Evidence map›Paper›PMID 20531426›Full record

ReviewNature reviews. Molecular cell biology2010

HSP90 at the hub of protein homeostasis: emerging mechanistic insights.

Mikko Taipale, Daniel F Jarosz, Susan Lindquist

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 987 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
987citing papers in PubMed, 1 pooled it
49.4field-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

987 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,800 citations in OpenAlex.

  1. Plant-Based HSP90 Inhibitors in Breast Cancer Models: A Systematic Review.International journal of molecular sciences · 2024
    Pooled it
  2. Article
  3. Article
  4. Article
  5. From aggregate structure to disease trajectory: the role of the proteostasis network.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Splicing-driven post-translational dysregulation: a new frontier for precision cancer medicine and immunotherapy.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Review
  14. Dynamic Effects ofBiology · 2026
    Article
  15. Biomolecules · 2026
    Article
  16. Structural analysis ofbioRxiv : the preprint server for biology · 2026
    Article
  17. Review
  18. Article
  19. Article
  20. Article

927 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

3 authors at 1 institution in 1 country.

Mikko TaipaleWhitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA.
Daniel F Jarosz
Susan Lindquist
Whitehead Institute for Biomedical Research · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched in signal transducers, including kinases and transcription factors. Therefore, HSP90 regulates diverse cellular functions and exerts marked effects on normal biology, disease and evolutionary processes. Recent structural and functional analyses have provided new insights on the transcriptional and biochemical regulation of HSP90 and the structural dynamics it uses to act on a diverse client repertoire. Comprehensive understanding of how HSP90 functions promises not only to provide new avenues for therapeutic intervention, but to shed light on fundamental biological questions.

Indexed as

AnimalsHSP90 Heat-Shock ProteinsHumansModels, BiologicalMolecular ChaperonesProtein FoldingProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesProteins

Identifiers

PMID20531426
OpenAlexW2115527176

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.