Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

Những quyển sách tương tự

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• The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter
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  Được phát hành: (1999)
• Targeting the Heat Shock Protein 90 Dimer with Dimeric Inhibitors
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• Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
  Bằng: Schulte, Theodor W., et al.
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• Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle
  Bằng: Ratzke, C., et al.
  Được phát hành: (2010)