Evidence map›Paper›PMID 17035236›Full record

ArticleThe Journal of biological chemistry2006

Post-meiotic shifts in HSPA2/HSP70.2 chaperone activity during mouse spermatogenesis.

Jérôme Govin, Cécile Caron, Emmanuelle Escoffier, Myriam Ferro, Lauriane Kuhn, Sophie Rousseaux, Edward M Eddy, Jérôme Garin, Saadi Khochbin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. 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
3.0field-weighted citation impact, top 9% 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, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Essential role of MgCell reports · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Circular RNAs fromScience advances · 2020
    Article
  16. A noncanonical role of NOD-like receptor NLRP14 in PGCLC differentiation and spermatogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  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

9 authors at 5 institutions in 2 countries.

Jérôme GovinINSERM, U309, Institut Albert Bonniot, F-38700 Grenoble, France.
Cécile Caron
Emmanuelle Escoffier
Myriam Ferro
Lauriane Kuhn
Sophie Rousseaux
Edward M Eddy
Jérôme Garin
Saadi Khochbin
Inserm · FRUniversité Joseph Fourier · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRLaboratoire de Chimie · FRResearch Triangle Park Foundation · US

Funding

Expression Of Heat Shock Genes In Mouse Spermatogenic CellsZIAES070077 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI EDDY, EDWARD MITCHELL · 2009 to 2014
$1.2M
THE EXPRESSION OF HEAT-SHOCK GENES IN MOUSE SPERMATOGENIC CELLSZ01ES070077 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI EDDY, EDWARD MITCHELL · 1987 to 2008
$704k
NIEHS NIH HHS Z01 ES070077-17
6 · The paper itself

Abstract

HSPA2 (formerly HSP70.2) is a testis-specific member of the HSP70 family known to play a critical role in the completion of meiosis during male germ cell differentiation. Although abundantly present in post-meiotic cells, its function during spermiogenesis remained obscure. Here, using a global proteomic approach to identify genome-organizing proteins in condensing spermatids, we discovered an unexpected role for HSPA2, which acquires new functions and becomes tightly associated with major spermatid DNA-packaging proteins, transition proteins 1 and 2. Hence, HSPA2 is identified here as the first transition protein chaperone, and these data shed a new light on the yet totally unknown process of genome-condensing structure assembly in spermatids.

Indexed as

AnimalsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA PackagingHSP70 Heat-Shock ProteinsIn Vitro TechniquesMaleMeiosisMiceNuclear ProteinsProtein BindingProteomicsSpermatidsSpermatogenesisChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHSP70 Heat-Shock ProteinsHspa2 protein, mouseNuclear Proteinsspermatid transition proteinsTnp2 protein, mouse

Identifiers

PMID17035236
PMCPMC1896149
OpenAlexW1969561254

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.