id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-295381-0dqu3p3y	Kamal, Adeela	Therapeutic and diagnostic implications of Hsp90 activation	2004-06-01		.txt	text/plain	5102	211	37	Recent work has identified the role of Hsp90 in multiple signal transduction pathways and revealed that the molecular mechanism of tumor selectivity by Hsp90 inhibitors is the result of an activated, high-affinity conformation of Hsp90 in tumors. A recent study reported that the Hsp90 in tumor cells is maintained in an activated conformation by the formation of multi-chaperone complexes that have increased ATPase activity and 100-fold greater binding affinity for 17-AAG compared with the uncomplexed, latent form of Hsp90 that is present in normal cells [28] . A model for Hsp90-dependent malignant progression has been proposed in which, as tumor cells gradually accumulate mutant and overexpressed signaling proteins, Hsp90 becomes engaged in the active chaperoning and stabilization of oncoproteins and adopts a high-affinity form that is induced by bound co-chaperone proteins ( Figure 3 ) [28] . FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases	./cache/cord-295381-0dqu3p3y.txt	./txt/cord-295381-0dqu3p3y.txt