Mechanisms for inhibition of the catalytic activity of adenylate cyclase by the guanine nucleotide-binding proteins serving as the substrate of islet-activating protein, pertussis toxin.

This publication has 40 references indexed in Scilit:

• Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein
  Nature, 1985
• Dual pathways of receptor-mediated cyclic GMP generation in NG108-15 cells as differentiated by susceptibility to islet-activating protein, pertussis toxin
  Archives of Biochemistry and Biophysics, 1985
• Stimulatory GTP regulatory unit Ns and the catalytic unit of adenylate cyclase are tightly associated: mechanistic consequences.
  Proceedings of the National Academy of Sciences, 1984
• Reconstitution of catecholamine-stimulated binding of guanosine 5'-O-(3-thiotriphosphate) to the stimulatory GTP-binding protein of adenylate cyclase
  Biochemistry, 1984
• G proteins and dual control of adenylate cyclase
  Cell, 1984
• Islet-activating protein, pertussis toxin: a probe for functions of the inhibitory guanine nucleotide regulatory component of adenylate cyclase
  Trends in Pharmacological Sciences, 1984
• Reconstitution of catecholamine-stimulated guanosine triphosphatase activity
  Biochemistry, 1983
• Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein.
  Proceedings of the National Academy of Sciences, 1982
• A highly sensitive adenylate cyclase assay
  Analytical Biochemistry, 1974
• A rapid, sensitive, and specific method for the determination of protein in dilute solution
  Analytical Biochemistry, 1973