title: Combining an Hsp70 inhibitor with either an N- or C-terminal Hsp90 inhibitor produces mechanistically distinct phenotypes.
abstract: Blocking the function of both heat shock protein 90 and 70 (Hsp90 and Hsp70) simultaneously limits these chaperones' cytoprotective effects on cancer cells. The unique phenotype associated with modulating Hsp90's C-terminus, when used in combination with Hsp70 inhibitors, produces a synergistic and highly relevant dual chemotherapy regimen.
authors: Department of Chemistry, Gate 2 High street, Dalton 219, University of New South Wales, Sydney, NSW 2052, Australia. s.mcalpine@unsw.edu.au.
authors: Y
authors: Y
authors: Wang
authors: S R
authors: SR
authors: McAlpine
mesh_terms: D015972:Gene Expression Regulation, Neoplastic; D045325:HCT116 Cells; D018840:HSP70 Heat-Shock Proteins / Q000037:antagonists & inhibitors*; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors*; D006801:Humans; D008156:Luciferases / Q000378:metabolism; D010641:Phenotype; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D012333:RNA, Messenger; D008156:Luciferases