ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2α (eIF2α) and protein phosphatase 1

Journal of Biological Chemistry

Volumn 286, Issue 28, 2011, Pages 24785-24792

  Li, Yapeng ^a   Zhang, Cuizhu ^a   Chen, Xiangdong ^a   Yu, Jia ^a   Wang, Yu ^a   Yang, Yin ^a   Du, Mingjuan ^a   Jin, Huali ^b   Ma, Yijie ^b   He, Bin ^b   Cao, Youjia ^a  

^a NANKAI UNIVERSITY   (China)

^b UNIVERSITY OF ILLINOIS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MOTIF; DELETION MUTATIONS; DEPHOSPHORYLATIONS; DNA DAMAGES; EUKARYOTIC INITIATION FACTOR; GROWTH ARREST; HERPES SIMPLEX VIRUS; HERPES SIMPLEX VIRUS TYPE 1; HUMAN GENES; IN-VITRO; INITIATION FACTORS; PROTEIN PHOSPHATASE; PROTEIN PHOSPHATASE-1; PROTEIN SYNTHESIS; PROTEIN TRANSLATION; VIRAL PROTEINS; VIRAL REPLICATION;

AMINO ACIDS; GENES; PHOSPHATASES; PHOSPHORYLATION; PROTEINS; VIRUSES;

BIOSYNTHESIS;

HERPES SIMPLEX VIRUS PROTEIN ICP34.5; INITIATION FACTOR 2ALPHA; PHOSPHOPROTEIN PHOSPHATASE 1; SERINE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ANIMAL CELL; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DNA DAMAGE; DNA HELIX; ENZYME SPECIFICITY; FLOW CYTOMETRY; GENE DELETION; GENE MUTATION; HERPES SIMPLEX VIRUS 1; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEPHOSPHORYLATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS INHIBITION; TRANSLATION INITIATION; VIRUS REPLICATION; WESTERN BLOTTING;

AMINO ACID MOTIFS; ANIMALS; BINDING SITES; CERCOPITHECUS AETHIOPS; EUKARYOTIC INITIATION FACTOR-2; HEK293 CELLS; HELA CELLS; HERPESVIRUS 1, HUMAN; HUMANS; PHOSPHORYLATION; PROTEIN BIOSYNTHESIS; PROTEIN PHOSPHATASE 1; SEQUENCE DELETION; VERO CELLS; VIRAL PROTEINS; VIRUS REPLICATION;

EUKARYOTA; HUMAN HERPESVIRUS 1; SIMPLEXVIRUS;

EID: 79960112123     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.232439     Document Type: Article

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