Essential role of the N-terminal domain in the regulation of RIG-I ATPase activity

Journal of Biological Chemistry

Volumn 283, Issue 14, 2008, Pages 9488-9496

  Gee, Peter ^a   Chua, Pong Kian ^a   Gevorkyan, Jirair ^a   Klumpp, Klaus ^a   Najera, Isabel ^a   Swinney, David C ^a   Deval, Jerome ^a  

^a ROCHE BIOSCIENCE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BINDING ENERGY; BIOCHEMISTRY; GLYCOPROTEINS; METAL IONS; METAL REFINING; MOLECULAR STRUCTURE; NUCLEIC ACIDS; PORT TERMINALS; SIGNAL TRANSDUCTION;

ACTIVE SITES; ANTIVIRAL RESPONSES; ATP HYDROLYSES; ATPASE ACTIVITIES; C TERMINUSES; CASPASE ACTIVATIONS; CELLULAR LEVELS; CYTOSOLIC RECEPTORS; DIVALENT CATIONS; DO-MAINS; ENZYMATIC FUNCTIONS; FUNCTIONAL PROTEINS; HELICASE; ION DEPENDENCES; RECEPTOR LEVELS; RETINOIC ACIDS; RNA BINDINGS; RNA LIGANDS; RNA STRUCTURES; SIGNAL ACTIVATIONS; TERMINAL DOMAINS; TRIPHOSPHATE; VIRAL RNAS;

RNA;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BETA INTERFERON; DIVALENT CATION; DOUBLE STRANDED RNA; METAL ION; RETINOIC ACID INDUCIBLE PROTEIN I; SINGLE STRANDED RNA; VIRUS RNA; CASPASE; METAL; RARRES3 PROTEIN, HUMAN; RECOMBINANT PROTEIN; RETINOIC ACID RECEPTOR; RNA BINDING PROTEIN;

ARTICLE; CLONING; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; HYDROLYSIS; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN RNA BINDING; RNA BINDING; RNA STRUCTURE; SIGNAL TRANSDUCTION; CELL LINE; ENZYME ACTIVATION; ENZYMOLOGY; GENETICS; IMMUNOLOGY; INNATE IMMUNITY; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; VIRUS INFECTION;

ADENOSINE TRIPHOSPHATASES; CASPASES; CATIONS, DIVALENT; CELL LINE; ENZYME ACTIVATION; HUMANS; IMMUNITY, NATURAL; INTERFERON-BETA; METALS; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, RETINOIC ACID; RECOMBINANT PROTEINS; RNA, VIRAL; RNA-BINDING PROTEINS; SIGNAL TRANSDUCTION; VIRUS DISEASES;

EID: 44049095441     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M706777200     Document Type: Article

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