메뉴 건너뛰기




Volumn 1, Issue 3, 2009, Pages 1240-1264

Interplay between herpesvirus infection and host defense by PML nuclear bodies

Author keywords

Antiviral defense; HDaxx; Herpesvirus; Interferon; Intrinsic immunity; Nuclear domain 10; PML; PML nuclear bodies; Sp100

Indexed keywords


EID: 79955047081     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v1031240     Document Type: Review
Times cited : (70)

References (156)
  • 1
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: A front-line defense against viral attack
    • Bieniasz, P.D. Intrinsic immunity: a front-line defense against viral attack. Nat. Immunol. 2004, 5, 1109-1115.
    • (2004) Nat. Immunol. , vol.5 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 2
    • 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, G.G. Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 2001, 20, 7234-7242.
    • (2001) Oncogene , vol.20 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 4
    • 0026019835 scopus 로고
    • Identification of a novel nuclear domain
    • Ascoli, C.A.; Maul, G.G. Identification of a novel nuclear domain. J. Cell Biol. 1991, 112, 785-795.
    • (1991) J. Cell Biol. , vol.112 , pp. 785-795
    • Ascoli, C.A.1    Maul, G.G.2
  • 5
    • 33644821166 scopus 로고    scopus 로고
    • Interactions between DNA viruses, ND10 and the DNA damage response
    • Everett, R.D. Interactions between DNA viruses, ND10 and the DNA damage response. Cell Microbiol. 2006, 8, 365-374.
    • (2006) Cell Microbiol. , vol.8 , pp. 365-374
    • Everett, R.D.1
  • 6
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • Dellaire, G.; Bazett-Jones, D.P. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 2004, 26, 963-977.
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 7
    • 34548288605 scopus 로고    scopus 로고
    • Beyond repair foci: Subnuclear domains and the cellular response to DNA damage
    • Dellaire, G.; Bazett-Jones, D.P. Beyond repair foci: subnuclear domains and the cellular response to DNA damage. Cell Cycle 2007, 6, 1864-1872.
    • (2007) Cell Cycle , vol.6 , pp. 1864-1872
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 9
    • 35848956344 scopus 로고    scopus 로고
    • Aggresomes and pericentriolar sites of virus assembly: Cellular defense or viral design?
    • Wileman, T. Aggresomes and pericentriolar sites of virus assembly: cellular defense or viral design? Annu. Rev. Microbiol. 2007, 61, 149-167.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 149-167
    • Wileman, T.1
  • 11
    • 0025633966 scopus 로고
    • Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis
    • Szostecki, C.; Guldner, H.H.; Netter, H.J.; Will, H. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J. Immunol. 1990, 145, 4338-4347.
    • (1990) J. Immunol. , vol.145 , pp. 4338-4347
    • Szostecki, C.1    Guldner, H.H.2    Netter, H.J.3    Will, H.4
  • 14
    • 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, R.D.; 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 ICP0. J. Virol. 2006, 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
  • 15
    • 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. 2006, 80, 8006-8018.
    • (2006) J. Virol. , vol.80 , pp. 8006-8018
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Leis, M.4    Stamminger, T.5
  • 16
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML
    • Kakizuka, A.; Miller, W.H., Jr.; Umesono, K.; Warrell, R.P., Jr.; Frankel, S.R.; Murty, V.V.; Dmitrovsky, E.; Evans, R.M. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 1991, 66, 663-674.
    • (1991) Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1    Miller Jr., W.H.2    Umesono, K.3    Warrell Jr., R.P.4    Frankel, S.R.5    Murty, V.V.6    Dmitrovsky, E.7    Evans, R.M.8
  • 17
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen, K.; Shiels, C.; Freemont, P.S. PML protein isoforms and the RBCC/TRIM motif. Oncogene 2001, 20, 7223-7233.
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 18
    • 0030027449 scopus 로고    scopus 로고
    • Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML
    • Le, X.F.; Yang, P.; Chang, K.S. Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML. J. Biol. Chem. 1996, 271, 130-135.
    • (1996) J. Biol. Chem. , vol.271 , pp. 130-135
    • Le, X.F.1    Yang, P.2    Chang, K.S.3
  • 20
    • 48449083440 scopus 로고    scopus 로고
    • A role for cytoplasmic PML in cellular resistance to viral infection
    • McNally, B.A.; Trgovcich, J.; Maul, G.G.; Liu, Y.; Zheng, P. A role for cytoplasmic PML in cellular resistance to viral infection. PLoS ONE. 2008, 3, e2277.
    • (2008) PLoS ONE. , vol.3
    • McNally, B.A.1    Trgovcich, J.2    Maul, G.G.3    Liu, Y.4    Zheng, P.5
  • 21
    • 0033380850 scopus 로고    scopus 로고
    • Cell cycle regulation of PML modification and ND10 composition
    • Everett, R.D.; Lomonte, P.; Sternsdorf, T.; van, D.R.; Orr, A. Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 1999, 112, 4581-4588.
    • (1999) J. Cell Sci. , vol.112 , pp. 4581-4588
    • Everett, R.D.1    Lomonte, P.2    Sternsdorf, T.3    van, D.R.4    Orr, A.5
  • 22
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani, T.; Nguyen, H.P.; Kito, K.; Fukuda-Kamitani, T.; Yeh, E.T. Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 1998, 273, 3117-3120.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 23
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller, S.; Matunis, M.J.; Dejean, A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 1998, 17, 61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 26
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors
    • Lin, D.Y.; Huang, Y.S.; Jeng, J.C.; Kuo, H.Y.; Chang, C.C.; Chao, T.T.; Ho, C.C.; Chen, Y.C.; Lin, T.P.; Fang, H.I. Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 2006, 24, 341-354.
    • (2006) Mol. Cell , vol.24 , pp. 341-354
    • Lin, D.Y.1    Huang, Y.S.2    Jeng, J.C.3    Kuo, H.Y.4    Chang, C.C.5    Chao, T.T.6    Ho, C.C.7    Chen, Y.C.8    Lin, T.P.9    Fang, H.I.10
  • 27
    • 0033168203 scopus 로고    scopus 로고
    • The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx
    • Hollenbach, A.D.; Sublett, J.E.; McPherson, C.J.; Grosveld, G. The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx. EMBO J. 1999, 18, 3702-3711.
    • (1999) EMBO J. , vol.18 , pp. 3702-3711
    • Hollenbach, A.D.1    Sublett, J.E.2    McPherson, C.J.3    Grosveld, G.4
  • 28
    • 0031440480 scopus 로고    scopus 로고
    • Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region
    • Kiriakidou, M.; Driscoll, D.A.; Lopez-Guisa, J.M.; Strauss, J.F., III Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region. DNA Cell Biol. 1997, 16, 1289-1298.
    • (1997) DNA Cell Biol. , vol.16 , pp. 1289-1298
    • Kiriakidou, M.1    Driscoll, D.A.2    Lopez-Guisa, J.M.3    Strauss III, J.F.4
  • 29
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • Li, H.; Leo, C.; Zhu, J.; Wu, X.; O'Neil, J.; Park, E.J.; Chen, J.D. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell Biol. 2000, 20, 1784-1796.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3    Wu, X.4    O'Neil, J.5    Park, E.J.6    Chen, J.D.7
  • 30
    • 0031847605 scopus 로고    scopus 로고
    • Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fasmediated cell death
    • Pluta, A.F.; Earnshaw, W.C.; Goldberg, I.G. Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fasmediated cell death. J. Cell Sci. 1998, 111, 2029-2041.
    • (1998) J. Cell Sci. , vol.111 , pp. 2029-2041
    • Pluta, A.F.1    Earnshaw, W.C.2    Goldberg, I.G.3
  • 31
    • 32644487258 scopus 로고    scopus 로고
    • Daxx: Death or survival protein?
    • Salomoni, P.; Khelifi, A.F. Daxx: death or survival protein? Trends Cell Biol. 2006, 16, 97-104.
    • (2006) Trends Cell Biol. , vol.16 , pp. 97-104
    • Salomoni, P.1    Khelifi, A.F.2
  • 32
    • 0034628443 scopus 로고    scopus 로고
    • EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes
    • Li, R.; Pei, H.; Watson, D.K.; Papas, T.S. EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes. Oncogene 2000, 19, 745-753.
    • (2000) Oncogene , vol.19 , pp. 745-753
    • Li, R.1    Pei, H.2    Watson, D.K.3    Papas, T.S.4
  • 34
    • 0037439945 scopus 로고    scopus 로고
    • RNAi reveals anti-apoptotic and transcriptionally repressive activities of DAXX
    • Michaelson, J.S.; Leder, P. RNAi reveals anti-apoptotic and transcriptionally repressive activities of DAXX. J. Cell Sci. 2003, 116, 345-352.
    • (2003) J. Cell Sci. , vol.116 , pp. 345-352
    • Michaelson, J.S.1    Leder, P.2
  • 35
    • 15444380557 scopus 로고    scopus 로고
    • Daxx mediates the small ubiquitinlike modifier-dependent transcriptional repression of Smad4
    • Chang, C.C.; Lin, D.Y.; Fang, H.I.; Chen, R.H.; Shih, H.M. Daxx mediates the small ubiquitinlike modifier-dependent transcriptional repression of Smad4. J. Biol. Chem. 2005, 280, 10164-10173.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10164-10173
    • Chang, C.C.1    Lin, D.Y.2    Fang, H.I.3    Chen, R.H.4    Shih, H.M.5
  • 36
    • 0345570517 scopus 로고    scopus 로고
    • Identification of Daxx interacting with p73, one of the p53 family, and its regulation of p53 activity by competitive interaction with PML
    • Kim, E.J.; Park, J.S.; Um, S.J. Identification of Daxx interacting with p73, one of the p53 family, and its regulation of p53 activity by competitive interaction with PML. Nucleic Acids Res. 2003, 31, 5356-5367.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5356-5367
    • Kim, E.J.1    Park, J.S.2    Um, S.J.3
  • 38
    • 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, A.D.; McPherson, C.J.; Mientjes, E.J.; Iyengar, R.; Grosveld, G. Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J. Cell Sci. 2002, 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
  • 40
    • 4444317361 scopus 로고    scopus 로고
    • Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX
    • Ishov, A.M.; Vladimirova, O.V.; Maul, G.G. Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J. Cell Sci. 2004, 117, 3807-3820.
    • (2004) J. Cell Sci. , vol.117 , pp. 3807-3820
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 41
    • 0141703327 scopus 로고    scopus 로고
    • The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies
    • Xue, Y.; Gibbons, R.; Yan, Z.; Yang, D.; McDowell, T.L.; Sechi, S.; Qin, J.; Zhou, S.; Higgs, D.; Wang, W. The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies. Proc. Natl. Acad. Sci. USA 2003, 100, 10635-10640.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10635-10640
    • Xue, Y.1    Gibbons, R.2    Yan, Z.3    Yang, D.4    McDowell, T.L.5    Sechi, S.6    Qin, J.7    Zhou, S.8    Higgs, D.9    Wang, W.10
  • 42
    • 0037067668 scopus 로고    scopus 로고
    • Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration
    • Lin, D.Y.; Shih, H.M. Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration. J. Biol. Chem. 2002, 277, 25446-25456.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25446-25456
    • Lin, D.Y.1    Shih, H.M.2
  • 43
    • 0029845262 scopus 로고    scopus 로고
    • LYSP100-associated nuclear domains (LANDs): Description of a new class of subnuclear structures and their relationship to PML nuclear bodies
    • Dent, A.L.; Yewdell, J.; Puvion-Dutilleul, F.; Koken, M.H.; de Thé, H.; Staudt, L.M. LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies. Blood 1996, 88, 1423-1426.
    • (1996) Blood , vol.88 , pp. 1423-1426
    • Dent, A.L.1    Yewdell, J.2    Puvion-Dutilleul, F.3    Koken, M.H.4    de Thé, H.5    Staudt, L.M.6
  • 44
    • 0035028618 scopus 로고    scopus 로고
    • Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: Role of SUMO modification
    • Seeler, J.S.; Marchio, A.; Losson, R.; Desterro, J.M.; Hay, R.T.; Chambon, P.; Dejean, A. Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification. Mol. Cell Biol. 2001, 21, 3314-3324.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3314-3324
    • Seeler, J.S.1    Marchio, A.2    Losson, R.3    Desterro, J.M.4    Hay, R.T.5    Chambon, P.6    Dejean, A.7
  • 45
    • 0032560477 scopus 로고    scopus 로고
    • Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment
    • Seeler, J.S.; Marchio, A.; Sitterlin, D.; Transy, C.; Dejean, A. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc. Natl. Acad. Sci. USA 1998, 95, 7316-7321.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7316-7321
    • Seeler, J.S.1    Marchio, A.2    Sitterlin, D.3    Transy, C.4    Dejean, A.5
  • 46
    • 0032999287 scopus 로고    scopus 로고
    • Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif
    • Guldner, H.H.; Szostecki, C.; Schroder, P.; Matschl, U.; Jensen, K.; Luders, C.; Will, H.; Sternsdorf, T. Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif. J. Cell Sci. 1999, 112, 733-747.
    • (1999) J. Cell Sci. , vol.112 , pp. 733-747
    • Guldner, H.H.1    Szostecki, C.2    Schroder, P.3    Matschl, U.4    Jensen, K.5    Luders, C.6    Will, H.7    Sternsdorf, T.8
  • 49
    • 33746406755 scopus 로고    scopus 로고
    • SP100B, a repressor of gene expression preferentially binds to DNA with unmethylated CpGs
    • Isaac, A.; Wilcox, K.W.; Taylor, J.L. SP100B, a repressor of gene expression preferentially binds to DNA with unmethylated CpGs. J. Cell Biochem. 2006, 98, 1106-1122.
    • (2006) J. Cell Biochem. , vol.98 , pp. 1106-1122
    • Isaac, A.1    Wilcox, K.W.2    Taylor, J.L.3
  • 50
    • 0036066181 scopus 로고    scopus 로고
    • Modification of Daxx by small ubiquitin-related modifier-1
    • Jang, M.S.; Ryu, S.W.; Kim, E. Modification of Daxx by small ubiquitin-related modifier-1. Biochem. Biophys. Res. Commun. 2002, 295, 495-500.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 495-500
    • Jang, M.S.1    Ryu, S.W.2    Kim, E.3
  • 51
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • Sternsdorf, T.; Jensen, K.; Will, H. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol. 1997, 139, 1621-1634.
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 52
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf, T.; Jensen, K.; Reich, B.; Will, H. The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 1999, 274, 12555-12566.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 53
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni, P.; Pandolfi, P.P. The role of PML in tumor suppression. Cell 2002, 108, 165-170.
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 55
    • 1642512435 scopus 로고    scopus 로고
    • Role of PML and the PML-nuclear body in the control of programmed cell death
    • Bernardi, R.; Pandolfi, P.P. Role of PML and the PML-nuclear body in the control of programmed cell death. Oncogene 2003, 22, 9048-9057.
    • (2003) Oncogene , vol.22 , pp. 9048-9057
    • Bernardi, R.1    Pandolfi, P.P.2
  • 56
    • 0029583591 scopus 로고
    • Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress
    • Maul, G.G.; Yu, E.; Ishov, A.M.; Epstein, A.L. Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress. J. Cell Biochem. 1995, 59, 498-513.
    • (1995) J. Cell Biochem. , vol.59 , pp. 498-513
    • Maul, G.G.1    Yu, E.2    Ishov, A.M.3    Epstein, A.L.4
  • 58
    • 0035908032 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation
    • Lallemand-Breitenbach, V.; Zhu, J.; Puvion, F.; Koken, M.; Honore, N.; Doubeikovsky, A.; Duprez, E.; Pandolfi, P.P.; Puvion, E.; Freemont, P. et al. Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation. J. Exp. Med. 2001, 193, 1361-1371.
    • (2001) J. Exp. Med. , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3    Koken, M.4    Honore, N.5    Doubeikovsky, A.6    Duprez, E.7    Pandolfi, P.P.8    Puvion, E.9    Freemont, P.10
  • 59
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S.; Salomoni, P.; Pandolfi, P.P. The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2000, 2, E85-E90.
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 60
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies
    • Borden, K.L. Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol. Cell Biol. 2002, 22, 5259-5269.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 61
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi, R.; Pandolfi, P.P. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 2007, 8, 1006-1016.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 62
    • 0035986065 scopus 로고    scopus 로고
    • The promyelocytic leukemia nuclear body: Sites of activity?
    • Eskiw, C.H.; Bazett-Jones, D.P. The promyelocytic leukemia nuclear body: sites of activity? Biochem. Cell Biol. 2002, 80, 301-310.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 301-310
    • Eskiw, C.H.1    Bazett-Jones, D.P.2
  • 63
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert, F.M.; Hendzel, M.J.; Bazett-Jones, D.P. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 2000, 148, 283-292.
    • (2000) J. Cell Biol. , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 64
    • 37749036302 scopus 로고    scopus 로고
    • Daxx mediates SUMO-dependent transcriptional control and subnuclear compartmentalization
    • Shih, H.M.; Chang, C.C.; Kuo, H.Y.; Lin, D.Y. Daxx mediates SUMO-dependent transcriptional control and subnuclear compartmentalization. Biochem. Soc. Trans. 2007, 35, 1397-1400.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1397-1400
    • Shih, H.M.1    Chang, C.C.2    Kuo, H.Y.3    Lin, D.Y.4
  • 65
    • 0035099686 scopus 로고    scopus 로고
    • The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases
    • Wu, W.S.; Vallian, S.; Seto, E.; Yang, W.M.; Edmondson, D.; Roth, S.; Chang, K.S. The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol. Cell Biol. 2001, 21, 2259-2268.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 2259-2268
    • Wu, W.S.1    Vallian, S.2    Seto, E.3    Yang, W.M.4    Edmondson, D.5    Roth, S.6    Chang, K.S.7
  • 66
    • 42149185026 scopus 로고    scopus 로고
    • Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation
    • Puto, L.A.; Reed, J.C. Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation. Genes Dev. 2008, 22, 998-1010.
    • (2008) Genes Dev. , vol.22 , pp. 998-1010
    • Puto, L.A.1    Reed, J.C.2
  • 69
    • 33644908213 scopus 로고    scopus 로고
    • PML-associated repressor of transcription (PAROT), a novel KRAB-zinc finger repressor, is regulated through association with PML nuclear bodies
    • Fleischer, S.; Wiemann, S.; Will, H.; Hofmann, T.G. PML-associated repressor of transcription (PAROT), a novel KRAB-zinc finger repressor, is regulated through association with PML nuclear bodies. Exp. Cell Res. 2006, 312, 901-912.
    • (2006) Exp. Cell Res. , vol.312 , pp. 901-912
    • Fleischer, S.1    Wiemann, S.2    Will, H.3    Hofmann, T.G.4
  • 70
    • 32044437861 scopus 로고    scopus 로고
    • Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein
    • Carbone, R.; Botrugno, O.A.; Ronzoni, S.; Insinga, A.; Di Croce, L.; Pelicci, P.G.; Minucci, S. Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein. Mol. Cell Biol. 2006, 26, 1288-1296.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 1288-1296
    • Carbone, R.1    Botrugno, O.A.2    Ronzoni, S.3    Insinga, A.4    Di Croce, L.5    Pelicci, P.G.6    Minucci, S.7
  • 72
    • 0035809924 scopus 로고    scopus 로고
    • The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body
    • Boisvert, F.M.; Kruhlak, M.J.; Box, A.K.; Hendzel, M.J.; Bazett-Jones, D.P. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J. Cell Biol. 2001, 152, 1099-1106.
    • (2001) J. Cell Biol. , vol.152 , pp. 1099-1106
    • Boisvert, F.M.1    Kruhlak, M.J.2    Box, A.K.3    Hendzel, M.J.4    Bazett-Jones, D.P.5
  • 73
    • 0032574737 scopus 로고    scopus 로고
    • Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body
    • LaMorte, V.J.; Dyck, J.A.; Ochs, R.L.; Evans, R.M. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc. Natl. Acad. Sci. USA 1998, 95, 4991-4996.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4991-4996
    • LaMorte, V.J.1    Dyck, J.A.2    Ochs, R.L.3    Evans, R.M.4
  • 74
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett, R.D. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 2001, 20, 7266-7273.
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 76
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul, G.G. Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 1998, 20, 660-667.
    • (1998) Bioessays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 77
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • Regad, T.; Chelbi-Alix, M.K. Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 2001, 20, 7274-7286.
    • (2001) Oncogene , vol.20 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 78
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • Everett, R.D.; Chelbi-Alix, M.K. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 2007, 89, 819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 80
    • 0027095906 scopus 로고
    • IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis
    • Guldner, H.H.; Szostecki, C.; Grotzinger, T.; Will, H. IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J. Immunol. 1992, 149, 4067-4073.
    • (1992) J. Immunol. , vol.149 , pp. 4067-4073
    • Guldner, H.H.1    Szostecki, C.2    Grotzinger, T.3    Will, H.4
  • 82
    • 0029816576 scopus 로고    scopus 로고
    • The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-gamma activation site and an imperfect IFN-stimulated response element which mediate type I IFN inducibility
    • Grotzinger, T.; Jensen, K.; Will, H. The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN-gamma activation site and an imperfect IFN-stimulated response element which mediate type I IFN inducibility. J. Biol. Chem. 1996, 271, 25253-25260.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25253-25260
    • Grotzinger, T.1    Jensen, K.2    Will, H.3
  • 83
    • 37049011429 scopus 로고    scopus 로고
    • Direct transcriptional activation of promyelocytic leukemia protein by IFN regulatory factor 3 induces the p53-dependent growth inhibition of cancer cells
    • Kim, T.K.; Lee, J.S.; Oh, S.Y.; Jin, X.; Choi, Y.J.; Lee, T.H.; Lee, E.; Choi, Y.K.; You, S.; Chung, Y.G. Direct transcriptional activation of promyelocytic leukemia protein by IFN regulatory factor 3 induces the p53-dependent growth inhibition of cancer cells. Cancer Res. 2007, 67, 11133-11140.
    • (2007) Cancer Res. , vol.67 , pp. 11133-11140
    • Kim, T.K.1    Lee, J.S.2    Oh, S.Y.3    Jin, X.4    Choi, Y.J.5    Lee, T.H.6    Lee, E.7    Choi, Y.K.8    You, S.9    Chung, Y.G.10
  • 84
    • 0029894340 scopus 로고    scopus 로고
    • Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML)
    • Grotzinger, T.; Sternsdorf, T.; Jensen, K.; Will, H. Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML). Eur. J. Biochem. 1996, 238, 554-560.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 554-560
    • Grotzinger, T.1    Sternsdorf, T.2    Jensen, K.3    Will, H.4
  • 85
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0)
    • Maul, G.G.; Guldner, H.H.; Spivack, J.G. Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J. Gen. Virol. 1993, 74, 2679-2690.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 86
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov, A.M.; Maul, G.G. The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J. Cell Biol. 1996, 134, 815-826.
    • (1996) J. Cell Biol. , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 87
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1
    • Maul, G.G.; Ishov, A.M.; Everett, R.D. Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology 1996, 217, 67-75.
    • (1996) Virology , vol.217 , pp. 67-75
    • Maul, G.G.1    Ishov, A.M.2    Everett, R.D.3
  • 88
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett, R.D.; Maul, G.G. HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 1994, 13, 5062-5069.
    • (1994) EMBO J. , vol.13 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 89
    • 0028352769 scopus 로고
    • The nuclear location of PML, a cellular member of the C3HC4 zincbinding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0
    • Maul, G.G.; Everett, R.D. The nuclear location of PML, a cellular member of the C3HC4 zincbinding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J. Gen. Virol. 1994, 75, 1223-1233.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 90
    • 0033624137 scopus 로고    scopus 로고
    • ICP0, a regulator of herpes simplex virus during lytic and latent infection
    • Everett, R.D. ICP0, a regulator of herpes simplex virus during lytic and latent infection. Bioessays 2000, 22, 761-770.
    • (2000) Bioessays , vol.22 , pp. 761-770
    • Everett, R.D.1
  • 91
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix, M.K.; de Thé, H. Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 1999, 18, 935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    de Thé, H.2
  • 92
    • 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, R.D.; Freemont, P.; Saitoh, H.; Dasso, M.; Orr, A.; Kathoria, M.; Parkinson, J. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110-and proteasome-dependent loss of several PML isoforms. J. Virol. 1998, 72, 6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 93
    • 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. 1999, 73, 5137-5143.
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 94
    • 0033779805 scopus 로고    scopus 로고
    • Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins
    • Parkinson, J.; Everett, R.D. Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J. Virol. 2000, 74, 10006-10017.
    • (2000) J. Virol. , vol.74 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 95
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell, C.; Sadis, S.; Everett, R.D. Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 2002, 76, 841-850.
    • (2002) J. Virol. , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 96
    • 0042808481 scopus 로고    scopus 로고
    • The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a
    • Gu, H.; Roizman, B. The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a. Proc. Natl. Acad. Sci. USA 2003, 100, 8963-8968.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8963-8968
    • Gu, H.1    Roizman, B.2
  • 97
    • 0036057893 scopus 로고    scopus 로고
    • The immediate-early protein, ICP0, is essential for the resistance of herpes simplex virus to interferon-alpha/beta
    • Harle, P.; Sainz, B., Jr.; Carr, D.J.; Halford, W.P. The immediate-early protein, ICP0, is essential for the resistance of herpes simplex virus to interferon-alpha/beta. Virology 2002, 293, 295-304.
    • (2002) Virology , vol.293 , pp. 295-304
    • Harle, P.1    Sainz Jr., B.2    Carr, D.J.3    Halford, W.P.4
  • 98
    • 0033935685 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 mutants are hypersensitive to interferon
    • Mossman, K.L.; Saffran, H.A.; Smiley, J.R. Herpes simplex virus ICP0 mutants are hypersensitive to interferon. J. Virol. 2000, 74, 2052-2056.
    • (2000) J. Virol. , vol.74 , pp. 2052-2056
    • Mossman, K.L.1    Saffran, H.A.2    Smiley, J.R.3
  • 100
    • 0037941647 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects
    • Chee, A.V.; Lopez, P.; Pandolfi, P.P.; Roizman, B. Promyelocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects. J. Virol. 2003, 77, 7101-7105.
    • (2003) J. Virol. , vol.77 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 101
    • 4644274478 scopus 로고    scopus 로고
    • Visualization by live-cell microscopy of disruption of ND10 during herpes simplex virus type 1 infection
    • Everett, R.D.; Zafiropoulos, A. Visualization by live-cell microscopy of disruption of ND10 during herpes simplex virus type 1 infection. J. Virol. 2004, 78, 11411-11415.
    • (2004) J. Virol. , vol.78 , pp. 11411-11415
    • Everett, R.D.1    Zafiropoulos, A.2
  • 102
    • 0036720433 scopus 로고    scopus 로고
    • Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins
    • Lopez, P.; Jacob, R.J.; Roizman, B. Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins. J. Virol. 2002, 76, 9355-9367.
    • (2002) J. Virol. , vol.76 , pp. 9355-9367
    • Lopez, P.1    Jacob, R.J.2    Roizman, B.3
  • 103
    • 54549109086 scopus 로고    scopus 로고
    • Replication of ICP0 null mutant herpes simplex virus type 1 is restricted by both PML and Sp100
    • Everett, R.D.; 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. 2007.
    • (2007) J. Virol.
    • Everett, R.D.1    Parada, C.2    Gripon, P.3    Sirma, H.4    Orr, A.5
  • 104
    • 65349103506 scopus 로고    scopus 로고
    • Differential functions of interferon-upregulated Sp100 isoforms: Herpes simplex virus type 1 promoter-based immediate-early gene suppression and PML protection from ICP0-mediated degradation
    • Negorev, D.G.; Vladimirova, O.V.; Maul, G.G. Differential functions of interferon-upregulated Sp100 isoforms: herpes simplex virus type 1 promoter-based immediate-early gene suppression and PML protection from ICP0-mediated degradation. J. Virol. 2009, 83, 5168-5180.
    • (2009) J. Virol. , vol.83 , pp. 5168-5180
    • Negorev, D.G.1    Vladimirova, O.V.2    Maul, G.G.3
  • 105
    • 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, D.G.; Vladimirova, O.V.; Ivanov, A.; Rauscher, F., III; Maul, G.G. Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression. J. Virol. 2006, 80, 8019-8029.
    • (2006) J. Virol. , vol.80 , pp. 8019-8029
    • Negorev, D.G.1    Vladimirova, O.V.2    Ivanov, A.3    Rauscher III, F.4    Maul, G.G.5
  • 106
    • 0030055588 scopus 로고    scopus 로고
    • Varicella-zoster virus
    • Arvin, A.M. Varicella-zoster virus. Clin. Microbiol. Rev. 1996, 9, 361-381.
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 361-381
    • Arvin, A.M.1
  • 107
    • 66149128368 scopus 로고    scopus 로고
    • Components of nuclear domain 10 bodies regulate varicellazoster virus replication
    • Kyratsous, C.A.; Silverstein, S.J. Components of nuclear domain 10 bodies regulate varicellazoster virus replication. J. Virol. 2009, 83, 4262-4274.
    • (2009) J. Virol. , vol.83 , pp. 4262-4274
    • Kyratsous, C.A.1    Silverstein, S.J.2
  • 108
    • 0026472080 scopus 로고
    • Varicella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP0
    • Moriuchi, H.; Moriuchi, M.; Smith, H.A.; Straus, S.E.; Cohen, J.I. Varicella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP0. J. Virol. 1992, 66, 7303-7308.
    • (1992) J. Virol. , vol.66 , pp. 7303-7308
    • Moriuchi, H.1    Moriuchi, M.2    Smith, H.A.3    Straus, S.E.4    Cohen, J.I.5
  • 109
    • 0027232936 scopus 로고
    • Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA
    • Moriuchi, H.; Moriuchi, M.; Straus, S.E.; Cohen, J.I. Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA. J. Virol. 1993, 67, 4290-4295.
    • (1993) J. Virol. , vol.67 , pp. 4290-4295
    • Moriuchi, H.1    Moriuchi, M.2    Straus, S.E.3    Cohen, J.I.4
  • 110
    • 70349756954 scopus 로고    scopus 로고
    • Complementation of a Herpes Simplex Virus ICP0 null mutant by Varicella Zoster Virus ORF61p
    • Kyratsous, C.A.; Walters, M.S.; Panagiotidis, C.A.; Silverstein, S.J. Complementation of a Herpes Simplex Virus ICP0 null mutant by Varicella Zoster Virus ORF61p. J. Virol. 2009, 83, 10637-10643.
    • (2009) J. Virol. , vol.83 , pp. 10637-10643
    • Kyratsous, C.A.1    Walters, M.S.2    Panagiotidis, C.A.3    Silverstein, S.J.4
  • 112
    • 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, J.H.; Hayward, G.S. 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. 1997, 71, 4599-4613.
    • (1997) J. Virol. , vol.71 , pp. 4599-4613
    • Ahn, J.H.1    Hayward, G.S.2
  • 113
    • 0030840687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate early interaction with host nuclear structures: Definition of an immediate transcript environment
    • Ishov, A.M.; Stenberg, R.M.; Maul, G.G. Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J. Cell Biol. 1997, 138, 5-16.
    • (1997) J. Cell Biol. , vol.138 , pp. 5-16
    • Ishov, A.M.1    Stenberg, R.M.2    Maul, G.G.3
  • 114
    • 0031922713 scopus 로고    scopus 로고
    • Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product
    • Wilkinson, G.W.; Kelly, C.; Sinclair, J.H.; Rickards, C. Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product. J. Gen. Virol. 1998, 79, 1233-1245.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1233-1245
    • Wilkinson, G.W.1    Kelly, C.2    Sinclair, J.H.3    Rickards, C.4
  • 115
    • 0030602019 scopus 로고    scopus 로고
    • The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1
    • Korioth, F.; Maul, G.G.; Plachter, B.; Stamminger, T.; Frey, J. The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1. Exp. Cell Res. 1996, 229, 155-158.
    • (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
  • 116
    • 0031877790 scopus 로고    scopus 로고
    • Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PML
    • Ahn, J.H.; Brignole, E.J., III; Hayward, G.S. Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PML. Mol. Cell Biol. 1998, 18, 4899-4913.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4899-4913
    • Ahn, J.H.1    Brignole III, E.J.2    Hayward, G.S.3
  • 117
    • 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, H.R.; Kim, D.J.; Lee, J.M.; Choi, C.Y.; Ahn, B.Y.; Hayward, G.S.; Ahn, J.H. 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. 2004, 78, 6527-6542.
    • (2004) J. Virol. , vol.78 , pp. 6527-6542
    • Lee, H.R.1    Kim, D.J.2    Lee, J.M.3    Choi, C.Y.4    Ahn, B.Y.5    Hayward, G.S.6    Ahn, J.H.7
  • 118
    • 0034755352 scopus 로고    scopus 로고
    • Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression
    • Xu, Y.; Ahn, J.H.; Cheng, M.; apRhys, C.M.; Chiou, C.J.; Zong, J.; Matunis, M.J.; Hayward, G.S. Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression. J. Virol. 2001, 75, 10683-10695.
    • (2001) J. Virol. , vol.75 , pp. 10683-10695
    • Xu, Y.1    Ahn, J.H.2    Cheng, M.3    apRhys, C.M.4    Chiou, C.J.5    Zong, J.6    Matunis, M.J.7    Hayward, G.S.8
  • 119
    • 33746824547 scopus 로고    scopus 로고
    • Inhibition of SUMOindependent PML oligomerization by the human cytomegalovirus IE1 protein
    • Kang, H.; Kim, E.T.; Lee, H.R.; Park, J.J.; Go, Y.Y.; Choi, C.Y.; Ahn, J.H. Inhibition of SUMOindependent PML oligomerization by the human cytomegalovirus IE1 protein. J. Gen. Virol. 2006, 87, 2181-2190.
    • (2006) J. Gen. Virol. , vol.87 , pp. 2181-2190
    • Kang, H.1    Kim, E.T.2    Lee, H.R.3    Park, J.J.4    Go, Y.Y.5    Choi, C.Y.6    Ahn, J.H.7
  • 120
    • 0034663128 scopus 로고    scopus 로고
    • Disruption of PML-associated nuclear bodies by IE1 correlates with efficient early stages of viral gene expression and DNA replication in human cytomegalovirus infection
    • Ahn, J.H.; Hayward, G.S. Disruption of PML-associated nuclear bodies by IE1 correlates with efficient early stages of viral gene expression and DNA replication in human cytomegalovirus infection. Virology 2000, 274, 39-55.
    • (2000) Virology , vol.274 , pp. 39-55
    • Ahn, J.H.1    Hayward, G.S.2
  • 121
    • 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. 2002, 76, 5769-5783.
    • (2002) J. Virol. , vol.76 , pp. 5769-5783
    • Hofmann, H.1    Sindre, H.2    Stamminger, T.3
  • 122
    • 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, A.M.; Vladimirova, O.V.; Maul, G.G. Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains. J. Virol. 2002, 76, 7705-7712.
    • (2002) J. Virol. , vol.76 , pp. 7705-7712
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 124
    • 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, S.R.; Bresnahan, W.A. Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication. J. Virol. 2005, 79, 7792-7802.
    • (2005) J. Virol. , vol.79 , pp. 7792-7802
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 125
    • 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, D.L.; Groves, I.J.; Reeves, M.B.; Wilkinson, G.; Sinclair, J.H. Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter. J. Biol. Chem. 2006, 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
  • 126
    • 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, R.T.; Kalejta, R.F. 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. 2006, 80, 3863-3871.
    • (2006) J. Virol. , vol.80 , pp. 3863-3871
    • Saffert, R.T.1    Kalejta, R.F.2
  • 127
    • 33646161949 scopus 로고    scopus 로고
    • Role of the cellular protein hDaxx in human cytomegalovirus immediate-early gene expression
    • Preston, C.M.; Nicholl, M.J. Role of the cellular protein hDaxx in human cytomegalovirus immediate-early gene expression. J. Gen. Virol. 2006, 87, 1113-1121.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1113-1121
    • Preston, C.M.1    Nicholl, M.J.2
  • 128
    • 33744908280 scopus 로고    scopus 로고
    • Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression of HCMV replication
    • Cantrell, S.R.; Bresnahan, W.A. Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression of HCMV replication. J. Virol. 2006, 80, 6188-6191.
    • (2006) J. Virol. , vol.80 , pp. 6188-6191
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 129
    • 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. 2008, 82, 126-137.
    • (2008) J. Virol. , vol.82 , pp. 126-137
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Stamminger, T.4
  • 130
    • 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, R.F. Proteasome-dependent, ubiquitin-independent degradation of Daxx by the viral pp71 protein in human cytomegalovirus-infected cells. Virology 2007, 367, 334-338.
    • (2007) Virology , vol.367 , pp. 334-338
    • Hwang, J.1    Kalejta, R.F.2
  • 131
    • 39649097641 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 blocks viral DNA replication and assembly of human cytomegalovirus
    • Kaspari, M.; Tavalai, N.; Stamminger, T.; Zimmermann, A.; Schilf, R.; Bogner, E. Proteasome inhibitor MG132 blocks viral DNA replication and assembly of human cytomegalovirus. FEBS Lett. 2008, 582, 666-672.
    • (2008) FEBS Lett. , vol.582 , pp. 666-672
    • Kaspari, M.1    Tavalai, N.2    Stamminger, T.3    Zimmermann, A.4    Schilf, R.5    Bogner, E.6
  • 132
    • 67449089255 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pp71 induces Daxx SUMOylation
    • Hwang, J.; Kalejta, R.F. Human cytomegalovirus protein pp71 induces Daxx SUMOylation. J. Virol. 2009, 83, 6591-6598.
    • (2009) J. Virol. , vol.83 , pp. 6591-6598
    • Hwang, J.1    Kalejta, R.F.2
  • 133
    • 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, R.D.; Preston, C.M. Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection. J. Virol. 2008, 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
  • 134
    • 0034687704 scopus 로고    scopus 로고
    • UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells
    • Bresnahan, W.A.; Shenk, T.E. UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells. Proc. Natl. Acad. Sci. USA 2000, 97, 14506-14511.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14506-14511
    • Bresnahan, W.A.1    Shenk, T.E.2
  • 135
    • 34548159689 scopus 로고    scopus 로고
    • Human cytomegalovirus gene expression is silenced by Daxxmediated intrinsic immune defense in model latent infections established in vitro
    • Saffert, R.T.; Kalejta, R.F. Human cytomegalovirus gene expression is silenced by Daxxmediated intrinsic immune defense in model latent infections established in vitro. J. Virol. 2007, 81, 9109-9120.
    • (2007) J. Virol. , vol.81 , pp. 9109-9120
    • Saffert, R.T.1    Kalejta, R.F.2
  • 136
    • 36248945635 scopus 로고    scopus 로고
    • Knockdown of hDaxx in normally non-permissive undifferentiated cells does not permit human cytomegalovirus immediate-early gene expression
    • Groves, I.J.; Sinclair, J.H. Knockdown of hDaxx in normally non-permissive undifferentiated cells does not permit human cytomegalovirus immediate-early gene expression. J. Gen. Virol. 2007, 88, 2935-2940.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2935-2940
    • Groves, I.J.1    Sinclair, J.H.2
  • 137
    • 77949269567 scopus 로고    scopus 로고
    • Chromatin structure regulates human cytomegalovirus gene expression during latency, reactivation and lytic infection
    • doi:10.1016/j.bbagrm.2009.08.001
    • Sinclair, J. Chromatin structure regulates human cytomegalovirus gene expression during latency, reactivation and lytic infection. Biochim. Biophys Acta 2009, doi:10.1016/j.bbagrm.2009.08.001.
    • (2009) Biochim. Biophys Acta
    • Sinclair, J.1
  • 138
    • 63849135037 scopus 로고    scopus 로고
    • PML nuclear bodies as sites of epigenetic regulation
    • Torok, D.; Ching, R.W.; Bazett-Jones, D.P. PML nuclear bodies as sites of epigenetic regulation. Front Biosci. 2009, 14, 1325-1336.
    • (2009) Front Biosci. , vol.14 , pp. 1325-1336
    • Torok, D.1    Ching, R.W.2    Bazett-Jones, D.P.3
  • 139
    • 70350495679 scopus 로고    scopus 로고
    • Lytic infection of permissive cells with human cytomegalovirus is regulated by an intrinsic 'pre-immediate-early' repression of viral gene expression mediated by histone post-translational modification
    • Groves, I.J.; Reeves, M.B.; Sinclair, J.H. Lytic infection of permissive cells with human cytomegalovirus is regulated by an intrinsic 'pre-immediate-early' repression of viral gene expression mediated by histone post-translational modification. J. Gen. Virol. 2009, 90, 2364-2374.
    • (2009) J. Gen. Virol. , vol.90 , pp. 2364-2374
    • Groves, I.J.1    Reeves, M.B.2    Sinclair, J.H.3
  • 140
    • 52649089194 scopus 로고    scopus 로고
    • Dynamic histone H3 acetylation and methylation at human cytomegalovirus promoters during replication in fibroblasts
    • Cuevas-Bennett, C.; Shenk, T. Dynamic histone H3 acetylation and methylation at human cytomegalovirus promoters during replication in fibroblasts. J. Virol. 2008, 82, 9525-9536.
    • (2008) J. Virol. , vol.82 , pp. 9525-9536
    • Cuevas-Bennett, C.1    Shenk, T.2
  • 141
    • 0036435166 scopus 로고    scopus 로고
    • Epstein-Barr virus in the pathogenesis of NPC
    • Raab-Traub, N. Epstein-Barr virus in the pathogenesis of NPC. Semin. Cancer Biol 2002, 12, 431-441.
    • (2002) Semin. Cancer Biol , vol.12 , pp. 431-441
    • Raab-Traub, N.1
  • 142
    • 0034467855 scopus 로고    scopus 로고
    • Lytic but not latent replication of epstein-barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins
    • Bell, P.; Lieberman, P.M.; Maul, G.G. Lytic but not latent replication of epstein-barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins. J. Virol. 2000, 74, 11800-11810.
    • (2000) J. Virol. , vol.74 , pp. 11800-11810
    • Bell, P.1    Lieberman, P.M.2    Maul, G.G.3
  • 143
    • 33646156633 scopus 로고    scopus 로고
    • Epstein-Barr virus origin of lytic replication mediates association of replicating episomes with promyelocytic leukaemia protein nuclear bodies and replication compartments
    • Amon, W.; White, R.E.; Farrell, P.J. Epstein-Barr virus origin of lytic replication mediates association of replicating episomes with promyelocytic leukaemia protein nuclear bodies and replication compartments. J. Gen. Virol. 2006, 87, 1133-1137.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1133-1137
    • Amon, W.1    White, R.E.2    Farrell, P.J.3
  • 144
    • 0035124377 scopus 로고    scopus 로고
    • Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies
    • Adamson, A.L.; Kenney, S. Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies. J. Virol. 2001, 75, 2388-2399.
    • (2001) J. Virol. , vol.75 , pp. 2388-2399
    • Adamson, A.L.1    Kenney, S.2
  • 145
    • 0034790899 scopus 로고    scopus 로고
    • Identification of acidic and aromatic residues in the Zta activation domain essential for Epstein-Barr virus reactivation
    • Deng, Z.; Chen, C.J.; Zerby, D.; Delecluse, H.J.; Lieberman, P.M. Identification of acidic and aromatic residues in the Zta activation domain essential for Epstein-Barr virus reactivation. J. Virol. 2001, 75, 10334-10347.
    • (2001) J. Virol. , vol.75 , pp. 10334-10347
    • Deng, Z.1    Chen, C.J.2    Zerby, D.3    Delecluse, H.J.4    Lieberman, P.M.5
  • 146
    • 15244359155 scopus 로고    scopus 로고
    • The Epstein-Barr virus EBNA-LP protein preferentially coactivates EBNA2-mediated stimulation of latent membrane proteins expressed from the viral divergent promoter
    • Peng, R.; Moses, S.C.; Tan, J.; Kremmer, E.; Ling, P.D. The Epstein-Barr virus EBNA-LP protein preferentially coactivates EBNA2-mediated stimulation of latent membrane proteins expressed from the viral divergent promoter. J. Virol. 2005, 79, 4492-4505.
    • (2005) J. Virol. , vol.79 , pp. 4492-4505
    • Peng, R.1    Moses, S.C.2    Tan, J.3    Kremmer, E.4    Ling, P.D.5
  • 147
    • 0029912985 scopus 로고    scopus 로고
    • The Epstein-Barr virus-encoded nuclear antigen EBNA-5 accumulates in PML-containing bodies
    • Szekely, L.; Pokrovskaja, K.; Jiang, W.Q.; de Thé, H.; Ringertz, N.; Klein, G. The Epstein-Barr virus-encoded nuclear antigen EBNA-5 accumulates in PML-containing bodies. J. Virol. 1996, 70, 2562-2568.
    • (1996) J. Virol. , vol.70 , pp. 2562-2568
    • Szekely, L.1    Pokrovskaja, K.2    Jiang, W.Q.3    de Thé, H.4    Ringertz, N.5    Klein, G.6
  • 149
    • 0032560469 scopus 로고    scopus 로고
    • Chromatin components as part of a putative transcriptional repressing complex
    • Lehming, N.; Le, S.A.; Schuller, J.; Ptashne, M. Chromatin components as part of a putative transcriptional repressing complex. Proc. Natl. Acad. Sci. USA 1998, 95, 7322-7326.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7322-7326
    • Lehming, N.1    Le, S.A.2    Schuller, J.3    Ptashne, M.4
  • 150
    • 54249135395 scopus 로고    scopus 로고
    • Regulation of Sp100A subnuclear localization and transcriptional function by EBNA-LP and interferon
    • Echendu, C.W.; Ling, P.D. Regulation of Sp100A subnuclear localization and transcriptional function by EBNA-LP and interferon. J. Interferon Cytokine Res. 2008, 28, 667-678.
    • (2008) J. Interferon Cytokine Res. , vol.28 , pp. 667-678
    • Echendu, C.W.1    Ling, P.D.2
  • 151
    • 55449133376 scopus 로고    scopus 로고
    • Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies
    • Sivachandran, N.; Sarkari, F.; Frappier, L. Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies. PLoS Pathog. 2008, 4, e1000170.
    • (2008) PLoS Pathog. , vol.4
    • Sivachandran, N.1    Sarkari, F.2    Frappier, L.3
  • 152
    • 0035152285 scopus 로고    scopus 로고
    • Originindependent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML
    • Wu, F.Y.; Ahn, J.H.; Alcendor, D.J.; Jang, W.J.; Xiao, J.; Hayward, S.D.; Hayward, G.S. Originindependent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML. J. Virol. 2001, 75, 1487-1506.
    • (2001) J. Virol. , vol.75 , pp. 1487-1506
    • Wu, F.Y.1    Ahn, J.H.2    Alcendor, D.J.3    Jang, W.J.4    Xiao, J.5    Hayward, S.D.6    Hayward, G.S.7
  • 153
    • 0035422278 scopus 로고    scopus 로고
    • Human-herpesvirus-8-encoded K8 protein colocalizes with the promyelocytic leukemia protein (PML) bodies and recruits p53 to the PML bodies
    • Katano, H.; Ogawa-Goto, K.; Hasegawa, H.; Kurata, T.; Sata, T. Human-herpesvirus-8-encoded K8 protein colocalizes with the promyelocytic leukemia protein (PML) bodies and recruits p53 to the PML bodies. Virology 2001, 286, 446-455.
    • (2001) Virology , vol.286 , pp. 446-455
    • Katano, H.1    Ogawa-Goto, K.2    Hasegawa, H.3    Kurata, T.4    Sata, T.5
  • 155
    • 49149094503 scopus 로고    scopus 로고
    • The murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PML and is essential for production of infectious virus
    • Ling, P.D.; Tan, J.; Sewatanon, J.; Peng, R. The murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PML and is essential for production of infectious virus. J. Virol. 2008.
    • (2008) J. Virol.
    • Ling, P.D.1    Tan, J.2    Sewatanon, J.3    Peng, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.