Visual arrestin binding to rhodopsin. Intramolecular interaction between the basic N terminus and acidic C terminus of arrestin may regulate binding selectivity.-Reference-Cited by-同舟云学术

Visual arrestin binding to rhodopsin. Intramolecular interaction between the basic N terminus and acidic C terminus of arrestin may regulate binding selectivity.

Published:1994-03 Issue:12 Volume:269 Page:8721-8727
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Gurevich V.V.,Chen C.Y.,Kim C.M.,Benovic J.L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference21 articles.

1. Amplification and Adaptation in Regulatory and Sensory Systems

2. Molecular Biology of Receptors and Transporters: Receptors;Hargrave,1992

3. Chapter 5 Interactions between photoexcited rhodopsin and light-activated enzymes in rods

4. Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites

5. 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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