Protein-Arginine N-Methyltransferase

Known as: Protein Methylase I, Arginine Methyltransferase, Protein, Protein-Arginine N-Methyltransferases [Chemical/Ingredient] 
Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. This enzyme is found in many organs… (More)
National Institutes of Health

Papers overview

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Highly Cited
2008
Highly Cited
2008
The SNAIL transcription factor contains C-terminal tandem zinc finger motifs and an N-terminal SNAG repression domain. The… (More)
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Highly Cited
2007
Highly Cited
2007
Enzymes that mediate reversible epigenetic modifications have not only been recognized as key in regulating gene expression and… (More)
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Highly Cited
2005
Highly Cited
2005
Protein arginine methylation is a common post-translational modification that has been implicated in signal transduction, RNA… (More)
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Highly Cited
2003
Highly Cited
2003
PRMT1 is the predominant type I protein arginine methyltransferase in mammals and highly conserved among all eukaryotes. It is… (More)
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Highly Cited
2001
Highly Cited
2001
Acetylation of core histone tails plays a fundamental role in transcription regulation. In addition to acetylation, other… (More)
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Highly Cited
2001
Highly Cited
2001
The preferential in vitro methylation of histone H3 by coactivator-associated arginine methyltransferase 1 (CARM1) has been… (More)
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Highly Cited
2000
Highly Cited
2000
Type I protein arginine methyltransferases catalyze the formation of asymmetric omega-N(G),N(G)-dimethylarginine residues by… (More)
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Highly Cited
2000
Highly Cited
2000
Protein arginine methylation has been implicated in signal transduction, nuclear transport and transcription regulation. Protein… (More)
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Highly Cited
1999
Highly Cited
1999
We used sequence motifs conserved in S-adenosylmethionine-dependent methyltransferases to identify 26 putative methyltransferases… (More)
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Highly Cited
1998
Highly Cited
1998
Methylation is one of the many post-translational modifications that modulate protein function. Although asymmetric NG,NG… (More)
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