Extensive shape shifting underlies functional versatility of arrestins

Current Opinion in Cell Biology

Volumn 27, Issue 1, 2014, Pages 1-9

  Gurevich, Vsevolod V ^a   Gurevich, Eugenia V ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE 12; MITOGEN ACTIVATED PROTEIN KINASE 3; RETINA S ANTIGEN; RHODOPSIN; PROTEIN BINDING;

BINDING SITE; CELLULAR DISTRIBUTION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DELETION MUTANT; ENZYME PHOSPHORYLATION; MICROTUBULE; PHYSIOLOGICAL PROCESS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; RECEPTOR BINDING; REVIEW; SHAPE SHIFTING; STOICHIOMETRY; UBIQUITINATION; ANIMAL; CHEMISTRY; HUMAN; METABOLISM; PHOSPHORYLATION; PROTEIN CONFORMATION; SIGNAL TRANSDUCTION;

ANIMALS; ARRESTINS; HUMANS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION;

EID: 84887572409     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2013.10.007     Document Type: Review

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