title: N-terminal and C-terminal modulation of Hsp90 produce dissimilar phenotypes.
abstract: Classic oncogenic heat shock protein 90 (Hsp90) inhibitors target the N-terminus of the protein, triggering a survival mechanism in cancer cells referred to as the heat shock response (HSR). Inhibiting Hsp90 by modulating the C-terminus does not trigger a HSR, making it a highly attractive chemotherapeutic approach.
authors.affiliation: Department of chemistry, Gate 2 High street, Dalton 219, University of New South Wales, Sydney, NSW 2052, Australia. s.mcalpine@unsw.edu.au.
authors.forename: Y
authors.initials: Y
authors.lastname: Wang
authors.forename: S R
authors.initials: SR
authors.lastname: McAlpine
mesh_terms: D016227:Benzoquinones / Q000494:pharmacology*; D045325:HCT116 Cells; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018869:Heat-Shock Response / Q000187:drug effects; D006801:Humans; D047029:Lactams, Macrocyclic / Q000494:pharmacology*; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism; D010456:Peptides, Cyclic / Q000494:pharmacology*; D010641:Phenotype; D011487:Protein Conformation; D017510:Protein Folding; D012333:RNA, Messenger / Q000378:metabolism
chemical_list: D016227:Benzoquinones; D018841:HSP90 Heat-Shock Proteins; D047029:Lactams, Macrocyclic; D010456:Peptides, Cyclic; D012333:RNA, Messenger; C000601038:SM122 cyclic peptide; C112765:tanespimycin