Results 11 to 20 of about 24,774 (261)
Beta-adrenergic receptor kinase. Agonist-dependent receptor binding promotes kinase activation.
Journal of Biological Chemistry, 1993 The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the activated form of multiple receptors such as the beta 2-adrenergic receptor (beta 2 AR) and rhodopsin. beta ARK also phosphorylates synthetic peptides, albeit with an approximately 10(4)-10(7)-fold lower Vmax/Km ratio as compared to receptors, with a clear preference for ...
Ching‐Yu Chen +3 more
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Journal of Biological Chemistry, 1994 The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the activated form of the beta 2-adrenergic receptor (beta 2AR) and related G protein-coupled receptors. To further elucidate the role of beta ARK in receptor desensitization, we generated a beta ARK dominant negative mutant by converting an invariant lysine residue in the ...
Guanghui Kong +2 more
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Journal of Biological Chemistry, 1993 Receptor-specific or homologous desensitization of beta 2-adrenergic receptors is thought to be effected via phosphorylation of the receptor by the beta-adrenergic receptor kinase (beta ARK), followed by binding of beta-arrestin. We have generated stably transfected Chinese hamster ovary cell lines overexpressing either of the two regulatory proteins ...
Susanne Pippig +6 more
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Purification and characterization of the beta-adrenergic receptor kinase.
Journal of Biological Chemistry, 1987 The beta-adrenergic receptor kinase (beta-ARK) is a recently discovered enzyme which specifically phosphorylates the agonist-occupied form of the beta-adrenergic receptor (beta-AR) as well as the light-bleached form of rhodopsin. beta-ARK is present in a wide variety of mammalian tissues.
Jeffrey Benovic +4 more
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Comparative rates of desensitization of beta-adrenergic receptors by the beta-adrenergic receptor kinase and the cyclic AMP-dependent protein kinase. [PDF]
Proceedings of the National Academy of Sciences, 1991 Three separate processes may contribute to rapid beta-adrenergic receptor desensitization: functional uncoupling from the stimulatory guanine nucleotide-binding protein Gs, mediated by phosphorylation of the receptors by two distinct kinases, the specific beta-adrenergic receptor kinase (beta ARK) and the cyclic AMP-dependent protein kinase A (PKA), as
Neil S. Roth +4 more
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Mechanism of beta-adrenergic receptor kinase activation by G proteins
Journal of Biological Chemistry, 1993 The beta-adrenergic receptor kinase (beta-ARK) specifically phosphorylates the activated form of various G protein-coupled receptors such as the beta 2-adrenergic receptor (beta 2-AR). Recently, G protein beta gamma subunits have been demonstrated to activate beta-ARK-mediated receptor phosphorylation.
C.M. Kim, Sarah Dion, Jeffrey Benovic
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The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase. [PDF]
Proceedings of the National Academy of Sciences, 1991 Light-dependent deactivation of rhodopsin as well as homologous desensitization of beta-adrenergic receptors involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase (RK) and beta-adrenergic receptor kinase (beta ARK), respectively. We report here the cloning of a complementary DNA for RK.
W Lorenz +5 more
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Reduced beta-adrenergic receptor activation decreases G-protein expression and beta-adrenergic receptor kinase activity in porcine heart. [PDF]
Journal of Clinical Investigation, 1995 To determine whether beta-adrenergic receptor agonist activation influences guanosine 5'-triphosphate-binding protein (G-protein) expression and beta-adrenergic receptor kinase activity in the heart, we examined the effects of chronic beta 1-adrenergic receptor antagonist treatment (bisoprolol, 0.2 mg/kg per d i.v., 35 d) on components of the ...
Peipei Ping +5 more
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