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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Bibliografski detalji
Glavni autori: Chadli, Ahmed, Felts, Sara J., Wang, Qin, Sullivan, William P., Botuyan, Maria Victoria, Fauq, Abdul, Ramirez-Alvarado, Marina, Mer, Georges
Format: Artigo
Jezik:Inglês
Izdano: American Society for Biochemistry and Molecular Biology 2010
Teme:
Protein Structure and Folding
Online pristup: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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