Evidence map›Paper›PMID 37295430›Full record

ArticleMolecular cell2023

The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions.

Janhavi A Kolhe, Neethu L Babu, Brian C Freeman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 45 citations in OpenAlex.

  1. Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. More than the 'master regulator of cytosolic proteostasis': new roles for HSF1 in promoting tissue health.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. Article
  4. Hsp90: A means to an end.Cell stress & chaperones · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
    Article
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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 1 institution in 1 country.

Janhavi A KolheDepartment of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL, USA.
Neethu L BabuDepartment of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL, USA.
Brian C FreemanDepartment of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL, USA. Electronic address: bfree@illinois.edu.
University of Illinois Urbana-Champaign · US

Funding

Regulation of the Native Protein Landscape in the Nucleus by Molecular ChaperonesR35GM136660 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Brian C Freeman · 2020 to 2026
$2.7M
NIGMS NIH HHS R35 GM136660
6 · The paper itself

Abstract

Molecular chaperones govern proteome health to support cell homeostasis. An essential eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology approach, we characterized the features driving the Hsp90 physical interactome. We found that Hsp90 associated with ∼20% of the yeast proteome using its three domains to preferentially target intrinsically disordered regions (IDRs) of client proteins. Hsp90 selectively utilized an IDR to regulate client activity as well as maintained IDR-protein health by preventing the transition to stress granules or P-bodies at physiological temperatures. We also discovered that Hsp90 controls the fidelity of ribosome initiation that triggers a heat shock response when disrupted. Our study provides insights into how this abundant molecular chaperone supports a dynamic and healthy native protein landscape.

Indexed as

Intrinsically Disordered ProteinsMolecular ChaperonesProteomeHSP90 Heat-Shock ProteinsHumansSaccharomyces cerevisiaeHSP90 Heat-Shock ProteinsIntrinsically Disordered ProteinsMolecular ChaperonesProteomefidelity of translation initiationHsp90intrinsically disordered regionsmolecular chaperoneproteostasis

Identifiers

PMID37295430
PMCPMC10297700
OpenAlexW4379880458

What OpenQuestion holds

Textmetadata
LicenceTDM
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.