Identification of Amino Acids Critical for the DNA Binding and Dimerization Properties of the Human Retinoic Acid Receptor α

This publication has 34 references indexed in Scilit:

• The Ligand Binding Domain of the Human Retinoic Acid Receptor γ Is Predominantly α-Helical with a Trp Residue in the Ligand Binding Site
  Published by Elsevier ,1995
• Structural Determinants of the Ligand-Binding Site of the Human Retinoic Acid Receptor .alpha.
  Biochemistry, 1995
• Purification and functional characterization of the ligand-binding domain from the retinoic acid receptor alpha: Evidence that sulfhydryl groups are involved in ligand-receptor interactions
  Biochemistry, 1993
• Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers.
  Genes & Development, 1993
• Determinants for selective RAR and TR recognition of direct repeat HREs.
  Genes & Development, 1993
• Identification of human, mouse, and rat retinoic acid receptor α using monoclonal antibodies
  Biochemical and Biophysical Research Communications, 1992
• Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling
  Nature, 1992
• Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors
  Nature, 1992
• Inhibition of glucocorticoid receptor transformation, subunit dissociation, and temperature-dependent inactivation by various N-substituted maleimides
  Biochemistry, 1988
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976