| Title | Authors | Date | PubMed ID |
|---|
| PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. | Miranda TB, Miranda M, Frankel A, Clarke S | 2004 May 28 | 15044439 |
| RNA and protein interactions modulated by protein arginine methylation. | Gary JD, Clarke S | 1998 | 9752719 |
| PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. | Tang J, Gary JD, Clarke S, Herschman HR | 1998 Jul 3 | 9642256 |
| Unique Features of Human Protein Arginine Methyltransferase 9 (PRMT9) and Its Substrate RNA Splicing Factor SF3B2. | Hadjikyriacou A, Yang Y, Espejo A, Bedford MT, Clarke SG | 2015 Jul 3 | 25979344 |
| Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop. | Feng Y, Hadjikyriacou A, Clarke SG | 2014 Nov 21 | 25294873 |
| Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. | Gonsalvez GB, Tian L, Ospina JK, Boisvert FM, Lamond AI, Matera AG | 2007 Aug 27 | 17709427 |
| The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. | Frankel A, Yadav N, Lee J, Branscombe TL, Clarke S, Bedford MT | 2002 Feb 1 | 11724789 |
| PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. | Branscombe TL, Frankel A, Lee JH, Cook JR, Yang Z, Pestka S, Clarke S | 2001 Aug 31 | 11413150 |
| PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells. | Tang J, Frankel A, Cook RJ, Kim S, Paik WK, Williams KR, Clarke S, Herschman HR | 2000 Mar 17 | 10713084 |
