Targeting the dynamic HSP90 complex in cancer.
The molecular chaperone heat shock protein 90 (HSP90) has been used by cancer cells to facilitate the function of numerous oncoproteins, and it can be argued that cancer cells are 'addicted' to HSP90. However, although recent reports of the early clinical efficacy of HSP90 inhibitors are encouraging, the optimal use of HSP90-targeted therapeutics will depend on understanding the complexity of HSP90 regulation and the degree to which HSP90 participates in both neoplastic and normal cellular physiology.
Trepel
Jane
J
Medical Oncology Branch Center for Cancer Research, National Cancer Institute, Building 10, room 1-5940, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Mollapour
Mehdi
M
Giaccone
Giuseppe
G
Neckers
Len
L
D000818:Animals; D042002:Chromatin Assembly and Disassembly; D002986:Clinical Trials as Topic; D004249:DNA Damage; D019008:Drug Resistance, Neoplasm; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000502:physiology; D006801:Humans; D009154:Mutation; D009369:Neoplasms / Q000188:drug therapy*; D010766:Phosphorylation; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D014158:Transcription, Genetic
D018841:HSP90 Heat-Shock Proteins