Targeting the dynamic HSP90 complex in cancer
By J. Trepel, M. Mollapour, G. Giaccone, L. Neckers. Nature Reviews. Cancer, 2010
1,490 citations recorded by the source corpus.
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.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/74479a651519b1cffad438a4add4c43b79aca1cb
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Citations in the corpus
- SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. (2014, background): “HSP90 is an evolutionarily conserved molecular chaperone that is known to participate in stabilizing and activating more than 200 proteins, referred to as HSP90 ‘‘clients’’, many of which are essential for constitutive cell signaling and adaptive responses to various stresses [1,2].”
- RNA-Seq of Single Prostate CTCs Implicates Noncanonical Wnt Signaling in Antiandrogen Resistance (2015, neutral): “A total of 711 genes were highly expressed in CTCs compared to primary tumors, with the most enriched being the molecular chaperone HSP90AA1, which regulates the activation and stability of AR, among other functions (12), and the non-coding RNA transcript MALAT1, which has been implicated in alterna”