Protein Arginine Methylation in Mammals: Who, What, and Why
Top Cited Papers
- 1 January 2009
- journal article
- review article
- Published by Elsevier in Molecular Cell
- Vol. 33 (1) , 1-13
- https://doi.org/10.1016/j.molcel.2008.12.013
Abstract
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This publication has 118 references indexed in Scilit:
- Protein lysine methyltransferase G9a acts on non-histone targetsNature Chemical Biology, 2008
- The histone‐binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5EMBO Reports, 2008
- CARM1 promotes adipocyte differentiation by coactivating PPARγEMBO Reports, 2008
- Protein Arginine Methyltransferase 1: Positively Charged Residues in Substrate Peptides Distal to the Site of Methylation Are Important for Substrate Binding and CatalysisBiochemistry, 2007
- Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusiveNature, 2007
- Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferaseThe EMBO Journal, 2007
- Functional insights from structures of coactivator-associated arginine methyltransferase 1 domainsThe EMBO Journal, 2007
- Phosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1Proceedings of the National Academy of Sciences, 2007
- Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphomaThe EMBO Journal, 2007
- Coactivator-associated arginine methyltransferase 1 (CARM1) is a positive regulator of the Cyclin E1 geneProceedings of the National Academy of Sciences, 2006