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Volumn 5, Issue 3, 2013, Pages 858-872

Deregulation of epigenetic mechanisms by the hepatitis b virus X protein in hepatocarcinogenesis

Author keywords

DNA methyl transferases (DNMTS); DNA methylation; Epigenetic regulation; HBV replication; HBV X protein; Hepatitis B virus (HBV); Hepatocellular carcinoma (HCC); LSD1 co REST HDAC1; MYM type 2; Polycomb repressive complex 2 (PRC2); Suppressor of zeste 12 homolog (Drosophila); Suz12; Zinc finger; Znf198

Indexed keywords

DNA METHYLTRANSFERASE 1; DNA METHYLTRANSFERASE 3A; DNA METHYLTRANSFERASE 3B; HEPATITIS B VIRUS X PROTEIN; HISTONE DEACETYLASE 1; HISTONE DEMETHYLASE; INTERLEUKIN 4; LYSINE DEMETHYLASE 1; METALLOTHIONEIN; METALLOTHIONEIN 1F; MICRORNA 100; POLO LIKE KINASE 1; POLYCOMB REPRESSIVE COMPLEX 2; PROTEIN; PROTEIN SUZ12; PROTEIN ZNF198; SOMATOMEDIN BINDING PROTEIN 3; SUFU PROTEIN; TIRAP PROTEIN; UNCLASSIFIED DRUG;

EID: 84875347265     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v5030858     Document Type: Review
Times cited : (27)

References (98)
  • 1
    • 0019451351 scopus 로고
    • Hepatocellular carcinoma and hepatitis B virus. A prospective study of 22,707 men in Taiwan
    • Beasley, R.P.; Hwang, L.Y.; Lin, C.C.; Chien, C.S. Hepatocellular carcinoma and hepatitis B virus. A prospective study of 22,707 men in Taiwan. Lancet 1981, 2, 1129-1133.
    • (1981) Lancet , vol.2 , pp. 1129-1133
    • Beasley, R.P.1    Hwang, L.Y.2    Lin, C.C.3    Chien, C.S.4
  • 3
    • 34250020201 scopus 로고    scopus 로고
    • Hepatocellular carcinoma: Epidemiology and molecular carcinogenesis
    • El-Serag, H.B.; Rudolph, K.L. Hepatocellular carcinoma: Epidemiology and molecular carcinogenesis. Gastroenterology 2007, 132, 2557-2576.
    • (2007) Gastroenterology , vol.132 , pp. 2557-2576
    • El-Serag, H.B.1    Rudolph, K.L.2
  • 4
    • 4444244978 scopus 로고    scopus 로고
    • International variation
    • Parkin, D.M. International variation. Oncogene 2004, 23, 6329-6340.
    • (2004) Oncogene , vol.23 , pp. 6329-6340
    • Parkin, D.M.1
  • 9
    • 0028013064 scopus 로고
    • Woodchuck hepatitis virus X protein is required for viral infection in vivo
    • Zoulim, F.; Saputelli, J.; Seeger, C. Woodchuck hepatitis virus X protein is required for viral infection in vivo. J. Virol. 1994, 68, 2026-2030.
    • (1994) J. Virol , vol.68 , pp. 2026-2030
    • Zoulim, F.1    Saputelli, J.2    Seeger, C.3
  • 11
    • 0042692926 scopus 로고    scopus 로고
    • Nuclear import of hepatitis B virus capsids and release of the viral genome
    • Rabe, B.; Vlachou, A.; Panté, N.; Helenius, A.; Kann, M. Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc. Natl. Acad. Sci. USA 2003, 100, 9849-9854.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9849-9854
    • Rabe, B.1    Vlachou, A.2    Panté, N.3    Helenius, A.4    Kann, M.5
  • 12
    • 0020619759 scopus 로고
    • Closed circular viral DNA and asymmetrical heterogeneous forms in livers of animals infected with ground squirrel hepatitis virus
    • Weiser, B.; Ganem, D.; Seeger, C.; Varmus, H.E. Closed circular viral DNA and asymmetrical heterogeneous forms in livers of animals infected with ground squirrel hepatitis virus. J. Virol. 1983, 48, 1-9.
    • (1983) J. Virol , vol.48 , pp. 1-9
    • Weiser, B.1    Ganem, D.2    Seeger, C.3    Varmus, H.E.4
  • 13
    • 0019949367 scopus 로고
    • Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate
    • Summers, J.; Mason, W.S. Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate. Cell 1982, 29, 403-415.
    • (1982) Cell , vol.29 , pp. 403-415
    • Summers, J.1    Mason, W.S.2
  • 14
    • 33846514081 scopus 로고    scopus 로고
    • Hepatitis B virus replication. World
    • Beck, J.; Nassal, M. Hepatitis B virus replication. World J. Gastroenterol. 2007, 13, 48-64.
    • (2007) J. Gastroenterol , vol.13 , pp. 48-64
    • Beck, J.1    Nassal, M.2
  • 15
    • 0028095561 scopus 로고
    • Hepatitis B virus genome is organized into nucleosomes in the nucleus of the infected cell
    • Bock, C.T.; Schranz, P.; Schröder, C.H.; Zentgraf, H. Hepatitis B virus genome is organized into nucleosomes in the nucleus of the infected cell. Virus Genes 1994, 8, 215-229.
    • (1994) Virus Genes , vol.8 , pp. 215-229
    • Bock, C.T.1    Schranz, P.2    Schröder, C.H.3    Zentgraf, H.4
  • 16
    • 33644854241 scopus 로고    scopus 로고
    • Hepatitis B virus replication is regulated by the acetylation status of hepatitis B virus cccDNA- bound H3 and H4 histones
    • Pollicino, T.; Belloni, L.; Raffa, G.; Pediconi, N.; Squadrito, G.; Raimondo, G.; Levrero, M. Hepatitis B virus replication is regulated by the acetylation status of hepatitis B virus cccDNA- bound H3 and H4 histones. Gastroenterology 2006, 130, 827-837.
    • (2006) Gastroenterology , vol.130 , pp. 827-837
    • Pollicino, T.1    Belloni, L.2    Raffa, G.3    Pediconi, N.4    Squadrito, G.5    Raimondo, G.6    Levrero, M.7
  • 19
    • 0028567172 scopus 로고
    • Extensive oxidative DNA damage in hepatocytes of transgenic mice with chronic active hepatitis destined to develop hepatocellular carcinoma
    • Hagen, T.M.; Huang, S.; Curnutte, J.; Fowler, P.; Martinez, V.; Wehr, C.M.; Ames, B.N.; Chisari, F.V. Extensive oxidative DNA damage in hepatocytes of transgenic mice with chronic active hepatitis destined to develop hepatocellular carcinoma. Proc. Natl. Acad. Sci. USA 1994, 91, 12808-12812.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12808-12812
    • Hagen, T.M.1    Huang, S.2    Curnutte, J.3    Fowler, P.4    Martinez, V.5    Wehr, C.M.6    Ames, B.N.7    Chisari, F.V.8
  • 20
    • 0031035764 scopus 로고    scopus 로고
    • The hepatitis B virus X gene potentiates c-myc-induced liver oncogenesis in transgenic mice
    • Terradillos, O.; Billet, O.; Renard, C.A.; Levy, R.; Molina, T.; Briand, P.; Buendia, M.A. The hepatitis B virus X gene potentiates c-myc-induced liver oncogenesis in transgenic mice. Oncogene 1997, 14, 395-404.
    • (1997) Oncogene , vol.14 , pp. 395-404
    • Terradillos, O.1    Billet, O.2    Renard, C.A.3    Levy, R.4    Molina, T.5    Briand, P.6    Buendia, M.A.7
  • 21
    • 0035084167 scopus 로고    scopus 로고
    • Hepatitis B virus X protein acts as a tumor promoter in development of diethylnitrosamine-induced preneoplastic lesions
    • Madden, C.R.; Finegold, M.J.; Slagle, B.L. Hepatitis B virus X protein acts as a tumor promoter in development of diethylnitrosamine-induced preneoplastic lesions. J. Virol. 2001, 75, 3851-3858.
    • (2001) J. Virol , vol.75 , pp. 3851-3858
    • Madden, C.R.1    Finegold, M.J.2    Slagle, B.L.3
  • 22
    • 78249270725 scopus 로고    scopus 로고
    • Significant association of different preS mutations with hepatitis B-related cirrhosis or hepatocellular carcinoma
    • Yin, J.; Xie, J.; Zhang, H.; Shen, Q.; Han, L.; Lu, W.; Han, Y.; Li, C.; Ni, W.; Wang, H.; et al. Significant association of different preS mutations with hepatitis B-related cirrhosis or hepatocellular carcinoma. J. Gastroenterol. 2010, 45, 1063-1071.
    • (2010) J. Gastroenterol , vol.45 , pp. 1063-1071
    • Yin, J.1    Xie, J.2    Zhang, H.3    Shen, Q.4    Han, L.5    Lu, W.6    Han, Y.7    Li, C.8    Ni, W.9    Wang, H.10
  • 23
    • 58249123434 scopus 로고    scopus 로고
    • Hepatitis B virus core protein inhibits TRAIL-induced apoptosis of hepatocytes by blocking DR5 expression
    • Du, J.; Liang, X.; Liu, Y.; Qu, Z.; Gao, L.; Han, L.; Liu, S.; Cui, M.; Shi, Y.; Zhang, Z.; et al. Hepatitis B virus core protein inhibits TRAIL-induced apoptosis of hepatocytes by blocking DR5 expression. Cell Death Differ. 2009, 16, 219-229.
    • (2009) Cell Death Differ , vol.16 , pp. 219-229
    • Du, J.1    Liang, X.2    Liu, Y.3    Qu, Z.4    Gao, L.5    Han, L.6    Liu, S.7    Cui, M.8    Shi, Y.9    Zhang, Z.10
  • 24
    • 0031898616 scopus 로고    scopus 로고
    • Expression of Hepatitis B virus X protein in HBV-infected human livers and hepatocellular carcinomas
    • Su, Q.; Schröder, C.H.; Hofmann, W.J.; Otto, G.; Pichlmayr, R.; Bannasch, P. Expression of Hepatitis B virus X protein in HBV-infected human livers and hepatocellular carcinomas. Hepatology 1998, 27, 1109-1120.
    • (1998) Hepatology , vol.27 , pp. 1109-1120
    • Su, Q.1    Schröder, C.H.2    Hofmann, W.J.3    Otto, G.4    Pichlmayr, R.5    Bannasch, P.6
  • 25
    • 0033867475 scopus 로고    scopus 로고
    • Genetics of hepatocellular carcinoma
    • Buendia, M.A. Genetics of hepatocellular carcinoma. Semin. Cancer Biol. 2000, 10, 185-200.
    • (2000) Semin. Cancer Biol , vol.10 , pp. 185-200
    • Buendia, M.A.1
  • 26
    • 0033176296 scopus 로고    scopus 로고
    • The transcriptional function of the hepatitis B virus X protein and its role in hepatocarcinogenesis
    • Andrisani, O.M.; Barnabas, S. The transcriptional function of the hepatitis B virus X protein and its role in hepatocarcinogenesis. Int. J. Oncol. 1999, 15, 373-379.
    • (1999) Int. J. Oncol , vol.15 , pp. 373-379
    • Andrisani, O.M.1    Barnabas, S.2
  • 27
    • 8644274040 scopus 로고    scopus 로고
    • The enigmatic X gene of hepatitis B virus
    • Bouchard, M.J.; Schneider, R.J. The enigmatic X gene of hepatitis B virus. J. Virol. 2004, 78, 12725-12734.
    • (2004) J. Virol , vol.78 , pp. 12725-12734
    • Bouchard, M.J.1    Schneider, R.J.2
  • 28
    • 80052411388 scopus 로고    scopus 로고
    • Hepatitis B virus X gene and hepatocarcinogenesis
    • Ng, S.A.; Lee, C. Hepatitis B virus X gene and hepatocarcinogenesis. J. Gastroenterol. 2011, 46, 974-990.
    • (2011) J. Gastroenterol , vol.46 , pp. 974-990
    • Ng, S.A.1    Lee, C.2
  • 29
    • 84870583212 scopus 로고    scopus 로고
    • Modulation of apoptotic signaling by the hepatisis B virus X protein
    • Rawat, S.; Clippinger, A.J.; Bouchard, M.J. Modulation of apoptotic signaling by the hepatisis B virus X protein. Viruses 2012, 4, 2945-2972
    • (2012) Viruses , vol.4 , pp. 2945-2972
    • Rawat, S.1    Clippinger, A.J.2    Bouchard, M.J.3
  • 30
    • 57649116077 scopus 로고    scopus 로고
    • Hepatitis B virus X protein increases the Cdt-1-to-geminin ratio inducing DNA re-replication and polyploidy
    • Rakotomalala, L.; Studach, L.; Wang, W.H.; Gregori, G.; Hullinger, R.L.; Andrisani, O. Hepatitis B virus X protein increases the Cdt-1-to-geminin ratio inducing DNA re-replication and polyploidy. J. Biol. Chem. 2008, 283, 28729-28740.
    • (2008) J. Biol. Chem , vol.283 , pp. 28729-28740
    • Rakotomalala, L.1    Studach, L.2    Wang, W.H.3    Gregori, G.4    Hullinger, R.L.5    Andrisani, O.6
  • 31
    • 68949169033 scopus 로고    scopus 로고
    • Polo-like kinase 1 inhibition suppresses hepatitis B virus X protein-induced transformation in an in vitro model of liver cancer progression
    • Studach, L.L.; Rakotomalala, L.; Wang, W.H.; Hullinger, R.L.; Cairo, S.; Buendia, M.A.; Andrisani, O.M. Polo-like kinase 1 inhibition suppresses hepatitis B virus X protein-induced transformation in an in vitro model of liver cancer progression. Hepatology 2009, 50, 414-423.
    • (2009) Hepatology , vol.50 , pp. 414-423
    • Studach, L.L.1    Rakotomalala, L.2    Wang, W.H.3    Hullinger, R.L.4    Cairo, S.5    Buendia, M.A.6    Andrisani, O.M.7
  • 32
    • 77956943757 scopus 로고    scopus 로고
    • Polo-like kinase 1 activated by the hepatitis B virus X protein attenuates both the DNA damage checkpoint and DNA repair resulting in partial polyploidy
    • Studach, L.; Wang, W.H.; Weber, G.; Tang, J.; Hullinger, R.L.; Malbrue, R.; Liu, X.; Andrisani, O. Polo-like kinase 1 activated by the hepatitis B virus X protein attenuates both the DNA damage checkpoint and DNA repair resulting in partial polyploidy. J. Biol. Chem. 2010, 285, 30282-30293.
    • (2010) J. Biol. Chem , vol.285 , pp. 30282-30293
    • Studach, L.1    Wang, W.H.2    Weber, G.3    Tang, J.4    Hullinger, R.L.5    Malbrue, R.6    Liu, X.7    Andrisani, O.8
  • 33
    • 0028243084 scopus 로고
    • Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5
    • Golsteyn, R.M.; Schultz, S.J.; Bartek, J.; Ziemiecki, A.; Ried, T.; Nigg, E.A. Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5. J. Cell. Sci. 1994, 107, 1509-1517.
    • (1994) J. Cell. Sci , vol.107 , pp. 1509-1517
    • Golsteyn, R.M.1    Schultz, S.J.2    Bartek, J.3    Ziemiecki, A.4    Ried, T.5    Nigg, E.A.6
  • 35
    • 0029821131 scopus 로고    scopus 로고
    • Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts
    • Kumagai, A.; Dunphy, W.G. Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts. Science 1996, 273, 1377-1380.
    • (1996) Science , vol.273 , pp. 1377-1380
    • Kumagai, A.1    Dunphy, W.G.2
  • 37
    • 84867742828 scopus 로고    scopus 로고
    • Sequential analysis of multistage hepatocarcinogenesis reveals that miR-100 and PLK1 dysregulation is an early event maintained along tumor progression
    • Petrelli, A.; Perra, A.; Schernhuber, K.; Cargnelutti, M.; Salvi, A.; Migliore, C.; Ghiso, E.; Benetti, A.; Barlati, S.; Ledda-Columbano, G.M.; et al. Sequential analysis of multistage hepatocarcinogenesis reveals that miR-100 and PLK1 dysregulation is an early event maintained along tumor progression. Oncogene 2012, 31, 4517-4526.
    • (2012) Oncogene , vol.31 , pp. 4517-4526
    • Petrelli, A.1    Perra, A.2    Schernhuber, K.3    Cargnelutti, M.4    Salvi, A.5    Migliore, C.6    Ghiso, E.7    Benetti, A.8    Barlati, S.9    Ledda-Columbano, G.M.10
  • 39
    • 84870061337 scopus 로고    scopus 로고
    • Switching Polo-like kinase-1 on and off in time and space
    • Bruinsma, W.; Raaijmakers, J.A.; Medema, R.H. Switching Polo-like kinase-1 on and off in time and space. Trends Biochem. Sci. 2012, 37, 534-542.
    • (2012) Trends Biochem. Sci , vol.37 , pp. 534-542
    • Bruinsma, W.1    Raaijmakers, J.A.2    Medema, R.H.3
  • 40
    • 79953765052 scopus 로고    scopus 로고
    • Proteins ZNF198 and SUZ12 are down-regulated in hepatitis B virus (HBV) X protein-mediated hepatocyte transformation and in HBV replication
    • Wang, W.H.; Studach, L.L.; Andrisani, O.M. Proteins ZNF198 and SUZ12 are down-regulated in hepatitis B virus (HBV) X protein-mediated hepatocyte transformation and in HBV replication. Hepatology 2011, 53, 1137-1147.
    • (2011) Hepatology , vol.53 , pp. 1137-1147
    • Wang, W.H.1    Studach, L.L.2    Andrisani, O.M.3
  • 42
    • 38049134281 scopus 로고    scopus 로고
    • Effects of rearrangement and allelic exclusion of JJAZ1/SUZ12 on cell proliferation and survival
    • Li, H.; Ma, X.; Wang, J.; Koontz, J.; Nucci, M.; Sklar, J. Effects of rearrangement and allelic exclusion of JJAZ1/SUZ12 on cell proliferation and survival. Proc. Natl. Acad. Sci. USA 2007, 104, 20001-20006.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20001-20006
    • Li, H.1    Ma, X.2    Wang, J.3    Koontz, J.4    Nucci, M.5    Sklar, J.6
  • 43
    • 16244373665 scopus 로고    scopus 로고
    • Chromosome alterations in human hepatocellular carcinomas correlate with aetiology and histological grade-results of an explorative CGH meta-analysis
    • Moinzadeh, P.; Breuhahn, K.; Stützer, H.; Schirmacher, P. Chromosome alterations in human hepatocellular carcinomas correlate with aetiology and histological grade-results of an explorative CGH meta-analysis. Br. J. Cancer 2005, 92, 935-941.
    • (2005) Br. J. Cancer , vol.92 , pp. 935-941
    • Moinzadeh, P.1    Breuhahn, K.2    Stützer, H.3    Schirmacher, P.4
  • 44
    • 84984578438 scopus 로고    scopus 로고
    • Molecular genetic evidence supporting a novel human hepatocellular carcinoma tumor suppressor locus at 13q12.11. Genes Chromosom
    • Chen, C.F.; Yeh, S.H.; Chen, D.S.; Chen, P.J.; Jou, Y.S. Molecular genetic evidence supporting a novel human hepatocellular carcinoma tumor suppressor locus at 13q12.11. Genes Chromosom. Cancer 2005, 44, 320-328.
    • (2005) Cancer , vol.44 , pp. 320-328
    • Chen, C.F.1    Yeh, S.H.2    Chen, D.S.3    Chen, P.J.4    Jou, Y.S.5
  • 46
    • 33750414820 scopus 로고    scopus 로고
    • ZNF198, a zinc finger protein rearranged in myeloproliferative disease, localizes to the PML nuclear bodies and interacts with SUMO-1 and PML. Exp
    • Kunapuli, P.; Kasyapa, C.S.; Chin, S.F.; Caldas, C.; Cowell, J.K. ZNF198, a zinc finger protein rearranged in myeloproliferative disease, localizes to the PML nuclear bodies and interacts with SUMO-1 and PML. Exp. Cell Res. 2006, 312, 3739-3751.
    • (2006) Cell Res , vol.312 , pp. 3739-3751
    • Kunapuli, P.1    Kasyapa, C.S.2    Chin, S.F.3    Caldas, C.4    Cowell, J.K.5
  • 47
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat
    • Bernardi, R.; Pandolfi, P.P. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 2007, 8, 1006-1016.
    • (2007) Rev. Mol. Cell Biol , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 48
    • 63849135037 scopus 로고    scopus 로고
    • PML nuclear bodies as sites of epigenetic regulation. Front
    • Torok, D.; Ching, R.W.; Bazett-Jones, D.P. PML nuclear bodies as sites of epigenetic regulation. Front. Biosci. 2009, 14, 1325-1336.
    • (2009) Biosci , vol.14 , pp. 1325-1336
    • Torok, D.1    Ching, R.W.2    Bazett-Jones, D.P.3
  • 49
    • 81755171460 scopus 로고    scopus 로고
    • Dual functions of histone-lysine N-methyltransferase Setdb1 protein at promyelocytic leukemia-nuclear body (PML-NB): Maintaining PML-NB structure and regulating the expression of its associated genes
    • Cho, S.; Park, J.S.; Kang, Y.K. Dual functions of histone-lysine N-methyltransferase Setdb1 protein at promyelocytic leukemia-nuclear body (PML-NB): Maintaining PML-NB structure and regulating the expression of its associated genes. J. Biol. Chem. 2011, 286, 41115-41124.
    • (2011) J. Biol. Chem , vol.286 , pp. 41115-41124
    • Cho, S.1    Park, J.S.2    Kang, Y.K.3
  • 50
    • 54249103056 scopus 로고    scopus 로고
    • Regulation of apoptosis by PML and the PML-NBs
    • Bernardi, R.; Papa, A.; Pandolfi, P.P. Regulation of apoptosis by PML and the PML-NBs. Oncogene 2008, 27, 6299-6312.
    • (2008) Oncogene , vol.27 , pp. 6299-6312
    • Bernardi, R.1    Papa, A.2    Pandolfi, P.P.3
  • 51
    • 33749547681 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR
    • Dellaire, G.; Ching, R.W.; Ahmed, K.; Jalali, F.; Tse, K.C.; Bristow, R.G.; Bazett-Jones, D.P. Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR. J. Cell. Biol. 2006, 175, 55-66.
    • (2006) J. Cell. Biol , vol.175 , pp. 55-66
    • Dellaire, G.1    Ching, R.W.2    Ahmed, K.3    Jalali, F.4    Tse, K.C.5    Bristow, R.G.6    Bazett-Jones, D.P.7
  • 52
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • Everett, R.D.; Chelbi-Alix, M.K. PML and PML nuclear bodies: Implications in antiviral defence. Biochimie 2007, 89, 819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 53
    • 79951477190 scopus 로고    scopus 로고
    • Viral disruption of promyelocytic leukemia (PML) nuclear bodies by hijacking host PML regulators
    • Frappier, L. Viral disruption of promyelocytic leukemia (PML) nuclear bodies by hijacking host PML regulators. Virulence 2001, 2, 58-62.
    • (2001) Virulence , vol.2 , pp. 58-62
    • Frappier, L.1
  • 54
    • 67651180759 scopus 로고    scopus 로고
    • Targeting promyelocytic leukemia protein: A means to regulating PML nuclear bodies
    • Reineke, E.L.; Kao, H.Y. Targeting promyelocytic leukemia protein: A means to regulating PML nuclear bodies. Int. J. Biol. Sci. 2009, 5, 366-376.
    • (2009) Int. J. Biol. Sci , vol.5 , pp. 366-376
    • Reineke, E.L.1    Kao, H.Y.2
  • 55
    • 58149399387 scopus 로고    scopus 로고
    • The two functions of herpes simplex virus 1 ICP0, inhibition of silencing by the CoREST/REST/HDAC complex and degradation of PML are executed in tandem
    • Gu, H.; Roizman, B. The two functions of herpes simplex virus 1 ICP0, inhibition of silencing by the CoREST/REST/HDAC complex and degradation of PML are executed in tandem. J. Virol. 2009, 83, 181-187.
    • (2009) J. Virol , vol.83 , pp. 181-187
    • Gu, H.1    Roizman, B.2
  • 56
    • 66149091440 scopus 로고    scopus 로고
    • Engagement of the lysine-specific demethylase/HDAC1/CoREST/REST complex by herpes simplex virus 1
    • Gu, H.; Roizman, B. Engagement of the lysine-specific demethylase/HDAC1/CoREST/REST complex by herpes simplex virus 1. J. Virol. 2009, 83, 4376-4385.
    • (2009) J. Virol , vol.83 , pp. 4376-4385
    • Gu, H.1    Roizman, B.2
  • 57
    • 72449166596 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies link the DNA damage repair pathway to hepatitis B virus replication: Implications for hepatitis B virus exacerbation during chemotherapy and radiotherapy. Mol
    • Chung, Y.L.; Tsai, T.Y. Promyelocytic leukemia nuclear bodies link the DNA damage repair pathway to hepatitis B virus replication: Implications for hepatitis B virus exacerbation during chemotherapy and radiotherapy. Mol. Cancer Res. 2009, 7, 1672-1685.
    • (2009) Cancer Res , vol.7 , pp. 1672-1685
    • Chung, Y.L.1    Tsai, T.Y.2
  • 58
    • 52449110702 scopus 로고    scopus 로고
    • ZNF198 stabilizes the LSD-1-CoREST-HDAC1 complex on chromatin through its MYM-type zinc fingers
    • Gocke, C.B.; Yu, H. ZNF198 stabilizes the LSD-1-CoREST-HDAC1 complex on chromatin through its MYM-type zinc fingers. PLoS One 2008, 3, e3255.
    • (2008) PLoS One , vol.e3255 , pp. 3
    • Gocke, C.B.1    Yu, H.2
  • 59
    • 3042801308 scopus 로고    scopus 로고
    • SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol
    • Cao, R.; Zhang, Y. SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol. Cell 2004, 15, 57-67.
    • (2004) Cell , vol.15 , pp. 57-67
    • Cao, R.1    Zhang, Y.2
  • 61
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: Knowns and unknowns
    • Simon, J.A.; Kingston, R.E. Mechanisms of polycomb gene silencing: Knowns and unknowns. Nat. Rev. Mol. Cell Biol. 2009, 10, 697-708.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 62
    • 33646870495 scopus 로고    scopus 로고
    • Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions
    • Bracken, A.P.; Dietrich, N.; Pasini, D.; Hansen, K.H.; Helin, K. Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions. Genes Dev. 2006, 20, 1123-1136.
    • (2006) Genes Dev , vol.20 , pp. 1123-1136
    • Bracken, A.P.1    Dietrich, N.2    Pasini, D.3    Hansen, K.H.4    Helin, K.5
  • 64
    • 77954758157 scopus 로고    scopus 로고
    • Polycomb group protein-mediated repression of transcription. Trends Biochem
    • Morey, L.; Helin, K. Polycomb group protein-mediated repression of transcription. Trends Biochem. Sci. 2010, 35, 323-332.
    • (2010) Sci , vol.35 , pp. 323-332
    • Morey, L.1    Helin, K.2
  • 65
    • 78751662908 scopus 로고    scopus 로고
    • The Polycomb complex PRC2 and its mark in life
    • Margueron, R.; Reinberg, D. The Polycomb complex PRC2 and its mark in life. Nature 2011, 469, 343-349.
    • (2011) Nature , vol.469 , pp. 343-349
    • Margueron, R.1    Reinberg, D.2
  • 66
    • 34248169728 scopus 로고    scopus 로고
    • The Polycomb group protein Suz12 is required for embryonic stem cell differentiation
    • Pasini, D.; Bracken, A.P.; Hansen, J.B.; Capillo, M.; Helin, K. The Polycomb group protein Suz12 is required for embryonic stem cell differentiation. Mol. Cell Biol. 2007, 27, 3769-3779.
    • (2007) Mol. Cell Biol , vol.27 , pp. 3769-3779
    • Pasini, D.1    Bracken, A.P.2    Hansen, J.B.3    Capillo, M.4    Helin, K.5
  • 67
    • 77956202054 scopus 로고    scopus 로고
    • Polycomb group proteins set the stage for early lineage commitment
    • Surface, L.E.; Thornton, S.R.; Boyer, L.A. Polycomb group proteins set the stage for early lineage commitment. Cell Stem. Cell 2010, 7, 288-298.
    • (2010) Cell Stem. Cell , vol.7 , pp. 288-298
    • Surface, L.E.1    Thornton, S.R.2    Boyer, L.A.3
  • 68
    • 84862154100 scopus 로고    scopus 로고
    • PRC2 during vertebrate organogenesis: A complex in transition
    • Aldiri, I.; Vetter, M.L. PRC2 during vertebrate organogenesis: A complex in transition. Dev. Biol. 2012, 367, 91-99.
    • (2012) Dev. Biol , vol.367 , pp. 91-99
    • Aldiri, I.1    Vetter, M.L.2
  • 69
    • 84867181392 scopus 로고    scopus 로고
    • A subset of Suz12/PRC2 target genes is activated during hepatitis B virus replication and liver carcinogenesis associated with hepatitis B virus X protein
    • Studach, L.L.; Menne, S.; Cairo, S.; Buendia, M.A; Hullinger, R.L.; Lefrançois, L.; Merle, P.; Andrisani, O.M. A subset of Suz12/PRC2 target genes is activated during hepatitis B virus replication and liver carcinogenesis associated with hepatitis B virus X protein. Hepatology 2012, 56, 1240-1251.
    • (2012) Hepatology , vol.56 , pp. 1240-1251
    • Studach, L.L.1    Menne, S.2    Cairo, S.3    Buendia, M.A.4    Hullinger, R.L.5    Lefrançois, L.6    Merle, P.7    Andrisani, O.M.8
  • 70
  • 71
  • 75
    • 77956547097 scopus 로고    scopus 로고
    • Struhl, K. Loss of miR-200 inhibition of Suz12 leads to polycomb-mediated repression required for the formation and maintenance of cancer stem cells
    • Iliopoulos, D.; Lindahl-Allen, M.; Polytarchou, C; Hirsch, H.A; Tsichlis, P.N.; Struhl, K. Loss of miR-200 inhibition of Suz12 leads to polycomb-mediated repression required for the formation and maintenance of cancer stem cells. Mol. Cell 2010, 39, 761-772.
    • (2010) Mol. Cell , vol.39 , pp. 761-772
    • Iliopoulos, D.1    Lindahl-Allen, M.2    Polytarchou, C.3    Hirsch, H.A.4    Tsichlis, P.N.5
  • 76
    • 80053586436 scopus 로고    scopus 로고
    • H3K27 demethylation by JMJD3 at a poised enhancer of anti-apoptotic gene BCL2 determines ERα ligand dependency
    • Svotelis, A.; Bianco, S.; Matore, J.; Huppé, G; Nordell-Markovits, A.; Mes-Masson, A.M.; Gévry, N. H3K27 demethylation by JMJD3 at a poised enhancer of anti-apoptotic gene BCL2 determines ERα ligand dependency. EMBO J. 2011, 30, 3947-3961.
    • (2011) EMBO J , vol.30 , pp. 3947-3961
    • Svotelis, A.1    Bianco, S.2    Matore, J.3    Huppé, G.4    Nordell-Markovits, A.5    Mes-Masson, A.M.6    Gévry, N.7
  • 82
    • 0021755233 scopus 로고
    • The role of stable complexes that repress and activate eukaryotic genes
    • Brown, D.D. The role of stable complexes that repress and activate eukaryotic genes. Philos Trans. R. Soc. Lond. B Biol. Sci. 1984, 307, 297-299.
    • (1984) Philos Trans. R. Soc. Lond. B Biol. Sci , vol.307 , pp. 297-299
    • Brown, D.D.1
  • 84
    • 14844324977 scopus 로고    scopus 로고
    • Sequential DNA methylation of the Nanog and Oct-4 upstream regions in human NT2 cells during neuronal differentiation
    • Deb-Rinker, P.; Ly, D.; Jezierski, A.; Sikorska, M.; Walker, P.R. Sequential DNA methylation of the Nanog and Oct-4 upstream regions in human NT2 cells during neuronal differentiation. J. Biol. Chem. 2005, 280, 6257-6260.
    • (2005) J. Biol. Chem , vol.280 , pp. 6257-6260
    • Deb-Rinker, P.1    Ly, D.2    Jezierski, A.3    Sikorska, M.4    Walker, P.R.5
  • 86
    • 51649129596 scopus 로고    scopus 로고
    • Lineage-specific polycomb targets and de novo DNA methylation define restriction and potential of neuronal progenitors
    • Mohn, F.; Weber, M.; Rebhan, M.; Roloff, T.C.; Richter, J.; Stadler, M.B.; Bibel, M.; Schübeler, D. Lineage-specific polycomb targets and de novo DNA methylation define restriction and potential of neuronal progenitors. Mol. Cell 2008, 30, 755-766.
    • (2008) Mol. Cell , vol.30 , pp. 755-766
    • Mohn, F.1    Weber, M.2    Rebhan, M.3    Roloff, T.C.4    Richter, J.5    Stadler, M.B.6    Bibel, M.7    Schübeler, D.8
  • 88
    • 65549107163 scopus 로고    scopus 로고
    • Distinct DNA methylation patterns characterize differentiated human embryonic stem cells and developing human fetal liver
    • Brunner, A.L.; Johnson, D.S.; Kim, S.W.; Valouev, A.; Reddy, T.E.; Neff, N.F.; Anton, E.; Medina, C.; Nguyen, L.; Chiao, E.; et al. Distinct DNA methylation patterns characterize differentiated human embryonic stem cells and developing human fetal liver. Genome Res. 2009, 19, 1044-1056.
    • (2009) Genome Res , vol.19 , pp. 1044-1056
    • Brunner, A.L.1    Johnson, D.S.2    Kim, S.W.3    Valouev, A.4    Reddy, T.E.5    Neff, N.F.6    Anton, E.7    Medina, C.8    Nguyen, L.9    Chiao, E.10
  • 89
    • 34247190634 scopus 로고    scopus 로고
    • Aberrant epigenetic modifications in hepatocarcinogenesis induced by hepatitis B virus X protein
    • Park, I.Y.; Sohn, B.H.; Yu, E.; Suh, D.J.; Chung, Y.H.; Lee, J.H.; Surzycki, S.J.; Lee, Y.I. Aberrant epigenetic modifications in hepatocarcinogenesis induced by hepatitis B virus X protein. Gastroenterology 2007, 132, 1476-1494.
    • (2007) Gastroenterology , vol.132 , pp. 1476-1494
    • Park, I.Y.1    Sohn, B.H.2    Yu, E.3    Suh, D.J.4    Chung, Y.H.5    Lee, J.H.6    Surzycki, S.J.7    Lee, Y.I.8
  • 90
    • 58149310908 scopus 로고    scopus 로고
    • Epigenetic modification induced by hepatitis B virus X protein via interaction with de novo DNA methyltransferase DNMT3A
    • Zheng, D.L.; Zhang, L.; Cheng, N.; Xu, X.; Deng, Q.; Teng, X.M.; Wang, K.S.; Zhang, X.; Huang, J.; Han, Z.G. Epigenetic modification induced by hepatitis B virus X protein via interaction with de novo DNA methyltransferase DNMT3A. J. Hepatol. 2009, 50, 377-387.
    • (2009) J. Hepatol , vol.50 , pp. 377-387
    • Zheng, D.L.1    Zhang, L.2    Cheng, N.3    Xu, X.4    Deng, Q.5    Teng, X.M.6    Wang, K.S.7    Zhang, X.8    Huang, J.9    Han, Z.G.10
  • 91
    • 34250854122 scopus 로고    scopus 로고
    • Expression of DNA methyltransferase 1 is activated by hepatitis B virus X protein via a regulatory circuit involving the p16INK4a-cyclin D1-CDK 4/6-pRb-E2F1pathway
    • Jung, K.J.; Arora, P.; Pagano, J.S.; Jang, K.L. Expression of DNA methyltransferase 1 is activated by hepatitis B virus X protein via a regulatory circuit involving the p16INK4a-cyclin D1-CDK 4/6-pRb-E2F1pathway. Cancer Res. 2007, 67, 5771-5778.
    • (2007) Cancer Res , vol.67 , pp. 5771-5778
    • Jung, K.J.1    Arora, P.2    Pagano, J.S.3    Jang, K.L.4
  • 92
    • 2642551522 scopus 로고    scopus 로고
    • Structure and function of eukaryotic DNA methyltransferases
    • Chen, T.; Li, E. Structure and function of eukaryotic DNA methyltransferases. Curr. Top. Dev. Biol. 2004, 60, 55-89.
    • (2004) Curr. Top. Dev. Biol , vol.60 , pp. 55-89
    • Chen, T.1    Li, E.2
  • 94
    • 37649007673 scopus 로고    scopus 로고
    • Hepatitis B viral DNA is methylated in liver tissues
    • Vivekanandan, P.; Thomas, D.; Torbenson, M. Hepatitis B viral DNA is methylated in liver tissues. J. Viral Hepat. 2008, 15, 103-107.
    • (2008) J. Viral Hepat , vol.15 , pp. 103-107
    • Vivekanandan, P.1    Thomas, D.2    Torbenson, M.3
  • 95
    • 65649090562 scopus 로고    scopus 로고
    • Methylation regulates hepatitis B viral protein expression
    • Vivekanandan, P.; Thomas, D.; Torbenson, M. Methylation regulates hepatitis B viral protein expression. J. Infect. Dis. 2009, 199, 1286-1291.
    • (2009) J. Infect. Dis , vol.199 , pp. 1286-1291
    • Vivekanandan, P.1    Thomas, D.2    Torbenson, M.3


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