Evidence map›Paper›PMID 23396352›Full record

ArticleNature structural & molecular biology2013

Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.

Jing Li, Klaus Richter, Jochen Reinstein, Johannes Buchner

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.7field-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

68 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. FRET Assays for the Identification ofPharmaceuticals (Basel, Switzerland) · 2024
    Article
  10. Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. The role of Aha1 in cancer and neurodegeneration.Frontiers in molecular neuroscience · 2024
    Review
  12. Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Aha1 Is an Autonomous Chaperone for SULT1A1.Chemical research in toxicology · 2022
    Article
  17. Review
  18. Review
  19. Review
  20. Review

8 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 3 institutions in 2 countries.

Jing LiCenter for Integrated Protein Science, Department Chemie, Technische Universität München, München, Germany.
Klaus Richter
Jochen Reinstein
Johannes Buchner
Technical University of Munich · DECenter for Integrated Protein Science Munich · DEMax Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat-shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that associates dynamically with various co-chaperones during its chaperone cycle. Here we analyzed the role of the activating co-chaperone Aha1 in the progression of the yeast Hsp90 chaperone cycle and identified a critical ternary Hsp90 complex containing the co-chaperones Aha1 and Cpr6. Aha1 accelerates the intrinsically slow conformational transitions of Hsp90 to an N-terminally associated state but does not fully close the nucleotide-binding pocket yet. Cpr6 increases the affinity between Aha1 and Hsp90 and further stimulates the Hsp90 ATPase activity. Synergistically, Aha1 and Cpr6 displace the inhibitory co-chaperone Sti1 from Hsp90. To complete the cycle, Aha1 is released by the co-chaperone p23. Thus, at distinct steps during the Hsp90 chaperone cycle, co-chaperones selectively trap statistically distributed Hsp90 conformers and thus turn Hsp90 into a deterministic machine.

Indexed as

Binding, CompetitiveChaperoninsCyclophilinsHeat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesPeptidyl-Prolyl Isomerase DPeptidyl-Prolyl Isomerase FProtein ConformationSaccharomyces cerevisiae ProteinsAHA1 protein, S cerevisiaeChaperoninsCPR6 protein, S cerevisiaeCyclophilinsHeat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesPeptidyl-Prolyl Isomerase DPeptidyl-Prolyl Isomerase FSaccharomyces cerevisiae ProteinsSBA1 protein, S cerevisiaeSTI1 protein, S cerevisiae

Identifiers

PMID23396352
OpenAlexW2054368237

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.