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arginine methyltransferase

 
National Institutes of Health

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PRMT2 protein, human

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Highly Cited
2018
Highly Cited
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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2016
2016
Protein arginine methyltransferase 5 regulates multiple signaling pathways to promote lung cancer cell proliferation
BackgroundProtein arginine methyltransferase 5 (PRMT5) catalyzes the formation of symmetrical dimethylation of arginine residues… Expand
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2016
2016
Protein arginine methyltransferase 5 is associated with malignant phenotype and peritoneal metastasis in gastric cancer.
Identification of novel gastric cancer (GC)-related molecules is necessary to improve management of patients with GC in both… Expand
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Highly Cited
2015
Highly Cited
2015
Aryl Pyrazoles as Potent Inhibitors of Arginine Methyltransferases: Identification of the First PRMT6 Tool Compound.
A novel aryl pyrazole series of arginine methyltransferase inhibitors has been identified. Synthesis of analogues within this… Expand
Highly Cited
2012
Highly Cited
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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Highly Cited
2009
Highly Cited
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
Highly Cited
2007
Highly Cited
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
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
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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2005
2005
Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide
The multifunctional Ewing Sarcoma (EWS) protein, a member of a large family of RNA‐binding proteins, is extensively… Expand
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