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Targeting Hsp90 in urothelial carcinoma

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Figure

Figure 2: Hsp90 chaperone cycle. ATP binding to the N-terminal domain of Hsp90 (red) in an “open” conformation promotes transient dimerization of the N-domains “closed” conformation leading to ATP hydrolysis [38]
Figure 3: Hsp90 is a central hub to bladder cancer signaling. Hsp90 is a critical signaling hub in the etiopathogenesis of urothelial carcinoma
Table 1: FDA-approved and investigational therapies for urothelial carcinoma
Table 2: Preclinical studies of Hsp90 inhibitors in bladder cancer

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