메뉴 건너뛰기




Volumn 22, Issue 3, 2015, Pages 360-372

Interaction between DNA/histone methyltransferases and their inhibitors

Author keywords

DNA methyltransferase; Drug discovery; Epigenetic therapy; Histone methyltransferase; Inhibitor

Indexed keywords

A 9; AMI 1; AMITROLE; AURINTRICARBOXYLIC ACID; AZ 505; AZACITIDINE; CBC 12; CHAETOCIN; CMPD 1; CP 4200; DECITABINE; DNA METHYLTRANSFERASE; DNA METHYLTRANSFERASE INHIBITOR; EPIGALLOCATECHIN GALLATE; EPZ 05687; GSK 126; HISTONE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE INHIBITOR; METHYLTRANSFERASE INHIBITOR; N (1 BENZYL 4 PIPERIDINYL) 2 (HEXAHYDRO 4 METHYL 1H 1,4 DIAZEPIN 1 YL) 6,7 DIMETHOXY 4 QUINAZOLINAMINE; N PHTHALOYLTRYPTOPHAN; NPEOC DAC; NSC 14778; NUCLEOTIDE DERIVATIVE; PROCAINAMIDE; RG 108 1; RM 65; SGI 1027; SID 49645275; SINEFUNGIN; UNCLASSIFIED DRUG; DNA (CYTOSINE 5) METHYLTRANSFERASE; ENZYME INHIBITOR; HISTONE LYSINE METHYLTRANSFERASE; PROTEIN BINDING;

EID: 84928687935     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867321666141106114538     Document Type: Article
Times cited : (12)

References (96)
  • 4
    • 0020699979 scopus 로고
    • Hypomethylation distinguishes genes of some human cancers from their normal counterparts
    • Feinberg, A. P.; Vogelstein, B. Hypomethylation distinguishes genes of some human cancers from their normal counterparts. Nature, 1983, 301(5895), 89-92.
    • (1983) Nature , vol.301 , Issue.5895 , pp. 89-92
    • Feinberg, A.P.1    Vogelstein, B.2
  • 5
    • 0037074010 scopus 로고    scopus 로고
    • Signaling network model of chromatin
    • Schreiber, S. L.; Bernstein, B. E. Signaling network model of chromatin. Cell, 2002, 111(6), 771-778.
    • (2002) Cell , vol.111 , Issue.6 , pp. 771-778
    • Schreiber, S.L.1    Bernstein, B.E.2
  • 8
    • 0033918563 scopus 로고    scopus 로고
    • Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3
    • Dammann, R.; Li, C.; Yoon, J. H.; Chin, P. L.; Bates, S.; Pfeifer, G. P. Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3. Nature Genet., 2000, 25(3), 315-319.
    • (2000) Nature Genet. , vol.25 , Issue.3 , pp. 315-319
    • Dammann, R.1    Li, C.2    Yoon, J.H.3    Chin, P.L.4    Bates, S.5    Pfeifer, G.P.6
  • 9
    • 50249091120 scopus 로고    scopus 로고
    • Chemical regulation of epigenetic modifications: Opportunities for new cancer therapy
    • Zheng, Y. G.; Wu, J.; Chen, Z.; Goodman, M. Chemical regulation of epigenetic modifications: opportunities for new cancer therapy. Med. Res. Rev., 2008, 28(5), 645-687.
    • (2008) Med. Res. Rev. , vol.28 , Issue.5 , pp. 645-687
    • Zheng, Y.G.1    Wu, J.2    Chen, Z.3    Goodman, M.4
  • 10
    • 48149096013 scopus 로고    scopus 로고
    • Epigenetic mechanisms in drug addiction
    • Renthal, W.; Nestler, E. J. Epigenetic mechanisms in drug addiction. Trends Mol. Med., 2008, 14(8), 341-350.
    • (2008) Trends Mol. Med. , vol.14 , Issue.8 , pp. 341-350
    • Renthal, W.1    Nestler, E.J.2
  • 11
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T.; Allis, C. D. Translating the histone code. Science, 2001, 293(5532), 1074-1080.
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 12
    • 15744396813 scopus 로고    scopus 로고
    • The key to development: Interpreting the histone code?
    • Margueron, R.; Trojer, P.; Reinberg, D. The key to development: interpreting the histone code? Curr. Opin. Genet. Dev., 2005, 15(2), 163-176.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , Issue.2 , pp. 163-176
    • Margueron, R.1    Trojer, P.2    Reinberg, D.3
  • 13
    • 34548526743 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer, part I: Covalent histone modifications
    • Wang, G. G.; Allis, C. D.; Chi, P. Chromatin remodeling and cancer, part I: covalent histone modifications. Trends Mol. Med., 2007, 13(9), 363-372.
    • (2007) Trends Mol. Med. , vol.13 , Issue.9 , pp. 363-372
    • Wang, G.G.1    Allis, C.D.2    Chi, P.3
  • 14
    • 84885181638 scopus 로고    scopus 로고
    • Computational methods for drug design and discovery: Focus on China
    • Zheng, M.; Liu, X.; Xu, Y.; Li, H.; Luo, C.; Jiang, H. Computational methods for drug design and discovery: focus on China. Trends Pharmacol. Sci., 2013, 34(10), 549-559.
    • (2013) Trends Pharmacol. Sci. , vol.34 , Issue.10 , pp. 549-559
    • Zheng, M.1    Liu, X.2    Xu, Y.3    Li, H.4    Luo, C.5    Jiang, H.6
  • 15
    • 79958002242 scopus 로고    scopus 로고
    • Natural products as DNA methyltransferase inhibitors: A computer-aided discovery approach
    • Medina-Franco, J. L.; Lopez-Vallejo, F.; Kuck, D.; Lyko, F. Natural products as DNA methyltransferase inhibitors: a computer-aided discovery approach. Mol. Divers., 2011, 15(2), 293-304.
    • (2011) Mol. Divers. , vol.15 , Issue.2 , pp. 293-304
    • Medina-Franco, J.L.1    Lopez-Vallejo, F.2    Kuck, D.3    Lyko, F.4
  • 16
    • 84876740124 scopus 로고    scopus 로고
    • Molecular modeling and virtual screening of DNA methyltransferase inhibitors
    • Medina-Franco, J. L.; Yoo, J. Molecular modeling and virtual screening of DNA methyltransferase inhibitors. Curr. Pharm. Des., 2013, 19(12), 2138-2147.
    • (2013) Curr. Pharm. Des. , vol.19 , Issue.12 , pp. 2138-2147
    • Medina-Franco, J.L.1    Yoo, J.2
  • 18
    • 76449100936 scopus 로고    scopus 로고
    • Novel and selective DNA methyltransferase inhibitors: Docking-based virtual screening and experimental evaluation
    • Kuck, D.; Singh, N.; Lyko, F.; Medina-Franco, J. L. Novel and selective DNA methyltransferase inhibitors: docking-based virtual screening and experimental evaluation. Bioorg. Med. Chem., 2010, 18(2), 822-829.
    • (2010) Bioorg. Med. Chem. , vol.18 , Issue.2 , pp. 822-829
    • Kuck, D.1    Singh, N.2    Lyko, F.3    Medina-Franco, J.L.4
  • 20
    • 74049130225 scopus 로고    scopus 로고
    • Solving the Dnmt2 enigma
    • Schaefer, M.; Lyko, F. Solving the Dnmt2 enigma. Chromosoma, 2010, 119(1), 35-40.
    • (2010) Chromosoma , vol.119 , Issue.1 , pp. 35-40
    • Schaefer, M.1    Lyko, F.2
  • 21
    • 40049094942 scopus 로고    scopus 로고
    • Mammalian DNA methyltransferases: A structural perspective
    • Cheng, X.; Blumenthal, R. M. Mammalian DNA methyltransferases: a structural perspective. Structure, 2008, 16(3), 341-350.
    • (2008) Structure , vol.16 , Issue.3 , pp. 341-350
    • Cheng, X.1    Blumenthal, R.M.2
  • 22
    • 79952053850 scopus 로고    scopus 로고
    • Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation
    • Song, J.; Rechkoblit, O.; Bestor, T. H.; Patel, D. J. Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation. Science, 2011, 331(6020), 1036-1040.
    • (2011) Science , vol.331 , Issue.6020 , pp. 1036-1040
    • Song, J.1    Rechkoblit, O.2    Bestor, T.H.3    Patel, D.J.4
  • 23
    • 80051544346 scopus 로고    scopus 로고
    • Homology modeling, docking and structure-based pharmacophore of inhibitors of DNA methyltransferase
    • Yoo, J.; Medina-Franco, J. L. Homology modeling, docking and structure-based pharmacophore of inhibitors of DNA methyltransferase. J. Comput.-Aided Mol. Des., 2011, 25(6), 555-567.
    • (2011) J. Comput.-Aided Mol. Des. , vol.25 , Issue.6 , pp. 555-567
    • Yoo, J.1    Medina-Franco, J.L.2
  • 25
    • 22244435605 scopus 로고    scopus 로고
    • Epigenetic reactivation of tumor suppressor genes by a novel small-molecule inhibitor of human DNA methyltransferases
    • Brueckner, B.; Boy, R. G.; Siedlecki, P.; Musch, T.; Kliem, H. C.; Zielenkiewicz, P.; Suhai, S.; Wiessler, M.; Lyko, F. Epigenetic reactivation of tumor suppressor genes by a novel small-molecule inhibitor of human DNA methyltransferases. Cancer Res., 2005, 65(14), 6305-6311.
    • (2005) Cancer Res. , vol.65 , Issue.14 , pp. 6305-6311
    • Brueckner, B.1    Boy, R.G.2    Siedlecki, P.3    Musch, T.4    Kliem, H.C.5    Zielenkiewicz, P.6    Suhai, S.7    Wiessler, M.8    Lyko, F.9
  • 26
    • 84861231717 scopus 로고    scopus 로고
    • Trimethylaurintricarboxylic acid inhibits human DNA methyltransferase 1: Insights from enzymatic and molecular modeling studies
    • Yoo, J.; Medina-Franco, J. L. Trimethylaurintricarboxylic acid inhibits human DNA methyltransferase 1: insights from enzymatic and molecular modeling studies. J. Mol. Model., 2012, 18(4), 1583-1589.
    • (2012) J. Mol. Model. , vol.18 , Issue.4 , pp. 1583-1589
    • Yoo, J.1    Medina-Franco, J.L.2
  • 28
    • 27144509196 scopus 로고    scopus 로고
    • DNA methyltransferase inhibitors and the development of epigenetic cancer therapies
    • Lyko, F.; Brown, R. DNA methyltransferase inhibitors and the development of epigenetic cancer therapies. JNCI-J. Natl. Cancer Inst., 2005, 97(20), 1498-1506.
    • (2005) JNCI-J. Natl. Cancer Inst. , vol.97 , Issue.20 , pp. 1498-1506
    • Lyko, F.1    Brown, R.2
  • 30
    • 84863731355 scopus 로고    scopus 로고
    • Inhibitors of DNA methyltransferases: Insights from computational studies
    • Yoo, J.; Medina-Franco, J. L. Inhibitors of DNA methyltransferases: insights from computational studies. Curr. Med. Chem., 2012, 19(21), 3475-3487.
    • (2012) Curr. Med. Chem. , vol.19 , Issue.21 , pp. 3475-3487
    • Yoo, J.1    Medina-Franco, J.L.2
  • 31
    • 45049086493 scopus 로고    scopus 로고
    • 2'-Deoxy-N4-[2-(4-nitrophenyl) ethoxycarbonyl]-5-azacytidine: A novel inhibitor of DNA methyltransferase that requires activation by human carboxylesterase 1
    • Byun, H. M.; Choi, S. H.; Laird, P. W.; Trinh, B.; Siddiqui, M. A.; Marquez, V. E.; Yang, A. S. 2'-Deoxy-N4-[2-(4-nitrophenyl) ethoxycarbonyl]-5-azacytidine: a novel inhibitor of DNA methyltransferase that requires activation by human carboxylesterase 1. Cancer Lett., 2008, 266(2), 238-248.
    • (2008) Cancer Lett. , vol.266 , Issue.2 , pp. 238-248
    • Byun, H.M.1    Choi, S.H.2    Laird, P.W.3    Trinh, B.4    Siddiqui, M.A.5    Marquez, V.E.6    Yang, A.S.7
  • 32
    • 43949136445 scopus 로고    scopus 로고
    • Modes of action of the DNA methyltransferase inhibitors azacytidine and decitabine
    • Stresemann, C.; Lyko, F. Modes of action of the DNA methyltransferase inhibitors azacytidine and decitabine. Int. J. Cancer, 2008, 123(1), 8-13.
    • (2008) Int. J. Cancer , vol.123 , Issue.1 , pp. 8-13
    • Stresemann, C.1    Lyko, F.2
  • 33
    • 2542520785 scopus 로고    scopus 로고
    • Green tea polyphenols and cancer chemoprevention: Multiple mechanisms and endpoints for phase II trials
    • Moyers, S. B.; Kumar, N. B. Green tea polyphenols and cancer chemoprevention: multiple mechanisms and endpoints for phase II trials. Nutr. Rev., 2004, 62(5), 204-211.
    • (2004) Nutr. Rev. , vol.62 , Issue.5 , pp. 204-211
    • Moyers, S.B.1    Kumar, N.B.2
  • 36
    • 84904761108 scopus 로고    scopus 로고
    • Epigenetic modulators from "The Big Blue": A treasure to fight against cancer
    • Schnekenburger, M.; Dicato, M.; Diederich, M. Epigenetic modulators from "The Big Blue": A treasure to fight against cancer. Cancer Lett., 2014, 351(2), 182-197.
    • (2014) Cancer Lett. , vol.351 , Issue.2 , pp. 182-197
    • Schnekenburger, M.1    Dicato, M.2    Diederich, M.3
  • 37
    • 74049094114 scopus 로고    scopus 로고
    • Design, synthesis, inhibitory activity, and binding mode study of novel DNA methyltransferase 1 inhibitors
    • Suzuki, T.; Tanaka, R.; Hamada, S.; Nakagawa, H.; Miyata, N. Design, synthesis, inhibitory activity, and binding mode study of novel DNA methyltransferase 1 inhibitors. Bioorg. Med. Chem. Lett., 2010, 20(3), 1124-1127.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.3 , pp. 1124-1127
    • Suzuki, T.1    Tanaka, R.2    Hamada, S.3    Nakagawa, H.4    Miyata, N.5
  • 39
    • 66249127951 scopus 로고    scopus 로고
    • A new class of quinolinebased DNA hypomethylating agents reactivates tumor suppressor genes by blocking DNA methyltransferase 1 activity and inducing its degradation
    • Datta, J.; Ghoshal, K.; Denny, W. A.; Gamage, S. A.; Brooke, D. G.; Phiasivongsa, P.; Redkar, S.; Jacob, S. T. A new class of quinolinebased DNA hypomethylating agents reactivates tumor suppressor genes by blocking DNA methyltransferase 1 activity and inducing its degradation. Cancer Res., 2009, 69(10), 4277-4285.
    • (2009) Cancer Res. , vol.69 , Issue.10 , pp. 4277-4285
    • Datta, J.1    Ghoshal, K.2    Denny, W.A.3    Gamage, S.A.4    Brooke, D.G.5    Phiasivongsa, P.6    Redkar, S.7    Jacob, S.T.8
  • 40
    • 84876737019 scopus 로고    scopus 로고
    • Molecular modeling studies of the novel inhibitors of DNA methyltransferases SGI-1027 and CBC12: Implications for the mechanism of inhibition of DNMTs
    • Yoo, J.; Choi, S.; Medina-Franco, J. L. Molecular modeling studies of the novel inhibitors of DNA methyltransferases SGI-1027 and CBC12: implications for the mechanism of inhibition of DNMTs. PLoS One, 2013, 8(4), e62152.
    • (2013) PLoS One , vol.8 , Issue.4 , pp. e62152
    • Yoo, J.1    Choi, S.2    Medina-Franco, J.L.3
  • 43
    • 84880703261 scopus 로고    scopus 로고
    • Docking of a novel DNA methyltransferase inhibitor identified from high-throughput screening: Insights to unveil inhibitors in chemical databases
    • Medina-Franco, J. L.; Yoo, J. Docking of a novel DNA methyltransferase inhibitor identified from high-throughput screening: insights to unveil inhibitors in chemical databases. Mol. Divers., 2013, 17(2), 337-344.
    • (2013) Mol. Divers. , vol.17 , Issue.2 , pp. 337-344
    • Medina-Franco, J.L.1    Yoo, J.2
  • 44
    • 79955983980 scopus 로고    scopus 로고
    • Advances in the computational development of DNA methyltransferase inhibitors
    • Medina-Franco, J. L.; Caulfield, T. Advances in the computational development of DNA methyltransferase inhibitors. Drug Discov. Today, 2011, 16(9-10), 418-425.
    • (2011) Drug Discov. Today , vol.16 , Issue.9-10 , pp. 418-425
    • Medina-Franco, J.L.1    Caulfield, T.2
  • 46
    • 84863843247 scopus 로고    scopus 로고
    • Chemical and biochemical approaches in the study of histone methylation and demethylation
    • Li, K. K.; Luo, C.; Wang, D.; Jiang, H.; Zheng, Y. G. Chemical and biochemical approaches in the study of histone methylation and demethylation. Med. Res. Rev., 2012, 32(4), 815-867.
    • (2012) Med. Res. Rev. , vol.32 , Issue.4 , pp. 815-867
    • Li, K.K.1    Luo, C.2    Wang, D.3    Jiang, H.4    Zheng, Y.G.5
  • 48
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • Bedford, M. T.; Clarke, S. G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell, 2009, 33(1), 1-13.
    • (2009) Mol. Cell , vol.33 , Issue.1 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 50
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: An emerging regulator of protein function
    • Bedford, M. T.; Richard, S. Arginine methylation: an emerging regulator of protein function. Mol. Cell, 2005, 18(3), 263-272.
    • (2005) Mol. Cell , vol.18 , Issue.3 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 51
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • Couture, J. F.; Collazo, E.; Brunzelle, J. S.; Trievel, R. C. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev., 2005, 19(12), 1455-1465.
    • (2005) Genes Dev. , vol.19 , Issue.12 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 52
    • 33845487512 scopus 로고    scopus 로고
    • SET domain protein lysine methyltransferases: Structure, specificity and catalysis
    • Qian, C.; Zhou, M. M. SET domain protein lysine methyltransferases: structure, specificity and catalysis. Cell. Mol. Life Sci., 2006, 63(23), 2755-2763.
    • (2006) Cell. Mol. Life Sci. , vol.63 , Issue.23 , pp. 2755-2763
    • Qian, C.1    Zhou, M.M.2
  • 53
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang, X.; Zhou, L.; Cheng, X. D. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. Embo J., 2000, 19(14), 3509-3519.
    • (2000) Embo J. , vol.19 , Issue.14 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.D.3
  • 54
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • Zhang, X.; Cheng, X. D. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure, 2003, 11(5), 509-520.
    • (2003) Structure , vol.11 , Issue.5 , pp. 509-520
    • Zhang, X.1    Cheng, X.D.2
  • 55
    • 80055019988 scopus 로고    scopus 로고
    • Selective inhibitors of histone methyltransferase dot1l: Design, synthesis, and crystallographic studies
    • Yao, Y.; Chen, P. H.; Diao, J. S.; Cheng, G.; Deng, L. S.; Anglin, J. L.; Prasad, B. V. V.; Song, Y. C. Selective inhibitors of histone methyltransferase dot1l: design, synthesis, and crystallographic studies. J. Am. Chem. Soc., 2011, 133(42), 16746-16749.
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.42 , pp. 16746-16749
    • Yao, Y.1    Chen, P.H.2    Diao, J.S.3    Cheng, G.4    Deng, L.S.5    Anglin, J.L.6    Prasad, B.V.V.7    Song, Y.C.8
  • 56
    • 84889240753 scopus 로고    scopus 로고
    • 3 lysine-79 methyltransferase DOT1L
    • 3 lysine-79 methyltransferase DOT1L. J. Med. Chem., 2013, 56(22), 8972-8983.
    • (2013) J. Med. Chem. , vol.56 , Issue.22 , pp. 8972-8983
    • Anglin, J.L.1    Song, Y.2
  • 58
    • 77949491799 scopus 로고    scopus 로고
    • Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases
    • Dowden, J.; Hong, W.; Parry, R. V.; Pike, R. A.; Ward, S. G. Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases. Bioorg. Med. Chem. Lett., 2010, 20(7), 2103-2105.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.7 , pp. 2103-2105
    • Dowden, J.1    Hong, W.2    Parry, R.V.3    Pike, R.A.4    Ward, S.G.5
  • 59
    • 30644474460 scopus 로고    scopus 로고
    • Identification of a specific inhibitor of the histone methyltransferase SU (VAR) 3-9
    • Greiner, D.; Bonaldi, T.; Eskeland, R.; Roemer, E.; Imhof, A. Identification of a specific inhibitor of the histone methyltransferase SU (VAR) 3-9. Nat. Chem. Biol., 2005, 1(3), 143-145.
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.3 , pp. 143-145
    • Greiner, D.1    Bonaldi, T.2    Eskeland, R.3    Roemer, E.4    Imhof, A.5
  • 60
    • 77958057390 scopus 로고    scopus 로고
    • General approach to epipolythiodiketopiperazine alkaloids: Total synthesis of (+)-chaetocins A and C and (+)-12, 12'-dideoxychetracin A
    • Kim, J.; Movassaghi, M. General approach to epipolythiodiketopiperazine alkaloids: total synthesis of (+)-chaetocins A and C and (+)-12, 12'-dideoxychetracin A. J. Am. Chem. Soc., 2010, 132(41), 14376-14378.
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.41 , pp. 14376-14378
    • Kim, J.1    Movassaghi, M.2
  • 64
    • 84874999346 scopus 로고    scopus 로고
    • General approach for preparing epidithiodioxopiperazines from trioxopiperazine precursors: Enantioselective total syntheses of (+)- and (-)-gliocladine C, (+)-leptosin D, (+)-T988C, (+)-bionectin A, and (+)-gliocladin A
    • De Lorbe, J. E.; Horne, D.; Jove, R.; Mennen, S. M.; Nam, S.; Zhang, F.-L.; Overman, L. E. General approach for preparing epidithiodioxopiperazines from trioxopiperazine precursors: enantioselective total syntheses of (+)- and (-)-gliocladine C, (+)-leptosin D, (+)-T988C, (+)-bionectin A, and (+)-gliocladin A. J. Am. Chem. Soc., 2013, 135(10), 4117-4128.
    • (2013) J. Am. Chem. Soc. , vol.135 , Issue.10 , pp. 4117-4128
    • De Lorbe, J.E.1    Horne, D.2    Jove, R.3    Mennen, S.M.4    Nam, S.5    Zhang, F.-L.6    Overman, L.E.7
  • 69
    • 79960191524 scopus 로고    scopus 로고
    • Novel 3, 5-bis (bromohydroxybenzylidene) piperidin-4-ones as coactivatorassociated arginine methyltransferase 1 inhibitors: Enzyme selectivity and cellular activity
    • Cheng, D.; Valente, S.; Castellano, S.; Sbardella, G.; Di Santo, R.; Costi, R.; Bedford, M. T.; Mai, A. Novel 3, 5-bis (bromohydroxybenzylidene) piperidin-4-ones as coactivatorassociated arginine methyltransferase 1 inhibitors: enzyme selectivity and cellular activity. J. Med. Chem., 2011, 54(13), 4928-4932.
    • (2011) J. Med. Chem. , vol.54 , Issue.13 , pp. 4928-4932
    • Cheng, D.1    Valente, S.2    Castellano, S.3    Sbardella, G.4    Di Santo, R.5    Costi, R.6    Bedford, M.T.7    Mai, A.8
  • 71
    • 84864140929 scopus 로고    scopus 로고
    • A smallmolecule probe of the histone methyltransferase G9a induces cellular senescence in pancreatic adenocarcinoma
    • Yuan, Y.; Wang, Q.; Paulk, J.; Kubicek, S.; Kemp, M. M.; Adams, D. J.; Shamji, A. F.; Wagner, B. K.; Schreiber, S. L. A smallmolecule probe of the histone methyltransferase G9a induces cellular senescence in pancreatic adenocarcinoma. ACS Chem. Biol., 2012, 7(7), 1152-1157.
    • (2012) ACS Chem. Biol. , vol.7 , Issue.7 , pp. 1152-1157
    • Yuan, Y.1    Wang, Q.2    Paulk, J.3    Kubicek, S.4    Kemp, M.M.5    Adams, D.J.6    Shamji, A.F.7    Wagner, B.K.8    Schreiber, S.L.9
  • 85
    • 84875221875 scopus 로고    scopus 로고
    • Novel symmetrical ureas as modulators of protein arginine methyl transferases
    • Fontan, N.; Garcia-Dominguez, P.; Alvarez, R.; de Lera, A. R. Novel symmetrical ureas as modulators of protein arginine methyl transferases. Bioorg. Med. Chem., 2013, 21(7), 2056-2067.
    • (2013) Bioorg. Med. Chem. , vol.21 , Issue.7 , pp. 2056-2067
    • Fontan, N.1    Garcia-Dominguez, P.2    Alvarez, R.3    De Lera, A.R.4
  • 86
    • 55949109901 scopus 로고    scopus 로고
    • Cancer treatment of the future: Inhibitors of histone methyltransferases
    • Spannhoff, A.; Sippl, W.; Jung, M. Cancer treatment of the future: Inhibitors of histone methyltransferases. Int. J. Biochem. Cell Biol., 2009, 41(1), 4-11.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , Issue.1 , pp. 4-11
    • Spannhoff, A.1    Sippl, W.2    Jung, M.3
  • 95
    • 84893182116 scopus 로고    scopus 로고
    • Structural context of disease-associated mutations and putative mechanism of autoinhibition revealed by x-ray crystallographic analysis of the EZH2-SET domain
    • Antonysamy, S.; Condon, B.; Druzina, Z.; Bonanno, J. B.; Gheyi, T.; Zhang, F.; MacEwan, I.; Zhang, A.; Ashok, S.; Rodgers, L.; Russell, M.; Luz, J. G. Structural context of disease-associated mutations and putative mechanism of autoinhibition revealed by x-ray crystallographic analysis of the EZH2-SET domain. PLoS One, 2013, 8 (12).
    • (2013) PLoS One , vol.8 , Issue.12
    • Antonysamy, S.1    Condon, B.2    Druzina, Z.3    Bonanno, J.B.4    Gheyi, T.5    Zhang, F.6    MacEwan, I.7    Zhang, A.8    Ashok, S.9    Rodgers, L.10    Russell, M.11    Luz, J.G.12
  • 96
    • 84877954369 scopus 로고    scopus 로고
    • Histone methyltransferase inhibitors: Novel epigenetic agents for cancer treatment
    • Zagni, C.; Chiacchio, U.; Rescifina, A. Histone methyltransferase inhibitors: novel epigenetic agents for cancer treatment. Curr. Med. Chem., 2013, 20(2), 167-185.
    • (2013) Curr. Med. Chem. , vol.20 , Issue.2 , pp. 167-185
    • Zagni, C.1    Chiacchio, U.2    Rescifina, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.