Evidence map›Paper›PMID 33937334›Full record

ArticleFrontiers in molecular biosciences2021

Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates.

Bruno Fauvet, Andrija Finka, Marie-Pierre Castanié-Cornet, Anne-Marie Cirinesi, Pierre Genevaux, Manfredo Quadroni, Pierre Goloubinoff

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  6. Article
  7. Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  8. Heat Shock Proteins and Breast Cancer.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Uncoupling the Hsp90 and DnaK chaperone activities revealed the in vivo relevance of their collaboration in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022
    Review
  14. Article
  15. Review
  16. The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021
    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

7 authors at 3 institutions in 3 countries.

Bruno FauvetDepartment of Plant Molecular Biology (DBMV), University of Lausanne, Lausanne, Switzerland.
Andrija FinkaDepartment of Ecology, Agronomy and Aquaculture, University of Zadar, Zadar, Croatia.
Marie-Pierre Castanié-CornetLaboratoire de Microbiologie et de Génétique Moléculaires, Center de Biologie Intégrative, CNRS, Université de Toulouse, Toulouse, France.
Anne-Marie CirinesiLaboratoire de Microbiologie et de Génétique Moléculaires, Center de Biologie Intégrative, CNRS, Université de Toulouse, Toulouse, France.
Pierre GenevauxLaboratoire de Microbiologie et de Génétique Moléculaires, Center de Biologie Intégrative, CNRS, Université de Toulouse, Toulouse, France.
Manfredo QuadroniProtein Analysis Facility, University of Lausanne, Lausanne, Switzerland.
Pierre GoloubinoffDepartment of Plant Molecular Biology (DBMV), University of Lausanne, Lausanne, Switzerland.
Centre National de la Recherche Scientifique · FRUniversity of Lausanne · CHUniversity of Zadar · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration with Hsp70 (DnaK) remains poorly characterized. To uncover physiological processes that depend on HtpG and DnaK, we performed comparative quantitative proteomic analyses of insoluble and total protein fractions from unstressed wild-type (WT)

Indexed as

chaperonesDnaJDnaKHslVHtpGproteostasis

Identifiers

PMID33937334
PMCPMC8082187
OpenAlexW3156758023

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.