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Histone-Lysine N-Methyltransferase

Known as: Protein Lysine Methyltransferase, Protein Methylase III, Methyltransferase, Histone-Lysine 
An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine… Expand
National Institutes of Health

Papers overview

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Highly Cited
2015
Highly Cited
2015
The gene encoding the lysine-specific histone methyltransferase KMT2D has emerged as one of the most frequently mutated genes in… Expand
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Review
2011
Review
2011
The discovery of Suv39h1, the first SET domain-containing histone lysine methyltransferase (HKMT), was reported in 2000. Since… Expand
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Highly Cited
2011
Highly Cited
2011
The histone lysine methyltransferase NSD2 (MMSET/WHSC1) is implicated in diverse diseases and commonly overexpressed in multiple… Expand
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Highly Cited
2009
Highly Cited
2009
Histone lysine methylation is an important epigenetic mark that regulates gene expression and chromatin organization. G9a and G9a… Expand
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Highly Cited
2007
Highly Cited
2007
Histone modifications induced by activated signalling cascades are crucial to cell-lineage decisions. Osteoblast and adipocyte… Expand
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Highly Cited
2005
Highly Cited
2005
Changes in the substrate specificities of factors that irreversibly modify the histone components of chromatin are expected to… Expand
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Highly Cited
2005
Highly Cited
2005
The growth factor independent 1 (Gfi1) transcriptional regulator oncoprotein plays a crucial role in hematopoietic, inner ear… Expand
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Highly Cited
2004
Highly Cited
2004
The Ezh2 protein endows the Polycomb PRC2 and PRC3 complexes with histone lysine methyltransferase (HKMT) activity that is… Expand
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Highly Cited
2004
Highly Cited
2004
Human Enhancer of Zeste homolog (Ezh2) is a histone lysine methyltransferase (HKMT) associated with transcriptional repression… Expand
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Highly Cited
2002
Highly Cited
2002
The N-terminal tails of core histones are subjected to multiple covalent modifications, including acetylation, methylation, and… Expand
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