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and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach. J Med Chem 57
(20):8340–8357. https://doi.org/10.1021/jm500777s
97. Teng YB, Jing H, Aramsangtienchai P, He B, Khan S, Hu J, Lin H, Hao Q (2015) Efficient
demyristoylase activity of SIRT2 revealed by kinetic and structural studies. Sci Rep 5:8529.
https://doi.org/10.1038/srep08529
98. Schiedel M, Rumpf T, Karaman B, Lehotzky A, Olah J, Gerhardt S, Ovadi J, Sippl W,
Einsle O, Jung M (2016) Aminothiazoles as potent and selective Sirt2 inhibitors: a
structure-activity relationship study. J Med Chem 59(4):1599–1612. https://doi.org/10.1021/
acs.jmedchem.5b01517
99. Smith BC, Denu JM (2009) Chemical mechanisms of histone lysine and arginine modifications. Biochim Biophys Acta 1789(1):45–57. https://doi.org/10.1016/j.bbagrm.2008.06.005
100. Qian C, Zhou MM (2006) SET domain protein lysine methyltransferases: structure, specificity and catalysis. Cell Mol Life Sci 63(23):2755–2763. https://doi.org/10.1007/s00018006-6274-5
101. Boisvert FM, Chenard CA, Richard S (2005) Protein interfaces in signaling regulated by
arginine methylation. Sci STKE 2005(271):re2. https://doi.org/10.1126/stke.2712005re2
102. Bedford MT (2007) Arginine methylation at a glance. J Cell Sci 120(24):4243–4246. https://
doi.org/10.1242/jcs.019885
103. Pal S, Sif S (2007) Interplay between chromatin remodelers and protein arginine
methyltransferases. J Cell Physiol 213(2):306–315. https://doi.org/10.1002/jcp.21180
104. Allis CD, Berger SL, Cote J, Dent S, Jenuwien T, Kouzarides T, Pillus L, Reinberg D, Shi Y,
Shiekhattar R, Shilatifard A, Workman J, Zhang Y (2007) New nomenclature for chromatinmodifying enzymes. Cell 131(4):633–636. https://doi.org/10.1016/j.cell.2007.10.039
105. Schneider R, Bannister AJ, Kouzarides T (2002) Unsafe SETs: histone lysine
methyltransferases and cancer. Trends Biochem Sci 27(8):396–402. PII: S0968-0004(02)
02141-2. https://doi.org/10.1016/S0968-0004(02)02141-2
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Jung M (2007) Target-based approach to inhibitors of histone arginine methyltransferases.
J Med Chem 50(10):2319–2325. https://doi.org/10.1021/jm061250e
107. Wolber G, Langer T (2005) LigandScout: 3-d pharmacophores derived from protein-bound
ligands and their use as virtual screening filters. J Chem Inf Model 45(1):160–169. https://doi.
org/10.1021/ci049885e
108. Heinke R, Spannhoff A, Meier R, Trojer P, Bauer I, Jung M, Sippl W (2009) Virtual screening
and biological characterization of novel histone arginine methyltransferase PRMT1 inhibitors.
ChemMedChem 4(1):69–77. https://doi.org/10.1002/cmdc.200800301
109. de Freitas RF, Eram MS, Smil D, Szewczyk MM, Kennedy S, Brown PJ, Santhakumar V,
Barsyte-Lovejoy D, Arrowsmith CH, Vedadi M, Schapira M (2016) Discovery of a potent and
selective coactivator associated arginine methyltransferase 1 (CARM1) inhibitor by virtual
screening. J Med Chem 59(14):6838–6847. https://doi.org/10.1021/acs.jmedchem.6b00668
110. Ye Y, Zhang BD, Mao RF, Zhang CH, Wang YL, Xing J, Liu YC, Luo XM, Ding H, Yang
YX, Zhou B, Jiang HL, Chen KX, Luo C, Zheng MY (2017) Discovery and optimization of
selective inhibitors of protein arginine methyltransferase 5 by docking-based virtual screening.
Org Biomol Chem 15(17):3648–3661. https://doi.org/10.1039/c7ob00070g
111. Kubicek S, O’Sullivan RJ, August EM, Hickey ER, Zhang Q, Teodoro ML, Rea S,
Mechtler K, Kowalski JA, Homon CA, Kelly TA, Jenuwein T (2007) Reversal of
H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase. Mol Cell 25
(3):473–481. https://doi.org/10.1016/j.molcel.2007.01.017
112. Liu F, Chen X, Allali-Hassani A, Quinn AM, Wasney GA, Dong AP, Barsyte D,
Kozieradzki I, Senisterra G, Chau I, Siarheyeva A, Kireev DB, Jadhav A, Herold JM, Frye
482
D. Robaa et al.