Arginine metabolism has been a key catabolic and anabolic process throughout the
evolution of the immune response. Accruing evidence indicates that arginine-catabolizing …

The covalent marking of proteins by methyl group addition to arginine residues can promote
their recognition by binding partners or can modulate their biological activity. A small family …

Arginine methylation is a common posttranslational modification (PTM). This type of PTM
occurs on both nuclear and cytoplasmic proteins, and is particularly abundant on shuttling …

Specific sites of histone tail methylation are associated with transcriptional activity at gene
loci. These methyl marks are interpreted by effector molecules, which harbor protein …

Abstract Information about the family of protein arginine methyltransferases (PRMTs) has
been growing rapidly over the last few years and the emerging role of arginine methylation …

Abstract Protein arginine methyltransferase 1 (PRMT1) is the major enzyme that generates
monomethylarginine and asymmetrical dimethylarginine. We report here a conditional null …

Protein arginine methyltransferases (PRMTs) mediate the methylation of a number of protein
substrates of arginine residues and serve critical functions in many cellular responses …

Methylation of arginine residues is a widespread post-translational modification of proteins
catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the …

Post-translational modifications are well-known effectors in DNA damage signaling and
epigenetic gene expression. Protein arginine methylation is a covalent modification that …

Fusion protein AML1-ETO, resulting from t (8; 21) translocation, is highly related to leukemia
development. It has been reported that full-length AML1-ETO blocks AML1 function and …