The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding

Journal of Neurochemistry

Volumn 84, Issue 5, 2003, Pages 1040-1050

  Raman, Dayanidhi ^a   Osawa, Shoji ^a   Gurevich, Vsevolod V ^b   Weiss, Ellen R ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Arrestin; Desensitization; GRK1; Retina; Rhodopsin; Rod

Indexed keywords

CALPAIN; G PROTEIN COUPLED RECEPTOR KINASE; RETINA S ANTIGEN; RHODOPSIN;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; DESENSITIZATION; DISSOCIATION; EMBRYO; HUMAN; HUMAN CELL; PHOTOTRANSDUCTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RETINA ROD;

AMINO ACID SUBSTITUTION; ANIMALS; ARRESTIN; CALPAIN; CATTLE; HUMANS; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RHODOPSIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0037340792     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.01598.x     Document Type: Article

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