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Volumn 8, Issue 10, 2016, Pages

The role of nuclear antiviral factors against invading DNA viruses: The immediate fate of incoming viral genomes

Author keywords

Adenovirus; Antiviral response; Herpesvirus; IFI16; Incoming viral genomes; Intrinsic immunity; PML nuclear body

Indexed keywords

SUMO 2 PROTEIN; DNA VIRUS;

EID: 84992747009     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v8100290     Document Type: Review
Times cited : (32)

References (105)
  • 1
    • 84941755669 scopus 로고    scopus 로고
    • Microbial sensing by Toll-like receptors and intracellular nucleic acid sensors
    • [CrossRef] [PubMed]
    • Pandey, S.; Kawai, T.; Akira, S. Microbial sensing by Toll-like receptors and intracellular nucleic acid sensors. Cold Spring Harb. Perspect. Biol. 2015, 7, a016246. [CrossRef] [PubMed]
    • (2015) Cold Spring Harb. Perspect. Biol , vol.7
    • Pandey, S.1    Kawai, T.2    Akira, S.3
  • 2
    • 84899131835 scopus 로고    scopus 로고
    • The cGAS-cGAMP-STING Pathway of Cytosolic DNA Sensing and Signaling
    • [CrossRef] [PubMed]
    • Cai, X.; Chiu, Y.-H.; Chen, Z.J. The cGAS-cGAMP-STING Pathway of Cytosolic DNA Sensing and Signaling. Molecular Cell 2014, 54, 289-296. [CrossRef] [PubMed]
    • (2014) Molecular Cell , vol.54 , pp. 289-296
    • Cai, X.1    Chiu, Y.-H.2    Chen, Z.J.3
  • 3
    • 84967215091 scopus 로고    scopus 로고
    • Viral evasion of intracellular DNA and RNA sensing
    • [CrossRef] [PubMed]
    • Chan, Y.K.; Gack, M.U. Viral evasion of intracellular DNA and RNA sensing. Nat. Immunol. 2016, 14, 360-373. [CrossRef] [PubMed]
    • (2016) Nat. Immunol , vol.14 , pp. 360-373
    • Chan, Y.K.1    Gack, M.U.2
  • 4
    • 84907515304 scopus 로고    scopus 로고
    • Cellular Sensing of Viral DNA and Viral Evasion Mechanisms
    • [CrossRef] [PubMed]
    • Orzalli, M.H.; Knipe, D.M. Cellular Sensing of Viral DNA and Viral Evasion Mechanisms. Annu. Rev. Microbiol. 2014, 68, 477-492. [CrossRef] [PubMed]
    • (2014) Annu. Rev. Microbiol. , vol.68 , pp. 477-492
    • Orzalli, M.H.1    Knipe, D.M.2
  • 5
    • 84879510185 scopus 로고    scopus 로고
    • The Spatial Organization of DNA Virus Genomes in the Nucleus
    • [CrossRef] [PubMed]
    • Everett, R.D. The Spatial Organization of DNA Virus Genomes in the Nucleus. PLoS Pathog. 2013, 9, e1003386. [CrossRef] [PubMed]
    • (2013) Plos Pathog , vol.9
    • Everett, R.D.1
  • 6
    • 79955047081 scopus 로고    scopus 로고
    • Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies
    • [CrossRef] [PubMed]
    • Tavalai, N.; Stamminger, T. Interplay between Herpesvirus Infection and Host Defense by PML Nuclear Bodies. Viruses 2009, 1, 1240-1264. [CrossRef] [PubMed]
    • (2009) Viruses , vol.1 , pp. 1240-1264
    • Tavalai, N.1    Stamminger, T.2
  • 7
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: A front-line defense against viral attack
    • [CrossRef] [PubMed]
    • Bieniasz, P.D. Intrinsic immunity: A front-line defense against viral attack. Nat. Immunol. 2004, 5, 1109-1115. [CrossRef] [PubMed]
    • (2004) Nat. Immunol , vol.5 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 8
    • 84863115198 scopus 로고    scopus 로고
    • Intrinsic antiviral immunity
    • [CrossRef] [PubMed]
    • Yan, N.; Chen, Z.J. Intrinsic antiviral immunity. Nat. Immunol. 2012, 13, 214-222. [CrossRef] [PubMed]
    • (2012) Nat. Immunol , vol.13 , pp. 214-222
    • Yan, N.1    Chen, Z.J.2
  • 10
    • 16844373902 scopus 로고    scopus 로고
    • PML bodies: A meeting place for genomic loci
    • [CrossRef] [PubMed]
    • Ching, R.W.; Dellaire, G.; Eskiw, C.H.; Bazett-Jones, D.P. PML bodies: A meeting place for genomic loci? J. Cell Sci. 2005, 118, 847-854. [CrossRef] [PubMed]
    • (2005) J. Cell Sci , vol.118 , pp. 847-854
    • Ching, R.W.1    Dellaire, G.2    Eskiw, C.H.3    Bazett-Jones, D.P.4
  • 11
    • 33750447586 scopus 로고    scopus 로고
    • The mechanisms of PML-nuclear body formation
    • [CrossRef] [PubMed]
    • Shen, T.H.; Lin, H.-K.; Scaglioni, P.P.; Yung, T.M.; Pandolfi, P.P. The mechanisms of PML-nuclear body formation. Mol. Cell 2006, 24, 331-339. [CrossRef] [PubMed]
    • (2006) Mol. Cell , vol.24 , pp. 331-339
    • Shen, T.H.1    Lin, H.-K.2    Scaglioni, P.P.3    Yung, T.M.4    Pandolfi, P.P.5
  • 12
    • 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
    • [CrossRef] [PubMed]
    • Ishov, A.M.; Sotnikov, A.G.; Negorev, D.; Vladimirova, O.V.; Neff, N.; Kamitani, T.; Yeh, E.T.; Strauss, J.F.; Maul, G.G. 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. 1999, 147, 221-234. [CrossRef] [PubMed]
    • (1999) J. Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6    Yeh, E.T.7    Strauss, J.F.8    Maul, G.G.9
  • 13
    • 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
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (1999) J. Biol. Chem , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 14
    • 33746809411 scopus 로고    scopus 로고
    • Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression
    • [CrossRef] [PubMed]
    • Negorev, D.G.; Vladimirova, O.V.; Ivanov, A.; Rauscher, F.; 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. [CrossRef] [PubMed]
    • (2006) J. Virol , vol.80 , pp. 8019-8029
    • Negorev, D.G.1    Vladimirova, O.V.2    Ivanov, A.3    Rauscher, F.4    Maul, G.G.5
  • 15
    • 0141703327 scopus 로고    scopus 로고
    • The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (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
  • 17
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (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
  • 18
    • 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
    • [PubMed]
    • 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. [PubMed]
    • (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
  • 19
    • 42149185026 scopus 로고    scopus 로고
    • Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation
    • [CrossRef] [PubMed]
    • Puto, L.A.; Reed, J.C. Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation. Genes Dev. 2008, 22, 998-1010. [CrossRef] [PubMed]
    • (2008) Genes Dev , vol.22 , pp. 998-1010
    • Puto, L.A.1    Reed, J.C.2
  • 20
    • 0029894340 scopus 로고    scopus 로고
    • Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML)
    • [CrossRef] [PubMed]
    • Grötzinger, 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. [CrossRef] [PubMed]
    • (1996) Eur. J. Biochem. , vol.238 , pp. 554-560
    • Grötzinger, T.1    Sternsdorf, T.2    Jensen, K.3    Will, H.4
  • 21
    • 0034948684 scopus 로고    scopus 로고
    • An essential role for Daxx in the inhibition of B lymphopoiesis by type I interferons
    • Gongora, R.; Stephan, R.P.; Zhang, Z.; Cooper, M.D. An essential role for Daxx in the inhibition of B lymphopoiesis by type I interferons. Immunity 2001, 14, 727-737.[CrossRef]
    • (2001) Immunity , vol.14 , pp. 727-737
    • Gongora, R.1    Stephan, R.P.2    Zhang, Z.3    Cooper, M.D.4
  • 23
    • 84888049352 scopus 로고    scopus 로고
    • The Viral Ubiquitin Ligase ICP0 Is neither Sufficient nor Necessary for Degradation of the Cellular DNA Sensor IFI16 during Herpes Simplex Virus 1 Infection
    • [CrossRef] [PubMed]
    • Cuchet-Lourenco, D.; Anderson, G.; Sloan, E.; Orr, A.; Everett, R.D. The Viral Ubiquitin Ligase ICP0 Is neither Sufficient nor Necessary for Degradation of the Cellular DNA Sensor IFI16 during Herpes Simplex Virus 1 Infection. J. Virol. 2013, 87, 13422-13432. [CrossRef] [PubMed]
    • (2013) J. Virol , vol.87 , pp. 13422-13432
    • Cuchet-Lourenco, D.1    Anderson, G.2    Sloan, E.3    Orr, A.4    Everett, R.D.5
  • 24
    • 84953924199 scopus 로고    scopus 로고
    • Dynamic Response of IFI16 and Promyelocytic Leukemia Nuclear Body Components to Herpes Simplex Virus 1 Infection
    • [CrossRef] [PubMed]
    • Everett, R.D. Dynamic Response of IFI16 and Promyelocytic Leukemia Nuclear Body Components to Herpes Simplex Virus 1 Infection. J. Virol. 2016, 90, 167-179. [CrossRef] [PubMed]
    • (2016) J. Virol , vol.90 , pp. 167-179
    • Everett, R.D.1
  • 25
    • 84975282892 scopus 로고    scopus 로고
    • Emerging Role of PML Nuclear Bodies in Innate Immune Signaling
    • [CrossRef] [PubMed]
    • Scherer, M.; Stamminger, T. Emerging Role of PML Nuclear Bodies in Innate Immune Signaling. J. Virol. 2016, 90, 5850-5854. [CrossRef] [PubMed]
    • (2016) J. Virol , vol.90 , pp. 5850-5854
    • Scherer, M.1    Stamminger, T.2
  • 26
    • 84958073943 scopus 로고    scopus 로고
    • An Adenovirus DNA Replication Factor, but Not Incoming Genome Complexes, Targets PML Nuclear Bodies
    • [CrossRef] [PubMed]
    • Komatsu, T.; Nagata, K.; Wodrich, H. An Adenovirus DNA Replication Factor, but Not Incoming Genome Complexes, Targets PML Nuclear Bodies. J. Virol. 2016, 90, 1657-1667. [CrossRef] [PubMed]
    • (2016) J. Virol. , vol.90 , pp. 1657-1667
    • Komatsu, T.1    Nagata, K.2    Wodrich, H.3
  • 27
    • 84961771272 scopus 로고    scopus 로고
    • Imaging analysis of nuclear antiviral factors through direct detection of incoming adenovirus genome complexes
    • [CrossRef] [PubMed]
    • Komatsu, T.; Will, H.; Nagata, K.; Wodrich, H. Imaging analysis of nuclear antiviral factors through direct detection of incoming adenovirus genome complexes. Biochem. Biophys. Res. Commun. 2016, 1-6. [CrossRef] [PubMed]
    • (2016) Biochem. Biophys. Res. Commun , pp. 1-6
    • Komatsu, T.1    Will, H.2    Nagata, K.3    Wodrich, H.4
  • 28
    • 84908199068 scopus 로고    scopus 로고
    • Role of ChIP-seq in the discovery of transcription factor binding sites, differential gene regulation mechanism, epigenetic marks and beyond
    • [CrossRef] [PubMed]
    • Mundade, R.; Ozer, H.G.; Wei, H.; Prabhu, L.; Lu, T. Role of ChIP-seq in the discovery of transcription factor binding sites, differential gene regulation mechanism, epigenetic marks and beyond. Cell Cycle 2014, 13, 2847-2852. [CrossRef] [PubMed]
    • (2014) Cell Cycle , vol.13 , pp. 2847-2852
    • Mundade, R.1    Ozer, H.G.2    Wei, H.3    Prabhu, L.4    Lu, T.5
  • 30
    • 84930346957 scopus 로고    scopus 로고
    • Selective Recruitment of Nuclear Factors to Productively Replicating Herpes Simplex Virus Genomes
    • [CrossRef] [PubMed]
    • Dembowski, J.A.; DeLuca, N.A. Selective Recruitment of Nuclear Factors to Productively Replicating Herpes Simplex Virus Genomes. PLoS Pathog. 2015, 11, e1004939. [CrossRef] [PubMed]
    • (2015) Plos Pathog , vol.11
    • Dembowski, J.A.1    Deluca, N.A.2
  • 31
    • 84938926553 scopus 로고    scopus 로고
    • Human Papillomavirus Infectious Entry and Trafficking Is a Rapid Process
    • [CrossRef] [PubMed]
    • Broniarczyk, J.; Massimi, P.; Bergant, M.; Banks, L. Human Papillomavirus Infectious Entry and Trafficking Is a Rapid Process. J. Virol. 2015, 89, 8727-8732. [CrossRef] [PubMed]
    • (2015) J. Virol , vol.89 , pp. 8727-8732
    • Broniarczyk, J.1    Massimi, P.2    Bergant, M.3    Banks, L.4
  • 32
    • 84904986129 scopus 로고    scopus 로고
    • An L2 SUMO interacting motif is important for PML localization and infection of human papillomavirus type 16
    • [CrossRef] [PubMed]
    • Bund, T.; Spoden, G.A.; Koynov, K.; Hellmann, N.; Boukhallouk, F.; Arnold, P.; Hinderberger, D.; Florin, L. An L2 SUMO interacting motif is important for PML localization and infection of human papillomavirus type 16. Cell Microbiol. 2014, 16, 1179-1200. [CrossRef] [PubMed]
    • (2014) Cell Microbiol , vol.16 , pp. 1179-1200
    • Bund, T.1    Spoden, G.A.2    Koynov, K.3    Hellmann, N.4    Boukhallouk, F.5    Arnold, P.6    Hinderberger, D.7    Florin, L.8
  • 33
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (1996) J. Cell Biol , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 34
    • 0030840687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate early interaction with host nuclear structures: Definition of an immediate transcript environment
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (1997) J. Cell Biol , vol.138 , pp. 5-16
    • Ishov, A.M.1    Stenberg, R.M.2    Maul, G.G.3
  • 35
    • 0037333386 scopus 로고    scopus 로고
    • Recruitment of Herpes Simplex Virus Type 1 Transcriptional Regulatory Protein ICP4 into Foci Juxtaposed to ND10 in Live, Infected Cells
    • [CrossRef] [PubMed]
    • Everett, R.D.; Sourvinos, G.; Orr, A. Recruitment of Herpes Simplex Virus Type 1 Transcriptional Regulatory Protein ICP4 into Foci Juxtaposed to ND10 in Live, Infected Cells. J. Virol. 2003, 77, 3680-3689. [CrossRef] [PubMed]
    • (2003) J. Virol , vol.77 , pp. 3680-3689
    • Everett, R.D.1    Sourvinos, G.2    Orr, A.3
  • 36
    • 0842304512 scopus 로고    scopus 로고
    • Formation of Nuclear Foci of the Herpes Simplex Virus Type 1 Regulatory Protein ICP4 at Early Times of Infection: Localization, Dynamics, Recruitment of ICP27, and Evidence for the De Novo Induction of ND10-Like Complexes
    • [CrossRef] [PubMed]
    • Everett, R.D.; Sourvinos, G.; Leiper, C.; Clements, J.B.; Orr, A. Formation of Nuclear Foci of the Herpes Simplex Virus Type 1 Regulatory Protein ICP4 at Early Times of Infection: Localization, Dynamics, Recruitment of ICP27, and Evidence for the De Novo Induction of ND10-Like Complexes. J. Virol. 2004, 78, 1903-1917. [CrossRef] [PubMed]
    • (2004) J. Virol , vol.78 , pp. 1903-1917
    • Everett, R.D.1    Sourvinos, G.2    Leiper, C.3    Clements, J.B.4    Orr, A.5
  • 37
    • 16244422998 scopus 로고    scopus 로고
    • ND10 Components Relocate to Sites Associated with Herpes Simplex Virus Type 1 Nucleoprotein Complexes during Virus Infection
    • [CrossRef] [PubMed]
    • Everett, R.D.; Murray, J. ND10 Components Relocate to Sites Associated with Herpes Simplex Virus Type 1 Nucleoprotein Complexes during Virus Infection. J. Virol. 2005, 79, 5078-5089. [CrossRef] [PubMed]
    • (2005) J. Virol , vol.79 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 38
    • 84874035038 scopus 로고    scopus 로고
    • Regulation of alphaherpesvirus infections by the ICP0 family of proteins
    • [CrossRef] [PubMed]
    • Boutell, C.; Everett, R.D. Regulation of alphaherpesvirus infections by the ICP0 family of proteins. J. General Virol. 2013, 94, 465-481. [CrossRef] [PubMed]
    • (2013) J. General Virol , vol.94 , pp. 465-481
    • Boutell, C.1    Everett, R.D.2
  • 39
    • 33746827706 scopus 로고    scopus 로고
    • Contributes to a Cellular Mechanism of Repression of Herpes Simplex Virus Type 1 Infection That Is Inactivated by ICP0
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (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
  • 40
    • 40149085109 scopus 로고    scopus 로고
    • Replication of ICP0-Null Mutant Herpes Simplex Virus Type 1 Is Restricted by both PML and Sp100
    • [CrossRef] [PubMed]
    • 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. 2008, 82, 2661-2672. [CrossRef] [PubMed]
    • (2008) J. Virol , vol.82 , pp. 2661-2672
    • Everett, R.D.1    Parada, C.2    Gripon, P.3    Sirma, H.4    Orr, A.5
  • 41
    • 77950515413 scopus 로고    scopus 로고
    • Regulation of ICP0-Null Mutant Herpes Simplex Virus Type 1 Infection by ND10 Components ATRX and hDaxx
    • [CrossRef] [PubMed]
    • Lukashchuk, V.; Everett, R.D. Regulation of ICP0-Null Mutant Herpes Simplex Virus Type 1 Infection by ND10 Components ATRX and hDaxx. J. Virol. 2010, 84, 4026-4040. [CrossRef] [PubMed]
    • (2010) J. Virol , vol.84 , pp. 4026-4040
    • Lukashchuk, V.1    Everett, R.D.2
  • 42
    • 0037941647 scopus 로고    scopus 로고
    • Promyelocytic Leukemia Protein Mediates Interferon-Based Anti-Herpes Simplex Virus 1 Effects
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2003) J. Virol , vol.77 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 43
    • 84923683601 scopus 로고    scopus 로고
    • The functional interactome of PYHIN immune regulators reveals IFIX is a sensor of viral DNA
    • [CrossRef] [PubMed]
    • Diner, B.A.; Li, T.; Greco, T.M.; Crow, M.S.; Fuesler, J.A.; Wang, J.; Cristea, I.M. The functional interactome of PYHIN immune regulators reveals IFIX is a sensor of viral DNA. Mol. Syst. Biol. 2015, 11, 787. [CrossRef] [PubMed]
    • (2015) Mol. Syst. Biol , vol.11 , pp. 787
    • Diner, B.A.1    Li, T.2    Greco, T.M.3    Crow, M.S.4    Fuesler, J.A.5    Wang, J.6    Cristea, I.M.7
  • 46
    • 84912108081 scopus 로고    scopus 로고
    • IFI16 Restricts HSV-1 Replication by Accumulating on the HSV-1 Genome, Repressing HSV-1 Gene Expression, and Directly or Indirectly Modulating Histone Modifications
    • [CrossRef] [PubMed]
    • Johnson, K.E.; Bottero, V.; Flaherty, S.; Dutta, S.; Singh, V.V.; Chandran, B. IFI16 Restricts HSV-1 Replication by Accumulating on the HSV-1 Genome, Repressing HSV-1 Gene Expression, and Directly or Indirectly Modulating Histone Modifications. PLoS Pathog. 2014, 10, e1004503. [CrossRef] [PubMed]
    • (2014) Plos Pathog , vol.10
    • Johnson, K.E.1    Bottero, V.2    Flaherty, S.3    Dutta, S.4    Singh, V.V.5    Chandran, B.6
  • 47
    • 84888122810 scopus 로고    scopus 로고
    • Nuclear interferon-inducible protein 16 promotes silencing of herpesviral and transfected DNA
    • [CrossRef] [PubMed]
    • Orzalli, M.H.; Conwell, S.E.; Berrios, C.; DeCaprio, J.A.; Knipe, D.M. Nuclear interferon-inducible protein 16 promotes silencing of herpesviral and transfected DNA. Proc. Natl. Acad. Sci. USA 2013, 110, E4492-E4501. [CrossRef] [PubMed]
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E4492-E4501
    • Orzalli, M.H.1    Conwell, S.E.2    Berrios, C.3    Decaprio, J.A.4    Knipe, D.M.5
  • 48
    • 84868095535 scopus 로고    scopus 로고
    • Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein
    • [CrossRef] [PubMed]
    • Orzalli, M.H.; DeLuca, N.A.; Knipe, D.M. Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein. Proc. Natl. Acad. Sci. USA 2012, 109, E3008-E3017. [CrossRef] [PubMed]
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. E3008-E3017
    • Orzalli, M.H.1    Deluca, N.A.2    Knipe, D.M.3
  • 49
    • 84940542596 scopus 로고    scopus 로고
    • Interactions of the Antiviral Factor Interferon Gamma-Inducible Protein 16 (IFI16) Mediate Immune Signaling and Herpes Simplex Virus-1 Immunosuppression
    • [CrossRef] [PubMed]
    • Diner, B.A.; Lum, K.K.; Javitt, A.; Cristea, I.M. Interactions of the Antiviral Factor Interferon Gamma-Inducible Protein 16 (IFI16) Mediate Immune Signaling and Herpes Simplex Virus-1 Immunosuppression. Mol. Cell Proteomics 2015, 14, 2341-2356. [CrossRef] [PubMed]
    • (2015) Mol. Cell Proteomics , vol.14 , pp. 2341-2356
    • Diner, B.A.1    Lum, K.K.2    Javitt, A.3    Cristea, I.M.4
  • 50
    • 84984624647 scopus 로고    scopus 로고
    • Relative Contributions of Herpes Simplex Virus 1 ICP0 and vhs to Loss of Cellular IFI16 Vary in Different Human Cell Types
    • [CrossRef] [PubMed]
    • Orzalli, M.H.; Broekema, N.M.; Knipe, D.M. Relative Contributions of Herpes Simplex Virus 1 ICP0 and vhs to Loss of Cellular IFI16 Vary in Different Human Cell Types. J. Virol. 2016, 90, 8351-8359. [CrossRef] [PubMed]
    • (2016) J. Virol. , vol.90 , pp. 8351-8359
    • Orzalli, M.H.1    Broekema, N.M.2    Knipe, D.M.3
  • 51
    • 84862976171 scopus 로고    scopus 로고
    • Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16
    • [CrossRef] [PubMed]
    • Li, T.; Diner, B.A.; Chen, J.; Cristea, I.M. Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16. Proc. Natl. Acad. Sci. USA 2012, 109, 10558-10563. [CrossRef] [PubMed]
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 10558-10563
    • Li, T.1    Diner, B.A.2    Chen, J.3    Cristea, I.M.4
  • 52
    • 84928889567 scopus 로고    scopus 로고
    • CGAS-mediated stabilization of IFI16 promotes innate signaling during herpes simplex virus infection
    • [CrossRef] [PubMed]
    • Orzalli, M.H.; Broekema, N.M.; Diner, B.A.; Hancks, D.C.; Elde, N.C.; Cristea, I.M.; Knipe, D.M. cGAS-mediated stabilization of IFI16 promotes innate signaling during herpes simplex virus infection. Proc. Natl. Acad. Sci. USA 2015, 112, E1773-E1781. [CrossRef] [PubMed]
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. E1773-E1781
    • Orzalli, M.H.1    Broekema, N.M.2    Diner, B.A.3    Hancks, D.C.4    Elde, N.C.5    Cristea, I.M.6    Knipe, D.M.7
  • 53
    • 35348888404 scopus 로고    scopus 로고
    • Recruitment of Human Cytomegalovirus Immediate-Early 2 Protein onto Parental Viral Genomes in Association with ND10 in Live-Infected Cells
    • [CrossRef] [PubMed]
    • Sourvinos, G.; Tavalai, N.; Berndt, A.; Spandidos, D.A.; Stamminger, T. Recruitment of Human Cytomegalovirus Immediate-Early 2 Protein onto Parental Viral Genomes in Association with ND10 in Live-Infected Cells. J. Virol. 2007, 81, 10123-10136. [CrossRef] [PubMed]
    • (2007) J. Virol , vol.81 , pp. 10123-10136
    • Sourvinos, G.1    Tavalai, N.2    Berndt, A.3    Spandidos, D.A.4    Stamminger, T.5
  • 54
    • 33746840094 scopus 로고    scopus 로고
    • Evidence for a Role of the Cellular ND10 Protein PML in Mediating Intrinsic Immunity against Human Cytomegalovirus Infections
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2006) J. Virol , vol.80 , pp. 8006-8018
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Leis, M.4    Stamminger, T.5
  • 55
    • 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
    • [PubMed]
    • Müller, 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. [PubMed]
    • (1999) J. Virol , vol.73 , pp. 5137-5143
    • Müller, S.1    Dejean, A.2
  • 56
    • 84871987427 scopus 로고    scopus 로고
    • The replication defect of ICP0-null mutant herpes simplex virus 1 can be largely complemented by the combined activities of human cytomegalovirus proteins IE1 and pp71
    • [CrossRef] [PubMed]
    • Everett, R.D.; Bell, A.J.; Lu, Y.; Orr, A. The replication defect of ICP0-null mutant herpes simplex virus 1 can be largely complemented by the combined activities of human cytomegalovirus proteins IE1 and pp71. J. Virol. 2013, 87, 978-990. [CrossRef] [PubMed]
    • (2013) J. Virol , vol.87 , pp. 978-990
    • Everett, R.D.1    Bell, A.J.2    Lu, Y.3    Orr, A.4
  • 57
    • 0036091745 scopus 로고    scopus 로고
    • Functional Interaction between the pp71 Protein of Human Cytomegalovirus and the PML-Interacting Protein Human Daxx
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2002) J. Virol. , vol.76 , pp. 5769-5783
    • Hofmann, H.1    Sindre, H.2    Stamminger, T.3
  • 58
    • 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
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2006) J. Virol , vol.80 , pp. 3863-3871
    • Saffert, R.T.1    Kalejta, R.F.2
  • 59
    • 57349108706 scopus 로고    scopus 로고
    • Human Cytomegalovirus Protein pp71 Displaces the Chromatin-Associated Factor ATRX from Nuclear Domain 10 at Early Stages of Infection
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2008) J. Virol , vol.82 , pp. 12543-12554
    • Lukashchuk, V.1    McFarlane, S.2    Everett, R.D.3    Preston, C.M.4
  • 60
    • 84893715483 scopus 로고    scopus 로고
    • Kaposi’s sarcoma associated herpesvirus tegument protein ORF75 is essential for viral lytic replication and plays a critical role in the antagonization of ND10-instituted intrinsic immunity
    • [CrossRef] [PubMed]
    • Full, F.; Jungnickl, D.; Reuter, N.; Bogner, E.; Brulois, K.; Scholz, B.; Stürzl, M.; Myoung, J.; Jung, J.U.; Stamminger, T. et al. Kaposi’s sarcoma associated herpesvirus tegument protein ORF75 is essential for viral lytic replication and plays a critical role in the antagonization of ND10-instituted intrinsic immunity. PLoS Pathog. 2014, 10, e1003863. [CrossRef] [PubMed]
    • (2014) Plos Pathog , vol.10
    • Full, F.1    Jungnickl, D.2    Reuter, N.3    Bogner, E.4    Brulois, K.5    Scholz, B.6    Stürzl, M.7    Myoung, J.8    Jung, J.U.9    Stamminger, T.10
  • 61
    • 81755166682 scopus 로고    scopus 로고
    • EBV Tegument Protein BNRF1 Disrupts DAXX-ATRX to Activate Viral Early Gene Transcription
    • [CrossRef] [PubMed]
    • Tsai, K.; Thikmyanova, N.; Wojcechowskyj, J.A.; Delecluse, H.-J.; Lieberman, P.M. EBV Tegument Protein BNRF1 Disrupts DAXX-ATRX to Activate Viral Early Gene Transcription. PLoS Pathog. 2011, 7, e1002376. [CrossRef] [PubMed]
    • (2011) Plos Pathog , vol.7
    • Tsai, K.1    Thikmyanova, N.2    Wojcechowskyj, J.A.3    Delecluse, H.-J.4    Lieberman, P.M.5
  • 62
    • 84887194503 scopus 로고    scopus 로고
    • Virion Factors That Target Daxx To Overcome Intrinsic Immunity
    • [CrossRef] [PubMed]
    • Schreiner, S.; Wodrich, H. Virion Factors That Target Daxx To Overcome Intrinsic Immunity. J. Virol. 2013, 87, 10412-10422. [CrossRef] [PubMed]
    • (2013) J. Virol , vol.87 , pp. 10412-10422
    • Schreiner, S.1    Wodrich, H.2
  • 63
    • 84992706544 scopus 로고    scopus 로고
    • Stimulation of the replication of ICP0-null mutant HSV-1 and pp71-deficient HCMV by EBV tegument protein BNRF1
    • [CrossRef] [PubMed]
    • Lu, Y.; Orr, A.; Everett, R.D. Stimulation of the replication of ICP0-null mutant HSV-1 and pp71-deficient HCMV by EBV tegument protein BNRF1. J. Virol. 2016. [CrossRef] [PubMed]
    • (2016) J. Virol
    • Lu, Y.1    Orr, A.2    Everett, R.D.3
  • 64
    • 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
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2008) J. Virol , vol.82 , pp. 126-137
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Stamminger, T.4
  • 65
    • 79959290376 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100
    • [CrossRef] [PubMed]
    • Adler, M.; Tavalai, N.; Muller, R.; Stamminger, T. Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100. J. General Virol. 2011, 92, 1532-1538. [CrossRef] [PubMed]
    • (2011) J. General Virol , vol.92 , pp. 1532-1538
    • Adler, M.1    Tavalai, N.2    Muller, R.3    Stamminger, T.4
  • 66
    • 84887929864 scopus 로고    scopus 로고
    • Human Cytomegalovirus Tegument Protein pUL83 Inhibits IFI16-Mediated DNA Sensing for Immune Evasion
    • Li, T.; Chen, J.; Cristea, I.M. Human Cytomegalovirus Tegument Protein pUL83 Inhibits IFI16-Mediated DNA Sensing for Immune Evasion. Cell Host Microbe 2013, 14, 591-599.
    • (2013) Cell Host Microbe , vol.14 , pp. 591-599
    • Li, T.1    Chen, J.2    Cristea, I.M.3
  • 67
    • 84901355951 scopus 로고    scopus 로고
    • Innate Nuclear Sensor IFI16 Translocates into the Cytoplasm during the Early Stage of In Vitro Human Cytomegalovirus Infection and Is Entrapped in the Egressing Virions during the Late Stage
    • Dell’Oste, V.; Gatti, D.; Gugliesi, F.; De Andrea, M.; Bawadekar, M.; Lo Cigno, I.; Biolatti, M.; Vallino, M.; Marschall, M.; Gariglio, M. et al. Innate Nuclear Sensor IFI16 Translocates into the Cytoplasm during the Early Stage of In Vitro Human Cytomegalovirus Infection and Is Entrapped in the Egressing Virions during the Late Stage. J. Virol. 2014, 88, 6970-6982.
    • (2014) J. Virol. , vol.88 , pp. 6970-6982
    • Dell’Oste, V.1    Gatti, D.2    Gugliesi, F.3    De Andrea, M.4    Bawadekar, M.5    Lo Cigno, I.6    Biolatti, M.7    Vallino, M.8    Marschall, M.9    Gariglio, M.10
  • 68
    • 84859337955 scopus 로고    scopus 로고
    • Chromatin structure of adenovirus DNA throughout infection
    • [CrossRef] [PubMed]
    • Giberson, A.N.; Davidson, A.R.; Parks, R.J. Chromatin structure of adenovirus DNA throughout infection. Nucleic Acids Res. 2012, 40, 2369-2376. [CrossRef] [PubMed]
    • (2012) Nucleic Acids Res , vol.40 , pp. 2369-2376
    • Giberson, A.N.1    Davidson, A.R.2    Parks, R.J.3
  • 69
    • 30344473323 scopus 로고    scopus 로고
    • Involvement of template-activating factor I/SET in transcription of adenovirus early genes as a positive-acting factor
    • [CrossRef] [PubMed]
    • Haruki, H.; Okuwaki, M.; Miyagishi, M.; Taira, K.; Nagata, K. Involvement of template-activating factor I/SET in transcription of adenovirus early genes as a positive-acting factor. J. Virol. 2006, 80, 794-801. [CrossRef] [PubMed]
    • (2006) J. Virol , vol.80 , pp. 794-801
    • Haruki, H.1    Okuwaki, M.2    Miyagishi, M.3    Taira, K.4    Nagata, K.5
  • 70
    • 0346366821 scopus 로고    scopus 로고
    • Ternary complex formation between DNA-adenovirus core protein VII and TAF-I_/SET, an acidic molecular chaperone
    • [CrossRef]
    • Haruki, H.; Gyurcsik, B.; Okuwaki, M.; Nagata, K. Ternary complex formation between DNA-adenovirus core protein VII and TAF-I_/SET, an acidic molecular chaperone. FEBS Lett. 2003, 555, 521-527. [CrossRef]
    • (2003) FEBS Lett , vol.555 , pp. 521-527
    • Haruki, H.1    Gyurcsik, B.2    Okuwaki, M.3    Nagata, K.4
  • 71
    • 79951571234 scopus 로고    scopus 로고
    • Cellular and viral chromatin proteins are positive factors in the regulation of adenovirus gene expression
    • [CrossRef] [PubMed]
    • Komatsu, T.; Haruki, H.; Nagata, K. Cellular and viral chromatin proteins are positive factors in the regulation of adenovirus gene expression. Nucleic Acids Res. 2011, 39, 889-901. [CrossRef] [PubMed]
    • (2011) Nucleic Acids Res , vol.39 , pp. 889-901
    • Komatsu, T.1    Haruki, H.2    Nagata, K.3
  • 72
    • 84947484144 scopus 로고    scopus 로고
    • A Method for Visualization of Incoming Adenovirus Chromatin Complexes in Fixed and Living Cells
    • [CrossRef] [PubMed]
    • Komatsu, T.; Dacheux, D.; Kreppel, F.; Nagata, K.; Wodrich, H. A Method for Visualization of Incoming Adenovirus Chromatin Complexes in Fixed and Living Cells. PLoS ONE 2015, 10, e0137102. [CrossRef] [PubMed]
    • (2015) Plos ONE , vol.10
    • Komatsu, T.1    Dacheux, D.2    Kreppel, F.3    Nagata, K.4    Wodrich, H.5
  • 73
    • 84956789542 scopus 로고    scopus 로고
    • E2F/Rb Family Proteins Mediate Interferon Induced Repression of Adenovirus Immediate Early Transcription to Promote Persistent Viral Infection
    • [CrossRef] [PubMed]
    • Zheng, Y.; Stamminger, T.; Hearing, P. E2F/Rb Family Proteins Mediate Interferon Induced Repression of Adenovirus Immediate Early Transcription to Promote Persistent Viral Infection. PLoS Pathog. 2016, 12, e1005415. [CrossRef] [PubMed]
    • (2016) Plos Pathog , vol.12
    • Zheng, Y.1    Stamminger, T.2    Hearing, P.3
  • 75
    • 47749134575 scopus 로고    scopus 로고
    • Cellular Proteins PML and Daxx Mediate an Innate Antiviral Defense Antagonized by the Adenovirus E4 ORF3 Protein
    • [CrossRef] [PubMed]
    • Ullman, A.J.; Hearing, P. Cellular Proteins PML and Daxx Mediate an Innate Antiviral Defense Antagonized by the Adenovirus E4 ORF3 Protein. J. Virol. 2008, 82, 7325-7335. [CrossRef] [PubMed]
    • (2008) J. Virol , vol.82 , pp. 7325-7335
    • Ullman, A.J.1    Hearing, P.2
  • 76
    • 0030052130 scopus 로고    scopus 로고
    • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure
    • [CrossRef] [PubMed]
    • Doucas, V.; Ishov, A.M.; Romo, A.; Juguilon, H.; Weitzman, M.D.; Evans, R.M.; Maul, G.G. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 1996, 10, 196-207. [CrossRef] [PubMed]
    • (1996) Genes Dev , vol.10 , pp. 196-207
    • Doucas, V.1    Ishov, A.M.2    Romo, A.3    Juguilon, H.4    Weitzman, M.D.5    Evans, R.M.6    Maul, G.G.7
  • 77
    • 0242439337 scopus 로고    scopus 로고
    • Adenovirus protein IX sequesters host-cell promyelocytic leukaemia protein and contributes to efficient viral proliferation
    • [CrossRef] [PubMed]
    • Rosa-Calatrava, M.; Puvion-Dutilleul, F.; Lutz, P.; Dreyer, D.; De Thé, H.; Chatton, B.; Kedinger, C. Adenovirus protein IX sequesters host-cell promyelocytic leukaemia protein and contributes to efficient viral proliferation. EMBO Rep. 2003, 4, 969-975. [CrossRef] [PubMed]
    • (2003) EMBO Rep , vol.4 , pp. 969-975
    • Rosa-Calatrava, M.1    Puvion-Dutilleul, F.2    Lutz, P.3    Dreyer, D.4    De Thé, H.5    Chatton, B.6    Kedinger, C.7
  • 79
    • 84942162738 scopus 로고    scopus 로고
    • Adenovirus E4-ORF3 Targets PIAS3 and Together with E1B-55K Remodels SUMO Interactions in the Nucleus and at Virus Genome Replication Domains
    • [CrossRef] [PubMed]
    • Higginbotham, J.M.; O’Shea, C.C. Adenovirus E4-ORF3 Targets PIAS3 and Together with E1B-55K Remodels SUMO Interactions in the Nucleus and at Virus Genome Replication Domains. J. Virol. 2015, 89, 10260-10272. [CrossRef] [PubMed]
    • (2015) J. Virol , vol.89 , pp. 10260-10272
    • Higginbotham, J.M.1    O’Shea, C.C.2
  • 80
    • 77953736164 scopus 로고    scopus 로고
    • Proteasome-Dependent Degradation of Daxx by the Viral E1B-55K Protein in Human Adenovirus-Infected Cells
    • [CrossRef] [PubMed]
    • Schreiner, S.; Wimmer, P.; Sirma, H.; Everett, R.D.; Blanchette, P.; Groitl, P.; Dobner, T. Proteasome-Dependent Degradation of Daxx by the Viral E1B-55K Protein in Human Adenovirus-Infected Cells. J. Virol. 2010, 84, 7029-7038. [CrossRef] [PubMed]
    • (2010) J. Virol , vol.84 , pp. 7029-7038
    • Schreiner, S.1    Wimmer, P.2    Sirma, H.3    Everett, R.D.4    Blanchette, P.5    Groitl, P.6    Dobner, T.7
  • 82
    • 84876038069 scopus 로고    scopus 로고
    • Control of human adenovirus type 5 gene expression by cellular Daxx/ATRX chromatin-associated complexes
    • [CrossRef] [PubMed]
    • Schreiner, S.; Burck, C.; Glass, M.; Groitl, P.; Wimmer, P.; Kinkley, S.; Mund, A.; Everett, R.D.; Dobner, T. Control of human adenovirus type 5 gene expression by cellular Daxx/ATRX chromatin-associated complexes. Nucleic Acids Res. 2013, 41, 3532-3550. [CrossRef] [PubMed]
    • (2013) Nucleic Acids Res , vol.41 , pp. 3532-3550
    • Schreiner, S.1    Burck, C.2    Glass, M.3    Groitl, P.4    Wimmer, P.5    Kinkley, S.6    Mund, A.7    Everett, R.D.8    Dobner, T.9
  • 83
    • 84871958784 scopus 로고    scopus 로고
    • The Adenoviral Oncogene E1A-13S Interacts with a Specific Isoform of the Tumor Suppressor PML to Enhance Viral Transcription
    • [CrossRef] [PubMed]
    • Berscheminski, J.; Groitl, P.; Dobner, T.; Wimmer, P.; Schreiner, S. The Adenoviral Oncogene E1A-13S Interacts with a Specific Isoform of the Tumor Suppressor PML to Enhance Viral Transcription. J. Virol. 2012, 87, 965-977. [CrossRef] [PubMed]
    • (2012) J. Virol. , vol.87 , pp. 965-977
    • Berscheminski, J.1    Groitl, P.2    Dobner, T.3    Wimmer, P.4    Schreiner, S.5
  • 84
    • 84985906472 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein isoform II inhibits infection by human adenovirus type 5 through effects on HSP70 and the interferon response
    • Woodman, A.; Wright, J.; Atwan, Z.; Leppard, K.N. Promyelocytic leukemia protein isoform II inhibits infection by human adenovirus type 5 through effects on HSP70 and the interferon response. J. General Virol. 2016, 97, 1955-1967.
    • (2016) J. General Virol , vol.97 , pp. 1955-1967
    • Woodman, A.1    Wright, J.2    Atwan, Z.3    Leppard, K.N.4
  • 85
    • 84888268767 scopus 로고    scopus 로고
    • SPOC1-Mediated Antiviral Host Cell Response Is Antagonized Early in Human Adenovirus Type 5 Infection
    • [CrossRef] [PubMed]
    • Schreiner, S.; Kinkley, S.; Bürck, C.; Mund, A.; Wimmer, P.; Schubert, T.; Groitl, P.; Will, H.; Dobner, T. SPOC1-Mediated Antiviral Host Cell Response Is Antagonized Early in Human Adenovirus Type 5 Infection. PLoS Pathog. 2013, 9, e1003775. [CrossRef] [PubMed]
    • (2013) Plos Pathog , vol.9
    • Schreiner, S.1    Kinkley, S.2    Bürck, C.3    Mund, A.4    Wimmer, P.5    Schubert, T.6    Groitl, P.7    Will, H.8    Dobner, T.9
  • 86
    • 0033814990 scopus 로고    scopus 로고
    • Replication but not transcription of simian virus 40 DNA is dependent on nuclear domain 10
    • [CrossRef] [PubMed]
    • Tang, Q.; Bell, P.; Tegtmeyer, P.; Maul, G.G. Replication but not transcription of simian virus 40 DNA is dependent on nuclear domain 10. J. Virol. 2000, 74, 9694-9700. [CrossRef] [PubMed]
    • (2000) J. Virol , vol.74 , pp. 9694-9700
    • Tang, Q.1    Bell, P.2    Tegtmeyer, P.3    Maul, G.G.4
  • 88
    • 79955079235 scopus 로고    scopus 로고
    • Functional reorganization of promyelocytic leukemia nuclear bodies during BK virus infection
    • [CrossRef] [PubMed]
    • Jiang, M.; Entezami, P.; Gamez, M.; Stamminger, T.; Imperiale, M.J. Functional reorganization of promyelocytic leukemia nuclear bodies during BK virus infection. mBio 2011, 2, e00281-10. [CrossRef] [PubMed]
    • (2011) Mbio , vol.2 , pp. e00281-e00310
    • Jiang, M.1    Entezami, P.2    Gamez, M.3    Stamminger, T.4    Imperiale, M.J.5
  • 89
    • 4644352291 scopus 로고    scopus 로고
    • Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression
    • [CrossRef] [PubMed]
    • Day, P.M.; Baker, C.C.; Lowy, D.R.; Schiller, J.T. Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression. Proc. Natl. Acad. Sci. USA 2004, 101, 14252-14257. [CrossRef] [PubMed]
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14252-14257
    • Day, P.M.1    Baker, C.C.2    Lowy, D.R.3    Schiller, J.T.4
  • 90
    • 0036061103 scopus 로고    scopus 로고
    • Reorganization of Nuclear Domain 10 Induced by Papillomavirus Capsid Protein L2
    • [CrossRef] [PubMed]
    • Florin, L.; Schäfer, F.; Sotlar, K.; Streeck, R.E.; Sapp, M. Reorganization of Nuclear Domain 10 Induced by Papillomavirus Capsid Protein L2. Virology 2002, 295, 97-107. [CrossRef] [PubMed]
    • (2002) Virology , vol.295 , pp. 97-107
    • Florin, L.1    Schäfer, F.2    Sotlar, K.3    Streeck, R.E.4    Sapp, M.5
  • 91
    • 84891602166 scopus 로고    scopus 로고
    • Sp100 Provides Intrinsic Immunity against Human Papillomavirus Infection
    • [CrossRef] [PubMed]
    • Stepp, W.H.; Meyers, J.M.; McBride, A.A. Sp100 Provides Intrinsic Immunity against Human Papillomavirus Infection. mBio 2013, 4, e00845-13. [CrossRef] [PubMed]
    • (2013) Mbio , vol.4 , pp. e00845-e00913
    • Stepp, W.H.1    Meyers, J.M.2    McBride, A.A.3
  • 92
    • 84937723908 scopus 로고    scopus 로고
    • The Nuclear DNA Sensor IFI16 Acts as a Restriction Factor for Human Papillomavirus Replication through Epigenetic Modifications of the Viral Promoters
    • [CrossRef] [PubMed]
    • Cigno, Lo I.; De Andrea, M.; Borgogna, C.; Albertini, S.; Landini, M.M.; Peretti, A.; Johnson, K.E.; Chandran, B.; Landolfo, S.; Gariglio, M. The Nuclear DNA Sensor IFI16 Acts as a Restriction Factor for Human Papillomavirus Replication through Epigenetic Modifications of the Viral Promoters. J. Virol. 2015, 89, 7506-7520. [CrossRef] [PubMed]
    • (2015) J. Virol , vol.89 , pp. 7506-7520
    • Cigno, L.I.1    De Andrea, M.2    Borgogna, C.3    Albertini, S.4    Landini, M.M.5    Peretti, A.6    Johnson, K.E.7    Chandran, B.8    Landolfo, S.9    Gariglio, M.10
  • 93
    • 79959848568 scopus 로고    scopus 로고
    • The Intrinsic Antiviral Defense to Incoming HSV-1 Genomes Includes Specific DNA Repair Proteins and Is Counteracted by the Viral Protein ICP0
    • [CrossRef] [PubMed]
    • Lilley, C.E.; Chaurushiya, M.S.; Boutell, C.; Everett, R.D.; Weitzman, M.D. The Intrinsic Antiviral Defense to Incoming HSV-1 Genomes Includes Specific DNA Repair Proteins and Is Counteracted by the Viral Protein ICP0. PLoS Pathog. 2011, 7, e1002084. [CrossRef] [PubMed]
    • (2011) Plos Pathog , vol.7
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Everett, R.D.4    Weitzman, M.D.5
  • 94
    • 79955446411 scopus 로고    scopus 로고
    • Adenovirus Core Protein VII Protects the Viral Genome from a DNA Damage Response at Early Times after Infection
    • [CrossRef] [PubMed]
    • Karen, K.A.; Hearing, P. Adenovirus Core Protein VII Protects the Viral Genome from a DNA Damage Response at Early Times after Infection. J. Virol. 2011, 85, 4135-4142. [CrossRef] [PubMed]
    • (2011) J. Virol , vol.85 , pp. 4135-4142
    • Karen, K.A.1    Hearing, P.2
  • 95
    • 84891933102 scopus 로고    scopus 로고
    • Cooperative assembly of IFI16 filaments on dsDNA provides insights into host defense strategy
    • [CrossRef] [PubMed]
    • Morrone, S.R.; Wang, T.; Constantoulakis, L.M.; Hooy, R.M.; Delannoy, M.J.; Sohn, J. Cooperative assembly of IFI16 filaments on dsDNA provides insights into host defense strategy. Proc. Natl. Acad. Sci. USA 2014, 111, E62-E71. [CrossRef] [PubMed]
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E62-E71
    • Morrone, S.R.1    Wang, T.2    Constantoulakis, L.M.3    Hooy, R.M.4    Delannoy, M.J.5    Sohn, J.6
  • 96
    • 84988646188 scopus 로고    scopus 로고
    • The innate immune sensor IFI16 recognizes foreign DNA in the nucleus by scanning along the duplex
    • [CrossRef] [PubMed]
    • Stratmann, S.A.; Morrone, S.R.; van Oijen, A.M.; Sohn, J. The innate immune sensor IFI16 recognizes foreign DNA in the nucleus by scanning along the duplex. Elife 2015, 4, 1-13. [CrossRef] [PubMed]
    • (2015) Elife , vol.4 , pp. 1-13
    • Stratmann, S.A.1    Morrone, S.R.2    Van Oijen, A.M.3    Sohn, J.4
  • 97
    • 84877940759 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO) pathway-mediated enhancement of human cytomegalovirus replication correlates with a recruitment of SUMO-1/3 proteins to viral replication compartments
    • [CrossRef] [PubMed]
    • Scherer, M.; Reuter, N.; Wagenknecht, N.; Otto, V.; Sticht, H.; Stamminger, T. Small ubiquitin-related modifier (SUMO) pathway-mediated enhancement of human cytomegalovirus replication correlates with a recruitment of SUMO-1/3 proteins to viral replication compartments. J. General Virol. 2013, 94, 1373-1384. [CrossRef] [PubMed]
    • (2013) J. General Virol , vol.94 , pp. 1373-1384
    • Scherer, M.1    Reuter, N.2    Wagenknecht, N.3    Otto, V.4    Sticht, H.5    Stamminger, T.6
  • 98
    • 84866174976 scopus 로고    scopus 로고
    • HSV-1 Genome Subnuclear Positioning and Associations with Host-Cell PML-NBs and Centromeres Regulate LAT Locus Transcription during Latency in Neurons
    • [CrossRef] [PubMed]
    • Catez, F.; Picard, C.; Held, K.; Gross, S.; Rousseau, A.; Theil, D.; Sawtell, N.; Labetoulle, M.; Lomonte, P. HSV-1 Genome Subnuclear Positioning and Associations with Host-Cell PML-NBs and Centromeres Regulate LAT Locus Transcription during Latency in Neurons. PLoS Pathog. 2012, 8, e1002852. [CrossRef] [PubMed]
    • (2012) Plos Pathog , vol.8
    • Catez, F.1    Picard, C.2    Held, K.3    Gross, S.4    Rousseau, A.5    Theil, D.6    Sawtell, N.7    Labetoulle, M.8    Lomonte, P.9
  • 99
    • 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
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2000) J. Virol , vol.74 , pp. 11800-11810
    • Bell, P.1    Lieberman, P.M.2    Maul, G.G.3
  • 100
    • 55449133376 scopus 로고    scopus 로고
    • Epstein-Barr Nuclear Antigen 1 Contributes to Nasopharyngeal Carcinoma through Disruption of PML Nuclear Bodies
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2008) Plos Pathog , vol.4
    • Sivachandran, N.1    Sarkari, F.2    Frappier, L.3
  • 101
    • 84863599916 scopus 로고    scopus 로고
    • Functions of the Epstein-Barr Virus EBNA1 Protein in Viral Reactivation and Lytic Infection
    • [CrossRef] [PubMed]
    • Sivachandran, N.; Wang, X.; Frappier, L. Functions of the Epstein-Barr Virus EBNA1 Protein in Viral Reactivation and Lytic Infection. J. Virol. 2012, 86, 6146-6158. [CrossRef] [PubMed]
    • (2012) J. Virol , vol.86 , pp. 6146-6158
    • Sivachandran, N.1    Wang, X.2    Frappier, L.3
  • 102
    • 84883388483 scopus 로고    scopus 로고
    • Kaposi’s Sarcoma-Associated Herpesvirus K-Rta Exhibits SUMO-Targeting Ubiquitin Ligase (STUbL) Like Activity and Is Essential for Viral Reactivation
    • [CrossRef] [PubMed]
    • Izumiya, Y.; Kobayashi, K.; Kim, K.Y.; Pochampalli, M.; Izumiya, C.; Shevchenko, B.; Wang, D.-H.; Huerta, S.B.; Martinez, A.; Campbell, M. et al. Kaposi’s Sarcoma-Associated Herpesvirus K-Rta Exhibits SUMO-Targeting Ubiquitin Ligase (STUbL) Like Activity and Is Essential for Viral Reactivation. PLoS Pathog. 2013, 9, e1003506. [CrossRef] [PubMed]
    • (2013) Plos Pathog , vol.9
    • Izumiya, Y.1    Kobayashi, K.2    Kim, K.Y.3    Pochampalli, M.4    Izumiya, C.5    Shevchenko, B.6    Wang, D.-H.7    Huerta, S.B.8    Martinez, A.9    Campbell, M.10
  • 103
    • 84905373394 scopus 로고    scopus 로고
    • Influence of ND10 Components on Epigenetic Determinants of Early KSHV Latency Establishment
    • [CrossRef] [PubMed]
    • Günther, T.; Schreiner, S.; Dobner, T.; Tessmer, U.; Grundhoff, A. Influence of ND10 Components on Epigenetic Determinants of Early KSHV Latency Establishment. PLoS Pathog. 2014, 10, e1004274. [CrossRef] [PubMed]
    • (2014) Plos Pathog , vol.10
    • Günther, T.1    Schreiner, S.2    Dobner, T.3    Tessmer, U.4    Grundhoff, A.5
  • 104
    • 84930959439 scopus 로고    scopus 로고
    • Contribution of the Major ND10 Proteins PML, hDaxx and Sp100 to the Regulation of Human Cytomegalovirus Latency and Lytic Replication in the Monocytic Cell Line THP-1
    • [CrossRef] [PubMed]
    • Wagenknecht, N.; Reuter, N.; Scherer, M.; Reichel, A.; Müller, R.; Stamminger, T. Contribution of the Major ND10 Proteins PML, hDaxx and Sp100 to the Regulation of Human Cytomegalovirus Latency and Lytic Replication in the Monocytic Cell Line THP-1. Viruses 2015, 7, 2884-2907. [CrossRef] [PubMed]
    • (2015) Viruses , vol.7 , pp. 2884-2907
    • Wagenknecht, N.1    Reuter, N.2    Scherer, M.3    Reichel, A.4    Müller, R.5    Stamminger, T.6
  • 105
    • 84990232152 scopus 로고    scopus 로고
    • Sensor IFI16 Is Degraded during Lytic Reactivation of Kaposi’s Sarcoma-Associated Herpesvirus (KSHV): Role of IFI16 in Maintenance of KSHV Latency
    • [CrossRef] [PubMed]
    • Roy, A.; Dutta, D.; Iqbal, J.; Pisano, G.; Gjyshi, O.; Ansari, M.A.; Kumar, B.; Chandran, B. Nuclear Innate Immune DNA Sensor IFI16 Is Degraded during Lytic Reactivation of Kaposi’s Sarcoma-Associated Herpesvirus (KSHV): Role of IFI16 in Maintenance of KSHV Latency. J. Virol. 2016, 90, 8822-8841. [CrossRef] [PubMed]
    • (2016) J. Virol , vol.90 , pp. 8822-8841
    • Roy, A.1    Dutta, D.2    Iqbal, J.3    Pisano, G.4    Gjyshi, O.5    Ansari, M.A.6    Kumar, B.7    Chandran, B.8    Nuclear Innate Immune, D.9


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