Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain

Current Biology

Volumn 12, Issue 12, 2002, Pages 1052-1058

  Feng, Qin ^a   Wang, Hengbin ^a   Ng, Huck Hui ^b   Erdjument Bromage, Hediye ^c   Tempst, Paul ^c   Struhl, Kevin ^b   Zhang, Yi ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; SACCHAROMYCETALES;

HISTONE; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; LYSINE; METHYLTRANSFERASE;

AMINO ACID SEQUENCE; ARTICLE; CELL CYCLE; ENZYME SPECIFICITY; HUMAN; METABOLISM; METHYLATION; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; YEAST;

AMINO ACID SEQUENCE; CELL CYCLE; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; METHYLATION; METHYLTRANSFERASES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; YEASTS;

EID: 0037172665     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(02)00901-6     Document Type: Article

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