Evidence map›Paper›PMID 21209834›Full record

ArticlePloS one2010

The molecular chaperone Hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse.

Iwona Grad, Christopher R Cederroth, Joël Walicki, Corinne Grey, Sofia Barluenga, Nicolas Winssinger, Bernard De Massy, Serge Nef, Didier Picard

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
4.1field-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

104 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
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  7. [EJNMMI radiopharmacy and chemistry · 2025
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  15. HSP90β prevents aging-related cataract formation through regulation of the charged multivesicular body protein (CHMP4B) and p53.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Organismal Roles of Hsp90.Biomolecules · 2023
    Review
  20. Review

44 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

9 authors at 4 institutions in 2 countries.

Iwona GradDépartement de Biologie Cellulaire, Université de Genève, Sciences III, Genève, Switzerland.
Christopher R Cederroth
Joël Walicki
Corinne Grey
Sofia Barluenga
Nicolas Winssinger
Bernard De Massy
Serge Nef
Didier Picard
University of Geneva · CHInstitut de Science et d'Ingénierie Supramoléculaires · FRCentre National de la Recherche Scientifique · FRInstitut de Génétique Humaine · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular chaperone Hsp90 has been found to be essential for viability in all tested eukaryotes, from the budding yeast to Drosophila. In mammals, two genes encode the two highly similar and functionally largely redundant isoforms Hsp90α and Hsp90β. Although they are co-expressed in most if not all cells, their relative levels vary between tissues and during development. Since mouse embryos lacking Hsp90β die at implantation, and despite the fact that Hsp90 inhibitors being tested as anti-cancer agents are relatively well tolerated, the organismic functions of Hsp90 in mammals remain largely unknown. We have generated mouse lines carrying gene trap insertions in the Hsp90α gene to investigate the global functions of this isoform. Surprisingly, mice without Hsp90α are apparently normal, with one major exception. Mutant male mice, whose Hsp90β levels are unchanged, are sterile because of a complete failure to produce sperm. While the development of the male reproductive system appears to be normal, spermatogenesis arrests specifically at the pachytene stage of meiosis I. Over time, the number of spermatocytes and the levels of the meiotic regulators and Hsp90 interactors Hsp70-2, NASP and Cdc2 are reduced. We speculate that Hsp90α may be required to maintain and to activate these regulators and/or to disassemble the synaptonemal complex that holds homologous chromosomes together. The link between fertility and Hsp90 is further supported by our finding that an Hsp90 inhibitor that can cross the blood-testis barrier can partially phenocopy the genetic defects.

Indexed as

Pachytene StageAnimalsBlood-Testis BarrierDisease ProgressionFemaleHSP90 Heat-Shock ProteinsMaleMeiosisMiceMolecular ChaperonesMutationPhenotypeSpermatocytesSpermatogenesisSpermatozoaTestisHSP90 Heat-Shock ProteinsHspca protein, mouseMolecular Chaperones

Identifiers

PMID21209834
PMCPMC3013136
OpenAlexW1974186916

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.