107. Zhang X et al (2000) Crystal structure of the conserved core of protein arginine
methyltransferase PRMT3. EMBO J 19:3509–3519
108. Frankel A, Clarke S (2000) PRMT3 is a distinct member of the protein arginine
N-methyltransferase family: conferral of substrate specificity by a zinc-finger domain. J Biol
Chem 275:32974–32982
109. Guo H et al (2014) Profiling substrates of protein arginine N-methyltransferase 3 with
S-adenosyl-L-methionine analogues. ACS Chem Biol 9:476–484
110. Singh V et al (2004) DAL-1/4.1B tumor suppressor interacts with protein arginine
N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and
in vivo. Oncogene 23:7761–7771
111. Siarheyeva A et al (2012) An allosteric inhibitor of protein arginine methyltransferase 3. Structure 20:1425–1435
112. Liu F et al (2013) Exploiting an allosteric binding site of PRMT3 yields potent and selective
inhibitors. J Med Chem 56:2110–2124
113. Kaniskan HÜ et al (2015) A potent, selective and cell-active allosteric inhibitor of protein
arginine methyltransferase 3 (PRMT3). Angew Chem Int Ed 54:5166–5170
114. Lee J (2002) PABP1 identified as an arginine methyltransferase substrate using high-density
protein arrays. EMBO Rep 3:268–273
115. Cheng D et al (2007) The arginine methyltransferase CARM1 regulates the coupling of
transcription and mRNA processing. Mol Cell 25:71–83
116. Schurter BT et al (2001) Methylation of histone H3 by coactivator-associated arginine
methyltransferase 1. Biochemistry 40:5747–5756
117. Jacques SL et al (2016) CARM1 preferentially methylates H3R17 over H3R26 through a
random kinetic mechanism. Biochemistry 55:1635–1644
118. Casadio F et al (2013) H3R42me2a is a histone modification with positive transcriptional
effects. Proc Natl Acad Sci 110:14894–14899
119. Feng Q et al (2006) Signaling within a coactivator complex: methylation of SRC-3/AIB1 is a
molecular switch for complex disassembly. Mol Cell Biol 26:7846–7857
120. Kuhn P et al (2011) Automethylation of CARM1 allows coupling of transcription and mRNA
splicing. Nucleic Acids Res 39:2717–2726
121. Daujat S et al (2002) Crosstalk between CARM1 methylation and CBP acetylation on histone
H3. Curr Biol 12:2090–2097
122. Charoensuksai P et al (2015) O-GlcNAcylation of co-activator-associated arginine
methyltransferase 1 regulates its protein substrate specificity. Biochem J 466:587–599
123. Cheng H et al (2013) Overexpression of CARM1 in breast cancer is correlated with poorly
characterized clinicopathologic parameters and molecular subtypes. Diagn Pathol 8:129
124. Kim Y-RR et al (2010) Differential CARM1 expression in prostate and colorectal cancers.
BMC Cancer 10:197
125. C-YY O et al (2011) A coactivator role of CARM1 in the dysregulation of -catenin activity in
colorectal cancer cell growth and gene expression. Mol Cancer Res 9:660–670
126. Hong H et al (2004) Aberrant expression of CARM1, a transcriptional coactivator of androgen
receptor, in the development of prostate carcinoma and androgen-independent status. Cancer
101:83–89
127. Osada S et al (2013) Elevated expression of coactivator-associated arginine methyltransferase
1 is associated with early hepatocarcinogenesis. Oncol Rep 30:1669–1674
128. Purandare AV et al (2008) Pyrazole inhibitors of coactivator associated arginine
methyltransferase 1 (CARM1). Bioorg Med Chem Lett 18:4438–4441
129. Allan M et al (2009) N-Benzyl-1-heteroaryl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamides
as inhibitors of co-activator associated arginine methyltransferase 1 (CARM1). Bioorg Med
Chem Lett 19:1218–1223
130. Huynh T et al (2009) Optimization of pyrazole inhibitors of coactivator associated arginine
methyltransferase 1 (CARM1). Bioorg Med Chem Lett 19:2924–2927
PRMT Inhibitors
193
methyltransferase PRMT3. EMBO J 19:3509–3519
108. Frankel A, Clarke S (2000) PRMT3 is a distinct member of the protein arginine
N-methyltransferase family: conferral of substrate specificity by a zinc-finger domain. J Biol
Chem 275:32974–32982
109. Guo H et al (2014) Profiling substrates of protein arginine N-methyltransferase 3 with
S-adenosyl-L-methionine analogues. ACS Chem Biol 9:476–484
110. Singh V et al (2004) DAL-1/4.1B tumor suppressor interacts with protein arginine
N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and
in vivo. Oncogene 23:7761–7771
111. Siarheyeva A et al (2012) An allosteric inhibitor of protein arginine methyltransferase 3. Structure 20:1425–1435
112. Liu F et al (2013) Exploiting an allosteric binding site of PRMT3 yields potent and selective
inhibitors. J Med Chem 56:2110–2124
113. Kaniskan HÜ et al (2015) A potent, selective and cell-active allosteric inhibitor of protein
arginine methyltransferase 3 (PRMT3). Angew Chem Int Ed 54:5166–5170
114. Lee J (2002) PABP1 identified as an arginine methyltransferase substrate using high-density
protein arrays. EMBO Rep 3:268–273
115. Cheng D et al (2007) The arginine methyltransferase CARM1 regulates the coupling of
transcription and mRNA processing. Mol Cell 25:71–83
116. Schurter BT et al (2001) Methylation of histone H3 by coactivator-associated arginine
methyltransferase 1. Biochemistry 40:5747–5756
117. Jacques SL et al (2016) CARM1 preferentially methylates H3R17 over H3R26 through a
random kinetic mechanism. Biochemistry 55:1635–1644
118. Casadio F et al (2013) H3R42me2a is a histone modification with positive transcriptional
effects. Proc Natl Acad Sci 110:14894–14899
119. Feng Q et al (2006) Signaling within a coactivator complex: methylation of SRC-3/AIB1 is a
molecular switch for complex disassembly. Mol Cell Biol 26:7846–7857
120. Kuhn P et al (2011) Automethylation of CARM1 allows coupling of transcription and mRNA
splicing. Nucleic Acids Res 39:2717–2726
121. Daujat S et al (2002) Crosstalk between CARM1 methylation and CBP acetylation on histone
H3. Curr Biol 12:2090–2097
122. Charoensuksai P et al (2015) O-GlcNAcylation of co-activator-associated arginine
methyltransferase 1 regulates its protein substrate specificity. Biochem J 466:587–599
123. Cheng H et al (2013) Overexpression of CARM1 in breast cancer is correlated with poorly
characterized clinicopathologic parameters and molecular subtypes. Diagn Pathol 8:129
124. Kim Y-RR et al (2010) Differential CARM1 expression in prostate and colorectal cancers.
BMC Cancer 10:197
125. C-YY O et al (2011) A coactivator role of CARM1 in the dysregulation of -catenin activity in
colorectal cancer cell growth and gene expression. Mol Cancer Res 9:660–670
126. Hong H et al (2004) Aberrant expression of CARM1, a transcriptional coactivator of androgen
receptor, in the development of prostate carcinoma and androgen-independent status. Cancer
101:83–89
127. Osada S et al (2013) Elevated expression of coactivator-associated arginine methyltransferase
1 is associated with early hepatocarcinogenesis. Oncol Rep 30:1669–1674
128. Purandare AV et al (2008) Pyrazole inhibitors of coactivator associated arginine
methyltransferase 1 (CARM1). Bioorg Med Chem Lett 18:4438–4441
129. Allan M et al (2009) N-Benzyl-1-heteroaryl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamides
as inhibitors of co-activator associated arginine methyltransferase 1 (CARM1). Bioorg Med
Chem Lett 19:1218–1223
130. Huynh T et al (2009) Optimization of pyrazole inhibitors of coactivator associated arginine
methyltransferase 1 (CARM1). Bioorg Med Chem Lett 19:2924–2927
PRMT Inhibitors
193