Protein arginine methyltransferases and cancer
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Earth and Planetary Sciences,General Environmental Science
Link
http://www.nature.com/articles/nrc3409.pdf
Reference196 articles.
1. Bedford, M. T. & Clarke, S. G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 33, 1–13 (2009).
2. Boffa, L. C., Karn, J., Vidali, G. & Allfrey, V. G. Distribution of NG, NG,-dimethylarginine in nuclear protein fractions. Biochem. Biophys. Res. Commun. 74, 969–976 (1977).
3. Tripsianes, K. et al. Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins. Nature Struct. Mol. Biol. 18, 1414–1420 (2011).
4. Swiercz, R., Cheng, D., Kim, D. & Bedford, M. T. Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice. J. Biol. Chem. 282, 16917–16923 (2007).
5. Yadav, N. et al. Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice. Proc. Natl Acad. Sci. USA 100, 6464–6468 (2003).
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