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

Eitemau Tebyg

• The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor
  gan: Bouhouche-Chatelier, Ilham, et al.
  Cyhoeddwyd: (2001)
• The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter
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  Cyhoeddwyd: (1999)
• Targeting the Heat Shock Protein 90 Dimer with Dimeric Inhibitors
  gan: Kusuma, Bhaskar Reddy, et al.
  Cyhoeddwyd: (2011)
• Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
  gan: Schulte, Theodor W., et al.
  Cyhoeddwyd: (1998)
• Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle
  gan: Ratzke, C., et al.
  Cyhoeddwyd: (2010)