Evidence map›Paper›PMID 38534118›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2024

Hsp90, a team player in protein quality control and the stress response in bacteria.

Anushka C Wickramaratne, Sue Wickner, Andrea N Kravats

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
  5. Article
  6. Review
  7. Hsp90, DnaK, and ClpB collaborate in protein reactivation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. 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

3 authors at 2 institutions in 1 country.

Anushka C WickramaratneLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA.ORCID 0000-0001-5358-8272
Sue WicknerLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA.ORCID 0009-0005-9131-210X
Andrea N KravatsDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio, USA.ORCID 0000-0001-8930-0170
National Institutes of Health · USMiami University · US

Funding

Molecular Chaperones and DNA ReplicationZIABC008710 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WICKNER, SUE H · 2009 to 2025
$24.5M
Elucidating the Mechanistic Details of the Grp94 Molecular Chaperone through an Integrated Computational and Experimental ApproachR35GM146963 · NIGMS · MIAMI UNIVERSITY OXFORD · PI Andrea N Kravats · 2022 to 2026
$1.7M
HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM146963Intramural Research Program of the NIH, NCI, Center for Cancer ResearchNIGMS NIH HHS R35 GM146963
6 · The paper itself

Abstract

SUMMARYHeat shock protein 90 (Hsp90) participates in proteostasis by facilitating protein folding, activation, disaggregation, prevention of aggregation, degradation, and protection against degradation of various cellular proteins. It is highly conserved from bacteria to humans. In bacteria, protein remodeling by Hsp90 involves collaboration with the Hsp70 molecular chaperone and Hsp70 cochaperones. In eukaryotes, protein folding by Hsp90 is more complex and involves collaboration with many Hsp90 cochaperones as well as Hsp70 and Hsp70 cochaperones. This review focuses primarily on bacterial Hsp90 and highlights similarities and differences between bacterial and eukaryotic Hsp90. Seminal research findings that elucidate the structure and the mechanisms of protein folding, disaggregation, and reactivation promoted by Hsp90 are discussed. Understanding the mechanisms of bacterial Hsp90 will provide fundamental insight into the more complex eukaryotic chaperone systems.

Indexed as

BacteriaBacterial ProteinsHSP90 Heat-Shock ProteinsProtein FoldingHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesProteostasisStress, PhysiologicalBacterial ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesclientcochaperoneDnaJDnaKHsp40Hsp70Hsp90HtpG

Identifiers

PMID38534118
PMCPMC11332350
OpenAlexW4393223328

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.