The Carboxyl Terminus of the γ-Subunit of Rod cGMP Phosphodiesterase Contains Distinct Sites of Interaction with the Enzyme Catalytic Subunits and the α-Subunit of Transducin
Open Access
- 1 June 1995
- journal article
- Published by Elsevier
- Vol. 270 (22) , 13210-13215
- https://doi.org/10.1074/jbc.270.22.13210
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Analysis and prediction of the different types of β-turn in proteinsPublished by Elsevier ,2004
- Functional regions of the inhibitory subunit of retinal rod cGMP phosphodiesterase identified by site-specific mutagenesis and fluorescence spectroscopyBiochemistry, 1992
- A site on rod G protein alpha subunit that mediates effector activationScience, 1992
- Identification of effector-activating residues of GsαCell, 1992
- Identification of the γ-subunit interaction sites in the retinal cyclic-GMP phosphodiesterase β-subunitBiochemical and Biophysical Research Communications, 1991
- Subunit stoichiometry of retinal rod cGMP phosphodiesteraseBiochemistry, 1990
- Active sites of the cyclic GMP phosphodiesterase γ‐subunit of retinal rod outer segmentsFEBS Letters, 1988
- Cyclic GMP phosphodiesterase from bovine retina Amino acid sequence of the α‐subunit and nucleotide sequence of the corresponding cDNAFEBS Letters, 1987
- Cyclic GMP phosphodiesterase from cattle retinaFEBS Letters, 1986
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976