Evidence map›Paper›PMID 42167645›Full record

ReviewCell stress & chaperones2026

Hsp90: A means to an end.

Katie M Whalen, Brian C Freeman

Abstract readReview
In one paragraph

Review in Cell stress & chaperones, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

2 authors.

Katie M WhalenDepartment of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL 61801, USA.
Brian C FreemanDepartment of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: bfree@illinois.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hsp90 molecular chaperone is a key component of the protein homeostasis (proteostasis) system. Hsp90 likely serves as a gatekeeper in a cell's protein quality control decision tree since this chaperone is linked to nascent polypeptide folding, client maturation, metastable protein maintenance, and polypeptide degradation. Interestingly, how a client protein is directed through the decision process is unclear. Minimally, modifications to the amino-terminal ATP-binding domain of Hsp90 can favor client degradation. As this includes a common class of Hsp90 inhibitors that trigger the breakdown of clinically relevant factors, a better understanding of Hsp90's role in quality control is merited. Here, we explore how Hsp90 links to both polypeptide biogenesis and triage, the events that regulate the decision route, and how Hsp90's connections to proteolysis pathways are being exploited for the development of new therapeutics.

Indexed as

HSP90 Heat-Shock ProteinsAnimalsHumansProtein FoldingProteolysisProteostasisHSP90 Heat-Shock ProteinsHsp90Molecular chaperoneProteolysisProteostasis

Identifiers

PMID42167645
PMCPMC13235355

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.