The Catalytic and GAF Domains of the Rod cGMP Phosphodiesterase (PDE6) Heterodimer Are Regulated by Distinct Regions of Its Inhibitory γ Subunit
Open Access
- 1 July 2001
- journal article
- Published by Elsevier
- Vol. 276 (29) , 27527-27534
- https://doi.org/10.1074/jbc.m103316200
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Amplification and kinetics of the activation steps in phototransductionPublished by Elsevier ,2003
- Probing Domain Functions of Chimeric PDE6α′/PDE5 cGMP-PhosphodiesterasePublished by Elsevier ,1998
- Residues within the Polycationic Region of cGMP Phosphodiesterase γ Subunit Crucial for the Interaction with Transducin α SubunitJournal of Biological Chemistry, 1997
- The γ Subunit of Rod cGMP-Phosphodiesterase Blocks the Enzyme Catalytic SiteJournal of Biological Chemistry, 1997
- An Interface of Interaction between Photoreceptor cGMP Phosphodiesterase Catalytic Subunits and Inhibitory γ SubunitsPublished by Elsevier ,1996
- High Affinity Interactions of GTPγS with the Heterotrimeric G Protein, TransducinPublished by Elsevier ,1996
- Discrimination of Two Functions of Photoreceptor cGMP Phosphodiesterase γ SubunitBiochemical and Biophysical Research Communications, 1996
- Activation of cGMP phosphodiesterase in retinal rods: mechanism of interaction with the GTP-binding protein (transducin)Biochemistry, 1989
- Active sites of the cyclic GMP phosphodiesterase γ‐subunit of retinal rod outer segmentsFEBS Letters, 1988
- Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reactionBiochemical Pharmacology, 1973