Sites of interaction between rod G-protein alpha-subunit and cGMP-phosphodiesterase gamma-subunit. Implications for the phosphodiesterase activation mechanism.

This publication has 27 references indexed in Scilit:

• Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP
  Nature, 1992
• Two-site high-affinity interaction between inhibitory and catalytic subunits of rod cyclic GMP phosphodiesterase
  Biochemical Journal, 1992
• Resonance energy transfer as a direct monitor of GTP-binding protein-effector interactions: activated .alpha.-transducin binding to the cGMP phosphodiesterase in the bovine phototransduction cascade
  Biochemistry, 1991
• A novel magnesium‐dependent mechanism for the activation of transducin by fluoride
  FEBS Letters, 1990
• Expression in bacteria of functional inhibitory subunit of retinal rod cGMP phosphodiesterase.
  Proceedings of the National Academy of Sciences, 1989
• G protein-effector coupling: binding of rod phosphodiesterase inhibitory subunit to transducin
  Biochemistry, 1989
• Molecular mechanism of visual transduction
  European Journal of Biochemistry, 1989
• cGMP phosphodiesterase of retinal rods is regulated by two inhibitory subunits.
  Proceedings of the National Academy of Sciences, 1988
• Activation of retinal rod cyclic GMP‐phosphodiesterase by transducin: Characterization of the complex formed by phosphodiesterase inhibitor and transducin α‐subunit
  Proteins-Structure Function and Bioinformatics, 1986
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976