Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase (Q28287485)

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English	Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase	scientific article

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Light-dependent phosphorylation of rhodopsin by beta-adrenergic receptor kinase (English)

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phosphorylation

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Robert Lefkowitz

5

object named as

R J Lefkowitz

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4

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M G Caron

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author name string

J L Benovic

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F Mayor

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R L Somers

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language of work or name

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321

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6073

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869-72

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Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments

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Adenylate cyclase-coupled beta-adrenergic receptors: structure and mechanisms of activation and desensitization

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Cloning of the gene and cDNA for mammalian beta-adrenergic receptor and homology with rhodopsin

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Molecular mechanisms of receptor desensitization using the beta-adrenergic receptor-coupled adenylate cyclase system as a model

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ATP mediates rapid reversal of cyclic GMP phosphodiesterase activation in visual receptor membranes

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Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments

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Light dependent phosphorylation of rhodopsin by ATP.

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Phosphorylation of frog photoreceptor membranes induced by light

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Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor

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The decay of long-lived photoproducts in the isolated bullfrog rod outer segment: Relationship to other dark reactions

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Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites

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The partial primary structure of bovine rhodopsin and its topography in the retinal rod cell disc membrane

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GTP binding protein: properties and lack of activation by phosphorylated rhodopsin.

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Phorbol esters promote alpha 1-adrenergic receptor phosphorylation and receptor uncoupling from inositol phospholipid metabolism

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Mammalian .beta.2-adrenergic receptor: purification and characterization

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Pure β-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclase

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Rhodopsin and bacteriorhodopsin: structure-function relationships

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10.1038/321869A0

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