Specificity and mechanism of the histone methyltransferase Pr-Set7

Genes and Development

Volumn 19, Issue 12, 2005, Pages 1444-1454

  Xiao, Bing ^a   Jing, Chun ^a   Kelly, Geoff ^a   Walker, Philip A ^a   Muskett, Frederick W ^a   Frenkiel, Thomas A ^a   Martin, Stephen R ^a   Sarma, Kavitha ^b   Reinberg, Danny ^b   Gamblin, Steven J ^a   Wilson, Jonathan R ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

Enzymes; Eukaryotic cells; H4 K20; Histones; Methyltransferase; Pr Set7

Indexed keywords

ENZYME PR SET7; HISTONE H4; LYSINE; METHYLTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DNA FLANKING REGION; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; NUCLEAR MAGNETIC RESONANCE; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN METHYLATION; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DROSOPHILA PROTEINS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; METHYLATION; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EUKARYOTA;

EID: 22344455665     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1315905     Document Type: Article

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