title: Arginine methylation an emerging regulator of protein function.
abstract: Arginine methylation is now coming out of the shadows of protein phosphorylation and entering the mainstream, largely due to the identification of the family of enzymes that lay down this modification. In addition, modification-specific antibodies and proteomic approaches have facilitated the identification of an array of substrates for the protein arginine methyltransferases. This review describes recent insights into the molecular processes regulated by arginine methylation in normal and diseased cells.
authors.affiliation: Department of Carcinogenesis, The University of Texas M.D. Anderson Cancer Center, Smithville, Texas 78957, USA. mtbedford@mdanderson.org
authors.forename: Mark T
authors.initials: MT
authors.lastname: Bedford
authors.forename: Stéphane
authors.initials: S
authors.lastname: Richard
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000378:metabolism; D000818:Animals; D001120:Arginine / Q000737:chemistry / Q000378:metabolism*; D004194:Disease; D006801:Humans; D008745:Methylation; D015394:Molecular Structure; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism*; D012323:RNA Processing, Post-Transcriptional; D015398:Signal Transduction / Q000502:physiology
chemical_list: D001120:Arginine; D000594:Amino Acid Oxidoreductases; D011484:Protein-Arginine N-Methyltransferases