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Sci. STKE, 31 July 2001 PROTOCOLSAnalysis of Protein Arginine Methylation and Protein Arginine-Methyltransferase ActivityKerri A. Mowen, and Michael David The authors are in the Division of Biology and University of Ccalifornia at San Diego Cancer Center, University of California, San Diego, Bonner Hall 3138, 9500 Gilman Drive, La Jolla, CA 92093, USA. E-mail: mdavid{at}biomail.ucsd.edu Abstract: Posttranslational modification of proteins allows cells to adapt and react quickly to their environment beyond the boundaries set forth by genetic code. Arginine methylation, a protein modification discovered almost 30 years ago, has recently experienced a renewed interest as several new arginine methyltransferases have been identified and numerous proteins were found to be regulated by methylation on arginine residues. Until recently, the detection of arginine methylation required the use of chromatography and mass-spectrometrical analysis. The following protocol provides guidelines for the straightforward identification of arginine-methylated proteins, made possible by the availability of novel, commercially available reagents. Citation: © 2001 American Association for the Advancement of Science
Citation: K. A. Mowen, M. David, Analysis of Protein Arginine Methylation and Protein Arginine-Methyltransferase Activity. Sci. STKE 2001, pl1 (2001). The editors suggest the following Related Resources on Science sites:In Science Signaling
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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)
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