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Volumn 87, Issue 19, 2013, Pages 10412-10422

Virion factors that target Daxx to overcome intrinsic immunity

Author keywords

[No Author keywords available]

Indexed keywords

DAXX PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; VIRUS DNA; VIRUS PROTEIN; VIRUS RNA;

EID: 84885968656     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00425-13     Document Type: Short Survey
Times cited : (36)

References (138)
  • 1
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang X, Khosravi-Far R, Chang HY, Baltimore D. 1997. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89:1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 2
    • 0037101953 scopus 로고    scopus 로고
    • Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek
    • Hollenbach AD, McPherson CJ, Mientjes EJ, Iyengar R, Grosveld G. 2002. Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J. Cell Sci. 115:3319-3330.
    • (2002) J. Cell Sci. , vol.115 , pp. 3319-3330
    • Hollenbach, A.D.1    McPherson, C.J.2    Mientjes, E.J.3    Iyengar, R.4    Grosveld, G.5
  • 4
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: dynamic sensors of DNA damage and cellular stress
    • Dellaire G, Bazett-Jones DP. 2004. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26:963-977.
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 6
    • 0033229827 scopus 로고    scopus 로고
    • Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs)
    • Torii S, Egan DA, Evans RA, Reed JC. 1999. Human Daxx regulates Fas-induced apoptosis from nuclear PML oncogenic domains (PODs). EMBO J. 18:6037-6049.
    • (1999) EMBO J. , vol.18 , pp. 6037-6049
    • Torii, S.1    Egan, D.A.2    Evans, R.A.3    Reed, J.C.4
  • 10
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies
    • Borden KL. 2002. Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol. Cell. Biol. 22: 5259-5269.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 11
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett RD, Chelbi-Alix MK. 2007. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89:819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 12
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai N, Stamminger T. 2008. New insights into the role of the subnuclear structure ND10 for viral infection. Biochim. Biophys. Acta 1783: 2207-2221.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 13
    • 34247262967 scopus 로고    scopus 로고
    • Herpesviruses
    • Baron S (ed), 4th ed, chapter 68. University of Texas Medical Branch at Galveston, Galveston, TX.
    • Whitley RJ. 1996. Herpesviruses. In Baron S (ed), Medical microbiology, 4th ed, chapter 68. University of Texas Medical Branch at Galveston, Galveston, TX. http://www.ncbi.nlm.nih.gov/pubmed/21413307.
    • (1996) Medical microbiology
    • Whitley, R.J.1
  • 14
    • 0034687704 scopus 로고    scopus 로고
    • UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells
    • Bresnahan WA, Shenk TE. 2000. UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells. Proc. Natl. Acad. Sci. U.S.A. 97:14506-14511.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14506-14511
    • Bresnahan, W.A.1    Shenk, T.E.2
  • 15
    • 0036091745 scopus 로고    scopus 로고
    • Functional interaction between the pp71 protein of human cytomegalovirus and the PMLinteracting protein human Daxx
    • Hofmann H, Sindre H, Stamminger T. 2002. Functional interaction between the pp71 protein of human cytomegalovirus and the PMLinteracting protein human Daxx. J. Virol. 76:5769-5783.
    • (2002) J. Virol. , vol.76 , pp. 5769-5783
    • Hofmann, H.1    Sindre, H.2    Stamminger, T.3
  • 16
    • 0032844234 scopus 로고    scopus 로고
    • Activation of herpesvirus gene expression by the human cytomegalovirus protein pp71
    • Homer EG, Rinaldi A, Nicholl MJ, Preston CM. 1999. Activation of herpesvirus gene expression by the human cytomegalovirus protein pp71. J. Virol. 73:8512-8518.
    • (1999) J. Virol. , vol.73 , pp. 8512-8518
    • Homer, E.G.1    Rinaldi, A.2    Nicholl, M.J.3    Preston, C.M.4
  • 17
    • 19944382805 scopus 로고    scopus 로고
    • Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication
    • Cantrell SR, Bresnahan WA. 2005. Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication. J. Virol. 79:7792-7802.
    • (2005) J. Virol. , vol.79 , pp. 7792-7802
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 18
    • 57349108706 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection
    • Lukashchuk V, McFarlane S, Everett RD, Preston CM. 2008. Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection. J. Virol. 82: 12543-12554.
    • (2008) J. Virol. , vol.82 , pp. 12543-12554
    • Lukashchuk, V.1    McFarlane, S.2    Everett, R.D.3    Preston, C.M.4
  • 19
    • 79953029146 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate early gene expression in the osteosarcoma line U2OS is repressed by the cell protein ATRX
    • McFarlane S, Preston CM. 2011. Human cytomegalovirus immediate early gene expression in the osteosarcoma line U2OS is repressed by the cell protein ATRX. Virus Res. 157:47-53.
    • (2011) Virus Res. , vol.157 , pp. 47-53
    • McFarlane, S.1    Preston, C.M.2
  • 20
    • 33645757807 scopus 로고    scopus 로고
    • Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expression
    • Saffert RT, Kalejta RF. 2006. Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expression. J. Virol. 80:3863-3871.
    • (2006) J. Virol. , vol.80 , pp. 3863-3871
    • Saffert, R.T.1    Kalejta, R.F.2
  • 21
    • 0036310441 scopus 로고    scopus 로고
    • Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains
    • Ishov AM, Vladimirova OV, Maul GG. 2002. Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains. J. Virol. 76: 7705-7712.
    • (2002) J. Virol. , vol.76 , pp. 7705-7712
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 22
    • 84871987427 scopus 로고    scopus 로고
    • The replication defect of ICP0-null mutant herpes simplex virus 1 can be largely complemented by the combined activities of human cytomegalovirus proteins IE1 and pp71
    • Everett RD, Bell AJ, Lu Y, Orr A. 2013. The replication defect of ICP0-null mutant herpes simplex virus 1 can be largely complemented by the combined activities of human cytomegalovirus proteins IE1 and pp71. J. Virol. 87:978-990.
    • (2013) J. Virol. , vol.87 , pp. 978-990
    • Everett, R.D.1    Bell, A.J.2    Lu, Y.3    Orr, A.4
  • 23
    • 16244422998 scopus 로고    scopus 로고
    • ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection
    • Everett RD, Murray J. 2005. ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J. Virol. 79:5078-5089.
    • (2005) J. Virol. , vol.79 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 24
    • 40149085109 scopus 로고    scopus 로고
    • Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100
    • Everett RD, Parada C, Gripon P, Sirma H, Orr A. 2008. Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100. J. Virol. 82:2661-2672.
    • (2008) J. Virol. , vol.82 , pp. 2661-2672
    • Everett, R.D.1    Parada, C.2    Gripon, P.3    Sirma, H.4    Orr, A.5
  • 25
    • 65349171799 scopus 로고    scopus 로고
    • Analysis of the functions of herpes simplex virus type 1 regulatory protein ICP0 that are critical for lytic infection and derepression of quiescent viral genomes
    • Everett RD, Parsy ML, Orr A. 2009. Analysis of the functions of herpes simplex virus type 1 regulatory protein ICP0 that are critical for lytic infection and derepression of quiescent viral genomes. J. Virol. 83:4963-4977.
    • (2009) J. Virol. , vol.83 , pp. 4963-4977
    • Everett, R.D.1    Parsy, M.L.2    Orr, A.3
  • 26
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • Everett RD, Rechter S, Papior P, Tavalai N, Stamminger T, Orr A. 2006. PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80: 7995-8005.
    • (2006) J. Virol. , vol.80 , pp. 7995-8005
    • Everett, R.D.1    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 27
    • 84861303373 scopus 로고    scopus 로고
    • Herpesvirus saimiri antagonizes nuclear domain 10-instituted intrinsic immunity via an ORF3-mediated selective degradation of cellular protein Sp100
    • Full F, Reuter N, Zielke K, Stamminger T, Ensser A. 2012. Herpesvirus saimiri antagonizes nuclear domain 10-instituted intrinsic immunity via an ORF3-mediated selective degradation of cellular protein Sp100. J. Virol. 86:3541-3553.
    • (2012) J. Virol. , vol.86 , pp. 3541-3553
    • Full, F.1    Reuter, N.2    Zielke, K.3    Stamminger, T.4    Ensser, A.5
  • 28
    • 0036173067 scopus 로고    scopus 로고
    • The human cytomegalovirus UL35 gene encodes two proteins with different functions
    • Liu Y, Biegalke BJ. 2002. The human cytomegalovirus UL35 gene encodes two proteins with different functions. J. Virol. 76:2460-2468.
    • (2002) J. Virol. , vol.76 , pp. 2460-2468
    • Liu, Y.1    Biegalke, B.J.2
  • 30
    • 4143152841 scopus 로고    scopus 로고
    • Human cytomegalovirus tegument proteins ppUL82 (pp71) and ppUL35 interact and cooperatively activate the major immediate-early enhancer
    • Schierling K, Stamminger T, Mertens T, Winkler M. 2004. Human cytomegalovirus tegument proteins ppUL82 (pp71) and ppUL35 interact and cooperatively activate the major immediate-early enhancer. J. Virol. 78:9512-9523.
    • (2004) J. Virol. , vol.78 , pp. 9512-9523
    • Schierling, K.1    Stamminger, T.2    Mertens, T.3    Winkler, M.4
  • 31
    • 79955880944 scopus 로고    scopus 로고
    • Nuclear body formation and PML body remodeling by the human cytomegalovirus protein UL35
    • Salsman J, Wang X, Frappier L. 2011. Nuclear body formation and PML body remodeling by the human cytomegalovirus protein UL35. Virology 414:119-129.
    • (2011) Virology , vol.414 , pp. 119-129
    • Salsman, J.1    Wang, X.2    Frappier, L.3
  • 32
    • 0031963969 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate early gene expression is stimulated by inhibition of protein synthesis
    • Preston CM, Rinaldi A, Nicholl MJ. 1998. Herpes simplex virus type 1 immediate early gene expression is stimulated by inhibition of protein synthesis. J. Gen. Virol. 79:117-124.
    • (1998) J. Gen. Virol. , vol.79 , pp. 117-124
    • Preston, C.M.1    Rinaldi, A.2    Nicholl, M.J.3
  • 34
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett RD. 2001. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20:7266-7273.
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 35
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul GG. 1998. Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 20:660-667.
    • (1998) Bioessays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 36
    • 84874035038 scopus 로고    scopus 로고
    • Regulation of alphaherpesvirus infections by the ICP0 family of proteins
    • Boutell C, Everett RD. 2013. Regulation of alphaherpesvirus infections by the ICP0 family of proteins. J. Gen. Virol. 94:465-481.
    • (2013) J. Gen. Virol. , vol.94 , pp. 465-481
    • Boutell, C.1    Everett, R.D.2
  • 37
    • 77950515413 scopus 로고    scopus 로고
    • Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx
    • Lukashchuk V, Everett RD. 2010. Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx. J. Virol. 84:4026-4040.
    • (2010) J. Virol. , vol.84 , pp. 4026-4040
    • Lukashchuk, V.1    Everett, R.D.2
  • 38
    • 79958126321 scopus 로고    scopus 로고
    • A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virus
    • Delboy MG, Nicola AV. 2011. A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virus. J. Virol. 85:5910-5918.
    • (2011) J. Virol. , vol.85 , pp. 5910-5918
    • Delboy, M.G.1    Nicola, A.V.2
  • 39
    • 81755166682 scopus 로고    scopus 로고
    • EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcription
    • doi:10 .1371/journal.ppat.1002376
    • Tsai K, Thikmyanova N, Wojcechowskyj JA, Delecluse HJ, Lieberman PM. 2011. EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcription. PLoS Pathog. 7:e1002376. doi:10 .1371/journal.ppat.1002376.
    • (2011) PLoS Pathog. , vol.7
    • Tsai, K.1    Thikmyanova, N.2    Wojcechowskyj, J.A.3    Delecluse, H.J.4    Lieberman, P.M.5
  • 40
    • 33748926792 scopus 로고    scopus 로고
    • Epstein-Barr virus BNRF1 protein allows efficient transfer from the endosomal compartment to the nucleus of primary B lymphocytes
    • Feederle R, Neuhierl B, Baldwin G, Bannert H, Hub B, Mautner J, Behrends U, Delecluse HJ. 2006. Epstein-Barr virus BNRF1 protein allows efficient transfer from the endosomal compartment to the nucleus of primary B lymphocytes. J. Virol. 80:9435-9443.
    • (2006) J. Virol. , vol.80 , pp. 9435-9443
    • Feederle, R.1    Neuhierl, B.2    Baldwin, G.3    Bannert, H.4    Hub, B.5    Mautner, J.6    Behrends, U.7    Delecluse, H.J.8
  • 42
    • 0000800331 scopus 로고    scopus 로고
    • Adenoviridae: the viruses and their replication
    • Knipe DM, Howley PM (ed). 4th ed, Lippincott-Raven, New York, NY.
    • Shenk T. 2001. Adenoviridae: the viruses and their replication, p 2265-2300. In Knipe DM, Howley PM (ed), Fields virology, 4th ed, vol 2. Lippincott-Raven, New York, NY.
    • (2001) Fields virology , vol.2 , pp. 2265-2300
    • Shenk, T.1
  • 43
    • 0029094097 scopus 로고
    • Adenovirus E1A: transcription regulation and alteration of cell growth control
    • Nevins JR. 1995. Adenovirus E1A: transcription regulation and alteration of cell growth control. Curr. Top. Microbiol. Immunol. 199(Pt. 3):25-32.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.199 , Issue.PART 3 , pp. 25-32
    • Nevins, J.R.1
  • 44
    • 0019801828 scopus 로고
    • Mechanism of activation of early viral transcription by the adenovirus E1A gene product
    • Nevins JR. 1981. Mechanism of activation of early viral transcription by the adenovirus E1A gene product. Cell 26:213-220.
    • (1981) Cell , vol.26 , pp. 213-220
    • Nevins, J.R.1
  • 45
    • 0037452979 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitinindependent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein
    • Kalejta RF, Shenk T. 2003. Proteasome-dependent, ubiquitinindependent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein. Proc. Natl. Acad. Sci. U.S.A. 100:3263-3268.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3263-3268
    • Kalejta, R.F.1    Shenk, T.2
  • 46
    • 77953736164 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells
    • Schreiner S, Wimmer P, Sirma H, Everett RD, Blanchette P, Groitl P, Dobner T. 2010. Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells. J. Virol. 84: 7029-7038.
    • (2010) J. Virol. , vol.84 , pp. 7029-7038
    • Schreiner, S.1    Wimmer, P.2    Sirma, H.3    Everett, R.D.4    Blanchette, P.5    Groitl, P.6    Dobner, T.7
  • 47
    • 13444311651 scopus 로고    scopus 로고
    • Adenovirus protein VI mediates membrane disruption following capsid disassembly
    • Wiethoff CM, Wodrich H, Gerace L, Nemerow GR. 2005. Adenovirus protein VI mediates membrane disruption following capsid disassembly. J. Virol. 79:1992-2000.
    • (2005) J. Virol. , vol.79 , pp. 1992-2000
    • Wiethoff, C.M.1    Wodrich, H.2    Gerace, L.3    Nemerow, G.R.4
  • 51
    • 0030922558 scopus 로고    scopus 로고
    • The product of the adenovirus intermediate gene IX is a transcriptional activator
    • Lutz P, Rosa-Calatrava M, Kedinger C. 1997. The product of the adenovirus intermediate gene IX is a transcriptional activator. J. Virol. 71: 5102-5109.
    • (1997) J. Virol. , vol.71 , pp. 5102-5109
    • Lutz, P.1    Rosa-Calatrava, M.2    Kedinger, C.3
  • 52
    • 0242439337 scopus 로고    scopus 로고
    • Adenovirus protein IX sequesters hostcell promyelocytic leukaemia protein and contributes to efficient viral proliferation
    • Rosa-Calatrava M, Puvion-Dutilleul F, Lutz P, Dreyer D, de The H, Chatton B, Kedinger C. 2003. Adenovirus protein IX sequesters hostcell promyelocytic leukaemia protein and contributes to efficient viral proliferation. EMBO Rep. 4:969-975.
    • (2003) EMBO Rep. , vol.4 , pp. 969-975
    • Rosa-Calatrava, M.1    Puvion-Dutilleul, F.2    Lutz, P.3    Dreyer, D.4    de The, H.5    Chatton, B.6    Kedinger, C.7
  • 53
    • 79955446411 scopus 로고    scopus 로고
    • Adenovirus core protein VII protects the viral genome from a DNA damage response at early times after infection
    • Karen KA, Hearing P. 2011. Adenovirus core protein VII protects the viral genome from a DNA damage response at early times after infection. J. Virol. 85:4135-4142.
    • (2011) J. Virol. , vol.85 , pp. 4135-4142
    • Karen, K.A.1    Hearing, P.2
  • 54
    • 79951571234 scopus 로고    scopus 로고
    • Cellular and viral chromatin proteins are positive factors in the regulation of adenovirus gene expression
    • Komatsu T, Haruki H, Nagata K. 2011. Cellular and viral chromatin proteins are positive factors in the regulation of adenovirus gene expression. Nucleic Acids Res. 39:889-901.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 889-901
    • Komatsu, T.1    Haruki, H.2    Nagata, K.3
  • 55
    • 14744285753 scopus 로고    scopus 로고
    • The papillomavirus life cycle
    • Doorbar J. 2005. The papillomavirus life cycle. J. Clin. Virol. 32(Suppl. 1):S7-S15.
    • (2005) J. Clin. Virol. , vol.32 , Issue.SUPPL. 1
    • Doorbar, J.1
  • 56
    • 84866170686 scopus 로고    scopus 로고
    • Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry
    • Bienkowska-Haba M, Williams C, Kim SM, Garcea RL, Sapp M. 2012. Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry. J. Virol. 86:9875-9887.
    • (2012) J. Virol. , vol.86 , pp. 9875-9887
    • Bienkowska-Haba, M.1    Williams, C.2    Kim, S.M.3    Garcea, R.L.4    Sapp, M.5
  • 57
    • 7644237129 scopus 로고    scopus 로고
    • The L2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors
    • Darshan MS, Lucchi J, Harding E, Moroianu J. 2004. The L2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors. J. Virol. 78:12179-12188.
    • (2004) J. Virol. , vol.78 , pp. 12179-12188
    • Darshan, M.S.1    Lucchi, J.2    Harding, E.3    Moroianu, J.4
  • 58
    • 61449235414 scopus 로고    scopus 로고
    • Establishment of human papillomavirus infection requires cell cycle progression
    • doi:10.1371/journal.ppat.1000318
    • Pyeon D, Pearce SM, Lank SM, Ahlquist P, Lambert PF. 2009. Establishment of human papillomavirus infection requires cell cycle progression. PLoS Pathog. 5:e1000318. doi:10.1371/journal.ppat.1000318.
    • (2009) PLoS Pathog. , vol.5
    • Pyeon, D.1    Pearce, S.M.2    Lank, S.M.3    Ahlquist, P.4    Lambert, P.F.5
  • 59
    • 0036061103 scopus 로고    scopus 로고
    • Reorganization of nuclear domain 10 induced by papillomavirus capsid protein L2
    • Florin L, Schafer F, Sotlar K, Streeck RE, Sapp M. 2002. Reorganization of nuclear domain 10 induced by papillomavirus capsid protein L2. Virology 295:97-107.
    • (2002) Virology , vol.295 , pp. 97-107
    • Florin, L.1    Schafer, F.2    Sotlar, K.3    Streeck, R.E.4    Sapp, M.5
  • 60
    • 0141680274 scopus 로고    scopus 로고
    • Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization
    • Becker KA, Florin L, Sapp C, Sapp M. 2003. Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization. Virology 314:161-167.
    • (2003) Virology , vol.314 , pp. 161-167
    • Becker, K.A.1    Florin, L.2    Sapp, C.3    Sapp, M.4
  • 61
    • 4644352291 scopus 로고    scopus 로고
    • Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression
    • Day PM, Baker CC, Lowy DR, Schiller JT. 2004. Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression. Proc. Natl. Acad. Sci. U.S.A. 101:14252-14257.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14252-14257
    • Day, P.M.1    Baker, C.C.2    Lowy, D.R.3    Schiller, J.T.4
  • 63
    • 0030801241 scopus 로고    scopus 로고
    • Repression of gene expression upon infection of cells with herpes simplex virus type 1 mutants impaired for immediate-early protein synthesis
    • Preston CM, Nicholl MJ. 1997. Repression of gene expression upon infection of cells with herpes simplex virus type 1 mutants impaired for immediate-early protein synthesis. J. Virol. 71:7807-7813.
    • (1997) J. Virol. , vol.71 , pp. 7807-7813
    • Preston, C.M.1    Nicholl, M.J.2
  • 64
    • 0024508798 scopus 로고
    • Complementation of a herpes simplex virus type 1 Vmw110 deletion mutant by human cytomegalovirus
    • Stow EC, Stow ND. 1989. Complementation of a herpes simplex virus type 1 Vmw110 deletion mutant by human cytomegalovirus. J. Gen. Virol. 70:695-704.
    • (1989) J. Gen. Virol. , vol.70 , pp. 695-704
    • Stow, E.C.1    Stow, N.D.2
  • 65
    • 10644281037 scopus 로고    scopus 로고
    • Human cytomegalovirus tegument protein pp71 directs long-term gene expression from quiescent herpes simplex virus genomes
    • Preston CM, Nicholl MJ. 2005. Human cytomegalovirus tegument protein pp71 directs long-term gene expression from quiescent herpes simplex virus genomes. J. Virol. 79:525-535.
    • (2005) J. Virol. , vol.79 , pp. 525-535
    • Preston, C.M.1    Nicholl, M.J.2
  • 67
    • 39749187576 scopus 로고    scopus 로고
    • Identification of cellular proteins that maintain retroviral epigenetic silencing: evidence for an antiviral response
    • Poleshko A, Palagin I, Zhang R, Boimel P, Castagna C, Adams PD, Skalka AM, Katz RA. 2008. Identification of cellular proteins that maintain retroviral epigenetic silencing: evidence for an antiviral response. J. Virol. 82:2313-2323.
    • (2008) J. Virol. , vol.82 , pp. 2313-2323
    • Poleshko, A.1    Palagin, I.2    Zhang, R.3    Boimel, P.4    Castagna, C.5    Adams, P.D.6    Skalka, A.M.7    Katz, R.A.8
  • 69
    • 33845968505 scopus 로고    scopus 로고
    • Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter
    • Woodhall DL, Groves IJ, Reeves MB, Wilkinson G, Sinclair JH. 2006. Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter. J. Biol. Chem. 281:37652-37660.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37652-37660
    • Woodhall, D.L.1    Groves, I.J.2    Reeves, M.B.3    Wilkinson, G.4    Sinclair, J.H.5
  • 70
    • 0029957833 scopus 로고    scopus 로고
    • Restricted expression of Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genes in Kaposi sarcoma
    • Zhong W, Wang H, Herndier B, Ganem D. 1996. Restricted expression of Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genes in Kaposi sarcoma. Proc. Natl. Acad. Sci. U.S.A. 93:6641-6646.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6641-6646
    • Zhong, W.1    Wang, H.2    Herndier, B.3    Ganem, D.4
  • 71
    • 0032978479 scopus 로고    scopus 로고
    • Kaposi's sarcomaassociated herpesvirus encodes a bZIP protein with homology to BZLF1 of Epstein-Barr virus
    • Lin SF, Robinson DR, Miller G, Kung HJ. 1999. Kaposi's sarcomaassociated herpesvirus encodes a bZIP protein with homology to BZLF1 of Epstein-Barr virus. J. Virol. 73:1909-1917.
    • (1999) J. Virol. , vol.73 , pp. 1909-1917
    • Lin, S.F.1    Robinson, D.R.2    Miller, G.3    Kung, H.J.4
  • 72
    • 0034842666 scopus 로고    scopus 로고
    • Function of Rta is essential for lytic replication of murine gammaherpesvirus 68
    • Wu TT, Tong L, Rickabaugh T, Speck S, Sun R. 2001. Function of Rta is essential for lytic replication of murine gammaherpesvirus 68. J. Virol. 75:9262-9273.
    • (2001) J. Virol. , vol.75 , pp. 9262-9273
    • Wu, T.T.1    Tong, L.2    Rickabaugh, T.3    Speck, S.4    Sun, R.5
  • 73
    • 37049006758 scopus 로고    scopus 로고
    • Overexpression of the Kaposi's sarcoma-associated herpesvirus transactivator K-Rta can complement a K-bZIP deletion BACmid and yields an enhanced growth phenotype
    • Kato-Noah T, Xu Y, Rossetto CC, Colletti K, Papouskova I, Pari GS. 2007. Overexpression of the Kaposi's sarcoma-associated herpesvirus transactivator K-Rta can complement a K-bZIP deletion BACmid and yields an enhanced growth phenotype. J. Virol. 81:13519-13532.
    • (2007) J. Virol. , vol.81 , pp. 13519-13532
    • Kato-Noah, T.1    Xu, Y.2    Rossetto, C.C.3    Colletti, K.4    Papouskova, I.5    Pari, G.S.6
  • 74
    • 2642586357 scopus 로고    scopus 로고
    • Kaposi's sarcomaassociated herpesvirus-encoded latency-associated nuclear antigen inhibits lytic replication by targeting Rta: a potential mechanism for virusmediated control of latency
    • Lan K, Kuppers DA, Verma SC, Robertson ES. 2004. Kaposi's sarcomaassociated herpesvirus-encoded latency-associated nuclear antigen inhibits lytic replication by targeting Rta: a potential mechanism for virusmediated control of latency. J. Virol. 78:6585-6594.
    • (2004) J. Virol. , vol.78 , pp. 6585-6594
    • Lan, K.1    Kuppers, D.A.2    Verma, S.C.3    Robertson, E.S.4
  • 75
    • 19944370134 scopus 로고    scopus 로고
    • Induction of Kaposi's sarcoma-associated herpesvirus latencyassociated nuclear antigen by the lytic transactivator RTA: a novel mechanism for establishment of latency
    • Lan K, Kuppers DA, Verma SC, Sharma N, Murakami M, Robertson ES. 2005. Induction of Kaposi's sarcoma-associated herpesvirus latencyassociated nuclear antigen by the lytic transactivator RTA: a novel mechanism for establishment of latency. J. Virol. 79:7453-7465.
    • (2005) J. Virol. , vol.79 , pp. 7453-7465
    • Lan, K.1    Kuppers, D.A.2    Verma, S.C.3    Sharma, N.4    Murakami, M.5    Robertson, E.S.6
  • 76
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. 2007. Chromatin modifications and their function. Cell 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 77
    • 34247146896 scopus 로고    scopus 로고
    • Stable gene expression occurs from a minority of integrated HIV-1-based vectors: transcriptional silencing is present in the majority
    • Mok HP, Javed S, Lever A. 2007. Stable gene expression occurs from a minority of integrated HIV-1-based vectors: transcriptional silencing is present in the majority. Gene Ther. 14:741-751.
    • (2007) Gene Ther. , vol.14 , pp. 741-751
    • Mok, H.P.1    Javed, S.2    Lever, A.3
  • 78
    • 39749199654 scopus 로고    scopus 로고
    • Chromatin, gene silencing and HIV latency
    • Mok HP, Lever AM. 2007. Chromatin, gene silencing and HIV latency. Genome Biol. 8:228.
    • (2007) Genome Biol. , vol.8 , pp. 228
    • Mok, H.P.1    Lever, A.M.2
  • 79
    • 34249802347 scopus 로고    scopus 로고
    • Chromatin-associated regulation of HIV-1 transcription: implications for the development of therapeutic strategies
    • Quivy V, De Walque S, Van Lint C. 2007. Chromatin-associated regulation of HIV-1 transcription: implications for the development of therapeutic strategies. Subcell. Biochem. 41:371-396.
    • (2007) Subcell. Biochem. , vol.41 , pp. 371-396
    • Quivy, V.1    De Walque, S.2    Van Lint, C.3
  • 81
    • 27744489220 scopus 로고    scopus 로고
    • Silencing and variegation of gammaretrovirus and lentivirus vectors
    • Ellis J. 2005. Silencing and variegation of gammaretrovirus and lentivirus vectors. Hum. Gene Ther. 16:1241-1246.
    • (2005) Hum. Gene Ther. , vol.16 , pp. 1241-1246
    • Ellis, J.1
  • 82
    • 22944464097 scopus 로고    scopus 로고
    • Retrovirus silencing and vector design: relevance to normal and cancer stem cells?
    • Ellis J, Yao S. 2005. Retrovirus silencing and vector design: relevance to normal and cancer stem cells? Curr. Gene Ther. 5:367-373.
    • (2005) Curr. Gene Ther. , vol.5 , pp. 367-373
    • Ellis, J.1    Yao, S.2
  • 83
    • 0034736521 scopus 로고    scopus 로고
    • Retroviruses in foreign species and the problem of provirus silencing
    • Svoboda J, Hejnar J, Geryk J, Elleder D, Vernerova Z. 2000. Retroviruses in foreign species and the problem of provirus silencing. Gene 261:181-188.
    • (2000) Gene , vol.261 , pp. 181-188
    • Svoboda, J.1    Hejnar, J.2    Geryk, J.3    Elleder, D.4    Vernerova, Z.5
  • 84
    • 0036277129 scopus 로고    scopus 로고
    • Mechanisms that regulate silencing of gene expression from retroviral vectors
    • Swindle CS, Klug CA. 2002. Mechanisms that regulate silencing of gene expression from retroviral vectors. J. Hematother. Stem Cell Res. 11: 449-456.
    • (2002) J. Hematother. Stem Cell Res. , vol.11 , pp. 449-456
    • Swindle, C.S.1    Klug, C.A.2
  • 85
    • 3042732990 scopus 로고    scopus 로고
    • Retrovirus silencing, variegation, extinction, and memory are controlled by a dynamic interplay of multiple epigenetic modifications
    • Yao S, Sukonnik T, Kean T, Bharadwaj RR, Pasceri P, Ellis J. 2004. Retrovirus silencing, variegation, extinction, and memory are controlled by a dynamic interplay of multiple epigenetic modifications. Mol. Ther. 10:27-36.
    • (2004) Mol. Ther. , vol.10 , pp. 27-36
    • Yao, S.1    Sukonnik, T.2    Kean, T.3    Bharadwaj, R.R.4    Pasceri, P.5    Ellis, J.6
  • 87
    • 16244383862 scopus 로고    scopus 로고
    • The cellular protein Daxx interacts with avian sarcoma virus integrase and viral DNA to repress viral transcription
    • Greger JG, Katz RA, Ishov AM, Maul GG, Skalka AM. 2005. The cellular protein Daxx interacts with avian sarcoma virus integrase and viral DNA to repress viral transcription. J. Virol. 79:4610-4618.
    • (2005) J. Virol. , vol.79 , pp. 4610-4618
    • Greger, J.G.1    Katz, R.A.2    Ishov, A.M.3    Maul, G.G.4    Skalka, A.M.5
  • 88
    • 84873853378 scopus 로고    scopus 로고
    • Retroviral DNAmethylation and epigenetic repression are mediated by the antiviral host protein Daxx
    • Shalginskikh N, Poleshko A, Skalka AM, Katz RA. 2013. Retroviral DNAmethylation and epigenetic repression are mediated by the antiviral host protein Daxx. J. Virol. 87:2137-2150.
    • (2013) J. Virol. , vol.87 , pp. 2137-2150
    • Shalginskikh, N.1    Poleshko, A.2    Skalka, A.M.3    Katz, R.A.4
  • 89
    • 33947373010 scopus 로고    scopus 로고
    • High-frequency epigenetic repression and silencing of retroviruses can be antagonized by histone deacetylase inhibitors and transcriptional activators, but uniform reacti-vation in cell clones is restricted by additional mechanisms
    • Katz RA, Jack-Scott E, Narezkina A, Palagin I, Boimel P, Kulkosky J, Nicolas E, Greger JG, Skalka AM. 2007. High-frequency epigenetic repression and silencing of retroviruses can be antagonized by histone deacetylase inhibitors and transcriptional activators, but uniform reacti-vation in cell clones is restricted by additional mechanisms. J. Virol. 81:2592-2604.
    • (2007) J. Virol. , vol.81 , pp. 2592-2604
    • Katz, R.A.1    Jack-Scott, E.2    Narezkina, A.3    Palagin, I.4    Boimel, P.5    Kulkosky, J.6    Nicolas, E.7    Greger, J.G.8    Skalka, A.M.9
  • 92
    • 77956282773 scopus 로고    scopus 로고
    • Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
    • Lewis PW, Elsaesser SJ, Noh KM, Stadler SC, Allis CD. 2010. Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14075-14080
    • Lewis, P.W.1    Elsaesser, S.J.2    Noh, K.M.3    Stadler, S.C.4    Allis, C.D.5
  • 93
    • 84859337955 scopus 로고    scopus 로고
    • Chromatin structure of adenovirus DNA throughout infection
    • Giberson AN, Davidson AR, Parks RJ. 2012. Chromatin structure of adenovirus DNA throughout infection. Nucleic Acids Res. 40:2369-2376.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2369-2376
    • Giberson, A.N.1    Davidson, A.R.2    Parks, R.J.3
  • 94
    • 79955391412 scopus 로고    scopus 로고
    • How to control an infectious bead string: nucleosome-based regulation and targeting of herpesvirus chromatin
    • Nevels M, Nitzsche A, Paulus C. 2011. How to control an infectious bead string: nucleosome-based regulation and targeting of herpesvirus chromatin. Rev. Med. Virol. 21:154-180.
    • (2011) Rev. Med. Virol. , vol.21 , pp. 154-180
    • Nevels, M.1    Nitzsche, A.2    Paulus, C.3
  • 95
    • 58049213801 scopus 로고    scopus 로고
    • Chromatin reassembly signals the end of DNA repair
    • Chen CC, Tyler J. 2008. Chromatin reassembly signals the end of DNA repair. Cell Cycle 7:3792-3797.
    • (2008) Cell Cycle , vol.7 , pp. 3792-3797
    • Chen, C.C.1    Tyler, J.2
  • 96
    • 60749120563 scopus 로고    scopus 로고
    • Identification of two independent SUMO-interacting motifs in Daxx: evolutionary conservation from Drosophila to humans and their biochemical functions
    • Santiago A, Godsey AC, Hossain J, Zhao LY, Liao D. 2009. Identification of two independent SUMO-interacting motifs in Daxx: evolutionary conservation from Drosophila to humans and their biochemical functions. Cell Cycle 8:76-87.
    • (2009) Cell Cycle , vol.8 , pp. 76-87
    • Santiago, A.1    Godsey, A.C.2    Hossain, J.3    Zhao, L.Y.4    Liao, D.5
  • 97
    • 0029849806 scopus 로고    scopus 로고
    • Hantaviruses: genome structure, expression and evolution
    • Plyusnin A, Vapalahti O, Vaheri A. 1996. Hantaviruses: genome structure, expression and evolution. J. Gen. Virol. 77:2677-2687.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2677-2687
    • Plyusnin, A.1    Vapalahti, O.2    Vaheri, A.3
  • 98
    • 84860529630 scopus 로고    scopus 로고
    • Alphaviruses (Togaviridae) and Flaviviruses (Flaviviridae)
    • Baron S (ed), 4th ed. University of Texas Medical Branch at Galveston, Galveston, TX.
    • Schmaljohn AL, McClain D. 1996. Alphaviruses (Togaviridae) and Flaviviruses (Flaviviridae). In Baron S (ed), Medical microbiology, 4th ed. University of Texas Medical Branch at Galveston, Galveston, TX.
    • (1996) Medical microbiology
    • Schmaljohn, A.L.1    McClain, D.2
  • 101
    • 0035138091 scopus 로고    scopus 로고
    • Hantavirus nucleocapsid protein is expressed as a membrane-associated protein in the perinuclear region
    • Ravkov EV, Compans RW. 2001. Hantavirus nucleocapsid protein is expressed as a membrane-associated protein in the perinuclear region. J. Virol. 75:1808-1815.
    • (2001) J. Virol. , vol.75 , pp. 1808-1815
    • Ravkov, E.V.1    Compans, R.W.2
  • 102
    • 23844454526 scopus 로고    scopus 로고
    • Hantavirus nucleocapsid protein: a multifunctional molecule with both housekeeping and ambassadorial duties
    • Kaukinen P, Vaheri A, Plyusnin A. 2005. Hantavirus nucleocapsid protein: a multifunctional molecule with both housekeeping and ambassadorial duties. Arch. Virol. 150:1693-1713.
    • (2005) Arch. Virol. , vol.150 , pp. 1693-1713
    • Kaukinen, P.1    Vaheri, A.2    Plyusnin, A.3
  • 104
    • 0020353721 scopus 로고
    • Bis-sulfated gangliotetraosylceramide from rat kidney
    • Tadano K, Ishizuka I, Matsuo M, Matsumoto S. 1982. Bis-sulfated gangliotetraosylceramide from rat kidney. J. Biol. Chem. 257:13413-13420.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13413-13420
    • Tadano, K.1    Ishizuka, I.2    Matsuo, M.3    Matsumoto, S.4
  • 107
    • 84874715033 scopus 로고    scopus 로고
    • Daxx upregulation within the cytoplasm of reovirus-infected cells is mediated by interferon and contributes to apoptosis
    • Dionne KR, Zhuang Y, Leser JS, Tyler KL, Clarke P. 2013. Daxx upregulation within the cytoplasm of reovirus-infected cells is mediated by interferon and contributes to apoptosis. J. Virol. 87:3447-3460.
    • (2013) J. Virol. , vol.87 , pp. 3447-3460
    • Dionne, K.R.1    Zhuang, Y.2    Leser, J.S.3    Tyler, K.L.4    Clarke, P.5
  • 108
    • 28244483929 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells
    • Herzer K, Weyer S, Krammer PH, Galle PR, Hofmann TG. 2005. Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells. Cancer Res. 65:10830-10837.
    • (2005) Cancer Res. , vol.65 , pp. 10830-10837
    • Herzer, K.1    Weyer, S.2    Krammer, P.H.3    Galle, P.R.4    Hofmann, T.G.5
  • 109
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov AM, Maul GG. 1996. The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J. Cell Biol. 134:815-826.
    • (1996) J. Cell Biol. , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 110
    • 0030840687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment
    • Ishov AM, Stenberg RM, Maul GG. 1997. Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J. Cell Biol. 138:5-16.
    • (1997) J. Cell Biol. , vol.138 , pp. 5-16
    • Ishov, A.M.1    Stenberg, R.M.2    Maul, G.G.3
  • 111
    • 84865074686 scopus 로고    scopus 로고
    • The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies
    • de The H, Le Bras M, Lallemand-Breitenbach V. 2012. The cell biology of disease: Acute promyelocytic leukemia, arsenic, and PML bodies. J. Cell Biol. 198:11-21.
    • (2012) J. Cell Biol. , vol.198 , pp. 11-21
    • de The, H.1    Le Bras, M.2    Lallemand-Breitenbach, V.3
  • 112
    • 1442307625 scopus 로고    scopus 로고
    • Induction of apoptosis and expression of cell cycle regulatory proteins in response to a phytosphingosine derivative in HaCaT human keratinocyte cells
    • Kim HJ, Lim SC, Kim SH, Kim TY. 2003. Induction of apoptosis and expression of cell cycle regulatory proteins in response to a phytosphingosine derivative in HaCaT human keratinocyte cells. Mol. Cells 16:331-337.
    • (2003) Mol. Cells , vol.16 , pp. 331-337
    • Kim, H.J.1    Lim, S.C.2    Kim, S.H.3    Kim, T.Y.4
  • 113
    • 0142060821 scopus 로고    scopus 로고
    • Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates enhancement of p53-dependent transcription by Daxx
    • Zhao LY, Colosimo AL, Liu Y, Wan Y, Liao D. 2003. Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates enhancement of p53-dependent transcription by Daxx. J. Virol. 77:11809-11821.
    • (2003) J. Virol. , vol.77 , pp. 11809-11821
    • Zhao, L.Y.1    Colosimo, A.L.2    Liu, Y.3    Wan, Y.4    Liao, D.5
  • 114
    • 0025853776 scopus 로고
    • Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line
    • Fakharzadeh SS, Trusko SP, George DL. 1991. Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line. EMBO J. 10:1565-1569.
    • (1991) EMBO J. , vol.10 , pp. 1565-1569
    • Fakharzadeh, S.S.1    Trusko, S.P.2    George, D.L.3
  • 115
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • Fuchs SY, Adler V, Buschmann T, Wu X, Ronai Z. 1998. Mdm2 association with p53 targets its ubiquitination. Oncogene 17:2543-2547.
    • (1998) Oncogene , vol.17 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronai, Z.5
  • 116
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. 1997. Mdm2 promotes the rapid degradation of p53. Nature 387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 117
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H. 1997. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420:25-27.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 118
    • 0037329056 scopus 로고    scopus 로고
    • The p53-Mdm2 module and the ubiquitin system
    • Michael D, Oren M. 2003. The p53-Mdm2 module and the ubiquitin system. Semin. Cancer Biol. 13:49-58.
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 119
    • 33746190705 scopus 로고    scopus 로고
    • Mouse cytomegalovirus crosses the species barrier with help from a few human cytomegalovirus proteins
    • Tang Q, Maul GG. 2006. Mouse cytomegalovirus crosses the species barrier with help from a few human cytomegalovirus proteins. J. Virol. 80:7510-7521.
    • (2006) J. Virol. , vol.80 , pp. 7510-7521
    • Tang, Q.1    Maul, G.G.2
  • 120
    • 33745755471 scopus 로고    scopus 로고
    • Induction of apoptosis limits cytomegalovirus cross-species infection
    • Jurak I, Brune W. 2006. Induction of apoptosis limits cytomegalovirus cross-species infection. EMBO J. 25:2634-2642.
    • (2006) EMBO J. , vol.25 , pp. 2634-2642
    • Jurak, I.1    Brune, W.2
  • 121
    • 42249088417 scopus 로고    scopus 로고
    • Differences between mouse and human cytomegalovirus interactions with their respective hosts at immediate early times of the replication cycle
    • Maul GG, Negorev D. 2008. Differences between mouse and human cytomegalovirus interactions with their respective hosts at immediate early times of the replication cycle. Med. Microbiol. Immunol. 197:241-249.
    • (2008) Med. Microbiol. Immunol. , vol.197 , pp. 241-249
    • Maul, G.G.1    Negorev, D.2
  • 122
    • 78650659323 scopus 로고    scopus 로고
    • Viral hit and run-oncogenesis: genetic and epigenetic scenarios
    • Niller HH, Wolf H, Minarovits J. 2011. Viral hit and run-oncogenesis: genetic and epigenetic scenarios. Cancer Lett. 305:200-217.
    • (2011) Cancer Lett. , vol.305 , pp. 200-217
    • Niller, H.H.1    Wolf, H.2    Minarovits, J.3
  • 124
    • 4444289803 scopus 로고    scopus 로고
    • Molecular, biological, and in vivo characterization of the guinea pig cytomegalovirus (CMV) homologs of the human CMV matrix proteins pp71 (UL82) and pp65 (UL83)
    • McGregor A, Liu F, Schleiss MR. 2004. Molecular, biological, and in vivo characterization of the guinea pig cytomegalovirus (CMV) homologs of the human CMV matrix proteins pp71 (UL82) and pp65 (UL83). J. Virol. 78:9872-9889.
    • (2004) J. Virol. , vol.78 , pp. 9872-9889
    • McGregor, A.1    Liu, F.2    Schleiss, M.R.3
  • 125
    • 58149287941 scopus 로고    scopus 로고
    • Analysis of the nucleotide sequence of the guinea pig cytomegalovirus (GPCMV) genome
    • Schleiss MR, McGregor A, Choi KY, Date SV, Cui X, McVoy MA. 2008. Analysis of the nucleotide sequence of the guinea pig cytomegalovirus (GPCMV) genome. Virol. J. 5:139.
    • (2008) Virol. J. , vol.5 , pp. 139
    • Schleiss, M.R.1    McGregor, A.2    Choi, K.Y.3    Date, S.V.4    Cui, X.5    McVoy, M.A.6
  • 126
    • 50649120325 scopus 로고    scopus 로고
    • Multiple functions for ORF75c in murid herpesvirus-4 infection
    • doi:10.1371/journal.pone.0002781
    • Gaspar M, Gill MB, Losing JB, May JS, Stevenson PG. 2008. Multiple functions for ORF75c in murid herpesvirus-4 infection. PLoS One 3:e2781. doi:10.1371/journal.pone.0002781.
    • (2008) PLoS One , vol.3
    • Gaspar, M.1    Gill, M.B.2    Losing, J.B.3    May, J.S.4    Stevenson, P.G.5
  • 127
    • 49149094503 scopus 로고    scopus 로고
    • Murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PMLand is essential for production of infectious virus
    • Ling PD, Tan J, Sewatanon J, Peng R. 2008. Murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PMLand is essential for production of infectious virus. J. Virol. 82:8000-8012.
    • (2008) J. Virol. , vol.82 , pp. 8000-8012
    • Ling, P.D.1    Tan, J.2    Sewatanon, J.3    Peng, R.4
  • 128
    • 0014295381 scopus 로고
    • An apparently new herpesvirus from primary kidney cultures of the squirrel monkey (Saimiri sciureus)
    • Melendez LV, Daniel MD, Hunt RD, Garcia FG. 1968. An apparently new herpesvirus from primary kidney cultures of the squirrel monkey (Saimiri sciureus). Lab. Anim. Care 18:374-381.
    • (1968) Lab. Anim. Care , vol.18 , pp. 374-381
    • Melendez, L.V.1    Daniel, M.D.2    Hunt, R.D.3    Garcia, F.G.4
  • 131
    • 84855836014 scopus 로고    scopus 로고
    • Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies
    • Maroui MA, Pampin M, Chelbi-Alix MK. 2011. Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies. J. Virol. 85:13164-13173.
    • (2011) J. Virol. , vol.85 , pp. 13164-13173
    • Maroui, M.A.1    Pampin, M.2    Chelbi-Alix, M.K.3
  • 132
    • 2642670320 scopus 로고    scopus 로고
    • An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm
    • Borden KL, Campbell Dwyer EJ, Salvato MS. 1998. An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm. J. Virol. 72:758-766.
    • (1998) J. Virol. , vol.72 , pp. 758-766
    • Borden, K.L.1    Campbell Dwyer, E.J.2    Salvato, M.S.3
  • 134
    • 8944262349 scopus 로고    scopus 로고
    • Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype
    • Ray RB, Lagging LM, Meyer K, Ray R. 1996. Hepatitis C virus core protein cooperates with ras and transforms primary rat embryo fibroblasts to tumorigenic phenotype. J. Virol. 70:4438-4443.
    • (1996) J. Virol. , vol.70 , pp. 4438-4443
    • Ray, R.B.1    Lagging, L.M.2    Meyer, K.3    Ray, R.4
  • 135
    • 0038205593 scopus 로고    scopus 로고
    • Localization of influenza virus proteins to nuclear dot 10 structures in influenza virus-infected cells
    • Sato Y, Yoshioka K, Suzuki C, Awashima S, Hosaka Y, Yewdell J, Kuroda K. 2003. Localization of influenza virus proteins to nuclear dot 10 structures in influenza virus-infected cells. Virology 310: 29-40.
    • (2003) Virology , vol.310 , pp. 29-40
    • Sato, Y.1    Yoshioka, K.2    Suzuki, C.3    Awashima, S.4    Hosaka, Y.5    Yewdell, J.6    Kuroda, K.7
  • 136
    • 0035033932 scopus 로고    scopus 로고
    • Viral and cellular factors that target the promyelocytic leukemia oncogenic domains strongly activate a glucocorticoid-responsive promoter
    • Wienzek S, Dobbelstein M. 2001. Viral and cellular factors that target the promyelocytic leukemia oncogenic domains strongly activate a glucocorticoid-responsive promoter. J. Virol. 75:5391-5397.
    • (2001) J. Virol. , vol.75 , pp. 5391-5397
    • Wienzek, S.1    Dobbelstein, M.2
  • 137
    • 0035796503 scopus 로고    scopus 로고
    • PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator
    • Regad T, Saib A, Lallemand-Breitenbach V, Pandolfi PP, de The H, Chelbi-Alix MK. 2001. PML mediates the interferon-induced antiviral state against a complex retrovirus via its association with the viral transactivator. EMBO J. 20:3495-3505.
    • (2001) EMBO J. , vol.20 , pp. 3495-3505
    • Regad, T.1    Saib, A.2    Lallemand-Breitenbach, V.3    Pandolfi, P.P.4    de The, H.5    Chelbi-Alix, M.K.6
  • 138
    • 18344406436 scopus 로고    scopus 로고
    • Ebola virus infection inversely correlates with the overall expression levels of promyelocytic leukaemia (PML) protein in cultured cells
    • Bjorndal AS, Szekely L, Elgh F. 2003. Ebola virus infection inversely correlates with the overall expression levels of promyelocytic leukaemia (PML) protein in cultured cells. BMC Microbiol. 3:6.
    • (2003) BMC Microbiol. , vol.3 , pp. 6
    • Bjorndal, A.S.1    Szekely, L.2    Elgh, F.3


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