How Does Arrestin Respond to the Phosphorylated State of Rhodopsin?
Open Access
- 1 April 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (17) , 11451-11454
- https://doi.org/10.1074/jbc.274.17.11451
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- The Selectivity of Visual Arrestin for Light-activated Phosphorhodopsin Is Controlled by Multiple Nonredundant MechanismsJournal of Biological Chemistry, 1998
- X-ray crystal structure of arrestin from bovine rod outer segmentsNature, 1998
- [26] Raster3D: Photorealistic molecular graphicsPublished by Elsevier ,1997
- [21] Use of bacteriophage RNA polymerase in RNA synthesisPublished by Elsevier ,1996
- Visual Arrestin Binding to RhodopsinJournal of Biological Chemistry, 1995
- Rhodopsin and phototransduction: a model system for G protein‐linked receptorsThe FASEB Journal, 1992
- Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin IIBiochemistry, 1989
- Inactivation of photoexcited rhodopsin in retinal rods: the roles of rhodopsin kinase and 48-kDa protein (arrestin)Biochemistry, 1988
- Primary and secondary structure of bovine retinal S antigen (48-kDa protein).Proceedings of the National Academy of Sciences, 1987
- Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments.Proceedings of the National Academy of Sciences, 1986