ArticleNature structural & molecular biology2016
Importance of cycle timing for the function of the molecular chaperone Hsp90.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
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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.
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.
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Who cites it
63 citing papers in PubMed, 102 citations in OpenAlex.
- Antifungal metallacarboranes modulate Hsp90 activity.Future medicinal chemistry · 2026Article
- Placental Heat Shock Protein (HSP) Expression in Fetal Growth Restriction (FGR) Pregnancies: A Case-Control Immunohistochemistry Study.International journal of molecular sciences · 2026Article
- Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome.Cell stress & chaperones · 2026Article
- Collaboration between two conserved sequence motifs drives ATPase stimulation of Hsp90 by Aha1.Protein science : a publication of the Protein Society · 2025Article
- Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025Article
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- Point mutations of the mitochondrial chaperone TRAP1 affect its functions and pro-neoplastic activity.Cell death & disease · 2025Article
- Ordered ATP hydrolysis in the Hsp90 chaperone is regulated by Aha1 and a conserved post-translational modification.Protein science : a publication of the Protein Society · 2025Article
- Dominant negative mutations in yeast Hsp90 indicate triage decision mechanism targeting client proteins for degradation.Molecular biology of the cell · 2025Article
- The known unknowns of the Hsp90 chaperone.eLife · 2024Review
- Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function.PLoS genetics · 2024Article
- Evolution of the conformational dynamics of the molecular chaperone Hsp90.Nature communications · 2024Article
- Review
- Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide that inhibits ATPase stimulation.EMBO reports · 2024Article
- Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions.Genetics · 2024Article
- Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Promising immunotherapeutic targets for treating candidiasis.Frontiers in cellular and infection microbiology · 2024Review
- Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024Review
- A Strategy Utilizing Protein-Protein Interaction Hubs for the Treatment of Cancer Diseases.International journal of molecular sciences · 2023Review
- Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.Essays in biochemistry · 2023Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 2 countries.
Funding
Abstract
Hsp90 couples ATP hydrolysis to large conformational changes essential for activation of client proteins. The structural transitions involve dimerization of the N-terminal domains and formation of 'closed states' involving the N-terminal and middle domains. Here, we used Hsp90 mutants that modulate ATPase activity and biological function as probes to address the importance of conformational cycling for Hsp90 activity. We found no correlation between the speed of ATP turnover and the in vivo activity of Hsp90: some mutants with almost normal ATPase activity were lethal, and some mutants with lower or undetectable ATPase activity were viable. Our analysis showed that it is crucial for Hsp90 to attain and spend time in certain conformational states: a certain dwell time in open states is required for optimal processing of client proteins, whereas a prolonged population of closed states has negative effects. Thus, the timing of conformational transitions is crucial for Hsp90 function and not cycle speed.
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What OpenQuestion holds
Registered trials
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.