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- W4385336915 abstract "Heat shock protein 90 (Hsp90), a highly conserved and widely expressed molecular chaperone, is mainly responsible for maintaining the correct folding of client proteins and is closely related to the stability and activation of tumour-related proteins. Hsp90α, the major isoform of Hsp90, can promote tumour cell migration and metastasis, and is abundantly secreted in highly invasive tumours. To date, most pan-Hsp90 inhibitors have been limited in their applications due to high toxicity. Herein, we described the candidate compound X10g based on a proteolysis-targeting chimaera (PROTAC) strategy that potently and selectively degraded Hsp90α. The results showed that X10g inhibited tumours better with lower toxicity in vivo. These findings demonstrate that synthesized selective Hsp90α degrader X10g provides a new strategy for breast cancer therapy." @default.
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- W4385336915 date "2023-11-01" @default.
- W4385336915 modified "2023-09-27" @default.
- W4385336915 title "Discovery of X10g as a selective PROTAC degrader of Hsp90α protein for treating breast cancer" @default.
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- W4385336915 doi "https://doi.org/10.1016/j.ejmech.2023.115690" @default.
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