Evidence map›Paper›PMID 39879241›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Hsp90, DnaK, and ClpB collaborate in protein reactivation.

Joel R Hoskins, Anushka C Wickramaratne, Connor P Jewell, Lisa M Jenkins, Sue Wickner

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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

5 authors.

Joel R Hoskins *Laboratory of Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892.
Anushka C Wickramaratne *Laboratory of Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892.
Connor P JewellLaboratory of Cell Biology, National Cancer Institute, NIH, Bethesda, MD 20892.
Lisa M JenkinsLaboratory of Cell Biology, National Cancer Institute, NIH, Bethesda, MD 20892.ORCID 0000-0003-1245-1338
Sue WicknerLaboratory of Molecular Biology, National Cancer Institute, NIH, Bethesda, MD 20892.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp70, Hsp90, and ClpB/Hsp100 are molecular chaperones that help regulate proteostasis. Bacterial and yeast Hsp70s and their cochaperones function synergistically with Hsp90s to reactivate inactive and aggregated proteins by a mechanism that requires a direct interaction between Hsp90 and Hsp70 both in vitro and in vivo.

Indexed as

Escherichia coliEscherichia coli ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsAdenosine TriphosphateEndopeptidase ClpHSP40 Heat-Shock ProteinsMolecular ChaperonesProtein AggregatesAdenosine TriphosphateClpB protein, E coliDnaJ protein, E colidnaK protein, E coliEndopeptidase ClpEscherichia coli ProteinsGrpE protein, E coliHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesProtein AggregatesDnaJHsp100Hsp70HtpGmolecular chaperones

Identifiers

PMID39879241
PMCPMC11804706

What OpenQuestion holds

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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.