84. Thomas D et al (2014) Protein arginine N-methyltransferase substrate preferences for different
Nη-substituted Arginyl peptides. Chembiochem 15:1607–1613
85. Osborne T et al (2008) In situ generation of a Bisubstrate analogue for protein arginine
methyltransferase 1. J Am Chem Soc 130:4574–4575
86. Luo Y et al (2006) Inhibitors and inactivators of protein arginine deiminase 4: functional and
structural characterization. Biochemistry 45:11727–11736
87. Obianyo O et al (2010) A chloroacetamidine-based inactivator of protein arginine
methyltransferase 1: design, synthesis, and in vitro and in vivo evaluation. Chembiochem
11:1219–1223
88. Obianyo O et al (2011) Activity-based protein profiling of protein arginine methyltransferase
1. ACS ChemBio 6:1127–1135
89. Weerapana E et al (2010) Quantitative reactivity profiling predicts functional cysteines in
proteomes. Nature 468:790–795
90. Zhang X, Cheng X (2003) Structure of the predominant protein arginine methyltransferase
PRMT1 and analysis of its binding to substrate peptides. Structure 11:509–520
91. Dillon MBC et al (2012) Novel inhibitors for PRMT1 discovered by high-throughput screening using activity-based fluorescence polarization. ACS Chem Biol 7:1198–1204
92. Yan L et al (2014) Diamidine compounds for selective inhibition of protein arginine
methyltransferase 1. J Med Chem 57:2611–2622
93. Zhang J et al (2017) Discovery of decamidine as a new and potent PRMT1 inhibitor.
Med Chem Commun 8:440–444
94. Sinha SH et al (2012) Synthesis and evaluation of carbocyanine dyes as PRMT inhibitors and
imaging agents. Eur J Med Chem 54:647–659
95. Hu H et al (2015) Exploration of cyanine compounds as selective inhibitors of protein arginine
methyltransferases: synthesis and biological evaluation. J Med Chem 58:1228–1243
96. Yu XR et al (2015) Discovery and structure-activity analysis of 4-((5-nitropyrimidin-4-yl)
amino)benzimidamide derivatives as novel protein arginine methyltransferase 1 (PRMT1)
inhibitors. Bioorg Med Chem Lett 25:5449–5453
97. Lakowski TM, Frankel A (2009) Kinetic analysis of human protein arginine
N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues
on histone H4. Biochem J 421:253–261
98. Cura V et al (2017) Structural studies of protein arginine methyltransferase 2 reveal its
interactions with potential substrates and inhibitors. FEBS J 284:77–96
99. Qi C (2002) Identification of protein arginine methyltransferase 2 as a coactivator for estrogen
receptor alpha. J Biol Chem 277:28624–28630
100. Meyer R et al (2007) PRMT2, a member of the protein arginine methyltransferase family, is a
coactivator of the androgen receptor. J Steroid Biochem Mol Biol 107:1–14
101. Vhuiyan MI et al (2017) PRMT2 interacts with splicing factors and regulates the alternative
splicing of BCL-X. J Biochem 162:17–25
102. Iwasaki H et al (2010) Disruption of protein arginine N-methyltransferase 2 regulates leptin
signaling and produces leanness in vivo through loss of STAT3 methylation. Circ Res
107:992–1001
103. Hussein MA et al (2015) LXR-mediated ABCA1 expression and function are modulated by
high glucose and PRMT2. PLoS One 10:6–8
104. Zhong J et al (2014) Nuclear loss of protein arginine N-methyltransferase 2 in breast carcinoma is associated with tumor grade and overexpression of cyclin D1 protein. Oncogene
33:5546–5558
105. Oh TG et al (2014) PRMT2 and RORγ expression are associated with breast cancer survival
outcomes. Mol Endocrinol 28:1166–1185
106. van Haren M et al (2015) Synthesis and evaluation of protein arginine N-methyltransferase
inhibitors designed to simultaneously occupy both substrate binding sites. Org Biomol Chem
13:549–560
192
M. J. van Haren and N. I. Martin
Nη-substituted Arginyl peptides. Chembiochem 15:1607–1613
85. Osborne T et al (2008) In situ generation of a Bisubstrate analogue for protein arginine
methyltransferase 1. J Am Chem Soc 130:4574–4575
86. Luo Y et al (2006) Inhibitors and inactivators of protein arginine deiminase 4: functional and
structural characterization. Biochemistry 45:11727–11736
87. Obianyo O et al (2010) A chloroacetamidine-based inactivator of protein arginine
methyltransferase 1: design, synthesis, and in vitro and in vivo evaluation. Chembiochem
11:1219–1223
88. Obianyo O et al (2011) Activity-based protein profiling of protein arginine methyltransferase
1. ACS ChemBio 6:1127–1135
89. Weerapana E et al (2010) Quantitative reactivity profiling predicts functional cysteines in
proteomes. Nature 468:790–795
90. Zhang X, Cheng X (2003) Structure of the predominant protein arginine methyltransferase
PRMT1 and analysis of its binding to substrate peptides. Structure 11:509–520
91. Dillon MBC et al (2012) Novel inhibitors for PRMT1 discovered by high-throughput screening using activity-based fluorescence polarization. ACS Chem Biol 7:1198–1204
92. Yan L et al (2014) Diamidine compounds for selective inhibition of protein arginine
methyltransferase 1. J Med Chem 57:2611–2622
93. Zhang J et al (2017) Discovery of decamidine as a new and potent PRMT1 inhibitor.
Med Chem Commun 8:440–444
94. Sinha SH et al (2012) Synthesis and evaluation of carbocyanine dyes as PRMT inhibitors and
imaging agents. Eur J Med Chem 54:647–659
95. Hu H et al (2015) Exploration of cyanine compounds as selective inhibitors of protein arginine
methyltransferases: synthesis and biological evaluation. J Med Chem 58:1228–1243
96. Yu XR et al (2015) Discovery and structure-activity analysis of 4-((5-nitropyrimidin-4-yl)
amino)benzimidamide derivatives as novel protein arginine methyltransferase 1 (PRMT1)
inhibitors. Bioorg Med Chem Lett 25:5449–5453
97. Lakowski TM, Frankel A (2009) Kinetic analysis of human protein arginine
N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues
on histone H4. Biochem J 421:253–261
98. Cura V et al (2017) Structural studies of protein arginine methyltransferase 2 reveal its
interactions with potential substrates and inhibitors. FEBS J 284:77–96
99. Qi C (2002) Identification of protein arginine methyltransferase 2 as a coactivator for estrogen
receptor alpha. J Biol Chem 277:28624–28630
100. Meyer R et al (2007) PRMT2, a member of the protein arginine methyltransferase family, is a
coactivator of the androgen receptor. J Steroid Biochem Mol Biol 107:1–14
101. Vhuiyan MI et al (2017) PRMT2 interacts with splicing factors and regulates the alternative
splicing of BCL-X. J Biochem 162:17–25
102. Iwasaki H et al (2010) Disruption of protein arginine N-methyltransferase 2 regulates leptin
signaling and produces leanness in vivo through loss of STAT3 methylation. Circ Res
107:992–1001
103. Hussein MA et al (2015) LXR-mediated ABCA1 expression and function are modulated by
high glucose and PRMT2. PLoS One 10:6–8
104. Zhong J et al (2014) Nuclear loss of protein arginine N-methyltransferase 2 in breast carcinoma is associated with tumor grade and overexpression of cyclin D1 protein. Oncogene
33:5546–5558
105. Oh TG et al (2014) PRMT2 and RORγ expression are associated with breast cancer survival
outcomes. Mol Endocrinol 28:1166–1185
106. van Haren M et al (2015) Synthesis and evaluation of protein arginine N-methyltransferase
inhibitors designed to simultaneously occupy both substrate binding sites. Org Biomol Chem
13:549–560
192
M. J. van Haren and N. I. Martin