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Identification of new drug sensitivity genes using genetic suppressor elements: protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents.
The Journal of biological chemistry, 279(22), 22902-22907 (2004-03-27)
We have identified a mammalian arginine N-methyltransferase, PRMT7, that can catalyze the formation of omega-NG-monomethylarginine in peptides. This protein is encoded by a gene on human chromosome 16q22.1 (human locus AK001502). We expressed a full-length human cDNA construct in Escherichia
A proteomic analysis of arginine methylated protein complexes
Boisvert, F. M., et al
Molecular and Cellular Proteomics, 2, 1319-1330 (2003)
Human protein arginine methyltransferases in vivo--distinct properties of eight canonical members of the PRMT family.
Self-renewal and pluripotency are two fundamental characteristics of embryonic stem cells (ESCs) and are controlled by diverse regulatory factors, including pluripotent factors, epigenetic regulators and microRNAs (miRNAs). Although histone methyltransferases are key epigenetic regulators, whether and how a histone methyltransferase
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