HSP90 and the chaperoning of cancer

By L. Whitesell, Susan Lindquist. Nature Reviews. Cancer, 2005

2,527 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e34790f37dfebc96fb1b498c2cc4be0e9b923259

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Citations in the corpus

HSP90 at the hub of protein homeostasis: emerging mechanistic insights (2010, background): “Structurally unrelated natural product inhibitors of HSP90 displace ATP and block HSP90 function with high specificit”
Successful applications of computer aided drug discovery: moving drugs from concept to the clinic. (2010, background): “The molecular chaperone heat shock protein 90 (HSP90) supports the correct conformation, stabilization, activation, and localization of ‘‘client’’ proteins, many of which are involved in tumor progression, hence HSP90 is an ideal and novel target in cancer therapy [71-74].”
Cholangiocarcinoma — evolving concepts and therapeutic strategies (2017, neutral): “HSP90 is a molecular chaperone required for essential cellular house keeping functions, such as protein folding and mediating posttranslational protein homeostasis, as well as for maintenance of oncoprotein stability 109 .”
SMYD2-dependent HSP90 methylation promotes cancer cell proliferation by regulating the chaperone complex formation. (2014, background): “293T cells were co-transfected with a FLAGSMYD2 expression vector and four different lengths of HA-HSP90AB1 vectors ([1–724], [1–500], [250–724] and [500–724]).”
Targeting the dynamic HSP90 complex in cancer (2010, background): “Therefore, HSP90 is recognized as a crucial facilitator of oncogene addiction and cancer cell surviva”
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. (2008, background): “…can influence the conformation and activities of a wide range of substrates such as p53 (Blagosklonny et al. 1996), HSF1 (Shi et al. 1998), and other transcription factors including steroid aporeceptors, in addition to kinases and phosphatases (Pratt and Toft 2003; Whitesell and Lindquist 2005).”
Anticancer activities of histone deacetylase inhibitors (2006, background): “Heat-shock protein 90 (Hsp90) is an abundant cellular chaperone whose overexpression in tumour cells correlates with poor prognosis and resistance to chemotherap”
Apoptosis and Molecular Targeting Therapy in Cancer (2014, background): “Conflict of Interests The authors declare that there is no conflict of interests regarding the publication of this paper.”
Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators. (2006, neutral): “Only two other existing drugs, cisplatin and novobiocin, act directly on HSP90 outside this fold by binding the C-terminal domain, and even these only induce HSP90 inhibition at high concentrations at which other mechanisms of action likely predominate (Marcu et al., 2000; Whitesell and Lindquist, ”
HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers. (2012, background): “These include elevated temperatures, oxidative agents, heavy metals, and low pH. Organisms respond by inducing heat-shock proteins (HSPs), which act as molecular chaperones to restore protein homeostasis (Shamovsky and Nudler, 2008; Whitesell and Lindquist, 2005).”