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

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In BloodProcess of secretion[myelin basic protein]-arginine N-methyltransferase activityantagonists & inhibitors
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PRMT6 protein, humancoactivator-associated arginine methyltransferase 1

Papers overview

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Highly Cited
2008
Highly Cited
2008
The LIM protein AJUBA recruits protein arginine methyltransferase 5 to mediate SNAIL-dependent transcriptional repression.
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
Protein arginine-methyltransferase-dependent oncogenesis
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
PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family.
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
Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides.
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
Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.
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
Methylation of histone H3 by coactivator-associated arginine methyltransferase 1.
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
PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells.
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
Crystal structure of the conserved core of protein arginine methyltransferase PRMT3.
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
S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase.
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
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation.
Methylation is one of the many post-translational modifications that modulate protein function. Although asymmetric NG,NG… (More)
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