Heat shock protein 90 (HSP90) is an ATP-dependent molecular chaperone which plays important roles in the development of cancer. Inhibition of the HSP90 chaperone function can disrupt multiple cancer dependent signaling pathways and result in potent anti-cancer effects, which has been a promising anti-cancer strategy. Up to now, HSP90 inhibitors with different mechanisms have been developed, including HSP90 N-terminal inhibitors (pan-isoform and isoform selective), C-terminal inhibitors and HSP90-cochaperone protein-protein interaction (PPI) inhibitors. In this chapter, we will review the current development of HSP90 inhibitors as anti-cancer agents.
CITATION STYLE
Jiang, F., Xu, X.-L., & You, Q.-D. (2019). HSP90 Inhibitors Blocking Multiple Oncogenic Signaling Pathways for the Treatment of Cancer (pp. 397–429). https://doi.org/10.1007/978-3-030-03952-3_20
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