Title : Hsp90 molecular chaperone inhibitors: are we there yet?

Pub. Date : 2012 Jan 1

PMID : 22215907






1 Functional Relationships(s)
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1 Investigators established Hsp90"s druggability using the natural products geldanamycin and radicicol, which mimic the unusual ATP structure adopted in the chaperone"s N-terminal nucleotide-binding pocket and cause potent and selective blockade of ATP binding/hydrolysis, inhibit chaperone function, deplete oncogenic clients, and show antitumor activity. monorden heat shock protein 90 alpha family class A member 1 Homo sapiens