Structure-activity analysis of semisynthetic nucleosomes: Mechanistic insights into the stimulation of Dot1L by ubiquitylated histone H2B

ACS Chemical Biology

Volumn 4, Issue 11, 2009, Pages 958-968

  McGinty, Robert K ^a   Köhn, Maja ^b   Chatterjee, Champak ^a   Chiang, Kyle P ^a,c   Pratt, Matthew R ^a,d   Muir, Tom W ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c aTyr Pharma   (United States)

^d UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2B; HISTONE H3; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; MUTANT PROTEIN; PROTEIN U(G76A)H2B; UBIQUITIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; KINETICS; METHYLATION; MOLECULAR MECHANICS; NUCLEOSOME; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SYNTHESIS; STOICHIOMETRY; STRUCTURE ACTIVITY RELATION; UBIQUITINATION;

ANIMALS; HISTONES; HUMANS; KINETICS; METHYLATION; METHYLTRANSFERASES; MODELS, MOLECULAR; MUTATION; NUCLEOSOMES; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; UBIQUITINATED PROTEINS; XENOPUS;

EID: 73449105394     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb9002255     Document Type: Article

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