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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Bibliografiska uppgifter
Huvudupphovsmän: Chadli, Ahmed, Felts, Sara J., Wang, Qin, Sullivan, William P., Botuyan, Maria Victoria, Fauq, Abdul, Ramirez-Alvarado, Marina, Mer, Georges
Materialtyp: Artigo
Språk:Inglês
Publicerad: American Society for Biochemistry and Molecular Biology 2010
Ämnen:
Protein Structure and Folding
Länkar: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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