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- W1536093676 abstract "This chapter focuses on the regulation of adrenergic receptor function by phosphorylation. The various subtypes of receptors for catecholamines, termed adrenergic receptors, represent excellent models for the study of receptor mediated transmembrane signaling systems. Adrenergic receptors represent the first point of interaction of catecholamines with their target cells. Hence, it seems intuitively likely that an important point of regulation for controlling cellular sensitivity to catecholamine action might be at the level of the receptors. Over the past decade a great deal of evidence has accumulated which indicates that the functional status of the receptors is not fixed but rather is subject to various forms of dynamic regulation. Moreover, quite recently it has become clear that a major mechanism for regulating adrenergic receptor function is by covalent modification involving phosphorylation-dephosphorylation reactions. A major development which has made the study of the covalent modification of adrenergic receptors possible has been the advent of techniques for purifying and characterizing these receptors. Two techniques provided the basis for these successes. These are biospecific affinity chromatography, highly specific affinity, and photoaffinity probes for covalent labeling of the receptor proteins at various stages during their purification." @default.
- W1536093676 created "2016-06-24" @default.
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- W1536093676 date "1986-01-01" @default.
- W1536093676 modified "2023-10-16" @default.
- W1536093676 title "Regulation of Adrenergic Receptor Function by Phosphorylation" @default.
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- W1536093676 doi "https://doi.org/10.1016/b978-0-12-152828-7.50007-x" @default.
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