Characterization of heat shock protein 90 in the shrimpMetapenaeus ensis: Evidence for its role in the regulation of vitellogenin synthesis

2008 ◽  
Vol 75 (5) ◽  
pp. 952-959 ◽  
Author(s):  
Long Tao Wu ◽  
Ka Hou Chu
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Vitellogenin Synthesis

Purification of heat shock protein 90 from calf uterus and rat liver and characterization of the highly hydrophobic region

1989 ◽  
Vol 992 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Masaomi Iwasaki ◽  
Hiroyuki Saito ◽  
Masahide Yamamoto ◽  
Kenneth S. Korach ◽  
Tsuneyoshi Hirogome ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Rat Liver ◽  
Heat Shock Protein 90 ◽  
Hydrophobic Region ◽  
Highly Hydrophobic

scholarly journals Functional characterization of heat-shock protein 90 fromOryza sativaand crystal structure of its N-terminal domain

2015 ◽  
Vol 71 (6) ◽  
pp. 688-696 ◽  
Author(s):  
Swetha Raman ◽  
Kaza Suguna
Keyword(s):  
Crystal Structure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Biochemical Characterization ◽  
Functional Characterization ◽  
Cell Signalling ◽  
Physiological Role ◽  
Heat Shock Protein 90 ◽  
Terminal Domain

Heat-shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is essential for the normal functioning of eukaryotic cells. It plays crucial roles in cell signalling, cell-cycle control and in maintaining proteome integrity and protein homeostasis. In plants, Hsp90s are required for normal plant growth and development. Hsp90s are observed to be upregulated in response to various abiotic and biotic stresses and are also involved in immune responses in plants. Although there are several studies elucidating the physiological role of Hsp90s in plants, their molecular mechanism of action is still unclear. In this study, biochemical characterization of an Hsp90 protein from rice (Oryza sativa; OsHsp90) has been performed and the crystal structure of its N-terminal domain (OsHsp90-NTD) was determined. The binding of OsHsp90 to its substrate ATP and the inhibitor 17-AAG was studied by fluorescence spectroscopy. The protein also exhibited a weak ATPase activity. The crystal structure of OsHsp90-NTD was solved in complex with the nonhydrolyzable ATP analogue AMPPCP at 3.1 Å resolution. The domain was crystallized by cross-seeding with crystals of the N-terminal domain of Hsp90 fromDictyostelium discoideum, which shares 70% sequence identity with OsHsp90-NTD. This is the second reported structure of a domain of Hsp90 from a plant source.

scholarly journals In vitro Biological Characterization of a Novel, Synthetic Diaryl Pyrazole Resorcinol Class of Heat Shock Protein 90 Inhibitors

2007 ◽  
Vol 67 (5) ◽  
pp. 2206-2216 ◽  
Author(s):  
Swee Y. Sharp ◽  
Kathy Boxall ◽  
Martin Rowlands ◽  
Chrisostomos Prodromou ◽  
S. Mark Roe ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Biological Characterization

696 CHARACTERIZATION OF A C-TERMINAL HEAT SHOCK PROTEIN 90 INHIBITOR IN PROSTATE CANCER CELLS

2010 ◽  
Vol 183 (4S) ◽  
Author(s):  
Heidi A. Penn ◽  
Craig A. Manthe ◽  
Shawna B. Comer ◽  
George A. Vielhauer ◽  
Roger J. Rajewski ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 90 ◽  
Prostate Cancer Cells
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