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• W2148065722 abstract "The correct target: The cell division cycle protein 37 (Cdc37) and the heat shock protein (Hsp90) are molecular chaperones crucial for the folding and stabilization of protein kinases including the oncogenic kinases. NMR studies show that celastrol, a recently identified triterpene targeting Hsp90, in fact binds to Cdc37 and disrupts the Cdc37–Hsp90 complex. Celastrol inactivates Cdc37 through a thiol-mediated mechanism. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article." @default.
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• W2148065722 date "2009-07-27" @default.
• W2148065722 modified "2023-10-01" @default.
• W2148065722 title "Molecular Mechanism of Inhibition of the Human Protein Complex Hsp90-Cdc37, a Kinome Chaperone-Cochaperone, by Triterpene Celastrol" @default.
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• W2148065722 doi "https://doi.org/10.1002/anie.200900929" @default.
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