Mechanism of Phosphorylation-Recognition by Visual Arrestin and the Transition of Arrestin into a High Affinity Binding State-Reference-Cited by-同舟云学术

Mechanism of Phosphorylation-Recognition by Visual Arrestin and the Transition of Arrestin into a High Affinity Binding State

Published:1997-01-01 Issue:1 Volume:51 Page:161-169
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

Gurevich Vsevolod V.,Benovic Jeffrey L.

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference25 articles.

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2. Inactivation of photoexcited rhodopsin in retinal rods: the roles of rhodopsin kinase and 48-kDa protein (arrestin)

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

4. Cell-free expression of visual arrestin: truncation mutagenesis identifies multiple domains involved in rhodopsin interaction.;Gurevich;J. Biol. Chem.,1992

5. Visual arrestin interaction with rhodopsin: sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin.;Gurevich;J. Biol. Chem.,1993

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