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Volumn 57, Issue 21, 2014, Pages 9028-9041

Identifying novel selective non-nucleoside DNA methyltransferase 1 inhibitors through docking-based virtual screening

Author keywords

[No Author keywords available]

Indexed keywords

1 [[1,3 DI (9H CARBAZOL 9 YL)PROPAN 2 YL]OXY] 3 (ISOPROPYLAMINO)PROPAN 2 OL; 1 [[2 (1H INDOL 3 YL)ETHYL]AMINO] 3 (9H CARBAZOL 9 YL)PROPAN 2 OL; 9 (OXIRAN 2 YLMETHYL) 9H CARBAZOLE; 9 (OXIRAN 2 YLMETHYL) 9H CARBAZOLYL; 9,9' [2 (OXIRAN 2 YLMETHOXY)PROPANE 1,3 DIYL]BIS(9H CARBAZOLE); ANTINEOPLASTIC AGENT; DNA METHYLTRANSFERASE 1; DNA METHYLTRANSFERASE INHIBITOR; NUCLEOSIDE ANALOG; UNCLASSIFIED DRUG; [2 (OXIRAN 2 YLMETHOXY)PROPANE 1,3 DIYL]BIS(9H CARBAZOLE); DNA (CYTOSINE 5) METHYLTRANSFERASE; DNA (CYTOSINE-5-)-METHYLTRANSFERASE 1; ENZYME INHIBITOR;

EID: 84923786336     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501134e     Document Type: Article
Times cited : (98)

References (44)
  • 1
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: Past, present and future
    • Yoo, C. B.; Jones, P. A. Epigenetic therapy of cancer: past, present and future Nat. Rev. Drug Discovery 2006, 5, 37-50
    • (2006) Nat. Rev. Drug Discovery , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 2
    • 40849139208 scopus 로고    scopus 로고
    • Epigenetics in cancer
    • Esteller, M. Epigenetics in cancer N. Engl. J. Med. 2008, 358, 1148-1159
    • (2008) N. Engl. J. Med. , vol.358 , pp. 1148-1159
    • Esteller, M.1
  • 3
    • 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, 1124-1127
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 1124-1127
    • Suzuki, T.1    Tanaka, R.2    Hamada, S.3    Nakagawa, H.4    Miyata, N.5
  • 5
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones, P. A.; Baylin, S. B. The epigenomics of cancer Cell 2007, 128, 683-692
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 6
    • 15744401773 scopus 로고    scopus 로고
    • Eukaryotic cytosine methyltransferases
    • Goll, M. G.; Bestor, T. H. Eukaryotic cytosine methyltransferases Annu. Rev. Biochem. 2005, 74, 481-514
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 481-514
    • Goll, M.G.1    Bestor, T.H.2
  • 7
    • 0033753779 scopus 로고    scopus 로고
    • The DNA methyltransferases of mammals
    • Bestor, T. H. The DNA methyltransferases of mammals Hum. Mol. Genet. 2000, 9, 2395-2402
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2395-2402
    • Bestor, T.H.1
  • 8
    • 0026439115 scopus 로고
    • A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei
    • Leonhardt, H.; Page, A. W.; Weier, H. U.; Bestor, T. H. A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei Cell 1992, 71, 865-873
    • (1992) Cell , vol.71 , pp. 865-873
    • Leonhardt, H.1    Page, A.W.2    Weier, H.U.3    Bestor, T.H.4
  • 10
    • 2642531973 scopus 로고    scopus 로고
    • Epigenetics in human disease and prospects for epigenetic therapy
    • Egger, G.; Liang, G.; Aparicio, A.; Jones, P. A. Epigenetics in human disease and prospects for epigenetic therapy Nature 2004, 429, 457-463
    • (2004) Nature , vol.429 , pp. 457-463
    • Egger, G.1    Liang, G.2    Aparicio, A.3    Jones, P.A.4
  • 11
    • 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, 8-13
    • (2008) Int. J. Cancer , vol.123 , pp. 8-13
    • Stresemann, C.1    Lyko, F.2
  • 13
    • 26444451123 scopus 로고    scopus 로고
    • Reversal of hypermethylation and reactivation of p16INK4a, RARbeta, and MGMT genes by genistein and other isoflavones from soy
    • Fang, M. Z.; Chen, D.; Sun, Y.; Jin, Z.; Christman, J. K.; Yang, C. S. Reversal of hypermethylation and reactivation of p16INK4a, RARbeta, and MGMT genes by genistein and other isoflavones from soy Clin. Cancer Res. 2005, 11, 7033-7041
    • (2005) Clin. Cancer Res. , vol.11 , pp. 7033-7041
    • Fang, M.Z.1    Chen, D.2    Sun, Y.3    Jin, Z.4    Christman, J.K.5    Yang, C.S.6
  • 14
    • 0345275879 scopus 로고    scopus 로고
    • Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines
    • Fang, M. Z.; Wang, Y.; Ai, N.; Hou, Z.; Sun, Y.; Lu, H.; Welsh, W.; Yang, C. S. Tea polyphenol (-)-epigallocatechin-3-gallate inhibits DNA methyltransferase and reactivates methylation-silenced genes in cancer cell lines Cancer Res. 2003, 63, 7563-7570
    • (2003) Cancer Res. , vol.63 , pp. 7563-7570
    • Fang, M.Z.1    Wang, Y.2    Ai, N.3    Hou, Z.4    Sun, Y.5    Lu, H.6    Welsh, W.7    Yang, C.S.8
  • 15
    • 84882386706 scopus 로고    scopus 로고
    • Laccaic acid A is a direct, DNA-competitive inhibitor of DNA methyltransferase 1
    • Fagan, R. L.; Cryderman, D. E.; Kopelovich, L.; Wallrath, L. L.; Brenner, C. Laccaic acid A is a direct, DNA-competitive inhibitor of DNA methyltransferase 1 J. Biol. Chem. 2013, 288, 23858-23867
    • (2013) J. Biol. Chem. , vol.288 , pp. 23858-23867
    • Fagan, R.L.1    Cryderman, D.E.2    Kopelovich, L.3    Wallrath, L.L.4    Brenner, C.5
  • 17
    • 0041939756 scopus 로고    scopus 로고
    • Procaine is a DNA-demethylating agent with growth-inhibitory effects in human cancer cells
    • Villar-Garea, A.; Fraga, M. F.; Espada, J.; Esteller, M. Procaine is a DNA-demethylating agent with growth-inhibitory effects in human cancer cells Cancer Res. 2003, 63, 4984-4989
    • (2003) Cancer Res. , vol.63 , pp. 4984-4989
    • Villar-Garea, A.1    Fraga, M.F.2    Espada, J.3    Esteller, M.4
  • 18
    • 0023936754 scopus 로고
    • Hydralazine and procainamide inhibit T-cell DNA methylation and induce autoreactivity
    • Cornacchia, E.; Golbus, J.; Maybaum, J.; Strahler, J.; Hanash, S.; Richardson, B. Hydralazine and procainamide inhibit T-cell DNA methylation and induce autoreactivity J. Immunol 1988, 140, 2197-2200
    • (1988) J. Immunol , vol.140 , pp. 2197-2200
    • Cornacchia, E.1    Golbus, J.2    Maybaum, J.3    Strahler, J.4    Hanash, S.5    Richardson, B.6
  • 20
    • 66249127951 scopus 로고    scopus 로고
    • A new class of quinoline-based 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 quinoline-based DNA hypomethylating agents reactivates tumor suppressor genes by blocking DNA methyltransferase 1 activity and inducing its degradation Cancer Res. 2009, 69, 4277-4285
    • (2009) Cancer Res. , vol.69 , 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
  • 22
    • 27644597195 scopus 로고    scopus 로고
    • Comparison of biological effects of non-nucleoside DNA methylation inhibitors versus 5-aza-2′-deoxycytidine
    • Chuang, J. C.; Yoo, C. B.; Kwan, J. M.; Li, T. W. H.; Liang, G. N.; Yang, A. S.; Jones, P. A. Comparison of biological effects of non-nucleoside DNA methylation inhibitors versus 5-aza-2′-deoxycytidine Mol. Cancer Ther. 2005, 4, 1515-1520
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1515-1520
    • Chuang, J.C.1    Yoo, C.B.2    Kwan, J.M.3    Li, T.W.H.4    Liang, G.N.5    Yang, A.S.6    Jones, P.A.7
  • 23
    • 33645086120 scopus 로고    scopus 로고
    • Functional diversity of DNA methyltransferase inhibitors in human cancer cell lines
    • Stresemann, C.; Brueckner, B.; Musch, T.; Stopper, H.; Lyko, F. Functional diversity of DNA methyltransferase inhibitors in human cancer cell lines Cancer Res. 2006, 66, 2794-2800
    • (2006) Cancer Res. , vol.66 , pp. 2794-2800
    • Stresemann, C.1    Brueckner, B.2    Musch, T.3    Stopper, H.4    Lyko, F.5
  • 30
    • 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, 815-867
    • (2012) Med. Res. Rev. , vol.32 , pp. 815-867
    • Li, K.K.1    Luo, C.2    Wang, D.3    Jiang, H.4    Zheng, Y.G.5
  • 31
    • 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, 822-829
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 822-829
    • Kuck, D.1    Singh, N.2    Lyko, F.3    Medina-Franco, J.L.4
  • 32
    • 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.; Yoo, J. Docking of a novel DNA methyltransferase inhibitor identified from high-throughput screening: insights to unveil inhibitors in chemical databases Mol. Diversity 2013, 17, 337-344
    • (2013) Mol. Diversity , vol.17 , pp. 337-344
    • Medina-Franco, J.1    Yoo, J.2
  • 33
    • 84856990498 scopus 로고    scopus 로고
    • Structure-based mechanistic insights into DNMT1-mediated maintenance DNA methylation
    • Song, J. K.; Teplova, M.; Ishibe-Murakami, S.; Patel, D. J. Structure-based mechanistic insights into DNMT1-mediated maintenance DNA methylation Science 2012, 335, 709-712
    • (2012) Science , vol.335 , pp. 709-712
    • Song, J.K.1    Teplova, M.2    Ishibe-Murakami, S.3    Patel, D.J.4
  • 34
    • 79957498244 scopus 로고    scopus 로고
    • Interaction of a ruthenium(II)-chalcone complex with double stranded DNA: Spectroscopic, molecular docking and nuclease properties
    • Gaur, R.; Khan, R. A.; Tabassum, S.; Shah, P.; Siddiqi, M. I.; Mishra, L. Interaction of a ruthenium(II)-chalcone complex with double stranded DNA: spectroscopic, molecular docking and nuclease properties J. Photochem. Photobiol. 2011, 220, 145-152
    • (2011) J. Photochem. Photobiol. , vol.220 , pp. 145-152
    • Gaur, R.1    Khan, R.A.2    Tabassum, S.3    Shah, P.4    Siddiqi, M.I.5    Mishra, L.6
  • 36
    • 0027415883 scopus 로고
    • The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats
    • Milner, C. M.; Campbell, R. D. The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats Biochem. J. 1993, 290, 811-818
    • (1993) Biochem. J. , vol.290 , pp. 811-818
    • Milner, C.M.1    Campbell, R.D.2
  • 37
    • 32044437861 scopus 로고    scopus 로고
    • Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein
    • Carbone, R.; Botrugno, O. A.; Ronzoni, S.; Insinga, A.; Di Croce, L.; Pelicci, P. G.; Minucci, S. Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein Mol. Cell. Biol. 2006, 26, 1288-1296
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1288-1296
    • Carbone, R.1    Botrugno, O.A.2    Ronzoni, S.3    Insinga, A.4    Di Croce, L.5    Pelicci, P.G.6    Minucci, S.7
  • 38
  • 39
    • 69949171492 scopus 로고    scopus 로고
    • On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex
    • Patel, A.; Dharmarajan, V.; Vought, V. E.; Cosgrove, M. S. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex J. Biol. Chem. 2009, 284, 24242-24256
    • (2009) J. Biol. Chem. , vol.284 , pp. 24242-24256
    • Patel, A.1    Dharmarajan, V.2    Vought, V.E.3    Cosgrove, M.S.4
  • 40
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • Kouskouti, A.; Scheer, E.; Staub, A.; Tora, L.; Talianidis, I. Gene-specific modulation of TAF10 function by SET9-mediated methylation Mol. Cell 2004, 14, 175-182
    • (2004) Mol. Cell , vol.14 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 41
    • 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. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides Structure 2003, 11, 509-520
    • (2003) Structure , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 42
    • 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, 3475-3487
    • (2012) Curr. Med. Chem. , vol.19 , pp. 3475-3487
    • Yoo, J.1    Medina-Franco, J.L.2
  • 44
    • 84894518920 scopus 로고    scopus 로고
    • Inhibition of DNA methylation reverses norepinephrine-induced cardiac hypertrophy in rats
    • Xiao, D.; Dasgupta, C.; Chen, M.; Zhang, K.; Buchholz, J.; Xu, Z.; Zhang, L. Inhibition of DNA methylation reverses norepinephrine-induced cardiac hypertrophy in rats Cardiovasc. Res. 2014, 101, 373-382
    • (2014) Cardiovasc. Res. , vol.101 , pp. 373-382
    • Xiao, D.1    Dasgupta, C.2    Chen, M.3    Zhang, K.4    Buchholz, J.5    Xu, Z.6    Zhang, L.7


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