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arginine methyltransferase

 
National Institutes of Health

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PRMT2 protein, human

Papers overview

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2018
2018
The LINC01138 drives malignancies via activating arginine methyltransferase 5 in hepatocellular carcinoma
Recurrent chromosomal aberrations have led to the discovery of oncogenes or tumour suppressors involved in carcinogenesis. Here… Expand
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2015
2015
Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression
Recent evidence points to the protein arginine methyltransferase (PRMT) family of enzymes playing critical roles in cancer. PRMT7… Expand
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2012
2012
Protein Arginine Methyltransferase 5 Functions in Opposite Ways in the Cytoplasm and Nucleus of Prostate Cancer Cells
Protein arginine methyltransferase 5 (PRMT5) plays multiple roles in a large number of cellular processes, and its subcellular… Expand
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2010
2010
Design, synthesis and biological evaluation of carboxy analogues of arginine methyltransferase inhibitor 1 (AMI-1).
Here we report the synthesis of a number of compounds structurally related to arginine methyltransferase inhibitor 1 (AMI-1). The… Expand
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2009
2009
Virtual screening and biological characterization of novel histone arginine methyltransferase PRMT1 inhibitors.
Lysine and arginine methyltransferases participate in the posttranslational modification of histones and regulate key cellular… Expand
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2009
2009
Colon cancer and protein arginine methyltransferase 1 gene expression.
BACKGROUND In this study, the possible relation of the expression pattern of arginine methyltransferase 1 and colon cancer… Expand
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2007
2007
A novel arginine methyltransferase inhibitor with cellular activity.
Via virtual screening we identified a thioglycolic amide as an arginine methyltransferase (PRMT) inhibitor and tested it and… Expand
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2007
2007
Arginine methylation of the HIV-1 nucleocapsid protein results in its diminished function.
OBJECTIVE The HIV-1 nucleocapsid protein (NC) is involved in transfer RNA3 annealing to the primer binding site of viral genomic… Expand
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Highly Cited
2006
Highly Cited
2006
Two functional modes of a nuclear receptor-recruited arginine methyltransferase in transcriptional activation.
Nuclear receptors, like other transcriptional activators, switch on gene transcription by recruiting a complex network of… Expand
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Highly Cited
2005
Highly Cited
2005
Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications.
PRMT1 is a histone methyltransferase that methylates Arg3 on histone H4. When we used siRNA to knock down PRMT1 in an erythroid… Expand
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