메뉴 건너뛰기




Volumn 3, Issue 3, 2008, Pages 265-277

Promyelocytic leukemia-nuclear body proteins: Herpesvirus enemies, accomplices, or both?

Author keywords

HCMV; HSV 1; Intrinsic immunity; PML NB

Indexed keywords

CELL PROTEIN; DAXX PROTEIN; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; IMMEDIATE EARLY PROTEIN; NUCLEAR PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN VP16; UBIQUITIN PROTEIN LIGASE; VIRUS PROTEIN;

EID: 44149083798     PISSN: 17460794     EISSN: None     Source Type: Journal    
DOI: 10.2217/17460794.3.3.265     Document Type: Review
Times cited : (39)

References (124)
  • 1
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: A front-line defense against viral attack
    • Bieniasz PD: Intrinsic immunity: a front-line defense against viral attack. Nat. Immunol. 5, 1109-1115 (2004).
    • (2004) Nat. Immunol , vol.5 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 2
    • 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: 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).
    • (2006) J. Virol , vol.80 , pp. 3863-3871
    • Saffert, R.T.1    Kalejta, R.F.2
  • 3
    • 33746840094 scopus 로고    scopus 로고
    • Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections
    • Tavalai N, Papior P, Rechter S, Leis M, Stamminger T: Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J. Virol. 80, 8006-8018 (2006).
    • (2006) J. Virol , vol.80 , pp. 8006-8018
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Leis, M.4    Stamminger, T.5
  • 4
    • 37349033209 scopus 로고    scopus 로고
    • Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection
    • Tavalai N, Papior P. Rechter S, Stamminger T: Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection. J. Virol. 82, 126-137 (2008).
    • (2008) J. Virol , vol.82 , pp. 126-137
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Stamminger, T.4
  • 5
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1
    • Ishov AM, Sotnikov AG. Negorev D et al.: PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147, 221-234 (1999).
    • (1999) J. Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3
  • 6
    • 0026019835 scopus 로고
    • Identification of a novel nuclear domain
    • Ascoli CA, Maul GG: Identification of a novel nuclear domain. J. Cell Biol. 112, 785-795 (1991).
    • (1991) J. Cell Biol , vol.112 , pp. 785-795
    • Ascoli, C.A.1    Maul, G.G.2
  • 7
    • 36349022047 scopus 로고    scopus 로고
    • The family Herpesviridae: A brief introduction
    • Knipe DM, Howley PM Eds, Lippincott Williams and Wilkins, Philadelphia, PA, USA. p
    • Pellett P. Roizman B: The family Herpesviridae: a brief introduction. In: Fields Virology (2). Knipe DM, Howley PM (Eds)., Lippincott Williams and Wilkins, Philadelphia, PA, USA. p. 2479-2500 (2007).
    • (2007) Fields Virology (2) , pp. 2479-2500
    • Pellett, P.1    Roizman, B.2
  • 8
    • 0028237175 scopus 로고
    • Preexisting nuclear architecture defines the intranuclear location of herpesvirus DNA replication structures
    • de Bruyn Kops A, Knipe DM: Preexisting nuclear architecture defines the intranuclear location of herpesvirus DNA replication structures. J. Virol. 68, 3512-3526 (1994).
    • (1994) J. Virol , vol.68 , pp. 3512-3526
    • de Bruyn Kops, A.1    Knipe, D.M.2
  • 9
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov AM, Maul GG: The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J. Cell Biol. 134, 815-826 (1996).
    • (1996) J. Cell Biol , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 10
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1
    • Maul GG, Ishov AM, Everett RD: Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology 217, 67-75 (1996).
    • (1996) Virology , vol.217 , pp. 67-75
    • Maul, G.G.1    Ishov, A.M.2    Everett, R.D.3
  • 11
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck JA, Maul GG, Miller WH Jr, Chen JD, Kakizuka A, Evans RM: A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76, 333-343 (1994).
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr, W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 12
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong S, Salomoni P, Pandolfi PP: The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2, E85-E90 (2000).
    • (2000) Nat. Cell Biol , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 13
    • 0033859313 scopus 로고    scopus 로고
    • The Daxx enigma
    • Michaelson JS: The Daxx enigma. Apoptasis 5, 217-220 (2000).
    • (2000) Apoptasis , vol.5 , pp. 217-220
    • Michaelson, J.S.1
  • 14
    • 32644487258 scopus 로고    scopus 로고
    • Daxx: Death or survival protein?
    • Salomoni P. Khelifi AF: Daxx: death or survival protein? Trends Cell Biol. 16, 97-104 (2006).
    • (2006) Trends Cell Biol , vol.16 , pp. 97-104
    • Salomoni, P.1    Khelifi, A.F.2
  • 15
    • 0031791875 scopus 로고    scopus 로고
    • PML is essential for multiple apoptotic pathways
    • Wang ZG, Ruggero D, Ronchetti S et al.: PML is essential for multiple apoptotic pathways. Nat. Genet. 20, 266-272 (1998).
    • (1998) Nat. Genet , vol.20 , pp. 266-272
    • Wang, Z.G.1    Ruggero, D.2    Ronchetti, S.3
  • 16
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni P. Pandolfi PP: The role of PML in tumor suppression. Cell 108, 165-170 (2002).
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 17
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • Everett RD, Chelbi-Alix MK: PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89, 819-830 (2007).
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 18
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi R, Pandolfi PP: Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev Mol. Cell Biol. 8, 1006-1016 (2007).
    • (2007) Nat. Rev Mol. Cell Biol , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 20
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot
    • Negorev D, Maul GG: Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 20, 7234-7242 (2001).
    • (2001) Oncogene , vol.20 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 21
    • 3142654673 scopus 로고    scopus 로고
    • Nuclear bodies and compartments: Functional roles and cellular signalling in health and disease
    • Zimber A, Nguyen QD, Gespach C: Nuclear bodies and compartments: functional roles and cellular signalling in health and disease. Cell Signal. 16, 1085-1104 (2004).
    • (2004) Cell Signal , vol.16 , pp. 1085-1104
    • Zimber, A.1    Nguyen, Q.D.2    Gespach, C.3
  • 22
    • 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: Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J. Cell Biol. 138, 5-16 (1997).
    • (1997) J. Cell Biol , vol.138 , pp. 5-16
    • Ishov, A.M.1    Stenberg, R.M.2    Maul, G.G.3
  • 23
    • 35148893559 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts
    • Everett RD, Murray J, Orr A, Preston CM: Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts. J. Virol. 81, 10991-11004 (2007).
    • (2007) J. Virol , vol.81 , pp. 10991-11004
    • Everett, R.D.1    Murray, J.2    Orr, A.3    Preston, C.M.4
  • 24
    • 0028979594 scopus 로고
    • The acute promyelocytic leukaemia-associated PML gene is induced by interferon
    • Lavau C, Marchio A, Fagioli M et al.: The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 11, 871-876 (1995).
    • (1995) Oncogene , vol.11 , pp. 871-876
    • Lavau, C.1    Marchio, A.2    Fagioli, M.3
  • 25
    • 0027095906 scopus 로고
    • IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis
    • Guldner HH, Szostecki C, Grotzinger T, Will H: IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J. Immunol. 149, 4067-4073 (1992).
    • (1992) J. Immunol , vol.149 , pp. 4067-4073
    • Guldner, H.H.1    Szostecki, C.2    Grotzinger, T.3    Will, H.4
  • 26
    • 0034948684 scopus 로고    scopus 로고
    • An essential role for Daxx in the inhibition of B lymphopoiesis by type I interferons
    • Gongora R, Stephan RP, Zhang Z, Cooper MD: An essential role for Daxx in the inhibition of B lymphopoiesis by type I interferons. J. Immunol. 14, 727-737 (2001).
    • (2001) J. Immunol , vol.14 , pp. 727-737
    • Gongora, R.1    Stephan, R.P.2    Zhang, Z.3    Cooper, M.D.4
  • 27
    • 0030912888 scopus 로고    scopus 로고
    • The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells
    • Ahn JH, Hayward GS: The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PML-associated nuclear bodies at very early times in infected permissive cells. J. Virol. 71, 4599-4613 (1997).
    • (1997) J. Virol , vol.71 , pp. 4599-4613
    • Ahn, J.H.1    Hayward, G.S.2
  • 28
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett RD, Maul GG: HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13, 5062-5069 (1994).
    • (1994) EMBO J , vol.13 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 29
    • 0030602019 scopus 로고    scopus 로고
    • The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1
    • Korioth F. Maul GG, Plachter B, Stamminger T, Frey J: The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1. Exp. Cell Res. 229, 155-158 (1996).
    • (1996) Exp. Cell Res , vol.229 , pp. 155-158
    • Korioth, F.1    Maul, G.G.2    Plachter, B.3    Stamminger, T.4    Frey, J.5
  • 30
    • 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: ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J. Virol. 79, 5078-5089 (2005).
    • (2005) J. Virol , vol.79 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 31
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett RD, Freemont P. Saitoh H et al.: The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72, 6581-6591 (1998).
    • (1998) J. Virol , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3
  • 32
    • 0033611590 scopus 로고    scopus 로고
    • Chelbi-Alix MK, de The H: Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18, 935-941 (1999).
    • Chelbi-Alix MK, de The H: Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18, 935-941 (1999).
  • 33
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell C, Sadis S, Everett RD: Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76, 841-850 (2002).
    • (2002) J. Virol , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 34
    • 0022978685 scopus 로고
    • Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110
    • Stow ND, Stow EC: Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110. J. Gen. Virol. 67(Pt 12), 2571-2585 (1986).
    • (1986) J. Gen. Virol , vol.67 , Issue.PART 12 , pp. 2571-2585
    • Stow, N.D.1    Stow, E.C.2
  • 35
    • 0028825230 scopus 로고
    • Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures
    • Everett R, O'Hare P, O'Rourke D, Barlow P. Orr A: Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures. J. Virol. 69, 7339-7344 (1995).
    • (1995) J. Virol , vol.69 , pp. 7339-7344
    • Everett, R.1    O'Hare, P.2    O'Rourke, D.3    Barlow, P.4    Orr, A.5
  • 36
    • 0034687704 scopus 로고    scopus 로고
    • UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells
    • Bresnahan WA, Shenk TE: UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells. Proc. Natl Acad Sci. USA 97, 14506-14511 (2000).
    • (2000) Proc. Natl Acad Sci. USA , vol.97 , pp. 14506-14511
    • Bresnahan, W.A.1    Shenk, T.E.2
  • 37
    • 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: Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication. J. Virology 79, 7792-7802 (2005).
    • (2005) J. Virology , vol.79 , pp. 7792-7802
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 38
    • 34848835708 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of Daxx by the viral pp71 protein in human cytomegalovirus-infected cells
    • Hwang J, Kalejta RF: Proteasome-dependent, ubiquitin-independent degradation of Daxx by the viral pp71 protein in human cytomegalovirus-infected cells. Virology 367, 334-338 (2007).
    • (2007) Virology , vol.367 , pp. 334-338
    • Hwang, J.1    Kalejta, R.F.2
  • 39
    • 33744908280 scopus 로고    scopus 로고
    • Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression of HCMV replication
    • Cantrell SR, Bresnahan WA: Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression of HCMV replication. J. Virol. 80, 6188-6191 (2006).
    • (2006) J. Virol , vol.80 , pp. 6188-6191
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 40
    • 33646161949 scopus 로고    scopus 로고
    • Role of the cellular protein hDaxx in human cytomegalovirus immediate-early gene expression
    • Preston CM, Nicholl MJ: Role of the cellular protein hDaxx in human cytomegalovirus immediate-early gene expression. J. Gen. Virol. 87, 1113-1121 (2006).
    • (2006) J. Gen. Virol , vol.87 , pp. 1113-1121
    • Preston, C.M.1    Nicholl, M.J.2
  • 41
    • 0026773361 scopus 로고
    • Human cytomegalovirus contains a tegument protein that enhances transcription from promoters with upstream ATF and AP-1 cis-acting elements
    • Liu B, Stinski MF: Human cytomegalovirus contains a tegument protein that enhances transcription from promoters with upstream ATF and AP-1 cis-acting elements. J. Virol. 66, 4434-4444 (1992).
    • (1992) J. Virol , vol.66 , pp. 4434-4444
    • Liu, B.1    Stinski, M.F.2
  • 42
    • 0036091745 scopus 로고    scopus 로고
    • Functional interaction between the pp71 protein of human cytomegalovirus and the PML-interacting protein human Daxx
    • Hofmann H, Sindre H, Stamminger T: Functional interaction between the pp71 protein of human cytomegalovirus and the PML-interacting protein human Daxx. J. Virol. 76, 5769-5783 (2002).
    • (2002) J. Virol , vol.76 , pp. 5769-5783
    • Hofmann, H.1    Sindre, H.2    Stamminger, T.3
  • 43
    • 2642574870 scopus 로고    scopus 로고
    • Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells
    • Lee HR, Kim DJ, Lee JM et al.: Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells. J. Virol. 78, 6527-6542 (2004).
    • (2004) J. Virol , vol.78 , pp. 6527-6542
    • Lee, H.R.1    Kim, D.J.2    Lee, J.M.3
  • 44
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Muller S, Dejean A: Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73, 5137-5143 (1999).
    • (1999) J. Virol , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 45
    • 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: 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).
    • (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
  • 46
    • 33746809411 scopus 로고    scopus 로고
    • Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression
    • Negorev DG, Vladimirova OV, Ivanov A, Rauscher F 3rd, Maul GG: Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression. J. Virol. 80, 8019-8029 (2006).
    • (2006) J. Virol , vol.80 , pp. 8019-8029
    • Negorev, D.G.1    Vladimirova, O.V.2    Ivanov, A.3    Rauscher 3rd, F.4    Maul, G.G.5
  • 47
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICPO
    • Everett RD, Rechter S, Papior P, Tavalai N, Stamminger T, Orr A: PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICPO. J. Virol. 80, 7995-8005 (2006).
    • (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
  • 48
    • 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: Replication of ICP0 null mutant herpes simplex virus type 1 is restricted by both PML and Sp100. J. Virol. 82(6), 2661-2672 (2008).
    • (2008) J. Virol , vol.82 , Issue.6 , pp. 2661-2672
    • Everett, R.D.1    Parada, C.2    Gripon, P.3    Sirma, H.4    Orr, A.5
  • 49
    • 0037941647 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects
    • Chee AV, Lopez P, Pandolfi PP, Roizman B: Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects. J. Virol. 77, 7101-7105 (2003).
    • (2003) J. Virol , vol.77 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 50
    • 0036720433 scopus 로고    scopus 로고
    • Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effeet on accumulation of infectious herpes simplex virus 1 or its proteins
    • Lopez P, Jacob RJ, Roizman B: Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effeet on accumulation of infectious herpes simplex virus 1 or its proteins. J. Virol. 76, 9355-9367 (2002).
    • (2002) J. Virol , vol.76 , pp. 9355-9367
    • Lopez, P.1    Jacob, R.J.2    Roizman, B.3
  • 51
    • 10344222687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate-early 1 protein facilitates viral replication by antagonizing histone deacetylation
    • Nevels M, Paulus C, Shenk T: Human cytomegalovirus immediate-early 1 protein facilitates viral replication by antagonizing histone deacetylation. Proc. Natl Acad. Sci. USA 101, 17234-17239 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 17234-17239
    • Nevels, M.1    Paulus, C.2    Shenk, T.3
  • 52
    • 0032581946 scopus 로고    scopus 로고
    • Cytodifferentiating agents affect the replication of herpes simplex virus type 1 in the absence of functional VP16
    • Preston CM, McFarlane M: Cytodifferentiating agents affect the replication of herpes simplex virus type 1 in the absence of functional VP16. Virology 249, 418-426 (1998).
    • (1998) Virology , vol.249 , pp. 418-426
    • Preston, C.M.1    McFarlane, M.2
  • 53
    • 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
    • Poon AP, Liang Y, Roizman B: 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 (2003).
    • (2003) J. Virol , vol.77 , pp. 12671-12678
    • Poon, A.P.1    Liang, Y.2    Roizman, B.3
  • 54
    • 36049038672 scopus 로고    scopus 로고
    • Terry-Allison T, Smith CA. DeLuca NA: Relaxed repression of herpes simplex virus type 1 genomes in murine trigeminal neurons. J. Virol. 81, 12394-12405 (2007).
    • Terry-Allison T, Smith CA. DeLuca NA: Relaxed repression of herpes simplex virus type 1 genomes in murine trigeminal neurons. J. Virol. 81, 12394-12405 (2007).
  • 55
    • 0035082504 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 promoter activity during latency establishment, maintenance, and reactivation in primary dorsal root neurons in vitro
    • Arthur JL, Scarpini CG, Connor V, Lachmann RH, Tolkovsky AM, Efstathiou S: Herpes simplex virus type 1 promoter activity during latency establishment, maintenance, and reactivation in primary dorsal root neurons in vitro. J. Virol. 75, 3885-3895 (2001).
    • (2001) J. Virol , vol.75 , pp. 3885-3895
    • Arthur, J.L.1    Scarpini, C.G.2    Connor, V.3    Lachmann, R.H.4    Tolkovsky, A.M.5    Efstathiou, S.6
  • 56
    • 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
    • Danaher RJ, Jacob RJ, Steiner MR, Allen WR, Hill JM, Miller CS: Histone deacetylase inhibitors induce reactivation of herpes simplex virus type 1 in a latency-associated transcript-independent manner in neuronal cells. J. Neurovirol. 11, 306-317 (2005).
    • (2005) J. Neurovirol , vol.11 , 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
  • 57
    • 2942672088 scopus 로고    scopus 로고
    • Functional interaction between class II histone deacetylases and ICPO of herpes simplex virus type 1
    • Lomonte P, Thomas J, Texier P, Caron C, Khochbin S, Epstein AL: Functional interaction between class II histone deacetylases and ICPO of herpes simplex virus type 1. J. Virol. 78, 6744-6757 (2004).
    • (2004) J. Virol , vol.78 , pp. 6744-6757
    • Lomonte, P.1    Thomas, J.2    Texier, P.3    Caron, C.4    Khochbin, S.5    Epstein, A.L.6
  • 58
    • 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
    • Gu H, Roizman B: 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 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 17134-17139
    • Gu, H.1    Roizman, B.2
  • 59
    • 19644384912 scopus 로고    scopus 로고
    • Gu H, Liang Y, Mandel G. Roizman B: 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 (2005).
    • Gu H, Liang Y, Mandel G. Roizman B: 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 (2005).
  • 60
    • 38349022497 scopus 로고    scopus 로고
    • Histone modifications associated with herpes simplex virus type 1 genomes during quiescence and following ICP0-mediated de-repression
    • Coleman HM, Connor V, Cheng ZS, Grey F, Preston CM, Efstathiou S: Histone modifications associated with herpes simplex virus type 1 genomes during quiescence and following ICP0-mediated de-repression. J. Gen. Virol. 89, 68-77 (2008).
    • (2008) J. Gen. Virol , vol.89 , pp. 68-77
    • Coleman, H.M.1    Connor, V.2    Cheng, Z.S.3    Grey, F.4    Preston, C.M.5    Efstathiou, S.6
  • 61
    • 0028970090 scopus 로고
    • Structure and function of transcriptional activation domains
    • Triezenberg SJ: Structure and function of transcriptional activation domains. Curr. Opin. Genet. Dev. 5, 190-196 (1995).
    • (1995) Curr. Opin. Genet. Dev , vol.5 , pp. 190-196
    • Triezenberg, S.J.1
  • 62
    • 0038434062 scopus 로고    scopus 로고
    • The herpes simplex virus VP16-induced complex: The makings of a regulatory switch
    • Wysocka J, Herr W: The herpes simplex virus VP16-induced complex: the makings of a regulatory switch. Trends Biochem. Sci. 28, 294-304 (2003).
    • (2003) Trends Biochem. Sci , vol.28 , pp. 294-304
    • Wysocka, J.1    Herr, W.2
  • 63
    • 0031451158 scopus 로고    scopus 로고
    • Viral transactivating proteins
    • Flint J, Shenk T: Viral transactivating proteins. Annu. Rev. Genet. 31, 177-212 (1997).
    • (1997) Annu. Rev. Genet , vol.31 , pp. 177-212
    • Flint, J.1    Shenk, T.2
  • 64
    • 34249950342 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • Knipe DM, Howley PM Eds, Lippincott Williams and Wilkins, Philadelphia, PA, USA, p
    • Rotzman B, Knipe DM, Whitley RJ: Herpes simplex viruses. In: Fields Virology (2). Knipe DM, Howley PM (Eds). Lippincott Williams and Wilkins, Philadelphia, PA, USA, p. 2501-2602 (2007).
    • (2007) Fields Virology (2) , pp. 2501-2602
    • Rotzman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 65
    • 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
    • Herrera FJ, Triezenberg SJ: VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection. J. Virol. 78, 9689-9696 (2004).
    • (2004) J. Virol , vol.78 , pp. 9689-9696
    • Herrera, F.J.1    Triezenberg, S.J.2
  • 66
    • 0028096996 scopus 로고
    • Requirements for activation of the herpes simplex virus glycoprotein C promoter in vitro by the viral regulatory protein ICP4
    • Gu B, DeLuca N: Requirements for activation of the herpes simplex virus glycoprotein C promoter in vitro by the viral regulatory protein ICP4. J. Virol. 68, 7953-7965 (1994).
    • (1994) J. Virol , vol.68 , pp. 7953-7965
    • Gu, B.1    DeLuca, N.2
  • 67
    • 0034469709 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 ICP4 promotes transcription preinitiation complex formation by enhancing the binding of TFIID to DNA
    • Grondin B, DeLuca N: Herpes simplex virus type 1 ICP4 promotes transcription preinitiation complex formation by enhancing the binding of TFIID to DNA. J. Virol. 74, 11504-11510 (2000).
    • (2000) J. Virol , vol.74 , pp. 11504-11510
    • Grondin, B.1    DeLuca, N.2
  • 68
    • 0029946735 scopus 로고    scopus 로고
    • Interaction of the viral activator protein ICP4 with TFIID through TAF250
    • Carrozza MJ, DeLuca NA: Interaction of the viral activator protein ICP4 with TFIID through TAF250. Mol. Cell Biol. 16. 3085-3093 (1996).
    • (1996) Mol. Cell Biol , vol.16 , pp. 3085-3093
    • Carrozza, M.J.1    DeLuca, N.A.2
  • 69
    • 39749144518 scopus 로고    scopus 로고
    • Binding of ICP4, TATA-binding protein, and RNA polymerase II to herpes simplex virus, type 1 immediate early, early and late promoters in virus-infected cells
    • Sampath P, Deluca NA: Binding of ICP4, TATA-binding protein, and RNA polymerase II to herpes simplex virus, type 1 immediate early, early and late promoters in virus-infected cells. J. Virol. 82(5), 2339-2349 (2008).
    • (2008) J. Virol , vol.82 , Issue.5 , pp. 2339-2349
    • Sampath, P.1    Deluca, N.A.2
  • 70
    • 0023680832 scopus 로고
    • Direct correlation between a negative autoregulatory response element at the cap site of the herpes simplex virus type 1 IE175 (alpha 4) promoter and a specific binding site for the IE175 (ICP4) protein
    • Roberts MS, Boundy A, O'Hare P, Pizzorno MC, Ciufo DM, Hayward GS: Direct correlation between a negative autoregulatory response element at the cap site of the herpes simplex virus type 1 IE175 (alpha 4) promoter and a specific binding site for the IE175 (ICP4) protein. J. Virol. 62, 4307-4320 (1988).
    • (1988) J. Virol , vol.62 , pp. 4307-4320
    • Roberts, M.S.1    Boundy, A.2    O'Hare, P.3    Pizzorno, M.C.4    Ciufo, D.M.5    Hayward, G.S.6
  • 71
    • 0027513386 scopus 로고
    • Repression of the herpes simplex virus 1 alpha 4 gene by its gene product occurs within the context of the viral genome and is associated with all three identified cognate sites
    • Michael N, Roizman B: Repression of the herpes simplex virus 1 alpha 4 gene by its gene product occurs within the context of the viral genome and is associated with all three identified cognate sites. Proc. Natl Acad. Sci USA 90, 2286-2290 (1993).
    • (1993) Proc. Natl Acad. Sci USA , vol.90 , pp. 2286-2290
    • Michael, N.1    Roizman, B.2
  • 72
    • 0028940542 scopus 로고
    • Repression of the herpes simplex virus 1 alpha 4 gene by its gene product (ICP4) within the context of the viral genome is conditioned by the distance and steroaxial alignment of the ICP4 DNA binding site relative to the TATA box
    • Leopardi R, Michael N, Roizman B: Repression of the herpes simplex virus 1 alpha 4 gene by its gene product (ICP4) within the context of the viral genome is conditioned by the distance and steroaxial alignment of the ICP4 DNA binding site relative to the TATA box. J. Virol. 69, 3042-3048 (1995).
    • (1995) J. Virol , vol.69 , pp. 3042-3048
    • Leopardi, R.1    Michael, N.2    Roizman, B.3
  • 73
    • 0037094414 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate early proteins and cell growth control
    • Castillo JP, Kowalik TF: Human cytomegalovirus immediate early proteins and cell growth control. Gene 290, 19-34 (2002).
    • (2002) Gene , vol.290 , pp. 19-34
    • Castillo, J.P.1    Kowalik, T.F.2
  • 74
    • 34548158284 scopus 로고    scopus 로고
    • Cytomegaloviruses
    • Knipe DM, Howley PM Eds, Lippincott Williams and Wilkins. Philadelphia, PA, USA, p
    • Mocarski ES, Shenk T, Pass RF: Cytomegaloviruses. In: Fields Virology. Knipe DM, Howley PM (Eds)., Lippincott Williams and Wilkins. Philadelphia, PA, USA, p. 2701-2772 (2007).
    • (2007) Fields Virology , pp. 2701-2772
    • Mocarski, E.S.1    Shenk, T.2    Pass, R.F.3
  • 75
    • 36749048614 scopus 로고    scopus 로고
    • Functional interaction of the human cytomegalovirus IE2 protein with histone deacetylase 2 in infected human fibroblasts
    • Park JJ, Kim YE, Pham HT, Kim ET, Chung YH, Ahn JH: Functional interaction of the human cytomegalovirus IE2 protein with histone deacetylase 2 in infected human fibroblasts. J. Gen. Virol. 88, 3214-3223 (2007).
    • (2007) J. Gen. Virol , vol.88 , pp. 3214-3223
    • Park, J.J.1    Kim, Y.E.2    Pham, H.T.3    Kim, E.T.4    Chung, Y.H.5    Ahn, J.H.6
  • 76
    • 33749496663 scopus 로고    scopus 로고
    • Autorepression of the human cytomegalovirus major immediate-early promoter/enhancer at late times of infection is mediated by the recruitment of chromatin remodeling enzymes by IE86
    • Reeves M, Murphy J, Greaves R, Fairley J, Brehm A, Sinclair J: Autorepression of the human cytomegalovirus major immediate-early promoter/enhancer at late times of infection is mediated by the recruitment of chromatin remodeling enzymes by IE86. J. Virol. 80, 9998-10009 (2006).
    • (2006) J. Virol , vol.80 , pp. 9998-10009
    • Reeves, M.1    Murphy, J.2    Greaves, R.3    Fairley, J.4    Brehm, A.5    Sinclair, J.6
  • 77
    • 0025778996 scopus 로고
    • Monocytes are a major site of persistence of human cytomegalovirus in peripheral blood mononuclear cells
    • Taylor-Wiedeman J, Sissons JG, Borysiewicz LK, Sinclair JH: Monocytes are a major site of persistence of human cytomegalovirus in peripheral blood mononuclear cells. J. Gen. Virol. 72(Pt 9). 2059-2064 (1991).
    • (1991) J. Gen. Virol , vol.72 , Issue.PART 9 , pp. 2059-2064
    • Taylor-Wiedeman, J.1    Sissons, J.G.2    Borysiewicz, L.K.3    Sinclair, J.H.4
  • 78
    • 0028158478 scopus 로고
    • Induction of endogenous human cytomegalovirus gene expression after differentiation of monocytes from healthy carriers
    • Taylor-Wiedeman J, Sissons P, Sinclair J: Induction of endogenous human cytomegalovirus gene expression after differentiation of monocytes from healthy carriers. J. Virol. 68, 1597-1604 (1994).
    • (1994) J. Virol , vol.68 , pp. 1597-1604
    • Taylor-Wiedeman, J.1    Sissons, P.2    Sinclair, J.3
  • 79
    • 0032584111 scopus 로고    scopus 로고
    • Cytomegalovirus remains latent in a common precursor of dendritic and myeloid cells
    • Hahn G, Jores R, Mocarski ES: Cytomegalovirus remains latent in a common precursor of dendritic and myeloid cells. Proc. Natl Acad. Sci. USA 95, 3937-3942 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3937-3942
    • Hahn, G.1    Jores, R.2    Mocarski, E.S.3
  • 80
    • 3442897153 scopus 로고    scopus 로고
    • Human cytomegalovirus persists in myeloid progenitors and is passed to the myeloid progeny in a latent form
    • Khalboullina SF, Maciejewski JP, Crapnell K et al.: Human cytomegalovirus persists in myeloid progenitors and is passed to the myeloid progeny in a latent form. Br. J. Haematol. 126, 410-417 (2004).
    • (2004) Br. J. Haematol , vol.126 , pp. 410-417
    • Khalboullina, S.F.1    Maciejewski, J.P.2    Crapnell, K.3
  • 81
    • 34547948217 scopus 로고    scopus 로고
    • Human cytomegalovirus sequences expressed in latently infected individuals promote a latent infection in vitro
    • Goodrum F, Reeves M, Sinclair J, High K, Shenk T: Human cytomegalovirus sequences expressed in latently infected individuals promote a latent infection in vitro. Blood 110, 937-945 (2007).
    • (2007) Blood , vol.110 , pp. 937-945
    • Goodrum, F.1    Reeves, M.2    Sinclair, J.3    High, K.4    Shenk, T.5
  • 82
    • 0037058914 scopus 로고    scopus 로고
    • Human cytomegalovirus gene expression during infection of primary hematopoietic progenitor cells: A model for latency
    • Goodrum FD, Jordan CT, High K, Shenk T: Human cytomegalovirus gene expression during infection of primary hematopoietic progenitor cells: a model for latency. Proc. Natl Acad. Sci. USA 99, 16255-16260 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16255-16260
    • Goodrum, F.D.1    Jordan, C.T.2    High, K.3    Shenk, T.4
  • 83
    • 27644534040 scopus 로고    scopus 로고
    • An in vitro model for the regulation of human cytomegalovirus latency and reactivation in dendritic cells by chromatin remodelling
    • Reeves MB, Lehner PJ, Sissons JG, Sinclair JH: An in vitro model for the regulation of human cytomegalovirus latency and reactivation in dendritic cells by chromatin remodelling. J. Gen. Virol. 86, 2949-2954 (2005).
    • (2005) J. Gen. Virol , vol.86 , pp. 2949-2954
    • Reeves, M.B.1    Lehner, P.J.2    Sissons, J.G.3    Sinclair, J.H.4
  • 84
    • 15244359130 scopus 로고    scopus 로고
    • Latency. chromatin remodeling, and reactivation of human cytomegalovirus in the dendritic cells of healthy carriers
    • Reeves MB, MacAry PA, Lehner PJ, Sissons JG, Sinclair JH: Latency. chromatin remodeling, and reactivation of human cytomegalovirus in the dendritic cells of healthy carriers. Proc. Natl Acad. Sci. USA 102, 4140-4145 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4140-4145
    • Reeves, M.B.1    MacAry, P.A.2    Lehner, P.J.3    Sissons, J.G.4    Sinclair, J.H.5
  • 85
    • 33845265081 scopus 로고    scopus 로고
    • Viral gene expression during the establishment of human cytomegalovirus latent infection in myeloid progenitor cells
    • Cheung AK, Abendroth A, Cunningham AL, Slobedman B: Viral gene expression during the establishment of human cytomegalovirus latent infection in myeloid progenitor cells. Blood 108, 3691-3699 (2006).
    • (2006) Blood , vol.108 , pp. 3691-3699
    • Cheung, A.K.1    Abendroth, A.2    Cunningham, A.L.3    Slobedman, B.4
  • 86
    • 33745589746 scopus 로고    scopus 로고
    • Latency and reactivation of human cytomegalovirus
    • Sinclair J, Sissons P: Latency and reactivation of human cytomegalovirus. J. Gen. Virol. 87, 1763-1779 (2006).
    • (2006) J. Gen. Virol , vol.87 , pp. 1763-1779
    • Sinclair, J.1    Sissons, P.2
  • 87
    • 0036500165 scopus 로고    scopus 로고
    • Control of cytomegalovirus lytic gene expression by histone acetylation
    • Murphy JC, Fischle W, Verdin E, Sinclair JH: Control of cytomegalovirus lytic gene expression by histone acetylation. EMBO J. 21, 1112-1120 (2002).
    • (2002) EMBO J , vol.21 , pp. 1112-1120
    • Murphy, J.C.1    Fischle, W.2    Verdin, E.3    Sinclair, J.H.4
  • 88
    • 33750954152 scopus 로고    scopus 로고
    • Control of human cytomegalovirus gene expression by differential histone modifications during lytic and latent infection of a monocytic cell line
    • Ioudinkova E, Arcangeletti MC, Rynditch A et al.: Control of human cytomegalovirus gene expression by differential histone modifications during lytic and latent infection of a monocytic cell line. Gene 384, 120-128 (2006).
    • (2006) Gene , vol.384 , pp. 120-128
    • Ioudinkova, E.1    Arcangeletti, M.C.2    Rynditch, A.3
  • 89
    • 34249933862 scopus 로고    scopus 로고
    • Reversal of human cytomegalovirus major immediate-early enhancer/ promoter silencing in quiescently infected cells via the cyclic-AMP signaling pathway
    • Keller MJ, Wu AW, Andrews JI, McGonagill PW, Tibesar EE, Meier JL: Reversal of human cytomegalovirus major immediate-early enhancer/ promoter silencing in quiescently infected cells via the cyclic-AMP signaling pathway. J. Virol.. 81, 6669-6681 (2007).
    • (2007) J. Virol , vol.81 , pp. 6669-6681
    • Keller, M.J.1    Wu, A.W.2    Andrews, J.I.3    McGonagill, P.W.4    Tibesar, E.E.5    Meier, J.L.6
  • 90
    • 0035136706 scopus 로고    scopus 로고
    • Reactivation of the human cytomegalovirus major immediate-early regulatory region and viral replication in embryonal NTera2 cells: Role of trichostatin A, retinoic acid, and deletion of the 21-base-pair repeats and modulator
    • Meier JL: Reactivation of the human cytomegalovirus major immediate-early regulatory region and viral replication in embryonal NTera2 cells: role of trichostatin A, retinoic acid, and deletion of the 21-base-pair repeats and modulator. J. Virol. 75, 1581-1593 (2001).
    • (2001) J. Virol , vol.75 , pp. 1581-1593
    • Meier, J.L.1
  • 91
    • 34247859153 scopus 로고    scopus 로고
    • Ectopic expression of HCMV IE72 and IE86 proteins is sufficient to induce early gene expression but not production of infectious virus in undifferentiated promonocytic THP-1 cells
    • Yee LF, Lin PL, Stinski MF: Ectopic expression of HCMV IE72 and IE86 proteins is sufficient to induce early gene expression but not production of infectious virus in undifferentiated promonocytic THP-1 cells. Virology, 363, 174-188 (2007).
    • (2007) Virology , vol.363 , pp. 174-188
    • Yee, L.F.1    Lin, P.L.2    Stinski, M.F.3
  • 92
    • 34548159689 scopus 로고    scopus 로고
    • Human cytomegalovirus gene expression is silenced by Daxx-mediated intrinsic immune defense in model latent infections established in vitro
    • Saffert RT, Kalejta RF: Human cytomegalovirus gene expression is silenced by Daxx-mediated intrinsic immune defense in model latent infections established in vitro. J. Virol. 81, 9109-9120 (2007).
    • (2007) J. Virol , vol.81 , pp. 9109-9120
    • Saffert, R.T.1    Kalejta, R.F.2
  • 93
    • 0030425424 scopus 로고    scopus 로고
    • Regulation of human cytomegalovirus immediate-early gene expression
    • Meier JL, Stinski MF: Regulation of human cytomegalovirus immediate-early gene expression. Intervirology 39: 331-342 (1996).
    • (1996) Intervirology , vol.39 , pp. 331-342
    • Meier, J.L.1    Stinski, M.F.2
  • 94
    • 36248945635 scopus 로고    scopus 로고
    • Knockdown of hDaxx in normally non-permissive undifferentiated cells does not permit human cytomegalovirus immediate-early gene expression
    • Groves IJ, Sinclair JH: Knockdown of hDaxx in normally non-permissive undifferentiated cells does not permit human cytomegalovirus immediate-early gene expression. J. Gen. Virol. 88. 2935-2940 (2007).
    • (2007) J. Gen. Virol , vol.88 , pp. 2935-2940
    • Groves, I.J.1    Sinclair, J.H.2
  • 95
    • 0040036654 scopus 로고    scopus 로고
    • HCF-dependent nuclear import of VP16
    • La Boissiere S, Hughes T, O'Hare P: HCF-dependent nuclear import of VP16. EMBO J. 18, 480-489 (1999).
    • (1999) EMBO J , vol.18 , pp. 480-489
    • La Boissiere, S.1    Hughes, T.2    O'Hare, P.3
  • 96
    • 0033573922 scopus 로고    scopus 로고
    • Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency
    • Kristie TM, Vogel JL, Sears AE: Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency. Proc. Natl Acad. Sci. USA 96, 1229-1233 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1229-1233
    • Kristie, T.M.1    Vogel, J.L.2    Sears, A.E.3
  • 97
    • 0026040485 scopus 로고
    • Expression of the herpes simplex virus 1 alpha transinducing factor (VP16) does not induce reactivation of latent virus or prevent the establishment of latency in mice
    • Sears AE, Hukkanen V, Labow MA, Levine AJ, Roizman B. Expression of the herpes simplex virus 1 alpha transinducing factor (VP16) does not induce reactivation of latent virus or prevent the establishment of latency in mice. J. Virol. 65, 2929-2935 (1991).
    • (1991) J. Virol , vol.65 , pp. 2929-2935
    • Sears, A.E.1    Hukkanen, V.2    Labow, M.A.3    Levine, A.J.4    Roizman, B.5
  • 98
    • 0031947861 scopus 로고    scopus 로고
    • Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins
    • Samaniego LA, Neiderhiser L, DeLuca NA: Persistence and expression of the herpes simplex virus genome in the absence of immediate-early proteins. J. Virol. 72, 3307-3320 (1998).
    • (1998) J. Virol , vol.72 , pp. 3307-3320
    • Samaniego, L.A.1    Neiderhiser, L.2    DeLuca, N.A.3
  • 99
    • 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: Human cytomegalovirus tegument protein pp71 directs long-term gene expression from quiescent herpes simplex virus genomes. J. Virus. 79, 525-535 (2005).
    • (2005) J. Virus , vol.79 , pp. 525-535
    • Preston, C.M.1    Nicholl, M.J.2
  • 100
    • 28844456962 scopus 로고    scopus 로고
    • Functional inaccessibility of quiescent herpes simplex virus genomes
    • Minaker RL, Mossman KL, Smiley JR: Functional inaccessibility of quiescent herpes simplex virus genomes. Virol. J. 2, 85 (2005).
    • (2005) Virol. J , vol.2 , pp. 85
    • Minaker, R.L.1    Mossman, K.L.2    Smiley, J.R.3
  • 101
    • 0035106881 scopus 로고    scopus 로고
    • Efficient activation of viral genomes by levels of herpes simplex virus ICPO insufficient to affect cellular gene expression or cell survival
    • Hobbs WE, Brough DE, Kovesdi I, DeLuca NA: Efficient activation of viral genomes by levels of herpes simplex virus ICPO insufficient to affect cellular gene expression or cell survival. J. Virol. 75, 3391-3403 (2001).
    • (2001) J. Virol , vol.75 , pp. 3391-3403
    • Hobbs, W.E.1    Brough, D.E.2    Kovesdi, I.3    DeLuca, N.A.4
  • 102
    • 0036239509 scopus 로고    scopus 로고
    • Neither LAT nor open reading frame P mutations increase expression of spliced or intron-containing ICPO transcripts in mouse ganglia latently infected with herpes simplex virus
    • Chen SH, Lee LY, Garber DA, Schaffer PA, Knipe DM, Coen DM: Neither LAT nor open reading frame P mutations increase expression of spliced or intron-containing ICPO transcripts in mouse ganglia latently infected with herpes simplex virus. J. Virol. 76, 4764-4772 (2002).
    • (2002) J. Virol , vol.76 , pp. 4764-4772
    • Chen, S.H.1    Lee, L.Y.2    Garber, D.A.3    Schaffer, P.A.4    Knipe, D.M.5    Coen, D.M.6
  • 103
    • 33748500436 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 latently infected neurons differentially express latency-associated and ICPO transcripts
    • Maillet S, Naas T, Crepin S et al.: Herpes simplex virus type 1 latently infected neurons differentially express latency-associated and ICPO transcripts. J. Virol. 80, 9310-9321 (2006).
    • (2006) J. Virol , vol.80 , pp. 9310-9321
    • Maillet, S.1    Naas, T.2    Crepin, S.3
  • 104
    • 0031925976 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 latency-associated transcripts suppress viral replication and reduce immediate-early gene mRNA levels in a neuronal cell line
    • Mador N, Goldenberg D, Cohen O, Panet A, Steiner I: Herpes simplex virus type 1 latency-associated transcripts suppress viral replication and reduce immediate-early gene mRNA levels in a neuronal cell line. J. Virol. 72, 5067-5075 (1998).
    • (1998) J. Virol , vol.72 , pp. 5067-5075
    • Mador, N.1    Goldenberg, D.2    Cohen, O.3    Panet, A.4    Steiner, I.5
  • 105
    • 0242300162 scopus 로고    scopus 로고
    • Thompson RL, Shieh MT. Sawtell NM: Analysis of herpes simplex virus ICPO promoter function in sensory neurons during acute infection, establishment of latency, and reactivation in vivo. J. Virol. 77, 12319-12330 (2003).
    • Thompson RL, Shieh MT. Sawtell NM: Analysis of herpes simplex virus ICPO promoter function in sensory neurons during acute infection, establishment of latency, and reactivation in vivo. J. Virol. 77, 12319-12330 (2003).
  • 106
    • 23844458876 scopus 로고    scopus 로고
    • Characterization of an antisense transcript spanning the UL81-82 locus of human cytomegalovirus
    • Bego M, Maciejewski J, Khaiboullina S. Pari G, St Jeor S: Characterization of an antisense transcript spanning the UL81-82 locus of human cytomegalovirus. J. Virol. 79, 11022-11034 (2005).
    • (2005) J. Virol , vol.79 , pp. 11022-11034
    • Bego, M.1    Maciejewski, J.2    Khaiboullina, S.3    Pari, G.4    St Jeor, S.5
  • 107
    • 39149132854 scopus 로고    scopus 로고
    • Chromatin control of herpes simplex virus lytic and latent infection
    • Knipe DM, Cliffe A: Chromatin control of herpes simplex virus lytic and latent infection. Nat. Rev. Microbiol. 6, 211-221 (2008).
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 211-221
    • Knipe, D.M.1    Cliffe, A.2
  • 108
    • 0035124377 scopus 로고    scopus 로고
    • Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies
    • Adamson AL, Kenney S: Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies. J Virol. 75, 2388-2399 (2001).
    • (2001) J Virol , vol.75 , pp. 2388-2399
    • Adamson, A.L.1    Kenney, S.2
  • 109
    • 0036842090 scopus 로고    scopus 로고
    • Stanton R, Fox JD, Caswell R, Sherratt E. Wilkinson GW: Analysis of the human herpesvirus-6 immediate-early 1 protein. J Gen. Virol. 83, 2811-2820 (2002).
    • Stanton R, Fox JD, Caswell R, Sherratt E. Wilkinson GW: Analysis of the human herpesvirus-6 immediate-early 1 protein. J Gen. Virol. 83, 2811-2820 (2002).
  • 110
    • 33644768122 scopus 로고    scopus 로고
    • Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption
    • Hoppe A, Beech SJ, Dimmock J, Leppard KN: Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption. J. Virol. 80, 3042-3049 (2006).
    • (2006) J. Virol , vol.80 , pp. 3042-3049
    • Hoppe, A.1    Beech, S.J.2    Dimmock, J.3    Leppard, K.N.4
  • 111
    • 34247562651 scopus 로고    scopus 로고
    • Adenovirus E4 ORF3 protein inhibits the interferon-mediated antiviral response
    • Ullman AJ, Reich NC, Hearing P: Adenovirus E4 ORF3 protein inhibits the interferon-mediated antiviral response. J. Virol, 81, 4744-4752 (2007).
    • (2007) J. Virol , vol.81 , pp. 4744-4752
    • Ullman, A.J.1    Reich, N.C.2    Hearing, P.3
  • 112
    • 2942711737 scopus 로고    scopus 로고
    • Guccione E. Lethbridge KJ,. Killick N, Leppard KN, Banks L: HPV E6 proteins Interact with specific PML isoforniAlmd allow distinctions to be made between different POD structures. Oncogene 23. 4662-4672 (2004).
    • Guccione E. Lethbridge KJ,. Killick N, Leppard KN, Banks L: HPV E6 proteins Interact with specific PML isoforniAlmd allow distinctions to be made between different POD structures. Oncogene 23. 4662-4672 (2004).
  • 113
    • 12844263583 scopus 로고    scopus 로고
    • Human papillomavirus oncoprotein E7 targets the promyelocytic leukemia protein and circumvents cellular senescence via the Rb and p53 tumor suppressor pathways
    • Bischof O, Nacerddine K, Dejean A: Human papillomavirus oncoprotein E7 targets the promyelocytic leukemia protein and circumvents cellular senescence via the Rb and p53 tumor suppressor pathways. Mol. Cell Blol. 25, 1013-1024 (2005).
    • (2005) Mol. Cell Blol , vol.25 , pp. 1013-1024
    • Bischof, O.1    Nacerddine, K.2    Dejean, A.3
  • 114
    • 0036061103 scopus 로고    scopus 로고
    • Reorganization of nuclear domain 10 induced by papillornavirus capsid protein 12
    • Florin L, Schafer F, Sotlar K, Streack RE, Sapp M: Reorganization of nuclear domain 10 induced by papillornavirus capsid protein 12. Virology 295, 97-107 (2002).
    • (2002) Virology , vol.295 , pp. 97-107
    • Florin, L.1    Schafer, F.2    Sotlar, K.3    Streack, R.E.4    Sapp, M.5
  • 115
    • 0035796503 scopus 로고    scopus 로고
    • PML mediates the interferon-induced anti viral 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: PML mediates the interferon-induced anti viral state against a complex retrovirus via its association with the viral transactivator. EMBO J. 20, 3495- 3505 (2001).
    • (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
  • 116
    • 16244383862 scopus 로고    scopus 로고
    • ne 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: ne cellular protein Daxx interacts with avian sarcoma virus Integrase and viral DNA to repress viral transcription. J. Virol. 79, 4610-4618 (2005).
    • (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
  • 117
    • 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 et al.: Identification of cellular proteins that maintain retroviral epigenetic silencing: evidence for an antiviral response. J. Virol. 82(5), 2313-2323 (2007).
    • (2007) J. Virol , vol.82 , Issue.5 , pp. 2313-2323
    • Poleshko, A.1    Palagin, I.2    Zhang, R.3
  • 118
    • 0031907092 scopus 로고    scopus 로고
    • Chelbi-Anx MK, Quignon F, Pelicano L, Koken MH, de The H: Resistance to virus infection conferred by the interferoninduced promyelocytic leukemia protein. J Virol. 72. 1043-1051 (1998).
    • Chelbi-Anx MK, Quignon F, Pelicano L, Koken MH, de The H: Resistance to virus infection conferred by the interferoninduced promyelocytic leukemia protein. J Virol. 72. 1043-1051 (1998).
  • 119
    • 0034022194 scopus 로고    scopus 로고
    • Hepatitis delta virus replication generates complexes of large hepatitis delta antigen and antigenomic RNA that affiliate with and alter nuclear domain 10
    • Bell P, Brazas R, Ganem D, Maul GG: Hepatitis delta virus replication generates complexes of large hepatitis delta antigen and antigenomic RNA that affiliate with and alter nuclear domain 10. J. Virol. 74, 5329-5336 (2000).
    • (2000) J. Virol , vol.74 , pp. 5329-5336
    • Bell, P.1    Brazas, R.2    Ganem, D.3    Maul, G.G.4
  • 120
    • 6344262160 scopus 로고    scopus 로고
    • Nuclear heat shock response and novel nuclear domain 10 reorganization in respiratory syncytial virus-infected a549 cells identified by high-resolution two-dimensional gel electrophoresis
    • Brasier AR, Spratt H, Wu Z et al.: Nuclear heat shock response and novel nuclear domain 10 reorganization in respiratory syncytial virus-infected a549 cells identified by high-resolution two-dimensional gel electrophoresis. J. Virol. 78, 11461-11476 (2004).
    • (2004) J. Virol , vol.78 , pp. 11461-11476
    • Brasier, A.R.1    Spratt, H.2    Wu, Z.3
  • 121
    • 0036208403 scopus 로고    scopus 로고
    • Hantavirus nucleocapsid protein interacts with the Fas-mediated apbptosis enhancer Daxx
    • Li XD, Makela TP, Guo D et al.: Hantavirus nucleocapsid protein interacts with the Fas-mediated apbptosis enhancer Daxx. J Gen. Virol. 83. 759-766 (2002).
    • (2002) J Gen. Virol , vol.83 , pp. 759-766
    • Li, X.D.1    Makela, T.P.2    Guo, D.3
  • 122
    • 34548290826 scopus 로고    scopus 로고
    • Sensitization to Fas-mediated apoptosis by dengue virus capsid protein
    • Limjindaporn T. Netsawang J, Noisakran S et al.: Sensitization to Fas-mediated apoptosis by dengue virus capsid protein. Biochem. Biophys. Res. Commun. 362, 334-339 (2007).
    • (2007) Biochem. Biophys. Res. Commun , vol.362 , pp. 334-339
    • Limjindaporn, T.1    Netsawang, J.2    Noisakran, S.3
  • 123
    • 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: Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells. Cancer Res. 65, 10830-10837 (2005).
    • (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
  • 124
    • 33845632023 scopus 로고    scopus 로고
    • Daxx interacts with phage Ph1C31 integrase and inhibits recombination
    • Chen JZ, Ji CN, Xu GL et al.: Daxx interacts with phage Ph1C31 integrase and inhibits recombination. Nucleic Acids Res. 34, 6298-6304 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 6298-6304
    • Chen, J.Z.1    Ji, C.N.2    Xu, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.