Celastrol Inhibits Hsp90 Chaperoning of Steroid Receptors by Inducing Fibrillization of the Co-chaperone p23

Hsp90 is an ATP-dependent molecular chaperone. The best characterized inhibitors of Hsp90 target its ATP binding pocket, causing nonselective degradation of Hsp90 client proteins. Here, we show that the small molecule celastrol inhibits the Hsp90 chaperoning machinery by inactivating the co-chaperon...

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Detalhes bibliográficos
Main Authors: Chadli, Ahmed, Felts, Sara J., Wang, Qin, Sullivan, William P., Botuyan, Maria Victoria, Fauq, Abdul, Ramirez-Alvarado, Marina, Mer, Georges
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2010
Assuntos:
Protein Structure and Folding
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2823561/
https://ncbi.nlm.nih.gov/pubmed/19996313
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.081018
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