Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 16, 2012, Pages

  Bheda, Poonam ^a   Swatkoski, Stephen ^a   Fiedler, Katherine L ^a   Boeke, Jef D ^a   Cotter, Robert J ^a   Wolberger, Cynthia ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; HISTONE H3; HISTONE H3 LYSINE 79; LYSINE; SILENT INFORMATION REGULATOR PROTEIN 2; UNCLASSIFIED DRUG;

ARTICLE; BIOTINYLATION; CONTROLLED STUDY; DEACETYLATION; HISTONE ACETYLATION; IN VITRO STUDY; IN VIVO STUDY; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL;

ACETYLATION; BIOTIN; BIOTINYLATION; HISTONES; LYSINE; MUTATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SILENT INFORMATION REGULATOR PROTEINS, SACCHAROMYCES CEREVISIAE; SIRTUIN 2; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SUBSTRATE SPECIFICITY;

EID: 84860014259     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1121471109     Document Type: Article

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