Evidence map›Paper›PMID 34937936›Full record

ArticleNature2022

Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.

Chari M Noddings, Ray Yu-Ruei Wang, Jill L Johnson, David A Agard

Open access · greenAbstract read
In one paragraph

Article in Nature, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
8.8field-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

82 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Hsp90: A means to an end.Cell stress & chaperones · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

22 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.

Chari M Noddings *Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA.ORCID http://orcid.org/0000-0003-0890-9035
Ray Yu-Ruei Wang *Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA.
Jill L JohnsonDepartment of Biological Sciences, University of Idaho, Moscow, ID, USA.ORCID http://orcid.org/0000-0003-3881-722X
David A AgardDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA. agard@msg.ucsf.edu.ORCID http://orcid.org/0000-0003-3512-695X
University of California, San Francisco · USUniversity of Idaho · US

Funding

Sequence-structure-function relationships in human visual photopigmentsP20GM104420 · NIGMS · UNIVERSITY OF IDAHO · PI WICHMAN, HOLLY A · 2015 to 2024
$22.9M
Structure & Mechanism: microtubule nucleation, centrosomes, phage cytoskeletonR35GM118099 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A. · 2016 to 2022
$3.6M
Acquisition of an electron microscope for high-resolution single particle cryo-EMS10OD021741 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2016 to 2016
$2.0M
Diversity Supplement: Determinants of Hsp90-client interactionR01GM127675 · NIGMS · UNIVERSITY OF IDAHO · PI JOHNSON, JILL L · 2019 to 2022
$1.2M
Linux cluster for near atomic resolution single particle cryo-EMS10OD020054 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2015 to 2015
$456k
Mechanism of Hsp90-Dependent Glucocorticoid Receptor ActivationF31CA265084 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI NODDINGS, CHARI · 2021 to 2022
$66k
Howard Hughes Medical InstituteNCI NIH HHS F31 CA265084NIGMS NIH HHS P20 GM104420NIGMS NIH HHS R01 GM127675NIGMS NIH HHS R35 GM118099NIH HHS S10 OD020054NIH HHS S10 OD021741
6 · The paper itself

Abstract

Hsp90 is a conserved and essential molecular chaperone responsible for the folding and activation of hundreds of 'client' proteins

Indexed as

Cryoelectron MicroscopyHSP90 Heat-Shock ProteinsProstaglandin-E SynthasesReceptors, GlucocorticoidHSP70 Heat-Shock ProteinsHumansLigandsMolecular ChaperonesProtein BindingHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsLigandsMolecular ChaperonesProstaglandin-E SynthasesPTGES3 protein, humanReceptors, Glucocorticoid

Identifiers

PMID34937936
PMCPMC8994517
OpenAlexW4200236070

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.