11. Tang J et al (1998) PRMT 3, a type I protein arginine N-methyltransferase that differs from
PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J
Biol Chem 273:16935–16945
12. Chen D (1999) Regulation of transcription by a protein methyltransferase. Science
284:2174–2177
13. Branscombe TL et al (2001) PRMT5 (Janus kinase-binding protein 1) catalyzes the formation
of symmetric dimethylarginine residues in proteins. J Biol Chem 276:32971–32976
14. Frankel A et al (2002) The novel human protein arginine N-methyltransferase PRMT6 is a
nuclear enzyme displaying unique substrate specificity. J Biol Chem 277:3537–3543
15. Lee JH et al (2005) PRMT7, a new protein arginine methyltransferase that synthesizes
symmetric dimethylarginine. J Biol Chem 280:3656–3664
16. Miranda TB et al (2004) PRMT7 is a member of the protein arginine methyltransferase family
with a distinct substrate specificity. J Biol Chem 279:22902–22907
17. Lee J et al (2005) PRMT8, a new membrane-bound tissue-specific member of the protein
arginine methyltransferase family. J Biol Chem 280:32890–32896
18. Cook JR et al (2006) FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues. Biochem Biophys Res Commun 342:472–481
19. Thompson PR, Fast W (2006) Histone citrullination by protein arginine deiminase: is arginine
methylation a green light or a roadblock? ACS Chem Biol 1:433–441
20. Chang B et al (2007) JMJD6 is a histone arginine demethylase. Science 318:444–447
21. Webby CJ et al (2009) Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated
with RNA splicing. Science 325:90–93
22. Unoki M et al (2013) Lysyl 5-hydroxylation, a novel histone modification, by jumonji domain
containing 6 (JMJD6). J Biol Chem 288:6053–6062
23. Wang F et al (2014) JMJD6 promotes Colon carcinogenesis through negative regulation of
p53 by hydroxylation. PLoS Biol 12:e1001819
24. Boeckel J-N et al (2011) Jumonji domain-containing protein 6 (Jmjd6) is required for
angiogenic sprouting and regulates splicing of VEGF-receptor 1. Proc Natl Acad Sci U S A
108:3276–3281
25. Han G et al (2012) The hydroxylation activity of Jmjd6 is required for its homooligomerization. J Cell Biochem 113:1663–1670
26. Böttger A et al (2015) The oxygenase Jmjd6–a case study in conflicting assignments. Biochem
J 468:191–202
27. Walport LJ et al (2016) Arginine demethylation is catalysed by a subset of JmjC histone lysine
demethylases. Nat Commun 7:11974
28. Uhlmann T et al (2012) A method for large-scale identification of protein arginine methylation.
Mol Cell Proteomics 11:1489–1499
29. Sylvestersen KB et al (2014) Proteomic analysis of arginine methylation sites in human cells
reveals dynamic regulation during transcriptional arrest. Mol Cell Proteomics 13:2072–2088
30. Larsen SC et al (2016) Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells. Sci Signal 9:rs9
31. Bedford MT, Clarke SG (2009) Protein arginine methylation in mammals: who, what, and
why. Mol Cell 33:1–13
32. Yang Y, Bedford MT (2013) Protein arginine methyltransferases and cancer. Nat Rev Cancer
13:37–50
33. Franceschelli S et al (2013) Biological functional relevance of asymmetric dimethylarginine
(ADMA) in cardiovascular disease. Int J Mol Sci 14:24412–24421
34. Zakrzewicz D, Eickelberg O (2009) From arginine methylation to ADMA: a novel mechanism
with therapeutic potential in chronic lung diseases. BMC Pulm Med 9:5
35. Zakrzewicz D et al (2012) Protein arginine methyltransferases (PRMTs): promising targets for
the treatment of pulmonary disorders. Int J Mol Sci 13:12383–12400
PRMT Inhibitors
189
PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J
Biol Chem 273:16935–16945
12. Chen D (1999) Regulation of transcription by a protein methyltransferase. Science
284:2174–2177
13. Branscombe TL et al (2001) PRMT5 (Janus kinase-binding protein 1) catalyzes the formation
of symmetric dimethylarginine residues in proteins. J Biol Chem 276:32971–32976
14. Frankel A et al (2002) The novel human protein arginine N-methyltransferase PRMT6 is a
nuclear enzyme displaying unique substrate specificity. J Biol Chem 277:3537–3543
15. Lee JH et al (2005) PRMT7, a new protein arginine methyltransferase that synthesizes
symmetric dimethylarginine. J Biol Chem 280:3656–3664
16. Miranda TB et al (2004) PRMT7 is a member of the protein arginine methyltransferase family
with a distinct substrate specificity. J Biol Chem 279:22902–22907
17. Lee J et al (2005) PRMT8, a new membrane-bound tissue-specific member of the protein
arginine methyltransferase family. J Biol Chem 280:32890–32896
18. Cook JR et al (2006) FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues. Biochem Biophys Res Commun 342:472–481
19. Thompson PR, Fast W (2006) Histone citrullination by protein arginine deiminase: is arginine
methylation a green light or a roadblock? ACS Chem Biol 1:433–441
20. Chang B et al (2007) JMJD6 is a histone arginine demethylase. Science 318:444–447
21. Webby CJ et al (2009) Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated
with RNA splicing. Science 325:90–93
22. Unoki M et al (2013) Lysyl 5-hydroxylation, a novel histone modification, by jumonji domain
containing 6 (JMJD6). J Biol Chem 288:6053–6062
23. Wang F et al (2014) JMJD6 promotes Colon carcinogenesis through negative regulation of
p53 by hydroxylation. PLoS Biol 12:e1001819
24. Boeckel J-N et al (2011) Jumonji domain-containing protein 6 (Jmjd6) is required for
angiogenic sprouting and regulates splicing of VEGF-receptor 1. Proc Natl Acad Sci U S A
108:3276–3281
25. Han G et al (2012) The hydroxylation activity of Jmjd6 is required for its homooligomerization. J Cell Biochem 113:1663–1670
26. Böttger A et al (2015) The oxygenase Jmjd6–a case study in conflicting assignments. Biochem
J 468:191–202
27. Walport LJ et al (2016) Arginine demethylation is catalysed by a subset of JmjC histone lysine
demethylases. Nat Commun 7:11974
28. Uhlmann T et al (2012) A method for large-scale identification of protein arginine methylation.
Mol Cell Proteomics 11:1489–1499
29. Sylvestersen KB et al (2014) Proteomic analysis of arginine methylation sites in human cells
reveals dynamic regulation during transcriptional arrest. Mol Cell Proteomics 13:2072–2088
30. Larsen SC et al (2016) Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells. Sci Signal 9:rs9
31. Bedford MT, Clarke SG (2009) Protein arginine methylation in mammals: who, what, and
why. Mol Cell 33:1–13
32. Yang Y, Bedford MT (2013) Protein arginine methyltransferases and cancer. Nat Rev Cancer
13:37–50
33. Franceschelli S et al (2013) Biological functional relevance of asymmetric dimethylarginine
(ADMA) in cardiovascular disease. Int J Mol Sci 14:24412–24421
34. Zakrzewicz D, Eickelberg O (2009) From arginine methylation to ADMA: a novel mechanism
with therapeutic potential in chronic lung diseases. BMC Pulm Med 9:5
35. Zakrzewicz D et al (2012) Protein arginine methyltransferases (PRMTs): promising targets for
the treatment of pulmonary disorders. Int J Mol Sci 13:12383–12400
PRMT Inhibitors
189