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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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Characterization of the Hydrophobic Region of Heat Shock Protein 90
The Journal of Biochemistry, 1991The modes of binding of heat shock protein 90 with phenyl-Sepharose, myristoylated AE-cellulose, and monomyristoylated lysozyme were studied to characterize a hydrophobic region(s) on the surface of the heat shock protein 90 molecule and the following results were obtained. (1) The binding of heat shock protein 90 with phenyl-Sepharose was inhibited by
M, Yamamoto +4 more
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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, a chaperone for folding and regulation
Cellular and Molecular Life Sciences, 2002Heat-shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone that is essential for viability in eukaryotes. Hsp90 fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins.
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