Results 261 to 270 of about 310,958 (294)
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Current Opinion in Oncology, 2003
Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability and function of a number of conditionally activated and/or expressed signaling proteins, as well as multiple mutated, chimeric, or overexpressed signaling proteins, which promote cancer cell growth or survival or both.
Len, Neckers, S Percy, Ivy
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Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability and function of a number of conditionally activated and/or expressed signaling proteins, as well as multiple mutated, chimeric, or overexpressed signaling proteins, which promote cancer cell growth or survival or both.
Len, Neckers, S Percy, Ivy
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Targeting Heat Shock Protein 90 for Malaria
Mini-Reviews in Medicinal Chemistry, 2013Heat shock protein 90 (Hsp90), an ATP-dependent molecular chaperone, is a highly conserved and ubiquitously expressed stress protein in eukaryotes. It is responsible for activation of various proteins involved in signal transduction, cell cycle control, hormone signaling, and transcription.
Anup S, Ramdhave +4 more
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Heat Shock Protein 90 Inhibitors as Therapeutic Agents
Recent Patents on Anti-Cancer Drug Discovery, 2012The molecular chaperone heat shock protein 90 (HSP90) is essential for the folding stability, intracellular disposition and proteolytic turnover of many of the key regulators of cell growth, differentiation and survival. These essential functions are used by the cells during the oncogenesis process to allow the tumor transformation and facilitate the ...
Gomez Monterrey I +3 more
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Heat-Shock Protein 90–Targeted Nano Anticancer Therapy
Journal of Pharmaceutical Sciences, 2016Suboptimal chemotherapy of anticancer drugs may be attributed to a variety of cellular mechanisms, which synergize to dodge the drug responses. Nearly 2 decades of heat-shock protein 90 (Hsp90)-targeted drug discovery has shown that the mono-therapy with Hsp90 inhibitors seems to be relatively ineffective compared with combination treatment due to ...
Ankit K, Rochani +4 more
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Heat Shock Protein 90: A Unique Chemotherapeutic Target
Seminars in Oncology, 2006A large body of work spanning the past decade has identified the molecular chaperone heat shock protein 90 (Hsp90) as a critical modulator of an extensive network of cellular signaling pathways. Many of the processes overseen by Hsp90 are deregulated in tumor cells, including cell cycle control, gene transcription, and apoptotic signaling.
Sara B, Cullinan, Luke, Whitesell
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The heat shock protein 90 of Leishmania donovani
Medical Microbiology and Immunology, 2001The 90-kDa heat shock protein (Hsp90) of Leishmania donovani is a highly abundant cytoplasmic protein and is involved in a variety of cellular processes. Pharmacological deactivation of Hsp90 leads to growth arrest and induces the synthesis of heat shock proteins. Moreover, treatment of promastigote parasites with Hsp90 inhibitors induces the synthesis
M, Wiesgigl, J, Clos
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Potent Triazolothione Inhibitor of Heat‐Shock Protein‐90
Chemical Biology & Drug Design, 2009Heat‐shock protein‐90 is an attractive target for anticancer drugs, as heat‐shock protein‐90 blockers such as the ansamycin 17‐(allylamino)‐17‐demethoxygeldanamycin greatly reduce the expression of many signaling molecules that are disregulated in cancer cells and are key drivers of tumor growth and metastasis.
Richard I, Feldman +22 more
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Heat Shock Protein 90: Truly Moonlighting!
2018Hsp90 is an essential and abundantly expressed molecular chaperone in any living cell. The multiplicity of Hsp90 cellular functions is driven by its interaction with a broad range of partner proteins and thereby establishing itself as a moonlighting molecule.
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The contemporary management of cancers of the sinonasal tract in adults
Ca-A Cancer Journal for Clinicians, 2023Rajat Thawani
exaly