Proteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest.

@article{Sylvestersen2014ProteomicAO,
  title={Proteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest.},
  author={Kathrine Beck Sylvestersen and Heiko Horn and Stephanie Jungmichel and Lars Juhl Jensen and Michael L Nielsen},
  journal={Molecular & cellular proteomics : MCP},
  year={2014},
  volume={13 8},
  pages={2072-88}
}
The covalent attachment of methyl groups to the side-chain of arginine residues is known to play essential roles in regulation of transcription, protein function, and RNA metabolism. The specific N-methylation of arginine residues is catalyzed by a small family of gene products known as protein arginine methyltransferases; however, very little is known about which arginine residues become methylated on target substrates. Here we describe a proteomics methodology that combines single-step… CONTINUE READING
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