Heat shock protein hsp90 regulates dioxin receptor function in vivo.

Míreanna Comhchosúla

• Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains.
  le: Antonsson, C, et al.
  Foilsithe: (1995)
• A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
  le: McGuire, J, et al.
  Foilsithe: (1994)
• The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein.
  le: Wilhelmsson, A, et al.
  Foilsithe: (1990)
• Definition of a novel ligand binding domain of a nuclear bHLH receptor: co-localization of ligand and hsp90 binding activities within the regulable inactivation domain of the dioxin receptor.
  le: Whitelaw, M L, et al.
  Foilsithe: (1993)
• The hsp90 Chaperone Complex Regulates Intracellular Localization of the Dioxin Receptor
  le: Kazlauskas, Arunas, et al.
  Foilsithe: (2001)