Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice
Neelu Yadav(HCG Cancer Centre), Mark T. Bedford(The University of Texas MD Anderson Cancer Center), Jeesun Kim(Western Sydney University), Jae Ho Lee(Konkuk University), Jianjun Shen(Commercial Aircraft Corporation of China (China)), Mickey C.‐T. Hu(Zhengzhou University), C. Marcelo Aldaz(The University of Texas MD Anderson Cancer Center)
Cited by 282
Related Papers
Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A
|Science|2006|448
Small Molecule Regulators of Protein Arginine Methyltransferases
|Journal of Biological Chemistry|2004|334
The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity
|Journal of Biological Chemistry|2002|331
Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
|Nature Structural & Molecular Biology|2009|306
Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine <i>N</i> -Methyltransferase 1
|Molecular Biology of the Cell|2003|261