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Volumn 35, Issue 4, 2010, Pages 647-663

Epigenetic modulation of host: New insights into immune evasion by viruses

Author keywords

Epigenetic modulation; HDAC inhibitors; histone deacetylases; immune evasion; methyl binding domains

Indexed keywords

ANTIVIRUS AGENT; BUTYRIC ACID; DEPSIPEPTIDE; ENTINOSTAT; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LATENT MEMBRANE PROTEIN 1; MICRORNA; MONOCYTE CHEMOTACTIC PROTEIN 1; PROTEIN P300; SINGLE STRANDED RNA; SIRTUIN; TETRAPEPTIDE; TRAPOXIN; TRICHOSTATIN A; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 78651290340     PISSN: 02505991     EISSN: 02505991     Source Type: Journal    
DOI: 10.1007/s12038-010-0072-9     Document Type: Review
Times cited : (37)

References (127)
  • 1
    • 33748159867 scopus 로고    scopus 로고
    • Effect of SWI/SNF chromatin remodeling complex on HIV-1 Tat activated transcription
    • DOI 10.1186/1742-4690-3-48
    • E. Agbottah L. Deng L. Dannenberg A. Pumfery F. Kashanchi 2006 Effect of SWI/SNF chromatin remodeling complex on HIV-1 Tat activated transcription Retrovirology 3 1 19 10.1186/1742-4690-3-48 1:CAS:528:DC%2BD28XhtVGlt7bJ (Pubitemid 44472637)
    • (2006) Retrovirology , vol.3 , pp. 48
    • Agbottah, E.1    Deng, L.2    Dannenberg, L.O.3    Pumfery, A.4    Kashanchi, F.5
  • 3
    • 0034283057 scopus 로고    scopus 로고
    • Viral mechanisms of immune evasion
    • 1:STN:280:DC%2BD3cvptlektg%3D%3D 10989308 10.1016/S0966-842X(00)01830-8
    • A. Alcami U. H. Koszinowski 2000 Viral mechanisms of immune evasion Trends Microbiol. 8 410 418 1:STN:280:DC%2BD3cvptlektg%3D%3D 10989308 10.1016/S0966-842X(00)01830-8
    • (2000) Trends Microbiol. , vol.8 , pp. 410-418
    • Alcami, A.1    Koszinowski, U.H.2
  • 4
    • 0035100475 scopus 로고    scopus 로고
    • Cellular transformation by SV40 large T antigen: Interaction with host proteins
    • DOI 10.1006/scbi.2000.0342
    • S. H. Ali J. A. Decaprio 2001 Cellular transformation by SV40 large T antigen: interaction with host proteins Semin. Cancer Biol. 11 15 23 1:CAS:528:DC%2BD3MXhslSntLc%3D 11243895 10.1006/scbi.2000.0342 (Pubitemid 32222747)
    • (2001) Seminars in Cancer Biology , vol.11 , Issue.1 , pp. 15-22
    • Ali, S.H.1    DeCaprio, J.A.2
  • 5
    • 77249159102 scopus 로고    scopus 로고
    • Attacking latent HIV provirus: From mechanism to therapeutic strategies
    • 19372797
    • N. Archin D. Margolis 2006 Attacking latent HIV provirus: from mechanism to therapeutic strategies Curr. Opin. HIV AIDS 1 134 140 19372797
    • (2006) Curr. Opin. HIV AIDS , vol.1 , pp. 134-140
    • Archin, N.1    Margolis, D.2
  • 6
    • 9244234507 scopus 로고    scopus 로고
    • The SV40 large T antigen and adenovirus E1A oncoproteins interact with distinct isoforms of the transcriptional co-activator, p300
    • 1:CAS:528:DyaK28XjtFyjt78%3D 8641289
    • M. Avantaggiati A. Graessmann Y. Nakatani B. Howard A. S. Levine 1996 The SV40 large T antigen and adenovirus E1A oncoproteins interact with distinct isoforms of the transcriptional co-activator, p300 EMBO J. 15 2236 2248 1:CAS:528:DyaK28XjtFyjt78%3D 8641289
    • (1996) EMBO J. , vol.15 , pp. 2236-2248
    • Avantaggiati, M.1    Graessmann, A.2    Nakatani, Y.3    Howard, B.4    Levine, A.S.5
  • 7
    • 0035169663 scopus 로고    scopus 로고
    • Methyl-CpG-binding proteins: Targeting specific gene repression
    • DOI 10.1046/j.1432-1327.2001.01869.x
    • E. Ballestar A. P. Wolffe 2001 Methyl-CpG-binding proteins Targeting specific gene repression Eur. J. Biochem. 268 1 6 1:CAS:528: DC%2BD3MXktVKqsw%3D%3D 11121095 10.1046/j.1432-1327.2001.01869.x (Pubitemid 32052241)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.1 , pp. 1-6
    • Ballestar, E.1    Wolffe, A.P.2
  • 10
    • 0028135497 scopus 로고
    • Hepatitis B virus HBx protein activates Ras-GTP complex formation and establishes a Ras, Raf, MAP kinase signaling cascade
    • DOI 10.1073/pnas.91.22.10350
    • J. Benn R. Schneider 1994 Hepatitis B virus HBx protein activates Ras-GTP complex formation and establishes a Ras, Raf, MAP kinase signaling cascade Proc. Natl. Acad. Sci. USA 91 10350 10354 1:CAS:528:DyaK2cXmslOrt7k%3D 7937954 10.1073/pnas.91.22.10350 (Pubitemid 24328994)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.22 , pp. 10350-10354
    • Benn, J.1    Schneider, R.J.2
  • 11
    • 0030442652 scopus 로고    scopus 로고
    • The relationship of DNA methylation to cancer
    • 1:CAS:528:DyaK2sXit1antb4%3D 8977030
    • A. Bird 1996 The relationship of DNA methylation to cancer Cancer Surv. 28 87 101 1:CAS:528:DyaK2sXit1antb4%3D 8977030
    • (1996) Cancer Surv. , vol.28 , pp. 87-101
    • Bird, A.1
  • 12
    • 0042968962 scopus 로고    scopus 로고
    • Molecular viral oncology of hepatocellular carcinoma
    • DOI 10.1038/sj.onc.1206557
    • T. Block A. Mehta C. Fimmel R. Jordan 2003 Molecular viral oncology of hepatocellular carcinoma Oncogene. 22 5093 5107 1:CAS:528:DC%2BD3sXmtFahu74%3D 12910247 10.1038/sj.onc.1206557 (Pubitemid 37059591)
    • (2003) Oncogene , vol.22 , Issue.REV. ISS. 2 , pp. 5093-5107
    • Block, T.M.1    Mehta, A.S.2    Fimmel, C.J.3    Jordan, R.4
  • 13
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • DOI 10.1038/nrd2133, PII NRD2133
    • J. E. Bolden M. J. Peart R. W. Johnstone 2006 Anticancer activities of histone deacetylase inhibitors Nat. Rev. Drug Discov. 5 769 784 1:CAS:528:DC%2BD28XptVCltrY%3D 16955068 10.1038/nrd2133 (Pubitemid 44348499)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 14
    • 0036094832 scopus 로고    scopus 로고
    • Increased production of interleukin-8 in primary human monocytes and in human epithelial and endothelial cell lines after dengue virus challenge
    • DOI 10.1128/JVI.76.11.5588-5597.2002
    • I. Bosch K. Xhaja L. Estevez G. Raines H. Melichar R. Warke M. Fournier Ennis, et al. 2002 Increased production of interleukin-8 in primary human monocytes and in human epithelial and endothelial cell lines after dengue virus challenge J. Virol. 76 5588 1:CAS:528:DC%2BD38XjslGntbc%3D 11991987 10.1128/JVI.76.11.5588-5597.2002 (Pubitemid 34517909)
    • (2002) Journal of Virology , vol.76 , Issue.11 , pp. 5588-5597
    • Bosch, I.1    Xhaja, K.2    Estevez, L.3    Raines, G.4    Melichar, H.5    Warke, R.V.6    Fournier, M.V.7    Ennis, F.A.8    Rothman, A.L.9
  • 15
    • 55549094833 scopus 로고    scopus 로고
    • Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain
    • 1:CAS:528:DC%2BD1cXhtFejtr3O 18614528 10.1074/jbc.M803514200
    • M. J. Bottomley P. Lo Surdo P. Di Giovine A. Cirillo R. Scarpelli F. Ferrigno P. Jones P. Neddermann, et al. 2008 Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain J. Biol. Chem. 283 26694 2704 1:CAS:528:DC%2BD1cXhtFejtr3O 18614528 10.1074/jbc.M803514200
    • (2008) J. Biol. Chem. , vol.283 , pp. 26694-2704
    • Bottomley, M.J.1    Lo Surdo, P.2    Di Giovine, P.3    Cirillo, A.4    Scarpelli, R.5    Ferrigno, F.6    Jones, P.7    Neddermann, P.8
  • 16
    • 0033522479 scopus 로고    scopus 로고
    • The E7 oncoprotein associates with Mi2 and histone deacetylase activity to promote cell growth
    • DOI 10.1093/emboj/18.9.2449
    • A. Brehm S. Nielsen E. Miska D. McCance 1999 The E7 oncoprotein associates with Mi2 and histone deacetylase activity to promote cell growth EMBO J. 18 2449 2458 1:CAS:528:DyaK1MXjtlKhs7s%3D 10228159 10.1093/emboj/18.9.2449 (Pubitemid 29213278)
    • (1999) EMBO Journal , vol.18 , Issue.9 , pp. 2449-2458
    • Brehm, A.1    Nielsen, S.J.2    Miska, E.A.3    McCance, D.J.4    Reid, J.L.5    Bannister, A.J.6    Kouzarides, T.7
  • 17
    • 0033524942 scopus 로고    scopus 로고
    • A viral mechanism for inhibition of P300 and PCAF acetyltransferase activity
    • DOI 10.1016/S0092-8674(00)80552-8
    • D. Chakravarti V. Ogryzko H. Y. Kao A. Nash H. Chen Y. Nakatani R. M. Evans 1999 A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity Cell 96 393 403 1:CAS:528:DyaK1MXht1eqs7s%3D 10025405 10.1016/S0092-8674(00)80552-8 (Pubitemid 29077593)
    • (1999) Cell , vol.96 , Issue.3 , pp. 393-403
    • Chakravarti, D.1    Ogryzko, V.2    Kao, H.-Y.3    Nash, A.4    Chen, H.5    Nakatani, Y.6    Evans, R.M.7
  • 18
    • 0035877189 scopus 로고    scopus 로고
    • Suppression of immune response and protective immunity to a Japanese encephalitis virus DNA vaccine by coadministration of an IL-12-expressing plasmid
    • 1:CAS:528:DC%2BD3MXksVOmsro%3D 11390494
    • H. W. Chen C. H. Pan H. W. Huan M. Y. Liau J. R. Chiang M. H. Tao 2001 Suppression of immune response and protective immunity to a Japanese encephalitis virus DNA vaccine by coadministration of an IL-12-expressing plasmid J. Immunol. 166 7419 426 1:CAS:528:DC%2BD3MXksVOmsro%3D 11390494
    • (2001) J. Immunol. , vol.166 , pp. 7419-426
    • Chen, H.W.1    Pan, C.H.2    Huan, H.W.3    Liau, M.Y.4    Chiang, J.R.5    Tao, M.H.6
  • 19
    • 58149145659 scopus 로고    scopus 로고
    • An Epstein-Barr virus-encoded microRNA targets PUMA to promote host cell survival
    • 1:CAS:528:DC%2BD1cXhtlWntL7O 18838543 10.1084/jem.20072581
    • E. Choy K. Siu K. Kok R. Lung C. Tsang K. To D. Kwong S. Tsao D. Jin 2008 An Epstein-Barr virus-encoded microRNA targets PUMA to promote host cell survival J. Exp. Med. 205 2551 2560 1:CAS:528:DC%2BD1cXhtlWntL7O 18838543 10.1084/jem.20072581
    • (2008) J. Exp. Med. , vol.205 , pp. 2551-2560
    • Choy, E.1    Siu, K.2    Kok, K.3    Lung, R.4    Tsang, C.5    To, K.6    Kwong, D.7    Tsao, S.8    Jin, D.9
  • 20
    • 0026697382 scopus 로고
    • The retinoblastoma protein and the regulation of cell cycling
    • 1:CAS:528:DyaK38Xls1yisb0%3D 1412705 10.1016/0968-0004(92)90443-D
    • D. Cobrinik S. F. Dowdy P. W. Hinds S. Mittnacht R. A. Weinberg 1992 The retinoblastoma protein and the regulation of cell cycling Trends Biochem. Sci. 17 312 315 1:CAS:528:DyaK38Xls1yisb0%3D 1412705 10.1016/0968-0004(92)90443-D
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 312-315
    • Cobrinik, D.1    Dowdy, S.F.2    Hinds, P.W.3    Mittnacht, S.4    Weinberg, R.A.5
  • 21
    • 35348829173 scopus 로고    scopus 로고
    • Polyomavirus small T antigen controls viral chromatin modifications through effects on kinetics of virus growth and cell cycle progression
    • DOI 10.1128/JVI.00821-07
    • J. Dahl H. I. Chen M. George T. L. Benjamin 2007 Polyomavirus small T antigen controls viral chromatin modifications through effects on kinetics of virus growth and cell cycle progression J. Virol. 81 10064 10071 1:CAS:528:DC%2BD2sXhtVehtL7J 17626093 10.1128/JVI.00821-07 (Pubitemid 350067710)
    • (2007) Journal of Virology , vol.81 , Issue.18 , pp. 10064-10071
    • Dahl, J.1    Chen, H.I.2    George, M.3    Benjamin, T.L.4
  • 22
    • 23744507862 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce reactivation of herpes simplex virus type 1 in a latency-associated transcript-independent manner in neuronal cells
    • DOI 10.1080/13550280590952817
    • R. J. Danaher R. J. Jacob M. R. Steiner W. R. Allen J. M. Hill C. S. Miller 2005 Histone deacetylase inhibitors induce reactivation of herpes simplex virus type 1 in a latencyassociated transcript-independent manner in neuronal cells J. Neurovirol. 11 306 317 1:CAS:528:DC%2BD2MXmt1GkurY%3D 16036811 10.1080/13550280590952817 (Pubitemid 41122419)
    • (2005) Journal of NeuroVirology , vol.11 , Issue.3 , pp. 306-317
    • Danaher, R.J.1    Jacob, R.J.2    Steiner, M.R.3    Allen, W.R.4    Hill, J.M.5    Miller, C.S.6
  • 23
    • 0037444803 scopus 로고    scopus 로고
    • Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • DOI 10.1042/BJ20021321
    • A. J. de Ruijter A. H. van Gennip H. N. Caron S. Kemp A. B. van Kuilenburg 2003 Histone deacetylases (HDACs): characterization of the classical HDAC family Biochem. J. 370 737 749 12429021 10.1042/BJ20021321 (Pubitemid 36399066)
    • (2003) Biochemical Journal , vol.370 , Issue.3 , pp. 737-749
    • De Ruijter, A.J.M.1    Van Gennip, A.H.2    Caron, H.N.3    Kemp, S.4    Van Kuilenburg, A.B.P.5
  • 24
    • 0023731010 scopus 로고
    • SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene
    • 1:CAS:528:DyaL1cXls1Kqs7Y%3D 2839300 10.1016/0092-8674(88)90559-4
    • J. A. Decaprio J. W. Ludlow J. Figge J. Y. Shew C. M. Huang W. H. Lee E. Marsilio E. Paucha D. M. Livingston 1988 SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene Cell 54 275 283 1:CAS:528:DyaL1cXls1Kqs7Y%3D 2839300 10.1016/0092-8674(88)90559-4
    • (1988) Cell , vol.54 , pp. 275-283
    • Decaprio, J.A.1    Ludlow, J.W.2    Figge, J.3    Shew, J.Y.4    Huang, C.M.5    Lee, W.H.6    Marsilio, E.7    Paucha, E.8    Livingston, D.M.9
  • 25
    • 57749101152 scopus 로고    scopus 로고
    • Specific activity of class II histone deacetylases in human breast cancer cells
    • 1:CAS:528:DC%2BD1cXhsV2iu7bI 19074835 10.1158/1541-7786.MCR-08-0299
    • V. Duong C. Bret L. Altucci A. Mai C. Duraffourd J. Loubersac P. Harmand S. Bonnet, et al. 2008 Specific activity of class II histone deacetylases in human breast cancer cells Mol. Cancer Res. 6 1908 1919 1:CAS:528: DC%2BD1cXhsV2iu7bI 19074835 10.1158/1541-7786.MCR-08-0299
    • (2008) Mol. Cancer Res. , vol.6 , pp. 1908-1919
    • Duong, V.1    Bret, C.2    Altucci, L.3    Mai, A.4    Duraffourd, C.5    Loubersac, J.6    Harmand, P.7    Bonnet, S.8
  • 26
    • 77957228862 scopus 로고    scopus 로고
    • Minocycline differentially modulates macrophage mediated peripheral immune response following Japanese encephalitis virus infection
    • 1:CAS:528:DC%2BC3cXht1CgtbnE 20153075 10.1016/j.imbio.2009.12.003
    • K. Dutta M. K. Mishra A. Nazmi K. L. Kumawat A. Basu 2010 Minocycline differentially modulates macrophage mediated peripheral immune response following Japanese encephalitis virus infection Immunobiology 215 884 893 1:CAS:528:DC%2BC3cXht1CgtbnE 20153075 10.1016/j.imbio.2009.12.003
    • (2010) Immunobiology , vol.215 , pp. 884-893
    • Dutta, K.1    Mishra, M.K.2    Nazmi, A.3    Kumawat, K.L.4    Basu, A.5
  • 27
    • 0024535228 scopus 로고
    • The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product
    • 1:CAS:528:DyaL1MXhslWjs7k%3D 2537532 10.1126/science.2537532
    • N. Dyson P. Howley K. Munger E. Harlow 1989 The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product Science 243 934 937 1:CAS:528:DyaL1MXhslWjs7k%3D 2537532 10.1126/science.2537532
    • (1989) Science , vol.243 , pp. 934-937
    • Dyson, N.1    Howley, P.2    Munger, K.3    Harlow, E.4
  • 29
    • 70349277568 scopus 로고    scopus 로고
    • Short communication: Activation of latent HIV type 1 gene expression by suberoylanilide hydroxamic acid (SAHA), an HDAC inhibitor approved for use to treat cutaneous T cell lymphoma
    • 1:CAS:528:DC%2BD1MXhtFars7jM 19689202 10.1089/aid.2008.0294
    • L. C. Edelstein S. Micheva-Viteva B. D. Phelan J. P. Dougherty 2009 Short communication: activation of latent HIV type 1 gene expression by suberoylanilide hydroxamic acid (SAHA), an HDAC inhibitor approved for use to treat cutaneous T cell lymphoma AIDS Res. Hum. Retroviruses 25 883 887 1:CAS:528:DC%2BD1MXhtFars7jM 19689202 10.1089/aid.2008.0294
    • (2009) AIDS Res. Hum. Retroviruses , vol.25 , pp. 883-887
    • Edelstein, L.C.1    Micheva-Viteva, S.2    Phelan, B.D.3    Dougherty, J.P.4
  • 30
    • 0037126388 scopus 로고    scopus 로고
    • The interaction of HTLV-1 tax with HDAC1 negatively regulates the viral gene expression
    • DOI 10.1038/sj.onc.1205701
    • T. Ego Y. Ariumi K. Shimotohno 2002 The interaction of HTLV-1 Tax with HDAC1 negatively regulates the viral gene expression Oncogene 21 7241 7246 1:CAS:528:DC%2BD38XnsFylu78%3D 12370815 10.1038/sj.onc.1205701 (Pubitemid 35305612)
    • (2002) Oncogene , vol.21 , Issue.47 , pp. 7241-7246
    • Ego, T.1    Ariumi, Y.2    Shimotohno, K.3
  • 31
    • 0032894113 scopus 로고    scopus 로고
    • Apoptosis: An innate immune response to virus infection
    • DOI 10.1016/S0966-842X(99)01487-0, PII S0966842X99014870
    • H. Everett G. McFadden 1999 Apoptosis: an innate immune response to virus infection Trends Microbiol. 7 160 165 1:STN:280:DyaK1M3jsFymsQ%3D%3D 10217831 10.1016/S0966-842X(99)01487-0 (Pubitemid 29229902)
    • (1999) Trends in Microbiology , vol.7 , Issue.4 , pp. 160-165
    • Everett, H.1    McFadden, G.2
  • 32
    • 0032092633 scopus 로고    scopus 로고
    • From sabotage to camouflage: Viral evasion of cytotoxic T lymphocyte and natural killer cell-mediated immunity
    • H. Farrell N. Davis-Poynter 1998 From sabotage to camouflage: viral evasion of cytotoxic T lymphocyte and natural killer cell-mediated immunity Semin. Cell Dev. Biol. 9 369 378 1:STN:280:DyaK1czms1ertA%3D%3D 9705659 10.1006/scdb.1998.0246 (Pubitemid 128350235)
    • (1998) Seminars in Cell and Developmental Biology , vol.9 , Issue.3 , pp. 369-378
    • Farrell, H.E.1    Davis-Poynter, N.J.2
  • 33
    • 0031808429 scopus 로고    scopus 로고
    • Signal transduction from the Epstein-Barr virus LMP-1 transforming protein
    • DOI 10.1016/S0966-842X(98)01262-1, PII S0966842X98012621
    • P. J. Farrell 1998 Signal transduction from the Epstein-Barr virus LMP-1 transforming protein Trends Microbiol. 6 175 178 1:STN:280:DyaK1c3ns1CktQ%3D%3D 9614338 10.1016/S0966-842X(98)01262-1 (Pubitemid 28259582)
    • (1998) Trends in Microbiology , vol.6 , Issue.5 , pp. 175-177
    • Farrell, P.J.1    Kieser, A.2    Gires, O.3    Hammerschmidt, W.4
  • 34
    • 0033276680 scopus 로고    scopus 로고
    • Butyrate switches the pattern of chemokine secretion by intestinal epithelial cells through histone acetylation
    • 1:CAS:528:DyaK1MXnvFaltLk%3D 10551904
    • R. D. Fusunyan J. J. Quinn M. Fujimoto R. P. MacDermott I. R. Sanderson 1999 Butyrate switches the pattern of chemokine secretion by intestinal epithelial cells through histone acetylation Mol. Med. 5 631 640 1:CAS:528:DyaK1MXnvFaltLk%3D 10551904
    • (1999) Mol. Med. , vol.5 , pp. 631-640
    • Fusunyan, R.D.1    Quinn, J.J.2    Fujimoto, M.3    MacDermott, R.P.4    Sanderson, I.R.5
  • 35
    • 57749094930 scopus 로고    scopus 로고
    • G9a and HP1 couple histone and DNA methylation to TNFα transcription silencing during endotoxin tolerance
    • 18809684 10.1074/jbc.M803446200 1:CAS:528:DC%2BD1cXhtlOjtL7I
    • M. Gazzar B. Yoza X. Chen J. Hu G. Hawkins C. McCall 2008 G9a and HP1 couple histone and DNA methylation to TNFα transcription silencing during endotoxin tolerance J. Biol. Chem. 283 32198 18809684 10.1074/jbc.M803446200 1:CAS:528:DC%2BD1cXhtlOjtL7I
    • (2008) J. Biol. Chem. , vol.283 , pp. 32198
    • Gazzar, M.1    Yoza, B.2    Chen, X.3    Hu, J.4    Hawkins, G.5    McCall, C.6
  • 36
    • 0033795196 scopus 로고    scopus 로고
    • Interferons: Cell signalling, immune modulation, antiviral response and virus countermeasures
    • 1:CAS:528:DC%2BD3cXnt12iu7o%3D 10993923
    • S. Goodbourn L. Didcock R. E. Randall 2000 Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures J. Gen. Virol. 81 2341 2364 1:CAS:528:DC%2BD3cXnt12iu7o%3D 10993923
    • (2000) J. Gen. Virol. , vol.81 , pp. 2341-2364
    • Goodbourn, S.1    Didcock, L.2    Randall, R.E.3
  • 37
    • 19644384912 scopus 로고    scopus 로고
    • Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells
    • DOI 10.1073/pnas.0502658102
    • H. Gu Y. Liang G. Mandel B. Roizman 2005 Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells Proc. Natl. Acad. Sci. USA 102 7571 7576 1:CAS:528:DC%2BD2MXkslOntbs%3D 15897453 10.1073/pnas.0502658102 (Pubitemid 40741012)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.21 , pp. 7571-7576
    • Gu, H.1    Liang, Y.2    Mandel, G.3    Roizman, B.4
  • 38
    • 36749032258 scopus 로고    scopus 로고
    • Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex
    • DOI 10.1073/pnas.0707266104
    • H. Gu B. Roizman 2007 Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex Proc. Natl. Acad. Sci. USA 104 17134 17139 1:CAS:528:DC%2BD2sXht1Kit7%2FL 17939992 10.1073/pnas.0707266104 (Pubitemid 350211004)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.43 , pp. 17134-17139
    • Gu, H.1    Roizman, B.2
  • 39
    • 66149091440 scopus 로고    scopus 로고
    • Engagement of the lysine-specific demethylase/HDAC1/CoREST/REST complex by herpes simplex virus 1
    • 1:CAS:528:DC%2BD1MXlt1Kqu70%3D 19193804 10.1128/JVI.02515-08
    • H. Gu B. Roizman 2009 Engagement of the lysine-specific demethylase/HDAC1/CoREST/REST complex by herpes simplex virus 1 J. Virol. 83 4376 4385 1:CAS:528:DC%2BD1MXlt1Kqu70%3D 19193804 10.1128/JVI.02515-08
    • (2009) J. Virol. , vol.83 , pp. 4376-4385
    • Gu, H.1    Roizman, B.2
  • 40
    • 0035136167 scopus 로고    scopus 로고
    • CREB-binding protein and histone deacetylase regulate the transcriptional activity of Kaposi's sarcoma-associated herpesvirus open reading frame 50
    • DOI 10.1128/JVI.75.4.1909-1917.2001
    • Y. Gwack H. Byun S. Hwang C. Lim J. Choe 2001 CREB-binding protein and histone deacetylase regulate the transcriptional activity of Kaposi's sarcoma-associated herpesvirus open reading frame 50 J. Virol. 75 1909 1917 1:CAS:528:DC%2BD3MXhtVSns7c%3D 11160690 10.1128/JVI.75.4.1909-1917.2001 (Pubitemid 32110181)
    • (2001) Journal of Virology , vol.75 , Issue.4 , pp. 1909-1917
    • Gwack, Y.1    Byun, H.2    Hwang, S.3    Lim, C.4    Choe, J.5
  • 41
    • 0033525094 scopus 로고    scopus 로고
    • Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A
    • DOI 10.1016/S0092-8674(00)80553-X
    • Y. Hamamori V. Sartorelli V. Ogryzko P. L. Puri H. Y. Wu J. Y. Wang Y. Nakatani L. Kedes 1999 Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A Cell 96 405 413 1:CAS:528:DyaK1MXht1eqs7g%3D 10025406 10.1016/S0092-8674(00)80553-X (Pubitemid 29077594)
    • (1999) Cell , vol.96 , Issue.3 , pp. 405-413
    • Hamamori, Y.1    Sartorelli, V.2    Ogryzko, V.3    Puri, P.L.4    Wu, H.-Y.5    Wang, J.Y.J.6    Nakatani, Y.7    Kedes, L.8
  • 42
    • 0031932893 scopus 로고    scopus 로고
    • Hepatitis B virus pX targets TFIIB in transcription coactivation
    • 1:CAS:528:DyaK1cXhtlehsrc%3D 9488473
    • I. Haviv M. Shamay G. Doitsh 1998 Hepatitis B virus pX targets TFIIB in transcription coactivation Mol Cell Biol. 18 1562 1569 1:CAS:528: DyaK1cXhtlehsrc%3D 9488473
    • (1998) Mol Cell Biol. , vol.18 , pp. 1562-1569
    • Haviv, I.1    Shamay, M.2    Doitsh, G.3
  • 43
    • 4444298521 scopus 로고    scopus 로고
    • VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection
    • DOI 10.1128/JVI.78.18.9689-9696.2004
    • F. Herrera S. Triezenberg 2004 VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection J. Virol. 78 9689 1:CAS:528:DC%2BD2cXnvVaku7s%3D 15331701 10.1128/JVI.78.18.9689-9696.2004 (Pubitemid 39187086)
    • (2004) Journal of Virology , vol.78 , Issue.18 , pp. 9689-9696
    • Herrera, F.J.1    Triezenberg, S.J.2
  • 44
    • 0344995285 scopus 로고    scopus 로고
    • Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0
    • 1:CAS:528:DyaK1MXlvFyrt7k%3D 10482575
    • W. Hobbs N. A. DeLuca 1999 Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0 J. Virol. 73 8245 8255 1:CAS:528:DyaK1MXlvFyrt7k%3D 10482575
    • (1999) J. Virol. , vol.73 , pp. 8245-8255
    • Hobbs, W.1    Deluca, N.A.2
  • 45
    • 33744921070 scopus 로고    scopus 로고
    • Trimethylation of histone H3 lysine 4 by Set1 in the lytic infection of human herpes simplex virus 1
    • DOI 10.1128/JVI.00169-06
    • J. Huang J. Kent B. Placek K. Whelan C. Hollow P. Zeng N. Fraser S. Berger 2006 Trimethylation of histone H3 lysine 4 by Set1 in the lytic infection of human herpes simplex virus 1 J. Virol. 80 5740 1:CAS:528: DC%2BD28XlsFWnur4%3D 16731913 10.1128/JVI.00169-06 (Pubitemid 43849152)
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 5740-5746
    • Huang, J.1    Kent, J.R.2    Placek, B.3    Whelan, K.A.4    Hollow, C.M.5    Zeng, P.-Y.6    Fraser, N.W.7    Berger, S.L.8
  • 46
    • 0034447617 scopus 로고    scopus 로고
    • Dengue virus infects human endothelial cells and induces IL-6 and IL-8 production
    • 1:STN:280:DC%2BD3M3mslGhtg%3D%3D 11357999
    • Y. H. Huang H. Y. Lei H. S. Liu Y. S. Lin C. C. Liu T. M. Yeh 2000 Dengue virus infects human endothelial cells and induces IL-6 and IL-8 production Am. J. Trop. Med. Hyg. 63 71 75 1:STN:280:DC%2BD3M3mslGhtg%3D%3D 11357999
    • (2000) Am. J. Trop. Med. Hyg. , vol.63 , pp. 71-75
    • Huang, Y.H.1    Lei, H.Y.2    Liu, H.S.3    Lin, Y.S.4    Liu, C.C.5    Yeh, T.M.6
  • 47
    • 34848876774 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E7 oncoprotein associates with the cullin 2 ubiquitin ligase complex, which contributes to degradation of the retinoblastoma tumor suppressor
    • DOI 10.1128/JVI.00881-07
    • K. Huh X. Zhou H. Hayakawa J. Cho 2007 Human papillomavirus type 16 E7 oncoprotein associates with the cullin 2 ubiquitin ligase complex, which contributes to degradation of the retinoblastoma tumor suppressor J. Virol. 81 9737 9747 1:CAS:528:DC%2BD2sXhtVeht7nI 17609271 10.1128/JVI.00881-07 (Pubitemid 350067678)
    • (2007) Journal of Virology , vol.81 , Issue.18 , pp. 9737-9747
    • Huh, K.1    Zhou, X.2    Hayakawa, H.3    Cho, J.-Y.4    Libermann, T.A.5    Jin, J.6    Harper, J.W.7    Munger, K.8
  • 48
    • 67849115954 scopus 로고    scopus 로고
    • Influenza A virus-induced caspase-3 cleaves the histone deacetylase 6 in infected epithelial cells
    • 1:CAS:528:DC%2BD1MXptlahu70%3D 19596000 10.1016/j.febslet.2009.07.005
    • M. Husain K. Harrod 2009 Influenza A virus-induced caspase-3 cleaves the histone deacetylase 6 in infected epithelial cells FEBS lett. 583 2517 2520 1:CAS:528:DC%2BD1MXptlahu70%3D 19596000 10.1016/j.febslet.2009.07.005
    • (2009) FEBS Lett. , vol.583 , pp. 2517-2520
    • Husain, M.1    Harrod, K.2
  • 49
    • 77952767617 scopus 로고    scopus 로고
    • Involvement of histone H3 Lysine 9 (H3K9) methyl transferase G9a in the maintenance of HIV-1 latency and its reactivation by BIX01294
    • 1:CAS:528:DC%2BC3cXmtlygs7g%3D 20335163 10.1074/jbc.M110.103531
    • K. Imai H. Togami T. Okamoto 2010 Involvement of histone H3 Lysine 9 (H3K9) methyl transferase G9a in the maintenance of HIV-1 latency and its reactivation by BIX01294 J. Biol. Chem. 285 16538 16545 1:CAS:528: DC%2BC3cXmtlygs7g%3D 20335163 10.1074/jbc.M110.103531
    • (2010) J. Biol. Chem. , vol.285 , pp. 16538-16545
    • Imai, K.1    Togami, H.2    Okamoto, T.3
  • 50
    • 33745632390 scopus 로고    scopus 로고
    • The epigenetic magic of histone lysine methylation: Delivered on 6 July 2005 at the 30th FEBS Congress in Budapest, Hungary
    • DOI 10.1111/j.1742-4658.2006.05343.x
    • T. Jenuwein 2006 The epigenetic magic of histone lysine methylation FEBS J. 273 3121 3135 1:CAS:528:DC%2BD28Xot1Cqu7s%3D 16857008 10.1111/j.1742-4658. 2006.05343.x (Pubitemid 43990918)
    • (2006) FEBS Journal , vol.273 , Issue.14 , pp. 3121-3135
    • Jenuwein, T.1
  • 51
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • T. Jenuwein C. D. Allis 2001 Translating the histone code Science 293 1074 1080 1:CAS:528:DC%2BD3MXmtVWltro%3D 11498575 10.1126/science.1063127 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 52
    • 46749124698 scopus 로고    scopus 로고
    • Position-Dependent Function for a Tandem MicroRNA miR-122-Binding Site Located in the Hepatitis C Virus RNA Genome
    • DOI 10.1016/j.chom.2008.05.013, PII S193131280800173X
    • C. Jopling S. Schutz P. Sarnow 2008 Position-dependent function for a tandem microRNA miR-122-binding site located in the hepatitis C virus RNA genome Cell Host Microbe. 4 77 85 1:CAS:528:DC%2BD1cXptF2mu7s%3D 18621012 10.1016/j.chom.2008.05.013 (Pubitemid 351944051)
    • (2008) Cell Host and Microbe , vol.4 , Issue.1 , pp. 77-85
    • Jopling, C.L.1    Schutz, S.2    Sarnow, P.3
  • 53
    • 0033959141 scopus 로고    scopus 로고
    • Inflammatory mediators in dengue virus infection in children: Interleukin-8 and its relationship to neutrophil degranulation
    • DOI 10.1128/IAI.68.2.702-707.2000
    • M. Juffrie G. M. van Der Meer C. E. Hack K. Haasnoot Sutaryo A. J. Veerman L. G. Thijs 2000 Inflammatory mediators in dengue virus infection in children: interleukin-8 and its relationship to neutrophil degranulation Infect. Immun. 68 702 707 1:CAS:528:DC%2BD3cXotFOltw%3D%3D 10639436 10.1128/IAI.68.2.702-707.2000 (Pubitemid 30056526)
    • (2000) Infection and Immunity , vol.68 , Issue.2 , pp. 702-707
    • Juffrie, M.1    Van Der Meer, G.M.2    Hack, C.E.3    Haasnoot, K.4    Sutaryo5    Veerman, A.J.P.6    Thijs, L.G.7
  • 54
    • 49349094196 scopus 로고    scopus 로고
    • The reversal of epigenetic silencing of the EBV genome is regulated by viral bZIP protein
    • 1:CAS:528:DC%2BD1cXoslCltL4%3D 18631132 10.1042/BST0360637
    • Q. H. Karlsson C. Schelcher E. Verrall C. Petosa A. J. Sinclair 2008 The reversal of epigenetic silencing of the EBV genome is regulated by viral bZIP protein Biochem. Soc. Trans. 36 637 639 1:CAS:528:DC%2BD1cXoslCltL4%3D 18631132 10.1042/BST0360637
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 637-639
    • Karlsson, Q.H.1    Schelcher, C.2    Verrall, E.3    Petosa, C.4    Sinclair, A.J.5
  • 55
    • 67650925025 scopus 로고    scopus 로고
    • Epigenetic regulation of HIV-1 latency by cytosine methylation
    • 19557157 10.1371/journal.ppat.1000495 1:CAS:528:DC%2BD1MXotVSkurc%3D
    • S. E. Kauder A. Bosque A. Lindqvist V. Planelles E. Verdin 2009 Epigenetic regulation of HIV-1 latency by cytosine methylation PLoS Pathog. 5 e1000495 19557157 10.1371/journal.ppat.1000495 1:CAS:528:DC%2BD1MXotVSkurc%3D
    • (2009) PLoS Pathog. , vol.5 , pp. 1000495
    • Kauder, S.E.1    Bosque, A.2    Lindqvist, A.3    Planelles, V.4    Verdin, E.5
  • 56
    • 4444250828 scopus 로고    scopus 로고
    • During lytic infection herpes simplex virus type 1 is associated with histones bearing modifications that correlate with active transcription
    • DOI 10.1128/JVI.78.18.10178-10186.2004
    • J. Kent P. Zeng D. Atanasiu J. Gardner N. Fraser S. Berger 2004 During lytic infection herpes simplex virus type 1 is associated with histones bearing modifications that correlate with active transcription J. Virol. 78 10178 10186 1:CAS:528:DC%2BD2cXnvVartro%3D 15331750 10.1128/JVI.78.18.10178-10186.2004 (Pubitemid 39187135)
    • (2004) Journal of Virology , vol.78 , Issue.18 , pp. 10178-10186
    • Kent, J.R.1    Zeng, P.-Y.2    Atanasiu, D.3    Gardner, J.4    Fraser, N.W.5    Berger, S.L.6
  • 57
    • 74849100521 scopus 로고    scopus 로고
    • Hepatitis B virus X protein overcomes stress-induced premature senescence by repressing p16INK4a expression via DNA methylation
    • 1:CAS:528:DC%2BC3cXhtlSju7w%3D 19656618 10.1016/j.canlet.2009.07.007
    • Y. Kim J. Jung S. Lee K. Jang 2010 Hepatitis B virus X protein overcomes stress-induced premature senescence by repressing p16INK4a expression via DNA methylation Cancer Lett. 288 226 235 1:CAS:528:DC%2BC3cXhtlSju7w%3D 19656618 10.1016/j.canlet.2009.07.007
    • (2010) Cancer Lett. , vol.288 , pp. 226-235
    • Kim, Y.1    Jung, J.2    Lee, S.3    Jang, K.4
  • 58
    • 40849139195 scopus 로고    scopus 로고
    • Curcumin inhibits herpes simplex virus immediate-early gene expression by a mechanism independent of p300/CBP histone acetyltransferase activity
    • 1:CAS:528:DC%2BD1cXjs1Wjurw%3D 18191976 10.1016/j.virol.2007.11.028
    • S. Kutluay J. Doroghazi M. Roemer S. Triezenberg 2008 Curcumin inhibits herpes simplex virus immediate-early gene expression by a mechanism independent of p300/CBP histone acetyltransferase activity Virology 373 239 247 1:CAS:528:DC%2BD1cXjs1Wjurw%3D 18191976 10.1016/j.virol.2007.11.028
    • (2008) Virology , vol.373 , pp. 239-247
    • Kutluay, S.1    Doroghazi, J.2    Roemer, M.3    Triezenberg, S.4
  • 59
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • DOI 10.1242/jcs.00493
    • M. Lachner R. O'sullivan T. Jenuwein 2003 An epigenetic road map for histone lysine methylation J. Cell Sci. 116 2117 2124 1:CAS:528: DC%2BD3sXkslCltLg%3D 12730288 10.1242/jcs.00493 (Pubitemid 36722358)
    • (2003) Journal of Cell Science , vol.116 , Issue.11 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 60
    • 0034142387 scopus 로고    scopus 로고
    • Modulating chemokines: More lessons from viruses
    • DOI 10.1016/S0167-5699(99)01556-X, PII S016756999901556X
    • A. Lalani J. Barrett G. McFadden 2000 Modulating chemokines: more lessons from viruses Immunol. Today 21 100 106 1:CAS:528:DC%2BD3cXpsFGrtg%3D%3D 10652469 10.1016/S0167-5699(99)01556-X (Pubitemid 30069624)
    • (2000) Immunology Today , vol.21 , Issue.2 , pp. 100-106
    • Lalani, A.S.1    Barrett, J.W.2    McFadden, G.3
  • 61
    • 17044392996 scopus 로고    scopus 로고
    • Role of protein methylation in regulation of transcription
    • 1:CAS:528:DC%2BD2MXjslGjsbc%3D 15479858 10.1210/er.2004-0008
    • D. Lee C. Teyssier B. Strahl M. Stallcup 2005 Role of protein methylation in regulation of transcription Endocr. Rev. 26 147 170 1:CAS:528: DC%2BD2MXjslGjsbc%3D 15479858 10.1210/er.2004-0008
    • (2005) Endocr. Rev. , vol.26 , pp. 147-170
    • Lee, D.1    Teyssier, C.2    Strahl, B.3    Stallcup, M.4
  • 62
    • 27144448810 scopus 로고    scopus 로고
    • Hepatitis B virus X protein represses E-cadherin expression via activation of DNA methyltransferase 1
    • DOI 10.1038/sj.onc.1208827, PII 1208827
    • J. Lee H. Kwun J. Jung K. Choi D. Min K. Jang 2005 Hepatitis B virus X protein represses E-cadherin expression via activation of DNA methyltransferase 1 Oncogene 24 6617 6625 1:CAS:528:DC%2BD2MXhtVOjsrzE 16007161 10.1038/sj.onc.1208827 (Pubitemid 41486792)
    • (2005) Oncogene , vol.24 , Issue.44 , pp. 6617-6625
    • Lee, J.-O.1    Hyun, J.K.2    Jin, K.J.3    Kyung, H.C.4    Do, S.M.5    Jang, K.L.6
  • 63
    • 33744951872 scopus 로고    scopus 로고
    • Tax-dependent displacement of nucleosomes during transcriptional activation of human T-cell leukemia virus type 1
    • DOI 10.1074/jbc.M512193200
    • I. Lemasson N. Polakowski P. Laybourn J. Nyborg 2006 Taxdependent displacement of nucleosomes during transcriptional activation of human T-cell leukemia virus type 1 J. Biol. Chem. 281 13075 13082 1:CAS:528: DC%2BD28Xkt1ymsrg%3D 16547351 10.1074/jbc.M512193200 (Pubitemid 43855217)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13075-13082
    • Lemasson, I.1    Polakowski, N.J.2    Laybourn, P.J.3    Nyborg, J.K.4
  • 64
    • 0025308658 scopus 로고
    • The p53 protein and its interactions with the oncogene products of the small DNA tumor viruses
    • DOI 10.1016/0042-6822(90)90505-L
    • A. Levine 1990 The p53 protein and its interactions with the oncogene products of the small DNA tumor viruses Virology 177 419 426 1:CAS:528:DyaK3cXltFSqurk%3D 2142553 10.1016/0042-6822(90)90505-L (Pubitemid 20235161)
    • (1990) Virology , vol.177 , Issue.2 , pp. 419-426
    • Levine, A.J.1
  • 65
    • 74549199294 scopus 로고    scopus 로고
    • Analysis of FOXP3+ regulatory T cells that display apparent viral antigen specificity during chronic hepatitis C virus infection
    • 20041222 10.1371/journal.ppat.1000707 1:CAS:528:DC%2BC3cXhtlCmtQ%3D%3D
    • S. Li S. Floess A. Hamann S. Gaudieri A. Lucas M. Hellard S. Roberts G. Paukovic M. Plebanski, et al. 2009 Analysis of FOXP3+ regulatory T cells that display apparent viral antigen specificity during chronic hepatitis C virus infection PLoS Pathog. 5 e1000707 20041222 10.1371/journal.ppat.1000707 1:CAS:528:DC%2BC3cXhtlCmtQ%3D%3D
    • (2009) PLoS Pathog. , vol.5 , pp. 1000707
    • Li, S.1    Floess, S.2    Hamann, A.3    Gaudieri, S.4    Lucas, A.5    Hellard, M.6    Roberts, S.7    Paukovic, G.8    Plebanski, M.9
  • 66
    • 0033554631 scopus 로고    scopus 로고
    • The human papilloma virus (HPV)-18 E6 oncoprotein physically associates with Tyk2 and impairs Jak-STAT activation by interferon-α
    • DOI 10.1038/sj.onc.1202960
    • S. Li S. Labrecque M. C. Gauzzi A. R. Cuddihy A. H. Wong S. Pellegrini G. J. Matlashewski A. E. Koromilas 1999 The human papilloma virus ( HPV) -18 E6 oncoprotein physically associates with Tyk2 and impairs Jak-STAT activation by interferon-alpha Oncogene 18 5727 5737 1:CAS:528:DyaK1MXnt1Klu70%3D 10523853 10.1038/sj.onc.1202960 (Pubitemid 29507426)
    • (1999) Oncogene , vol.18 , Issue.42 , pp. 5727-5737
    • Li, S.1    Labrecque, S.2    Gauzzi, M.C.3    Cuddihy, A.R.4    Wong, A.H.5    Pellegrini, S.6    Matlashewski, G.J.7    Koromilas, A.E.8
  • 67
    • 59449084559 scopus 로고    scopus 로고
    • Combination of proteasome and HDAC inhibitors for uterine cervical cancer treatment
    • 1:CAS:528:DC%2BD1MXlvFertA%3D%3D 19147762 10.1158/1078-0432.CCR-08-1813
    • Z. Lin M. Bazzaro M. Wang K. C. Chan S. Peng R. B. Roden 2009 Combination of proteasome and HDAC inhibitors for uterine cervical cancer treatment Clin. Cancer Res. 15 570 577 1:CAS:528:DC%2BD1MXlvFertA%3D%3D 19147762 10.1158/1078-0432.CCR-08-1813
    • (2009) Clin. Cancer Res. , vol.15 , pp. 570-577
    • Lin, Z.1    Bazzaro, M.2    Wang, M.3    Chan, K.C.4    Peng, S.5    Roden, R.B.6
  • 68
    • 67449098259 scopus 로고    scopus 로고
    • Hepatitis B virus DNA-induced carcinogenesis of human normal liver cells by virtue of nonmethylated CpG DNA
    • 1:CAS:528:DC%2BD1MXmsVaqtLw%3D 19287992 10.3892/or-00000394
    • X. Liu Q. Xu W. Chen H. Cao R. Zheng G. Li 2009 Hepatitis B virus DNA-induced carcinogenesis of human normal liver cells by virtue of nonmethylated CpG DNA Oncol. Rep. 21 941 947 1:CAS:528:DC%2BD1MXmsVaqtLw%3D 19287992 10.3892/or-00000394
    • (2009) Oncol. Rep. , vol.21 , pp. 941-947
    • Liu, X.1    Xu, Q.2    Chen, W.3    Cao, H.4    Zheng, R.5    Li, G.6
  • 69
    • 2942652424 scopus 로고    scopus 로고
    • Tax relieves transcriptional repression by promoting histone deacetylase 1 release from the human T-cell leukemia virus type 1 long terminal repeat
    • DOI 10.1128/JVI.78.13.6735-6743.2004
    • H. Lu C. Pise-Masison R. Linton H. Park R. Schiltz V. Sartorelli J. Brady 2004 Tax relieves transcriptional repression by promoting histone deacetylase 1 release from the human T-cell leukemia virus type 1 long terminal repeat J. Virol. 78 6735 6743 1:CAS:528:DC%2BD2cXltFOju7s%3D 15194748 10.1128/JVI.78.13. 6735-6743.2004 (Pubitemid 38781510)
    • (2004) Journal of Virology , vol.78 , Issue.13 , pp. 6735-6743
    • Lu, H.1    Pise-Masison, C.A.2    Linton, R.3    Park, H.U.4    Schiltz, R.L.5    Sartorelli, V.6    Brady, J.N.7
  • 70
    • 0025060176 scopus 로고
    • The retinoblastoma susceptibility gene product undergoes cell cycle-dependent dephosphorylation and binding to and release from SV40 large T
    • DOI 10.1016/0092-8674(90)90590-B
    • J. W. Ludlow J. Shon J. M. Pipas D. M. Livingston J. A. Decaprio 1990 The retinoblastoma susceptibility gene product undergoes cell cycle-dependent dephosphorylation and binding to and release from SV40 large T Cell 60 387 396 1:CAS:528:DyaK3cXhsFKjtr0%3D 2154332 10.1016/0092-8674(90)90590-B (Pubitemid 20060868)
    • (1990) Cell , vol.60 , Issue.3 , pp. 387-396
    • Ludlow, J.W.1    Shon, J.2    Pipas, J.M.3    Livingston, D.M.4    DeCaprio, J.A.5
  • 71
    • 56149090684 scopus 로고    scopus 로고
    • Epi-drugs to fight cancer: From chemistry to cancer treatment, the road ahead
    • 1:CAS:528:DC%2BD1cXhsVWnu7zI 18790076 10.1016/j.biocel.2008.08.020
    • A. Mai L. Altucci 2009 Epi-drugs to fight cancer: from chemistry to cancer treatment, the road ahead Int. J. Biochem. Cell. Biol. 41 199 213 1:CAS:528:DC%2BD1cXhsVWnu7zI 18790076 10.1016/j.biocel.2008.08.020
    • (2009) Int. J. Biochem. Cell. Biol. , vol.41 , pp. 199-213
    • Mai, A.1    Altucci, L.2
  • 72
    • 77249123298 scopus 로고    scopus 로고
    • Mechanisms of HIV latency: An emerging picture of complexity
    • 20425056 10.1007/s11904-009-0033-9
    • D. M. Margolis 2010 Mechanisms of HIV latency: an emerging picture of complexity Curr. HIV/AIDS Rep. 7 37 43 20425056 10.1007/s11904-009-0033-9
    • (2010) Curr. HIV/AIDS Rep. , vol.7 , pp. 37-43
    • Margolis, D.M.1
  • 73
    • 34547996646 scopus 로고    scopus 로고
    • Complete suppression of viral gene expression is associated with the onset and progression of lymphoid malignancy: Observations in Bovine Leukemia Virus-infected sheep
    • 10.1186/1742-4690-4-51 1:CAS:528:DC%2BD2sXpslehtbg%3D
    • M. Merimi P. Klener M. Szynal Y. Cleuter C. Bagnis P. Kerkhofs A. Burny P. Martiat A. Van den Broeke 2007 Complete suppression of viral gene expression is associated with the onset and progression of lymphoid malignancy: observations in Bovine Leukemia Virus-infected sheep Retrovirology 4 1 9 10.1186/1742-4690-4-51 1:CAS:528:DC%2BD2sXpslehtbg%3D
    • (2007) Retrovirology , vol.4 , pp. 1-9
    • Merimi, M.1    Klener, P.2    Szynal, M.3    Cleuter, Y.4    Bagnis, C.5    Kerkhofs, P.6    Burny, A.7    Martiat, P.8    Van Den Broeke, A.9
  • 74
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • DOI 10.1038/nrc1779
    • S. Minucci P. G. Pelicci 2006 Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer Nat. Rev. Cancer 6 38 51 1:CAS:528:DC%2BD28Xht1GgsA%3D%3D 16397526 10.1038/nrc1779 (Pubitemid 43054973)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 75
    • 0032563244 scopus 로고    scopus 로고
    • A viral mechanism for inhibition of the cellular phosphatase calcineurin
    • DOI 10.1126/science.281.5376.562
    • J. Miskin C. Abrams L. Goatley L. Dixon 1998 A viral mechanism for inhibition of the cellular phosphatase calcineurin Science 281 562 565 1:CAS:528:DyaK1cXkvFCqs7s%3D 9677199 10.1126/science.281.5376.562 (Pubitemid 28357371)
    • (1998) Science , vol.281 , Issue.5376 , pp. 562-565
    • Miskin, J.E.1    Abrams, C.C.2    Goatley, L.C.3    Dixon, L.K.4
  • 76
    • 0027408679 scopus 로고
    • DNA tumour virus transforming proteins and the cell cycle
    • 1:CAS:528:DyaK3sXitV2kt7s%3D 8453277 10.1016/S0959-437X(05)80342-9
    • E. Moran 1993 DNA tumour virus transforming proteins and the cell cycle Curr. Opin. Genet. Dev. 3 63 70 1:CAS:528:DyaK3sXitV2kt7s%3D 8453277 10.1016/S0959-437X(05)80342-9
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 63-70
    • Moran, E.1
  • 77
    • 64649083498 scopus 로고    scopus 로고
    • Diverse herpesvirus microRNAs target the stress-induced immune ligand MICB to escape recognition by natural killer cells
    • 1:CAS:528:DC%2BD1MXls1Sqtrk%3D 19380116 10.1016/j.chom.2009.03.003
    • D. Nachmani N. Stern-Ginossar R. Sarid O. Mandelboim 2009 Diverse herpesvirus microRNAs target the stress-induced immune ligand MICB to escape recognition by natural killer cells Cell Host Microbe. 5 376 385 1:CAS:528:DC%2BD1MXls1Sqtrk%3D 19380116 10.1016/j.chom.2009.03.003
    • (2009) Cell Host Microbe. , vol.5 , pp. 376-385
    • Nachmani, D.1    Stern-Ginossar, N.2    Sarid, R.3    Mandelboim, O.4
  • 78
    • 0037052539 scopus 로고    scopus 로고
    • 0 cells
    • DOI 10.1126/science.1069861
    • H. Ogawa K. Ishiguro S. Gaubatz D. M. Livingston Y. Nakatani 2002 A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells Science 296 1132 1136 1:CAS:528:DC%2BD38XjslamtLY%3D 12004135 10.1126/science.1069861 (Pubitemid 34517133)
    • (2002) Science , vol.296 , Issue.5570 , pp. 1132-1136
    • Ogawa, H.1    Ishiguro, K.-I.2    Gaubatz, S.3    Livingston, D.M.4    Nakatani, Y.5
  • 79
    • 1342279571 scopus 로고    scopus 로고
    • The HSV-1 Us3 protein kinase is sufficient to block apoptosis induced by overexpression of a variety of Bcl-2 family members
    • DOI 10.1016/j.virol.2003.10.019
    • s3 protein kinase is sufficient to block apoptosis induced by overexpression of a variety of Bcl-2 family members Virology 319 212 224 1:CAS:528:DC%2BD2cXhsFWks7o%3D 14980482 10.1016/j.virol.2003.10.019 (Pubitemid 38251263)
    • (2004) Virology , vol.319 , Issue.2 , pp. 212-224
    • Ogg, P.D.1    McDonell, P.J.2    Ryckman, B.J.3    Knudson, C.M.4    Roller, R.J.5
  • 80
    • 41149097014 scopus 로고    scopus 로고
    • Temporal association of the herpes simplex virus genome with histone proteins during a lytic infection
    • DOI 10.1128/JVI.00586-07
    • J. Oh N. Fraser 2008 Temporal association of the herpes simplex virus genome with histone proteins during a lytic infection J. Virol. 82 3530 3537 1:CAS:528:DC%2BD1cXjvFensbs%3D 18160436 10.1128/JVI.00586-07 (Pubitemid 351429928)
    • (2008) Journal of Virology , vol.82 , Issue.7 , pp. 3530-3537
    • Oh, J.1    Fraser, N.W.2
  • 81
    • 0033486062 scopus 로고    scopus 로고
    • Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1
    • 1:CAS:528:DC%2BD3cXhslOqsQ%3D%3D 10581239 10.1093/emboj/18.23.6653
    • I. Ohki N. Shimotake N. Fujita M. Nakao M. Shirakawa 1999 Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1 EMBO. J. 18 6653 6661 1:CAS:528: DC%2BD3cXhslOqsQ%3D%3D 10581239 10.1093/emboj/18.23.6653
    • (1999) EMBO. J. , vol.18 , pp. 6653-6661
    • Ohki, I.1    Shimotake, N.2    Fujita, N.3    Nakao, M.4    Shirakawa, M.5
  • 82
    • 57349090221 scopus 로고    scopus 로고
    • Epigenetic silencing of human immunodeficiency virus (HIV) transcription by formation of restrictive chromatin structures at the viral long terminal repeat drives the progressive entry of HIV into latency
    • 1:CAS:528:DC%2BD1cXhsVymsL%2FF 18829756 10.1128/JVI.01383-08
    • R. Pearson Y. K. Kim J. Hokello K. Lassen J. Friedman M. Tyagi J. Karn 2008 Epigenetic silencing of human immunodeficiency virus (HIV) transcription by formation of restrictive chromatin structures at the viral long terminal repeat drives the progressive entry of HIV into latency J. Virol. 82 12291 12303 1:CAS:528:DC%2BD1cXhsVymsL%2FF 18829756 10.1128/JVI.01383-08
    • (2008) J. Virol. , vol.82 , pp. 12291-12303
    • Pearson, R.1    Kim, Y.K.2    Hokello, J.3    Lassen, K.4    Friedman, J.5    Tyagi, M.6    Karn, J.7
  • 83
    • 0035861594 scopus 로고    scopus 로고
    • Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation
    • 1:CAS:528:DC%2BD3MXpt1GlsLg%3D 11602581 10.1074/jbc.M105590200
    • M. K. Pflum J. K. Tong W. S. Lane S. L. Schreiber 2001 Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation J. Biol. Chem. 276 47733 47741 1:CAS:528:DC%2BD3MXpt1GlsLg%3D 11602581 10.1074/jbc.M105590200
    • (2001) J. Biol. Chem. , vol.276 , pp. 47733-47741
    • Pflum, M.K.1    Tong, J.K.2    Lane, W.S.3    Schreiber, S.L.4
  • 84
    • 0242661003 scopus 로고    scopus 로고
    • Herpes Simplex Virus 1 Gene Expression Is Accelerated by Inhibitors of Histone Deacetylases in Rabbit Skin Cells Infected with a Mutant Carrying a cDNA Copy of the Infected-Cell Protein No. 0
    • DOI 10.1128/JVI.77.23.12671-12678.2003
    • A. P. Poon Y. Liang B. Roizman 2003 Herpes simplex virus 1 gene expression is accelerated by inhibitors of histone deacetylases in rabbit skin cells infected with a mutant carrying a cDNA copy of the infected-cell protein no 0 J. Virol. 77 12671 12678 1:CAS:528:DC%2BD3sXptFOjs70%3D 14610189 10.1128/JVI.77.23.12671-12678.2003 (Pubitemid 37430662)
    • (2003) Journal of Virology , vol.77 , Issue.23 , pp. 12671-12678
    • Poon, A.P.W.1    Liang, Y.2    Roizman, B.3
  • 85
    • 33745617128 scopus 로고    scopus 로고
    • S3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression
    • DOI 10.1073/pnas.0604142103
    • s3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression Proc. Natl. Acad. Sci. USA 103 9993 9998 1:CAS:528:DC%2BD28XmvVajurw%3D 16785443 10.1073/pnas.0604142103 (Pubitemid 43993611)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.26 , pp. 9993-9998
    • Poon, A.P.W.1    Gu, H.2    Roizman, B.3
  • 86
    • 3242683268 scopus 로고    scopus 로고
    • P53 targets simian virus 40 large T antigen for acetylation by CBP
    • DOI 10.1128/JVI.78.15.8245-8253.2004
    • D. L. Poulin A. L. Kung J. A. Decaprio 2004 p53 targets Simian Virus 40 large T antigen for acetylation by CBP J. Virol. 78 8245 8253 1:CAS:528:DC%2BD2cXmtFCjsLk%3D 15254196 10.1128/JVI.78.15.8245-8253.2004 (Pubitemid 38944308)
    • (2004) Journal of Virology , vol.78 , Issue.15 , pp. 8245-8253
    • Poulin, D.L.1    Kung, A.L.2    DeCaprio, J.A.3
  • 87
    • 77955425193 scopus 로고    scopus 로고
    • MiR-122-induced down-regulation of HO-1 negatively affects miR-122-mediated suppression of HBV
    • 1:CAS:528:DC%2BC3cXpvFKgurg%3D 20633528 10.1016/j.bbrc.2010.07.021
    • L. Qiu H. Fan W. Jin B. Zhao Y. Wang Y. Ju 2010 miR-122-induced down-regulation of HO-1 negatively affects miR-122-mediated suppression of HBV Biochem. Biophys. Res. Commun. 398 771 777 1:CAS:528:DC%2BC3cXpvFKgurg%3D 20633528 10.1016/j.bbrc.2010.07.021
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 771-777
    • Qiu, L.1    Fan, H.2    Jin, W.3    Zhao, B.4    Wang, Y.5    Ju, Y.6
  • 88
    • 0032991714 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription
    • 1:CAS:528:DyaK1MXjvFyksb0%3D 10364319
    • S. A. Radkov R. Touitou A. Brehm M. Rowe M. West T. Kouzarides M. J. Allday 1999 Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription J. Virol. 73 5688 5697 1:CAS:528: DyaK1MXjvFyksb0%3D 10364319
    • (1999) J. Virol. , vol.73 , pp. 5688-5697
    • Radkov, S.A.1    Touitou, R.2    Brehm, A.3    Rowe, M.4    West, M.5    Kouzarides, T.6    Allday, M.J.7
  • 90
    • 0036304760 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: A new class of potential therapeutic agents for cancer treatment
    • 11895892
    • V. M. Richon J. P. O'Brien 2002 Histone deacetylase inhibitors: a new class of potential therapeutic agents for cancer treatment Clin. Cancer Res. 8 662 664 11895892
    • (2002) Clin. Cancer Res. , vol.8 , pp. 662-664
    • Richon, V.M.1    O'Brien, J.P.2
  • 91
    • 72249089735 scopus 로고    scopus 로고
    • Epigenetic silencing of interferon-kappa in human papillomavirus type 16-positive cells
    • 1:CAS:528:DC%2BD1MXhtl2rtr7M 19887612 10.1158/0008-5472.CAN-09-0550
    • B. Rincon-Orozco G. Halec S. Rosenberger D. Muschik I. Nindl A. Bachmann T. M. Ritter B. Dondog, et al. 2009 Epigenetic silencing of interferon-kappa in human papillomavirus type 16-positive cells Cancer Res. 69 8718 8725 1:CAS:528:DC%2BD1MXhtl2rtr7M 19887612 10.1158/0008-5472.CAN-09-0550
    • (2009) Cancer Res. , vol.69 , pp. 8718-8725
    • Rincon-Orozco, B.1    Halec, G.2    Rosenberger, S.3    Muschik, D.4    Nindl, I.5    Bachmann, A.6    Ritter, T.M.7    Dondog, B.8
  • 92
    • 6344281172 scopus 로고    scopus 로고
    • Identification of mammalian microRNA host genes and transcription units
    • DOI 10.1101/gr.2722704
    • A. Rodriguez S. Griffiths-Jones J. Ashurst A. Bradley 2004 Identification of mammalian microRNA host genes and transcription units Genome Res. 14 1902 1910 1:CAS:528:DC%2BD2cXotl2hu7w%3D 15364901 10.1101/gr.2722704 (Pubitemid 39386503)
    • (2004) Genome Research , vol.14 , Issue.10 , pp. 1902-1910
    • Rodriguez, A.1    Griffiths-Jones, S.2    Ashurst, J.L.3    Bradley, A.4
  • 93
    • 9144246375 scopus 로고    scopus 로고
    • Comparative study of methyl-CpG-binding domain proteins
    • DOI 10.1186/1471-2164-4-1
    • T. C. Roloff H. H. Ropers U. A. Nuber 2003 Comparative study of methyl-CpG-binding domain proteins BMC Genomics 4 1 12529184 10.1186/1471-2164-4-1 (Pubitemid 39546608)
    • (2003) BMC Genomics , vol.4 , pp. 1
    • Roloff, T.C.1    Ropers, H.H.2    Nuber, U.A.3
  • 94
    • 73149083473 scopus 로고    scopus 로고
    • Functions of Tat: The versatile protein of human immunodeficiency virus type 1
    • 1:CAS:528:DC%2BC3cXmtVyjtw%3D%3D 19812265 10.1099/vir.0.016303-0
    • B. Romani S. Engelbrecht R. Glashoff 2010 Functions of Tat: the versatile protein of human immunodeficiency virus type 1 J. Gen. Virol. 91 1 12 1:CAS:528:DC%2BC3cXmtVyjtw%3D%3D 19812265 10.1099/vir.0.016303-0
    • (2010) J. Gen. Virol. , vol.91 , pp. 1-12
    • Romani, B.1    Engelbrecht, S.2    Glashoff, R.3
  • 95
    • 2942631126 scopus 로고    scopus 로고
    • Localized domains of G9a-mediated histone methylation are required for silencing of neuronal genes
    • DOI 10.1016/j.molcel.2004.05.026, PII S109727650400303X
    • A. Roopra R. Qazi B. Schoenike T. Daley J. Morrison 2004 Localized domains of G9a-mediated histone methylation are required for silencing of neuronal genes Mol. Cell. 14 727 738 1:CAS:528:DC%2BD2cXlslemtr4%3D 15200951 10.1016/j.molcel.2004.05.026 (Pubitemid 38780847)
    • (2004) Molecular Cell , vol.14 , Issue.6 , pp. 727-738
    • Roopra, A.1    Qazi, R.2    Schoenike, B.3    Daley, T.J.4    Morrison, J.F.5
  • 96
    • 0027243333 scopus 로고
    • The effect of DNA methylation on gene regulation of human papillomaviruses
    • 8388016 10.1099/0022-1317-74-5-791
    • F. Rosl A. Arab B. Klevenz 1993 The effect of DNA methylation on gene regulation of human papillomaviruses J. Gen. Virol. 74 791 801 8388016 10.1099/0022-1317-74-5-791
    • (1993) J. Gen. Virol. , vol.74 , pp. 791-801
    • Rosl, F.1    Arab, A.2    Klevenz, B.3
  • 97
    • 23744456548 scopus 로고    scopus 로고
    • Valproic acid: A potential role in treating latent HIV infection
    • DOI 10.1016/S0140-6736(05)67074-2, PII S0140673605670742
    • J. Routy 2005 Valproic acid: a potential role in treating latent HIV infection Lancet 366 523 524 16099272 10.1016/S0140-6736(05)67074-2 (Pubitemid 41140313)
    • (2005) Lancet , vol.366 , Issue.9485 , pp. 523-524
    • Routy, J.-P.1
  • 99
    • 26444541842 scopus 로고    scopus 로고
    • T-cell tropism and the role of ORF66 protein in pathogenesis of varicella-zoster virus infection
    • DOI 10.1128/JVI.79.20.12921-12933.2005
    • A. Schaap J. F. Fortin M. Sommer L. Zerboni S. Stamatis C. C. Ku G. P. Nolan A. M. Arvin 2005 T-cell tropism and the role of ORF66 protein in pathogenesis of varicella-zoster virus infection J. Virol. 79 12921 12933 1:CAS:528:DC%2BD2MXhtFWisbrP 16188994 10.1128/JVI.79.20.12921-12933.2005 (Pubitemid 41433211)
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 12921-12933
    • Schaap, A.1    Fortin, J.-F.2    Sommer, M.3    Zerboni, L.4    Stamatis, S.5    Ku, C.-C.6    Nolan, G.P.7    Arvin, A.M.8
  • 100
    • 45549095066 scopus 로고    scopus 로고
    • Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity
    • 1:CAS:528:DC%2BD1cXkvVSgtrw%3D 18285338 10.1074/jbc.M707362200
    • A. Schuetz J. Min A. Allali-Hassani M. Schapira M. Shuen P. Loppnau R. Mazitschek N. P. Kwiatkowski, et al. 2008 Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity J. Biol. Chem. 283 11355 11363 1:CAS:528:DC%2BD1cXkvVSgtrw%3D 18285338 10.1074/jbc.M707362200
    • (2008) J. Biol. Chem. , vol.283 , pp. 11355-11363
    • Schuetz, A.1    Min, J.2    Allali-Hassani, A.3    Schapira, M.4    Shuen, M.5    Loppnau, P.6    Mazitschek, R.7    Kwiatkowski, N.P.8
  • 101
    • 0032913880 scopus 로고    scopus 로고
    • New insights into the mechanism of inhibition of p53 by simian virus 40 large T antigen
    • 1:CAS:528:DyaK1MXit1amtL0%3D 10082540
    • H. M. Sheppard S. I. Corneilli C. Espiritu A. Gatti X. Liu 1999 New insights into the mechanism of inhibition of p53 by simian virus 40 large T antigen Mol. Cell. Biol. 19 2746 2753 1:CAS:528:DyaK1MXit1amtL0%3D 10082540
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2746-2753
    • Sheppard, H.M.1    Corneilli, S.I.2    Espiritu, C.3    Gatti, A.4    Liu, X.5
  • 102
    • 0037455979 scopus 로고    scopus 로고
    • P16 Hypermethylation in the early stage of hepatitis B virus-associated hepatocarcinogenesis
    • DOI 10.1016/S0304-3835(02)00613-4
    • Y. Shim G. Yoon H. Choi Y. Chung E. Yu 2003 p16 Hypermethylation in the early stage of hepatitis B virusassociated hepatocarcinogenesis Cancer Lett. 190 213 219 1:CAS:528:DC%2BD3sXmsV2mtw%3D%3D 12565176 10.1016/S0304-3835(02)00613-4 (Pubitemid 36136020)
    • (2003) Cancer Letters , vol.190 , Issue.2 , pp. 213-219
    • Shim, Y.-H.1    Yoon, G.-S.2    Choi, H.-J.3    Chung, Y.H.4    Yu, E.5
  • 104
    • 0030696143 scopus 로고    scopus 로고
    • Vaccinia virus immune evasion
    • 1:CAS:528:DyaK2sXnvFKrtbs%3D 9416508 10.1111/j.1600-065X.1997.tb01012.x
    • G. L. Smith J. A. Symons A. Khanna A. Vanderplasschen A. Alcamí 1997 Vaccinia virus immune evasion Immunol. Rev. 159 137 54 1:CAS:528: DyaK2sXnvFKrtbs%3D 9416508 10.1111/j.1600-065X.1997.tb01012.x
    • (1997) Immunol. Rev. , vol.159 , pp. 137-54
    • Smith, G.L.1    Symons, J.A.2    Khanna, A.3    Vanderplasschen, A.4    Alcamí, A.5
  • 105
    • 0029965776 scopus 로고    scopus 로고
    • One step ahead of the game: Viral immunomodulatory molecules
    • DOI 10.1146/annurev.immunol.14.1.101
    • M. Spriggs 1996 One step ahead of the game: viral immunomodulatory molecules Annu. Rev Immunol. 14 101 130 1:CAS:528:DyaK28XitlCgt7c%3D 8717509 10.1146/annurev.immunol.14.1.101 (Pubitemid 26130179)
    • (1996) Annual Review of Immunology , vol.14 , pp. 101-130
    • Spriggs, M.K.1
  • 106
    • 0028009537 scopus 로고
    • Characterization of the putative protein kinases specified by varicella-zoster virus genes 47 and 66
    • 1:CAS:528:DyaK2cXkt12lsbo%3D 8113753 10.1099/0022-1317-75-2-317
    • D. Stevenson K. L. Colman A. J. Davison 1994 Characterization of the putative protein kinases specified by varicella-zoster virus genes 47 and 66 J. Gen. Virol. 75 317 326 1:CAS:528:DyaK2cXkt12lsbo%3D 8113753 10.1099/0022-1317- 75-2-317
    • (1994) J. Gen. Virol. , vol.75 , pp. 317-326
    • Stevenson, D.1    Colman, K.L.2    Davison, A.J.3
  • 107
    • 20444446357 scopus 로고    scopus 로고
    • SV40-encoded microRNAs regulate viral gene expression and reduce susceptibility to cytotoxic T cells
    • DOI 10.1038/nature03576
    • C. Sullivan A. Grundhoff S. Tevethia J. Pipas D. Ganem 2005 SV40-encoded microRNAs regulate viral gene expression and reduce susceptibility to cytotoxic T cells Nature (London) 435 682 686 1:CAS:528:DC%2BD2MXks1Ogtb8%3D 10.1038/nature03576 (Pubitemid 40825513)
    • (2005) Nature , vol.435 , Issue.7042 , pp. 682-686
    • Sullivan, C.S.1    Grundhoff, A.T.2    Tevethia, S.3    Pipas, J.M.4    Ganem, D.5
  • 108
    • 63549120842 scopus 로고    scopus 로고
    • Murine Polyomavirus encodes a microRNA that cleaves early RNA transcripts but is not essential for experimental infection
    • 1:CAS:528:DC%2BD1MXkt1Sjsr4%3D 19272626 10.1016/j.virol.2009.02.017
    • C. Sullivan C. Sung C. Pack A. Grundhoff A. Lukacher T. Benjamin D. Ganem 2009 Murine Polyomavirus encodes a microRNA that cleaves early RNA transcripts but is not essential for experimental infection Virology 387 157 167 1:CAS:528:DC%2BD1MXkt1Sjsr4%3D 19272626 10.1016/j.virol.2009.02.017
    • (2009) Virology , vol.387 , pp. 157-167
    • Sullivan, C.1    Sung, C.2    Pack, C.3    Grundhoff, A.4    Lukacher, A.5    Benjamin, T.6    Ganem, D.7
  • 109
    • 0035816682 scopus 로고    scopus 로고
    • Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3
    • 1:CAS:528:DC%2BD3MXlt1ans7s%3D 11316813 10.1074/jbc.M101914200
    • M. Tachibana K. Sugimoto T. Fukushima Y. Shinkai 2001 Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3 J. Biol. Chem. 276 25309 25317 1:CAS:528:DC%2BD3MXlt1ans7s%3D 11316813 10.1074/jbc.M101914200
    • (2001) J. Biol. Chem. , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 110
    • 0034968671 scopus 로고    scopus 로고
    • Histone acetylation and disease
    • 1:CAS:528:DC%2BD3MXlt1ait7s%3D 11437234 10.1007/PL00000896
    • S. Timmermann H. Lehrmann A. Polesskaya A. Harel-Bellan 2001 Histone acetylation and disease Cell Mol Life Sci. 58 728 736 1:CAS:528: DC%2BD3MXlt1ait7s%3D 11437234 10.1007/PL00000896
    • (2001) Cell Mol Life Sci. , vol.58 , pp. 728-736
    • Timmermann, S.1    Lehrmann, H.2    Polesskaya, A.3    Harel-Bellan, A.4
  • 112
    • 49649119633 scopus 로고    scopus 로고
    • MicroRNAs expressed by herpes simplex virus 1 during latent infection regulate viral mRNAs
    • 1:CAS:528:DC%2BD1cXps1Snt74%3D
    • J. Umbach M. Kramer I. Jurak H. Karnowski D. Coen B. Cullen 2008 MicroRNAs expressed by herpes simplex virus 1 during latent infection regulate viral mRNAs Nature (London) 454 780 783 1:CAS:528:DC%2BD1cXps1Snt74%3D
    • (2008) Nature (London) , vol.454 , pp. 780-783
    • Umbach, J.1    Kramer, M.2    Jurak, I.3    Karnowski, H.4    Coen, D.5    Cullen, B.6
  • 113
    • 44649158252 scopus 로고    scopus 로고
    • HDAC6: A key regulator of cytoskeleton, cell migration and cell-cell interactions
    • 18472263 10.1016/j.tcb.2008.04.003 1:CAS:528:DC%2BD1cXmvVymu7g%3D
    • A. Valenzuela-Fernández J. R. Cabrero J. M. Serrador F. Sánchez-Madrid 2008 HDAC6: a key regulator of cytoskeleton, cell migration and cell-cell interactions Trends Cell Biol. 18 291 297 18472263 10.1016/j.tcb.2008.04.003 1:CAS:528:DC%2BD1cXmvVymu7g%3D
    • (2008) Trends Cell Biol. , vol.18 , pp. 291-297
    • Valenzuela-Fernández, A.1    Cabrero, J.R.2    Serrador, J.M.3    Sánchez-Madrid, F.4
  • 114
    • 0038239257 scopus 로고    scopus 로고
    • The SV40 T antigen modulates CBP histone acetyltransferase activity
    • DOI 10.1093/nar/gkg418
    • E. Valls 2003 The SV40 T antigen modulates CBP histone acetyltransferase activity Nucleic Acids Res. 31 3114 3122 1:CAS:528:DC%2BD3sXks1Wqt7g%3D 12799439 10.1093/nar/gkg418 (Pubitemid 37441771)
    • (2003) Nucleic Acids Research , vol.31 , Issue.12 , pp. 3114-3122
    • Valls, E.1    De La Cruz, X.2    Martinez-Balbas, M.A.3
  • 115
    • 34247892499 scopus 로고    scopus 로고
    • Involvement of chromatin and histone deacetylation in SV40T antigen transcription regulation
    • DOI 10.1093/nar/gkl1113
    • E. Valls N. Blanco-García N. Aquizu D. Piedra C. Estarás X. de la Cruz M. A. Martínez-Balbás 2007 Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation Nucleic Acids Res. 35 1958 1968 1:CAS:528:DC%2BD2sXlsV2ru7w%3D 17341466 10.1093/nar/gkl1113 (Pubitemid 47061662)
    • (2007) Nucleic Acids Research , vol.35 , Issue.6 , pp. 1958-1968
    • Valls, E.1    Blanco-Garcia, N.2    Aquizu, N.3    Piedra, D.4    Estaras, C.5    De La Cruz, X.6    Martinez-Balbas, M.A.7
  • 116
    • 0034566127 scopus 로고    scopus 로고
    • Role of chromatin in HIV-1 transcriptional regulation
    • 10987090 10.1016/S1054-3589(00)48005-1
    • C. Van Lint 2000 Role of chromatin in HIV-1 transcriptional regulation Adv Pharmacol. 48 121 160 10987090 10.1016/S1054-3589(00)48005-1
    • (2000) Adv Pharmacol. , vol.48 , pp. 121-160
    • Van Lint, C.1
  • 117
    • 0035542974 scopus 로고    scopus 로고
    • Methyl CpG-binding proteins and transcriptional repression
    • DOI 10.1002/bies.10008
    • P. A. Wade 2001 Methyl CpG-binding proteins and transcriptional repression Bioessays 23 1131 1137 1:CAS:528:DC%2BD38XksFOluw%3D%3D 11746232 10.1002/bies.10008 (Pubitemid 34021016)
    • (2001) BioEssays , vol.23 , Issue.12 , pp. 1131-1137
    • Luo, H.1    Dearolf, C.R.2
  • 119
    • 66049111715 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as novel anticancer therapeutics
    • 1:STN:280:DC%2BD1cjjvFOmuw%3D%3D 19008999
    • D. R. Walkinshaw X. J. Yang 2008 Histone deacetylase inhibitors as novel anticancer therapeutics Curr. Oncol. 15 237 243 1:STN:280:DC%2BD1cjjvFOmuw%3D%3D 19008999
    • (2008) Curr. Oncol. , vol.15 , pp. 237-243
    • Walkinshaw, D.R.1    Yang, X.J.2
  • 120
    • 70350278896 scopus 로고    scopus 로고
    • Histone deacetylases 1 and 2 are phosphorylated at novel sites during varicella-zoster virus infection
    • 1:CAS:528:DC%2BC3cXksFKqsbs%3D 19740981 10.1128/JVI.01318-09
    • M. S. Walters A. Erazo P. R. Kinchington S. Silverstein 2009 Histone deacetylases 1 and 2 are phosphorylated at novel sites during varicella-zoster virus infection J. Virol. 83 11502 11513 1:CAS:528:DC%2BC3cXksFKqsbs%3D 19740981 10.1128/JVI.01318-09
    • (2009) J. Virol. , vol.83 , pp. 11502-11513
    • Walters, M.S.1    Erazo, A.2    Kinchington, P.R.3    Silverstein, S.4
  • 121
    • 73449117582 scopus 로고    scopus 로고
    • Immunomodulatory effects of deacetylase inhibitors: Therapeutic targeting of FOXP3+ regulatory T cells
    • 1:CAS:528:DC%2BD1MXhtlSqsLfP 19855427
    • L. Wang E. F. de Zoeten M. I. Greene W. W. Hancock 2009 Immunomodulatory effects of deacetylase inhibitors: therapeutic targeting of FOXP3+ regulatory T cells Nat. Rev. Drug. Discov. 8 969 981 1:CAS:528:DC%2BD1MXhtlSqsLfP 19855427
    • (2009) Nat. Rev. Drug. Discov. , vol.8 , pp. 969-981
    • Wang, L.1    De Zoeten, E.F.2    Greene, M.I.3    Hancock, W.W.4
  • 122
    • 0025271203 scopus 로고
    • Association of human papillomavirus types 16 and 18 E6 proteins with p53
    • 1:CAS:528:DyaK3cXktF2ltL0%3D 2157286 10.1126/science.2157286
    • B. Werness A. Levine P. Howley 1990 Association of human papillomavirus types 16 and 18 E6 proteins with p53 Science 248 76 79 1:CAS:528: DyaK3cXktF2ltL0%3D 2157286 10.1126/science.2157286
    • (1990) Science , vol.248 , pp. 76-79
    • Werness, B.1    Levine, A.2    Howley, P.3
  • 123
    • 0033485338 scopus 로고    scopus 로고
    • Changes in chromatin organization at the neutrophil elastase locus associated with myeloid cell differentiation
    • 1:CAS:528:DyaK1MXnslyktLw%3D 10572086
    • E. Wong D. Jenne M. Zimmer S. Porter C. Gilks 1999 Changes in chromatin organization at the neutrophil elastase locus associated with myeloid cell differentiation Blood 94 3730 3736 1:CAS:528:DyaK1MXnslyktLw%3D 10572086
    • (1999) Blood , vol.94 , pp. 3730-3736
    • Wong, E.1    Jenne, D.2    Zimmer, M.3    Porter, S.4    Gilks, C.5
  • 124
    • 0025969253 scopus 로고
    • Simian virus 40 large-T antigen expresses a biological activity complementary to the p300-associated transforming function of the adenovirus E1A gene products
    • 1:CAS:528:DyaK3MXitVSrtbg%3D 1848672
    • P. Yaciuk M. C. Carter J. M. Pipas E. Moran 1991 Simian virus 40 large-T antigen expresses a biological activity complementary to the p300-associated transforming function of the adenovirus E1A gene products Mol. Cell. Biol. 11 2116 2124 1:CAS:528:DyaK3MXitVSrtbg%3D 1848672
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2116-2124
    • Yaciuk, P.1    Carter, M.C.2    Pipas, J.M.3    Moran, E.4
  • 127
    • 77956649731 scopus 로고    scopus 로고
    • Joining the dots: From chromatin remodeling to neuronal plasticity
    • 1:CAS:528:DC%2BC3cXhtFyiu7%2FL 20471240 10.1016/j.conb.2010.04.005
    • L. Zocchi P. Sassone-Corsi 2010 Joining the dots: from chromatin remodeling to neuronal plasticity Curr. Opin. Neurobiol. 20 432 440 1:CAS:528:DC%2BC3cXhtFyiu7%2FL 20471240 10.1016/j.conb.2010.04.005
    • (2010) Curr. Opin. Neurobiol. , vol.20 , pp. 432-440
    • Zocchi, L.1    Sassone-Corsi, P.2


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