Results 211 to 220 of about 137,496 (252)

Heat shock protein 90

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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Targeting Heat Shock Protein 90 for Malaria

Mini-Reviews in Medicinal Chemistry, 2013
Heat 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, Dhaval, Patel, I, Ramya, Mukesh, Nandave, Prashant S, Kharkar   +4 more
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The heat shock protein 90 of Leishmania donovani

Medical Microbiology and Immunology, 2001
The 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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Heat Shock Protein 90 Inhibitors as Therapeutic Agents

Recent Patents on Anti-Cancer Drug Discovery, 2012
The 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, SALA, MARINA, Musella S, CAMPIGLIA, Pietro   +3 more
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EC144 Is a Potent Inhibitor of the Heat Shock Protein 90

Journal of Medicinal Chemistry, 2012
Alkyne 40, 5-(2-amino-4-chloro-7-((4-methoxy-3,5-dimethylpyridin-2-yl)methyl)-7H-pyrrolo[2,3-d]pyrimidin-5-yl)-2-methylpent-4-yn-2-ol (EC144), is a second generation inhibitor of heat shock protein 90 (Hsp90) and is substantially more potent in vitro and in vivo than the first generation inhibitor 14 (BIIB021) that completed phase II clinical trials ...
Jiandong, Shi, Ryan, Van de Water, Kevin, Hong, Ryan B, Lamer, Kenneth W, Weichert, Cristina M, Sandoval, Srinivas R, Kasibhatla, Marcus F, Boehm, Jianhua, Chao, Karen, Lundgren, Noelito, Timple, Rachel, Lough, Gerardo, Ibanez, Christina, Boykin, Francis J, Burrows, Marilyn R, Kehry, Theodore J, Yun, Erin K, Harning, Christine, Ambrose, Jeffrey, Thompson, Sarah A, Bixler, Anthone, Dunah, Pamela, Snodgrass-Belt, Joseph, Arndt, Istvan J, Enyedy, Ping, Li, Victor S, Hong, Andres, McKenzie, Marco A, Biamonte   +28 more
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Heat Shock Protein 90: A Unique Chemotherapeutic Target

Seminars in Oncology, 2006
A 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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Potent Triazolothione Inhibitor of Heat‐Shock Protein‐90

Chemical Biology & Drug Design, 2009
Heat‐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, Bob, Mintzer, Daguang, Zhu, James M, Wu, Sandra L, Biroc, Shendong, Yuan, Kumar, Emayan, Zheng, Chang, Deborah, Chen, Damian O, Arnaiz, Judi, Bryant, Xue Snow, Ge, Marc, Whitlow, Marc, Adler, Mark A, Polokoff, Wei-Wei, Li, Mike, Ferrer, Takashi, Sato, Jian-Ming, Gu, Jun, Shen, Jih-Lie, Tseng, Harald, Dinter, Brad, Buckman   +22 more
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Characterization of the Hydrophobic Region of Heat Shock Protein 90

The Journal of Biochemistry, 1991
The 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, Y, Takahashi, K, Inano, T, Horigome, H, Sugano   +4 more
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Heat-shock protein 90

Life Sciences, 2000
Valérie Montel, Florence Gardrat, Jean-Louis Azanza, Jacques Raymond   +3 more
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Heat-shock protein 90, a chaperone for folding and regulation

Cellular and Molecular Life Sciences, 2002
Heat-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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