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

Class:Id	LiteratureReference:5634728
_displayName	Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
_timestamp	2014-11-05 12:02:39
author	[Person:5634721] Feng, Qin [Person:3301879] Wang, Hengbin [Person:5634722] Ng, Huck Hui [Person:162386] Erdjument-Bromage, H [Person:162385] Tempst, P [Person:5634726] Struhl, Kevin [Person:3214868] Zhang, Yi
created	[InstanceEdit:5634718] Jupe, Steve, 2014-11-05
journal	Curr. Biol.
pages	1052-8
pubMedIdentifier	12123582
title	Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
volume	12
year	2002
(literatureReference)	[Summation:3214819] Lysine methyltransferases (KMTs) and arginine methyltransfer... [Reaction:5649764] DOT1L (KMT4) methylates methyl-lysine-80 of histone H3 (H3K79) [Homo sapiens] [Reaction:5649799] DOT1L (KMT4) methylates dimethyl-lysine-80 of histone H3 (H3K79) [Homo sapiens] [Reaction:5649801] DOT1L (KMT4) methylates lysine-80 of histone H3 (H3K79) [Homo sapiens]
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