Purification and characterization of the beta-adrenergic receptor kinase.

This publication has 26 references indexed in Scilit:

• Light-dependent phosphorylation of rhodopsin by β-adrenergic receptor kinase
  Nature, 1986
• Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin
  Nature, 1986
• A novel catecholamine-activated adenosine cyclic 3',5'-phosphate independent pathway for .beta.-adrenergic receptor phosphorylation in wild-type and mutant S49 lymphoma cells: mechanism of homologous desensitization of adenylate cyclase
  Biochemistry, 1986
• Molecular mechanisms of receptor desensitization using the β-adrenergic receptor-coupled adenylate cyclase system as a model
  Nature, 1985
• Mammalian .beta.2-adrenergic receptor: purification and characterization
  Biochemistry, 1984
• Pure β-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclase
  Nature, 1983
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Phosphorylation of rhodopsin: Most rhodopsin molecules are not phosphorylated
  Biochemical and Biophysical Research Communications, 1974
• Light dependent phosphorylation of rhodopsin by ATP
  FEBS Letters, 1972
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970