Targeting the dynamic HSP90 complex in cancer
J Trepel, M Mollapour, G Giaccone, L Neckers - Nature reviews cancer, 2010 - nature.com
J Trepel, M Mollapour, G Giaccone, L Neckers
Nature reviews cancer, 2010•nature.comThe 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.
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.
Abstract
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.
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