@inbook{e6f9e092058f4eb5a5d0ed0f30ef196a,
title = "Methods applied to the study of protein arginine methylation",
abstract = "Arginine methylation was discovered in the mid-1960s. About 15 years ago, the first protein arginine N-methyltransferase (PRMT) enzyme was described. The PRMT family now stands at nine members, and these enzymes play a key role in regulating a multitude of cellular events. The majority of the PRMTs have been deleted in mice, thus providing genetically tractable systems for in vivo and cell-based studies. These studies have implicated this posttranslational modification in chromatin remodeling, transcriptional regulation, RNA processing, protein/RNA trafficking, signal transduction, and DNA repair. In this chapter, we introduce different approaches that have been developed to assess protein arginine methylation levels and characterize PRMT substrates.",
keywords = "CARM1, Epigenetic, Histone methylation, PRMT1, PRMT5",
author = "Donghang Cheng and Vidyasiri Vemulapalli and Bedford, {Mark T.}",
note = "Funding Information: Thanks to Ms. Hilary Graham and Ms. Rebecca Deen for editing assistance. Mark Bedford is supported by NIH grant number DK62248 and, in part, by institutional grant NIEHS ES07784.",
year = "2012",
doi = "10.1016/B978-0-12-391940-3.00004-4",
language = "English (US)",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "71--92",
booktitle = "Methods in Enzymology",
}