G-Protein-Coupled Receptor Kinase 1
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Subject Areas on Research
- Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor.
- Ca(2+)-dependent interaction of recoverin with rhodopsin kinase.
- Cyclic phosphorylation-dephosphorylation of rhodopsin in retina by protein kinase FA (the activator of ATP.Mg-dependent protein phosphatase).
- G protein-coupled receptor kinase and beta-arrestin-mediated desensitization of the angiotensin II type 1A receptor elucidated by diacylglycerol dynamics.
- G-protein-coupled receptors: regulatory role of receptor kinases and arrestin proteins.
- Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases.
- Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase.
- Mechanistic basis for the failure of cone transducin to translocate: why cones are never blinded by light.
- Onset of feedback reactions underlying vertebrate rod photoreceptor light adaptation.
- Phosphorylation of G protein-coupled receptor kinase 1 (GRK1) is regulated by light but independent of phototransduction in rod photoreceptors.
- Protein kinases that phosphorylate activated G protein-coupled receptors.
- Purification and characterization of the beta-adrenergic receptor kinase.
- RGS expression rate-limits recovery of rod photoresponses.
- Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems.
- Rhodopsin phosphorylation: from terminating single photon responses to photoreceptor dark adaptation.
- Role of acidic amino acids in peptide substrates of the beta-adrenergic receptor kinase and rhodopsin kinase.
- Role of beta-adrenergic receptor signaling and desensitization in heart failure: new concepts and prospects for treatment.
- The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase.