Evidence map›Paper›PMID 10716925›Full record

ArticleThe EMBO journal2000

Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates.

B M Lange, A Bachi, M Wilm, C González

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.0field-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

43 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
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  4. Arsenic impairsbioRxiv : the preprint server for biology · 2024
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  5. Hsp70 and Hsp90 Elaborately Regulate RNAi Efficiency inInternational journal of molecular sciences · 2023
    Article
  6. Plk4 Is a Novel Substrate of Protein Phosphatase 5.International journal of molecular sciences · 2023
    Article
  7. Article
  8. Proteins of the Ciliated Protozoan ParasitePathogens (Basel, Switzerland) · 2021
    Article
  9. Journal of cell science · 2020
    Article
  10. Over-expression of Hsp83 in grossly depletedJournal of biosciences · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Therapeutic potential of HSP90 inhibition for neurofibromatosis type 2.Clinical cancer research : an official journal of the American Association for Cancer Research · 2013
    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

4 authors at 1 institution in 1 country.

B M LangeCell Biology and Cell Biophysics Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
A Bachi
M Wilm
C González
European Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To determine the molecular composition of the centrosome of a higher eukaryote, we carried out a systematic nano-electrospray tandem or MALDI mass spectrometry analysis of the polypeptides present in highly enriched preparations of immunoisolated Drosophila centrosomes. One of the proteins identified is Hsp83, a member of the highly conserved Hsp90 family including chaperones known to maintain the activity of many proteins but suspected to have other essential, unidentified functions. We have found that a fraction of the total Hsp90 pool is localized at the centrosome throughout the cell cycle at different stages of development in Drosophila and vertebrates. This association between Hsp90 and the centrosome can be observed in purified centrosomes and after treatment with microtubule depolymerizing drugs, two criteria normally used to define core centrosomal components. Disruption of Hsp90 function by mutations in the Drosophila gene or treatment of mammalian cells with the Hsp90 inhibitor geldanamycin, results in abnormal centrosome separation and maturation, aberrant spindles and impaired chromosome segregation. This suggests that another role of Hsp90 might be to ensure proper centrosome function.

Indexed as

Cell CycleAdsorptionAnimalsAntibodiesBenzoquinonesBrainCell LineCentriolesCentrosomeChromosome SegregationDrosophila melanogasterFluorescent Antibody TechniqueHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicLarvaAntibodiesBenzoquinonesgeldanamycinHSP90 Heat-Shock ProteinsLactams, MacrocyclicQuinones

Identifiers

PMID10716925
PMCPMC305666
OpenAlexW2019114976

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.