Histone acetylation facilitates association of nucleosomes with SET domain of ALL-1 methyltransferase in vitro

Biochemical and Biophysical Research Communications

Volumn 397, Issue 1, 2010, Pages 112-116

  Krajewski, Wladyslaw A ^a   Vassiliev, Oleg L ^a  

^a KOL TSOV INSTITUTE OF DEVELOPMENTAL BIOLOGY   (Russian Federation)

Author keywords

Active chromatin; Histone acetylation; Nucleosomes; SET domain; Transcription

Indexed keywords

HISTONE; HISTONE METHYLTRANSFERASE;

ACETYLATION; ARTICLE; BINDING AFFINITY; CELL DIFFERENTIATION; CHROMATIN; CONTROLLED STUDY; GENE ACTIVITY; HELA CELL; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN METHYLATION;

ACETYLATION; HELA CELLS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; MYELOID-LYMPHOID LEUKEMIA PROTEIN; NUCLEOSOMES; PROTEIN STRUCTURE, TERTIARY;

EID: 77953621614     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.05.080     Document Type: Article

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