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Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family.

Rho J, Choi S, Seong YR, Cho WK, Kim SH, Im DS.

J Biol Chem. 2001 Apr 6;276(14):11393-401. Epub 2001 Jan 10.


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.

J Biol Chem. 2001 Aug 31;276(35):32971-6. Epub 2001 Jun 18.


PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity.

Miranda TB, Miranda M, Frankel A, Clarke S.

J Biol Chem. 2004 May 28;279(22):22902-7. Epub 2004 Mar 24.


Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.

Miranda TB, Sayegh J, Frankel A, Katz JE, Miranda M, Clarke S.

Biochem J. 2006 May 1;395(3):563-70.


Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver.

Lim Y, Kwon YH, Won NH, Min BH, Park IS, Paik WK, Kim S.

Biochim Biophys Acta. 2005 May 25;1723(1-3):240-7. Epub 2005 Mar 17.


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.

J Biol Chem. 2015 Jul 3;290(27):16723-43. doi: 10.1074/jbc.M115.659433. Epub 2015 May 15.


Entamoeba histolytica: protein arginine transferase 1a methylates arginine residues and potentially modify the H4 histone.

Borbolla-Vázquez J, Orozco E, Betanzos A, Rodríguez MA.

Parasit Vectors. 2015 Apr 10;8:219. doi: 10.1186/s13071-015-0820-7.


Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4.

Boulanger MC, Miranda TB, Clarke S, Di Fruscio M, Suter B, Lasko P, Richard S.

Biochem J. 2004 Apr 15;379(Pt 2):283-9.


Histone methyltransferases in Aspergillus nidulans: evidence for a novel enzyme with a unique substrate specificity.

Trojer P, Dangl M, Bauer I, Graessle S, Loidl P, Brosch G.

Biochemistry. 2004 Aug 24;43(33):10834-43.


Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide.

Pahlich S, Bschir K, Chiavi C, Belyanskaya L, Gehring H.

Proteins. 2005 Oct 1;61(1):164-75.


Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.

Zurita-Lopez CI, Sandberg T, Kelly R, Clarke SG.

J Biol Chem. 2012 Mar 9;287(11):7859-70. doi: 10.1074/jbc.M111.336271. Epub 2012 Jan 12.


FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues.

Cook JR, Lee JH, Yang ZH, Krause CD, Herth N, Hoffmann R, Pestka S.

Biochem Biophys Res Commun. 2006 Apr 7;342(2):472-81. Epub 2006 Feb 8.


The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae.

Gary JD, Lin WJ, Yang MC, Herschman HR, Clarke S.

J Biol Chem. 1996 May 24;271(21):12585-94.


Ki-1/57 interacts with PRMT1 and is a substrate for arginine methylation.

Passos DO, Bressan GC, Nery FC, Kobarg J.

FEBS J. 2006 Sep;273(17):3946-61. Epub 2006 Jul 19.


The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity.

Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S.

J Biol Chem. 1999 Oct 29;274(44):31531-42.

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