Results 11 to 20 of about 60,329 (293)
Altered expression of beta-adrenergic receptor kinase and beta 1-adrenergic receptors in the failing human heart. [PDF]
Circulation, 1993 BACKGROUND In chronic heart failure, the positive inotropic effects of beta-adrenergic receptor agonists are greatly reduced, in part as a result of two alterations of the cardiac beta-adrenergic receptors: loss of their function (receptor uncoupling) and reduction of their number (downregulation).
Martin Ungerer +4 more
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Rapid desensitization of neonatal rat liver beta-adrenergic receptors. A role for beta-adrenergic receptor kinase. [PDF]
Journal of Clinical Investigation, 1994 Exposure of beta-adrenergic receptors (BAR) to agonists often leads to a rapid loss of receptor responsiveness. The proposed mechanisms of such rapid receptor desensitization include receptor phosphorylation by either cAMP-dependent protein kinase or the specific beta-adrenergic receptor kinase (BARK), leading to functional uncoupling from adenylyl ...
Irene García-Higuera, Federico Mayor
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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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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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Journal of Biological Chemistry, 1987 Desensitization of the beta-adrenergic receptor, a receptor which is coupled to the stimulation of adenylate cyclase, may be regulated via phosphorylation by a unique protein kinase. This recently discovered enzyme, known as the beta-adrenergic receptor kinase, only phosphorylates the agonist-occupied form of the beta-adrenergic receptor.
J.L. Benovic +7 more
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Inhibition of beta-adrenergic receptor kinase prevents rapid homologous desensitization of beta 2-adrenergic receptors. [PDF]
Proceedings of the National Academy of Sciences, 1989 Homologous (agonist-specific) desensitization of beta-adrenergic receptors (beta ARs) is accompanied by and appears to require phosphorylation of the receptors. We have recently described a novel protein kinase, beta AR kinase, which phosphorylates beta ARs in vitro in an agonist-dependent manner.
Martin J. Lohse +3 more
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Essential role of beta-adrenergic receptor kinase 1 in cardiac development and function [PDF]
Proceedings of the National Academy of Sciences, 2021 The β-adrenergic receptor kinase 1 (βARK1) is a member of the G protein-coupled receptor kinase (GRK) family that mediates the agonist-dependent phosphorylation and desensitization of G protein-coupled receptors. We have cloned and disrupted the βARK1 gene in mice by homologous recombination. No homozygote βARK1 −/−
Mohamed Jaber +9 more
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Rapid agonist‐induced beta‐adrenergic receptor kinase translocation in C6 glioma cells [PDF]
FEBS Letters, 1992 Exposure of C6 glioma cells to 1 μM isoproterenol leads to fast desensitization of the β‐adrenergic receptor/adenylyl cyclase system and transient receptor sequestration. It also triggers a very rapid and transient translocation to the plasma membrane or β‐adrenergic receptor kinase (βARK), a specific cytoplasmic kinase that phosphorylates only the ...
Irene García-Higuera, Federico Mayor
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