title: HSP90 and the chaperoning of cancer.
abstract: Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily conserved class of proteins that guide the normal folding, intracellular disposition and proteolytic turnover of many of the key regulators of cell growth, differentiation and survival. This essential guardian function is subverted during oncogenesis to allow malignant transformation and to facilitate rapid somatic evolution. Pharmacologically 'bribing' the essential guard duty of the chaperone HSP90 (heat-shock protein of 90 kDa) seems to offer a unique anticancer strategy of considerable promise.
authors.affiliation: Steele Memorial Children's Research Center, University of Arizona, Tucson, Arizona 85724, USA. Whitesell@wi.mit.edu
authors.forename: Luke
authors.initials: L
authors.lastname: Whitesell
authors.forename: Susan L
authors.initials: SL
authors.lastname: Lindquist
mesh_terms: D000818:Animals; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D009369:Neoplasms / Q000188:drug therapy / Q000209:etiology*
chemical_list: D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones