Characterization of the Phosphorylation Sites Involved in G Protein-coupled Receptor Kinase- and Protein Kinase C-mediated Desensitization of the α1B-Adrenergic Receptor
Open Access
- 1 November 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (45) , 28712-28719
- https://doi.org/10.1074/jbc.272.45.28712
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Effect of Different G Protein-coupled Receptor Kinases on Phosphorylation and Desensitization of the α1B-Adrenergic ReceptorJournal of Biological Chemistry, 1996
- Rhodopsin Kinase AutophosphorylationPublished by Elsevier ,1995
- Control of Rhodopsin Multiple PhosphorylationBiochemistry, 1994
- Sequential phosphorylation of rhodopsin at multiple sitesBiochemistry, 1993
- The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase.Proceedings of the National Academy of Sciences, 1991
- MODEL SYSTEMS FOR THE STUDY OF SEVEN-TRANSMEMBRANE-SEGMENT RECEPTORSAnnual Review of Biochemistry, 1991
- Turning off the signal: desensitization of β‐adrenergic receptor functionThe FASEB Journal, 1990
- Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein).Proceedings of the National Academy of Sciences, 1987
- Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor.Proceedings of the National Academy of Sciences, 1986
- 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