Negative regulation of interferon-induced transmembrane protein 3 by SET7-mediated lysine monomethylation

Journal of Biological Chemistry

Volumn 288, Issue 49, 2013, Pages 35093-35103

  Shan, Zhao ^a   Han, Qinglin ^a   Nie, Jia ^a   Cao, Xuezhi ^a   Chen, Zuojia ^a   Yin, Shuying ^a   Gao, Yayi ^a   Lin, Fang ^a   Zhou, Xiaohui ^b   Xu, Ke ^a   Fan, Huimin ^b   Qian, Zhikang ^a   Sun, Bing ^a   Zhong, Jin ^a   Li, Bin ^a   Tsun, Andy ^a  

^a INSTITUTE PASTEUR OF SHANGHAI   (China)

^b TONGJI UNIVERSITY SCHOOL OF MEDICINE   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRAL ACTIVITIES; INFLUENZA A VIRUS; MONOMETHYLATION; RNA VIRUS; THERAPEUTIC STRATEGY; TRANS-MEMBRANE PROTEINS; VESICULAR STOMATITIS VIRUS;

AMINO ACIDS;

VIRUSES;

ALPHA INTERFERON; HISTONE LYSINE METHYLTRANSFERASE; HISTONE LYSINE METHYLTRANSFERASE SET7; INTERFERON INDUCED TRANSMEMBRANE PROTEIN 3; LYSINE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

ANTIVIRAL ACTIVITY; ARTICLE; CONTROLLED STUDY; DRUG DETERMINATION; DRUG TARGETING; HUMAN; HUMAN CELL; INFLUENZA A; INFLUENZA VIRUS A; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN METHYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; REGULATORY MECHANISM; RESIDUE ANALYSIS; RHABDOVIRUS INFECTION; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION; VESICULAR STOMATITIS VIRUS; VESICULAR STOMATITIS VIRUS INFECTION; VIRUS CELL INTERACTION; VIRUS VIRULENCE;

ANTIVIRAL AGENTS; ANTIVIRAL HOST RESTRICTION FACTORS; HOST DEFENSE; HOST-PATHOGEN INTERACTIONS; IFITM3; LYSINE METHYLATION; POST-TRANSLATIONAL MODIFICATION; PROTEIN METHYLATION; SET7;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CERCOPITHECUS AETHIOPS; GENE KNOCKDOWN TECHNIQUES; HEK293 CELLS; HISTONE-LYSINE N-METHYLTRANSFERASE; HUMANS; INFLUENZA A VIRUS; INTERFERON TYPE I; LYSINE; MEMBRANE PROTEINS; METHYLATION; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; RNA-BINDING PROTEINS; SIGNAL TRANSDUCTION; VERO CELLS; VESICULOVIRUS; VIRUS DISEASES;

EID: 84890291515     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.511949     Document Type: Article

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