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G protein effector coupling interaction of recombinant inhibitory gamma subunit and its mutant forms with transducin and catalytic subunits of the cyclic gmp phosphodiesterase


G protein effector coupling interaction of recombinant inhibitory gamma subunit and its mutant forms with transducin and catalytic subunits of the cyclic gmp phosphodiesterase



Journal of Cellular Biochemistry Suppl (14 Part C): 141



ISSN/ISBN: 0730-2312


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Accession: 031527947

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Related references

G protein-effector coupling: interactions of recombinant inhibitory gamma subunit with transducin and phosphodiesterase. Biochemistry 28(15): 6145-6150, 1989

G protein-effector coupling: interactions of recombinant inhibitory c subunit with transducin and phosphodiesterase. Biochemistry (American Chemical Society) 28: 45-50, 1989

G protein-effector coupling: interactions of recombinant inhibitory γ-subunit with transducin and phosphodiesterase. Biochemistry (Easton) 28(15): 6145-6150, 1989

Photoreceptor phosphodiesterase: interaction of inhibitory gamma subunit and cyclic GMP with specific binding sites on catalytic subunits. Methods 14(1): 93-104, 1998

Site-directed mutagenesis of the cGMP phosphodiesterase inhibitory gamma subunit from bovine rod outer segments: A new hypothesis on the mechanisms of catalytic subunits inhibition by gamma subunit and holoenzyme activation by transducin. Bioorganicheskaya Khimiya 20(8-9): 821-832, 1994

G protein-effector coupling: binding of rod phosphodiesterase inhibitory subunit to transducin. Biochemistry 28(8): 3133-3137, 1989

The carboxyl terminus of the gamma-subunit of rod cGMP phosphodiesterase contains distinct sites of interaction with the enzyme catalytic subunits and the alpha-subunit of transducin. Journal of Biological Chemistry 270(22): 13210-13215, 1995

Site-directed mutagenesis of the cGMP phosphodiesterase gamma subunit from bovine rod outer segments: role of separate amino acid residues in the interaction with catalytic subunits and transducin alpha subunit. Biochimica et Biophysica Acta 1176(3): 250-256, 1993

Oligonucleotide-directed mutagenesis of inhibitory gamma-subunits of cGMP phosphodiesterase from bovine outer rod segments. A new hypothesis on mechanisms for inhibiting catalytic subunits by gamma-subunits and activation of a holoenzyme by transducin. Bioorganicheskaia Khimiia 20(8-9): 821-832, 1994

Binding of the gamma-subunit of retinal rod-outer-segment phosphodiesterase with both transducin and the catalytic subunits of phosphodiesterase. Biochemical Journal 271(3): 721-727, 1990

Binding of gamma subunit of retinal rod outer segment phosphodiesterase with both transducin and the catalytic subunits of phosphodiesterase. Biochemical Journal 271(3): 721-728, 1990

Identification of the retinal cyclic GMP phosphodiesterase inhibitory gamma-subunit interaction sites on the catalytic alpha-subunit. Journal of Biological Chemistry 266(25): 16607-16613, 1991

The carboxyl terminus of the c-subunit of rod cGMP phosphodiesterase contains distinct sites of interaction with the enzyme catalytic subunits and the a-subunit of transducin. The Journal of Biological Chemistry 270: 210-15, 1995

Site-directed mutagenesis of the cGMP phosphodiesterase γ subunit from bovine rod outer segments : role of separate amino acid residues in the interaction with catalytic subunits and transducin α subunit. Biochimica et Biophysica Acta. Molecular cell Research 1176(3): 250-256, 1993

Site-directed mutagenesis of the cGMP phosphodiesterase subunit from bovine rod outer segments: Role of separate amino acid residues in the interaction with catalytic subunits and transducin a subunit. Biochimica et Biophysica Acta - Molecular Cell Research 1176(3): 250-256, 1993