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- W2983060111 endingPage "491" @default.
- W2983060111 startingPage "473" @default.
- W2983060111 abstract "The molecular chaperone Hsp90 is at the heart of protein homeostasis control. A wide range of pathologies disturbs protein homeostasis, thus placing Hsp90 at the crossroads of many diseases. Here, we evaluate the impact of recent progress in understanding the molecular mechanism of Hsp90-client interactions and their role in disease. We discuss the role of Hsp90 for hormonal imbalances, cancer and neurodegenerative disorders. For each disease class we discuss implications of complexes in which Hsp90 binds to a paradigmatic client: the transcription factor Glucocorticoid Receptor, the kinase Cdk4 and the microtubule stabilizer Tau. The mechanistic insights allow us to elaborate on possible therapeutic intervention routes. Hsp90 is a druggable chaperone. Thus, understanding Hsp90 biology at molecular resolution offers an interesting approach to tackle protein-related diseases." @default.
- W2983060111 created "2019-11-22" @default.
- W2983060111 creator A5078271011 @default.
- W2983060111 creator A5078715883 @default.
- W2983060111 date "2019-01-01" @default.
- W2983060111 modified "2023-10-18" @default.
- W2983060111 title "Hsp90 Chaperone in Disease" @default.
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