ArticleChemphyschem : a European journal of chemical physics and physical chemistry2018
Effects of Inhibitors on Hsp90's Conformational Dynamics, Cochaperone and Client Interactions.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Single-molecule FRET and tracking of transfected biomolecules in living cells.Biophysical journal · 2026Article
- Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors.Nature communications · 2025Article
- The known unknowns of the Hsp90 chaperone.eLife · 2024Review
- The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding.Nature communications · 2024Article
- Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.Essays in biochemistry · 2023Article
- How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view.Structure (London, England : 1993) · 2023Article
- Hsp90 interaction networks in fungi-tools and techniques.FEMS yeast research · 2021Review
- Article
- Molecular insights into the interaction of Hsp90 with allosteric inhibitors targeting the C-terminal domain.MedChemComm · 2018Article
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
Abstract
The molecular chaperone and heat-shock protein Hsp90 has become a central target in anti-cancer therapy. Nevertheless, the effect of Hsp90 inhibition is still not understood at the molecular level, preventing a truly rational drug design. Here we report on the effect of the most prominent drug candidates, namely, radicicol, geldanamycin, derivatives of purine, and novobiocin, on Hsp90's characteristic conformational dynamics and the binding of three interaction partners. Unexpectedly, the global opening and closing transitions are hardly affected by Hsp90 inhibitors. Moreover, we find no significant changes in the binding of the cochaperones Aha1 and p23 nor of the model substrate Δ131Δ. This holds true for competitive and allosteric inhibitors. Therefore, direct inhibition mechanisms affecting only one molecular interaction are unlikely. We suggest that the inhibitory action observed in vivo is caused by a combination of subtle effects, which can be used in the search for novel Hsp90 inhibition mechanisms.
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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.