The bromodomain of gcn5 regulates site specificity of lysine acetylation on histone H3

Molecular and Cellular Proteomics

Volumn 13, Issue 11, 2014, Pages 2896-2910

  Cieniewicz, Anne M ^a   Moreland, Linley ^b   Ringel, Alison E ^a   Mackintosh, Samuel G ^b   Raman, Ana ^a   Gilbert, Tonya M ^a   Wolberger, Cynthia ^a   Tackett, Alan J ^b   Taverna, Sean D ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ACETYLTRANSFERASE GCN5; HISTONE H3; LYSINE; ADA2 PROTEIN, S CEREVISIAE; GCN5 PROTEIN, S CEREVISIAE; HISTONE; HISTONE ACETYLTRANSFERASE; NGG1 PROTEIN, S CEREVISIAE; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSCRIPTION FACTOR;

ARTICLE; CHROMATIN; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; EPIGENETICS; GEL; GENE EXPRESSION; HISTONE ACETYLATION; IN VITRO STUDY; MASS SPECTROMETRY; MUTATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROCESSING; QUANTITATIVE ANALYSIS; SIGNAL TRANSDUCTION; WILD TYPE; ACETYLATION; ANIMAL; BINDING SITE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; TRANSCRIPTION INITIATION;

ACETYLATION; ANIMALS; BINDING SITES; HISTONE ACETYLTRANSFERASES; HISTONES; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TRANSCRIPTION FACTORS; TRANSCRIPTIONAL ACTIVATION;

EID: 84910650721     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.038174     Document Type: Article

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