford University · US

Funding

Biotechnology and Biological Sciences Research Council G06123Biotechnology and Biological Sciences Research Council G07295Biotechnology and Biological Sciences Research Council G13757Biotechnology and Biological Sciences Research Council G13761Biotechnology and Biological Sciences Research Council G19181Medical Research Council G0501487Medical Research Council G0501487(76596)Medical Research Council G0700216Wellcome Trust 069903Wellcome Trust 074376Wellcome Trust 078047
6 · The paper itself

Abstract

The mechanisms that regulate sarcomere assembly during myofibril formation are poorly understood. In this study, we characterise the zebrafish sloth(u45) mutant, in which the initial steps in sarcomere assembly take place, but thick filaments are absent and filamentous I-Z-I brushes fail to align or adopt correct spacing. The mutation only affects skeletal muscle and mutant embryos show no other obvious phenotypes. Surprisingly, we find that the phenotype is due to mutation in one copy of a tandemly duplicated hsp90a gene. The mutation disrupts the chaperoning function of Hsp90a through interference with ATPase activity. Despite being located only 2 kb from hsp90a, hsp90a2 has no obvious role in sarcomere assembly. Loss of Hsp90a function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a and several other genes encoding proteins that may act with Hsp90a during sarcomere assembly. Our studies reveal a surprisingly specific developmental role for a single Hsp90 gene in a regulatory pathway controlling late steps in sarcomere assembly.

Indexed as

Adenosine TriphosphatasesAnimalsBase SequenceBinding SitesDNA PrimersHeat-Shock ResponseHSP90 Heat-Shock ProteinsMicroscopy, Electron, TransmissionModels, MolecularMuscle DevelopmentMuscle, SkeletalMutationMyofibrilsPhenotypeSarcomeresZebrafishAdenosine TriphosphatasesDNA PrimersHSP90 Heat-Shock ProteinsZebrafish Proteins

Identifiers

PMID18256191
PMCPMC2358948
OpenAlexW2121908416

What OpenQuestion holds

Textmetadata
LicenceTDM
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.