Evidence map›Paper›PMID 37524848›Full record

ReviewNature reviews. Molecular cell biology2023

Structural and functional complexity of HSP90 in cellular homeostasis and disease.

Gabriela Chiosis, Chander S Digwal, Jane B Trepel, Len Neckers

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
27.9field-weighted citation impact, top 1% 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

102 citing papers in PubMed, 181 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Expanding the chaperone code.Cell stress & chaperones · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Structural analysis ofbioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
    Article
  20. Article

42 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Gabriela ChiosisChemical Biology Program, Memorial Sloan Kettering Institute, New York, NY, USA. chiosisg@mskcc.org.ORCID 0000-0003-0486-6920
Chander S DigwalChemical Biology Program, Memorial Sloan Kettering Institute, New York, NY, USA.ORCID 0000-0001-8784-1096
Jane B TrepelDevelopmental Therapeutics Branch, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.
Len NeckersUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA. neckersl@mail.nih.gov.ORCID 0000-0001-9639-7249
Memorial Sloan Kettering Cancer Center · USNational Cancer Institute · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4M
Uncovering Alzheimer's disease risk mechanisms through neuron-specific analysis of autophagy and endosomal-lysosomal functionP01AG017617 · NIA · NATHAN S. KLINE INSTITUTE FOR PSYCH RES · PI NIXON, RALPH A. · 2000 to 2021
$40.0M
TAU, AB, SYNUCLEIN AND NITRATIVE/OXIDATIVE DAMAGE IN MCIP01AG014449 · NIA · UNIVERSITY OF PITTSBURGH · PI MUFSON, ELLIOTT JAY · 1997 to 2024
$39.7M
Project 3: Structural Basis for grp94 Drug Development and Chaperone FunctionP01CA186866 · NCI · OHIO STATE UNIVERSITY · PI LI, ZIHAI · 2015 to 2019
$6.7M
Impact of sex differences on the trajectory of interactome dysfunctions across the AD spectrumR01AG074004 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA, GINSBERG, STEPHEN D · 2021 to 2025
$6.0M
Chaperome networks in Alzheimer's diseaseR01AG067598 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI ARANCIO, OTTAVIO, CHIOSIS, GABRIELA · 2021 to 2025
$5.9M
Selective interactome vulnerability across the Alzheimer’s disease spectrumR01AG072599 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI GABRIELA CHIOSIS, STEPHEN D GINSBERG · 2023 to 2026
$5.4M
[18F]-PU-AD epichaperome PET imaging probeRF1AG071805 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA, DUNPHY, MARK P. · 2022 to 2025
$4.8M
Neuropathology and inflammation in a nonhuman primate model of insulin resistance/metabolic syndromeR01AG085572 · NIA · UNIVERSITY OF CALIFORNIA AT DAVIS · PI STEPHEN D GINSBERG, PETER J HAVEL · 2024 to 2026
$3.8M
Small molecule Hsp90 inhibitors in AD treatmentU01AG032969 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA · 2010 to 2014
$3.5M
Biomarkers for predicting response to Hsp90 therapyR01CA172546 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA, DUNPHY, MARK P. · 2013 to 2017
$2.9M
A chemical chaperomics platform for ADR56AG061869 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA · 2018 to 2019
$1.8M
NCI NIH HHS P01 CA186866NCI NIH HHS P30 CA008748NCI NIH HHS R01 CA172546NIA NIH HHS P01 AG014449NIA NIH HHS P01 AG017617NIA NIH HHS R01 AG067598NIA NIH HHS R01 AG072599NIA NIH HHS R01 AG074004NIA NIH HHS R01 AG085572NIA NIH HHS R56 AG061869NIA NIH HHS R56 AG072599NIA NIH HHS RF1 AG071805NIA NIH HHS U01 AG032969
6 · The paper itself

Abstract

Heat shock protein 90 (HSP90) is a chaperone with vital roles in regulating proteostasis, long recognized for its function in protein folding and maturation. A view is emerging that identifies HSP90 not as one protein that is structurally and functionally homogeneous but, rather, as a protein that is shaped by its environment. In this Review, we discuss evidence of multiple structural forms of HSP90 in health and disease, including homo-oligomers and hetero-oligomers, also termed epichaperomes, and examine the impact of stress, post-translational modifications and co-chaperones on their formation. We describe how these variations influence context-dependent functions of HSP90 as well as its interaction with other chaperones, co-chaperones and proteins, and how this structural complexity of HSP90 impacts and is impacted by its interaction with small molecule modulators. We close by discussing recent developments regarding the use of HSP90 inhibitors in cancer and how our new appreciation of the structural and functional heterogeneity of HSP90 invites a re-evaluation of how we discover and implement HSP90 therapeutics for disease treatment.

Indexed as

HSP90 Heat-Shock ProteinsMolecular ChaperonesHomeostasisProtein FoldingProteostasisHSP90 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID37524848
PMCPMC10592246
OpenAlexW4385416872

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.