ArticleACS chemical biology2014
Cruentaren A binds F1F0 ATP synthase to modulate the Hsp90 protein folding machinery.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- CryoEM Structure with ATP Synthase Enables Late-Stage Diversification of Cruentaren A.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Manassantin A inhibits tumour growth under hypoxia through the activation of chaperone-mediated autophagy by modulating Hsp90 activity.British journal of cancer · 2023Article
- Native Size-Exclusion Chromatography-Based Mass Spectrometry Reveals New Components of the Early Heat Shock Protein 90 Inhibition Response Among Limited Global Changes.Molecular & cellular proteomics : MCP · 2023Article
- Copper-Catalyzed Diboron-MediatedMolecules (Basel, Switzerland) · 2022Article
- Heat Shock Protein 90 (HSP90) Inhibitors as Anticancer Medicines: A Review on the Computer-Aided Drug Discovery Approaches over the Past Five Years.Computational and mathematical methods in medicine · 2022Review
- The therapeutic potential of mitochondrial toxins.The Journal of antibiotics · 2021Review
- Myxobacteria and their products: current trends and future perspectives in industrial applications.Folia microbiologica · 2021Review
- The disruption of protein-protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition.Acta pharmaceutica Sinica. B · 2021Review
- Natural products and other inhibitors of FEuropean journal of medicinal chemistry · 2020Review
- Natural Product Inspired N-Terminal Hsp90 Inhibitors: From Bench to Bedside?Medicinal research reviews · 2016Review
- Anticancer Inhibitors of Hsp90 Function: Beyond the Usual Suspects.Advances in cancer research · 2016Review
- Cucurbitacin D Is a Disruptor of the HSP90 Chaperone Machinery.Journal of natural products · 2015Article
- Alternative approaches to Hsp90 modulation for the treatment of cancer.Future medicinal chemistry · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The molecular chaperone Hsp90 requires the assistance of immunophilins, co-chaperones, and partner proteins for the conformational maturation of client proteins. Hsp90 inhibition represents a promising anticancer strategy due to the dependence of numerous oncogenic signaling pathways upon Hsp90 function. Historically, small molecules have been designed to inhibit ATPase activity at the Hsp90 N-terminus; however, these molecules also induce the pro-survival heat shock response (HSR). Therefore, inhibitors that exhibit alternative mechanisms of action that do not elicit the HSR are actively sought. Small molecules that disrupt Hsp90-co-chaperone interactions can destabilize the Hsp90 complex without induction of the HSR, which leads to inhibition of cell proliferation. In this article, selective inhibition of F1F0 ATP synthase by cruentaren A was shown to disrupt the Hsp90-F1F0 ATP synthase interaction and result in client protein degradation without induction of the HSR.
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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.