메뉴 건너뛰기




Volumn 87, Issue 4, 2013, Pages 2174-2185

Components of promyelocytic leukemia nuclear bodies (nd10) act cooperatively to repress herpesvirus infection

Author keywords

[No Author keywords available]

Indexed keywords

DAXX PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN NUCLEAR DOMAIN 10; PROTEIN SP100; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84873816597     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02950-12     Document Type: Article
Times cited : (92)

References (85)
  • 1
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: a front-line defense against viral attack
    • Bieniasz PD. 2004. Intrinsic immunity: a front-line defense against viral attack. Nat. Immunol. 5:1109-1115.
    • (2004) Nat. Immunol. , vol.5 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 2
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai N, Stamminger T. 2008. New insights into the role of the subnuclear structure ND10 for viral infection. Biochim. Biophys. Acta 1783: 2207-2221.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 3
    • 79955047081 scopus 로고    scopus 로고
    • Interplay between herpesvirus infection and host defense by PML nuclear bodies
    • Tavalai N, Stamminger T. 2009. Interplay between herpesvirus infection and host defense by PML nuclear bodies. Viruses 1:1240-1264.
    • (2009) Viruses , vol.1 , pp. 1240-1264
    • Tavalai, N.1    Stamminger, T.2
  • 4
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by humanAPOBEC3Gthrough lethal editing of nascent reverse transcripts
    • Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D. 2003. Broad antiretroviral defence by humanAPOBEC3Gthrough lethal editing of nascent reverse transcripts. Nature 424:99-103.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 5
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil SJ, Zang T, Bieniasz PD. 2008. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451:425-430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 6
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ, Kiessling M, Autissier P, Sodroski J. 2004. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 427:848-853.
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 7
    • 79952219169 scopus 로고    scopus 로고
    • Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against varicella-zoster virus
    • Reichelt M, Wang L, Sommer M, Perrino J, Nour AM, Sen N, Baiker A, Zerboni L, Arvin AM. 2011. Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against varicella-zoster virus. PLoS Pathog. 7:e1001266. doi:10.1371/journal.ppat.1001266.
    • (2011) PLoS Pathog , vol.7
    • Reichelt, M.1    Wang, L.2    Sommer, M.3    Perrino, J.4    Nour, A.M.5    Sen, N.6    Baiker, A.7    Zerboni, L.8    Arvin, A.M.9
  • 8
    • 81755166682 scopus 로고    scopus 로고
    • EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcription
    • Tsai K, Thikmyanova N, Wojcechowskyj JA, Delecluse HJ, Lieberman PM. 2011. EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcription. PLoS Pathog. 7:e1002376. doi:10.1371 /journal.ppat.1002376.
    • (2011) PLoS Pathog , vol.7
    • Tsai, K.1    Thikmyanova, N.2    Wojcechowskyj, J.A.3    Delecluse, H.J.4    Lieberman, P.M.5
  • 9
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett RD, Chelbi-Alix MK. 2007. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89:819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 10
    • 40149085109 scopus 로고    scopus 로고
    • Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100
    • Everett RD, Parada C, Gripon P, Sirma H, Orr A. 2008. Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100. J. Virol. 82:2661-2672.
    • (2008) J. Virol. , vol.82 , pp. 2661-2672
    • Everett, R.D.1    Parada, C.2    Gripon, P.3    Sirma, H.4    Orr, A.5
  • 11
    • 77950515413 scopus 로고    scopus 로고
    • Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx
    • Lukashchuk V, Everett RD. 2010. Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx. J. Virol. 84:4026-4040.
    • (2010) J. Virol. , vol.84 , pp. 4026-4040
    • Lukashchuk, V.1    Everett, R.D.2
  • 12
    • 34548159689 scopus 로고    scopus 로고
    • Human cytomegalovirus gene expression is silenced by Daxx-mediated intrinsic immune defense in model latent infections established in vitro
    • Saffert RT, Kalejta RF. 2007. Human cytomegalovirus gene expression is silenced by Daxx-mediated intrinsic immune defense in model latent infections established in vitro. J. Virol. 81:9109-9120.
    • (2007) J. Virol. , vol.81 , pp. 9109-9120
    • Saffert, R.T.1    Kalejta, R.F.2
  • 14
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi R, Pandolfi PP. 2007. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 8:1006-1016.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 15
    • 77449089538 scopus 로고    scopus 로고
    • A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
    • Van Damme E, Laukens K, Dang TH, Van Ostade X. 2010. A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics. Int. J. Biol. Sci. 6: 51-67.
    • (2010) Int. J. Biol. Sci. , vol.6 , pp. 51-67
    • Van Damme, E.1    Laukens, K.2    Dang, T.H.3    Van Ostade, X.4
  • 16
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul GG. 1998. Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 20:660-667.
    • (1998) Bioessays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 18
    • 16244422998 scopus 로고    scopus 로고
    • ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection
    • Everett RD, Murray J. 2005. ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J. Virol. 79:5078-5089.
    • (2005) J. Virol. , vol.79 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 19
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: dynamic sensors of DNA damage and cellular stress
    • Dellaire G, Bazett-Jones DP. 2004. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26:963-977.
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 20
    • 33845871732 scopus 로고    scopus 로고
    • Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus
    • Kumar PP, Bischof O, Purbey PK, Notani D, Urlaub H, Dejean A, Galande S. 2007. Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus. Nat. Cell Biol. 9:45-56.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 45-56
    • Kumar, P.P.1    Bischof, O.2    Purbey, P.K.3    Notani, D.4    Urlaub, H.5    Dejean, A.6    Galande, S.7
  • 21
    • 0037979238 scopus 로고    scopus 로고
    • PML colocalizes with and stabilizes theDNAdamage response protein TopBP1
    • Xu ZX, Timanova-Atanasova A, Zhao RX, Chang KS. 2003. PML colocalizes with and stabilizes theDNAdamage response protein TopBP1. Mol. Cell. Biol. 23:4247-4256.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4247-4256
    • Xu, Z.X.1    Timanova-Atanasova, A.2    Zhao, R.X.3    Chang, K.S.4
  • 22
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong S, Salomoni P, Pandolfi PP. 2000. The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2:E85-E90. doi:10.1038/35010583.
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 23
    • 33746406755 scopus 로고    scopus 로고
    • SP100B, a repressor of gene expression preferentially binds to DNA with unmethylated CpGs. J. Cell
    • Isaac A, Wilcox KW, Taylor JL. 2006. SP100B, a repressor of gene expression preferentially binds to DNA with unmethylated CpGs. J. Cell. Biochem. 98:1106-1122.
    • (2006) Biochem , vol.98 , pp. 1106-1122
    • Isaac, A.1    Wilcox, K.W.2    Taylor, J.L.3
  • 24
    • 0032560477 scopus 로고    scopus 로고
    • Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemiaassociated nuclear bodies and the chromatin compartment
    • Seeler JS, Marchio A, Sitterlin D, Transy C, Dejean A. 1998. Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemiaassociated nuclear bodies and the chromatin compartment. Proc. Natl. Acad. Sci. U. S. A. 95:7316-7321.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7316-7321
    • Seeler, J.S.1    Marchio, A.2    Sitterlin, D.3    Transy, C.4    Dejean, A.5
  • 25
    • 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 EJ, Chen JD. 2000. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell. Biol. 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
  • 26
    • 0037439945 scopus 로고    scopus 로고
    • RNAi reveals anti-apoptotic and transcriptionally repressive activities of DAXX
    • Michaelson JS, Leder P. 2003. RNAi reveals anti-apoptotic and transcriptionally repressive activities of DAXX. J. Cell Sci. 116:345-352.
    • (2003) J. Cell Sci. , vol.116 , pp. 345-352
    • Michaelson, J.S.1    Leder, P.2
  • 27
    • 80052408033 scopus 로고    scopus 로고
    • HIRA and Daxx constitute two independent histone H3 3-containing predeposition complexes
    • Elsaesser SJ, Allis CD. 2010. HIRA and Daxx constitute two independent histone H3.3-containing predeposition complexes. Cold Spring Harb. Symp. Quant. Biol. 75:27-34.
    • (2010) Cold Spring Harb. Symp. Quant. Biol. , vol.75 , pp. 27-34
    • Elsaesser, S.J.1    Allis, C.D.2
  • 28
    • 0037101953 scopus 로고    scopus 로고
    • Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek
    • Hollenbach AD, McPherson CJ, Mientjes EJ, Iyengar R, Grosveld G. 2002. Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J. Cell Sci. 115:3319-3330.
    • (2002) J. Cell Sci. , vol.115 , pp. 3319-3330
    • Hollenbach, A.D.1    McPherson, C.J.2    Mientjes, E.J.3    Iyengar, R.4    Grosveld, G.5
  • 29
    • 77956282773 scopus 로고    scopus 로고
    • Daxx is an H33-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
    • Lewis PW, Elsaesser SJ, Noh KM, Stadler SC, Allis CD. 2010. Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U. S. A. 107:14075-14080.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 14075-14080
    • Lewis, P.W.1    Elsaesser, S.J.2    Noh, K.M.3    Stadler, S.C.4    Allis, C.D.5
  • 31
    • 33744908280 scopus 로고    scopus 로고
    • Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression ofHCMV replication
    • Cantrell SR, Bresnahan WA. 2006. Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression ofHCMV replication. J. Virol. 80:6188-6191.
    • (2006) J. Virol. , vol.80 , pp. 6188-6191
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 32
    • 33646161949 scopus 로고    scopus 로고
    • Role of the cellular protein hDaxx in human cytomegalovirus immediate-early gene expression
    • Preston CM, Nicholl MJ. 2006. Role of the cellular protein hDaxx in human cytomegalovirus immediate-early gene expression. J. Gen. Virol. 87:1113-1121.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1113-1121
    • Preston, C.M.1    Nicholl, M.J.2
  • 33
    • 33845968505 scopus 로고    scopus 로고
    • Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter
    • Woodhall DL, Groves IJ, Reeves MB, Wilkinson G, Sinclair JH. 2006. Human Daxx-mediated repression of human cytomegalovirus gene expression correlates with a repressive chromatin structure around the major immediate early promoter. J. Biol. Chem. 281:37652-37660.
    • (2006) J. Biol. Chem , vol.281 , pp. 37652-37660
    • Woodhall, D.L.1    Groves, I.J.2    Reeves, M.B.3    Wilkinson, G.4    Sinclair, J.H.5
  • 34
    • 80052490932 scopus 로고    scopus 로고
    • Evidence for a dual antiviral role of the major nuclear domain 10 component Sp100 during the immediate-early and late phases of the human cytomegalovirus replication cycle
    • Tavalai N, Adler M, Scherer M, Riedl Y, Stamminger T. 2011. Evidence for a dual antiviral role of the major nuclear domain 10 component Sp100 during the immediate-early and late phases of the human cytomegalovirus replication cycle. J. Virol. 85:9447-9458.
    • (2011) J. Virol. , vol.85 , pp. 9447-9458
    • Tavalai, N.1    Adler, M.2    Scherer, M.3    Riedl, Y.4    Stamminger, T.5
  • 35
    • 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. 2006. Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J. Virol. 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
  • 36
    • 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. 2008. Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection. J. Virol. 82:126-137.
    • (2008) J. Virol. , vol.82 , pp. 126-137
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Stamminger, T.4
  • 37
    • 33746824547 scopus 로고    scopus 로고
    • Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein
    • Kang H, Kim ET, Lee HR, Park JJ, Go YY, Choi CY, Ahn JH. 2006. Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein. J. Gen. Virol. 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
  • 38
    • 80655143462 scopus 로고    scopus 로고
    • Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression
    • Kim YE, Lee JH, Kim ET, Shin HJ, Gu SY, Seol HS, Ling PD, Lee CH, Ahn JH. 2011. Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression. J. Virol. 85:11928-11937.
    • (2011) J. Virol. , vol.85 , pp. 11928-11937
    • Kim, Y.E.1    Lee, J.H.2    Kim, E.T.3    Shin, H.J.4    Gu, S.Y.5    Seol, H.S.6    Ling, P.D.7    Lee, C.H.8    Ahn, J.H.9
  • 39
    • 0030602019 scopus 로고    scopus 로고
    • The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1
    • Korioth F, Maul GG, Plachter B, Stamminger T, Frey J. 1996. The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1. Exp. Cell Res. 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
  • 40
    • 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. 1999. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73:5137-5143.
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 41
    • 0031922713 scopus 로고    scopus 로고
    • Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product
    • Wilkinson GW, Kelly C, Sinclair JH, Rickards C. 1998. Disruption of PML-associated nuclear bodies mediated by the human cytomegalovirus major immediate early gene product. J. Gen. Virol. 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
  • 42
    • 19944382805 scopus 로고    scopus 로고
    • Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediateearly gene expression and viral replication
    • Cantrell SR, Bresnahan WA. 2005. Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediateearly gene expression and viral replication. J. Virol. 79:7792-7802.
    • (2005) J. Virol. , vol.79 , pp. 7792-7802
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 43
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasomedependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix MK, de The H. 1999. Herpes virus induced proteasomedependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18:935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    de The, H.2
  • 44
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett RD, Freemont P, Saitoh H, Dasso M, Orr A, Kathoria M, Parkinson J. 1998. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:6581-6591.
    • (1998) 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
  • 45
    • 80055083504 scopus 로고    scopus 로고
    • The role of ICP0 in counteracting intrinsic cellular resistance to virus infection
    • Weller SK (ed), Caister Academic Press, Norfolk, United Kingdom
    • Everett RD. 2011. The role of ICP0 in counteracting intrinsic cellular resistance to virus infection, p 39-50. In Weller SK (ed), Alphaherpesviruses: molecular virology. Caister Academic Press, Norfolk, United Kingdom.
    • (2011) Alphaherpesviruses: molecular virology , pp. 39-50
    • Everett, R.D.1
  • 46
    • 65349171799 scopus 로고    scopus 로고
    • Analysis of the functions of herpes simplex virus type 1 regulatory protein ICP0 that are critical for lytic infection and derepression of quiescent viral genomes
    • Everett RD, Parsy ML, Orr A. 2009. Analysis of the functions of herpes simplex virus type 1 regulatory protein ICP0 that are critical for lytic infection and derepression of quiescent viral genomes. J. Virol. 83:4963-4977.
    • (2009) J. Virol. , vol.83 , pp. 4963-4977
    • Everett, R.D.1    Parsy, M.L.2    Orr, A.3
  • 47
    • 1242342140 scopus 로고    scopus 로고
    • Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1
    • Hagglund R, Roizman B. 2004. Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1. J. Virol. 78:2169-2178.
    • (2004) J. Virol. , vol.78 , pp. 2169-2178
    • Hagglund, R.1    Roizman, B.2
  • 48
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • Everett RD, Rechter S, Papior P, Tavalai N, Stamminger T, Orr A. 2006. PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80:7995-8005.
    • (2006) J. Virol. , vol.80 , pp. 7995-8005
    • Everett, R.D.1    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 49
    • 79959290376 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100
    • Adler M, Tavalai N, Muller R, Stamminger T. 2011. Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100. J. Gen. Virol. 92:1532-1538.
    • (2011) J. Gen. Virol. , vol.92 , pp. 1532-1538
    • Adler, M.1    Tavalai, N.2    Muller, R.3    Stamminger, T.4
  • 51
    • 0022978685 scopus 로고
    • Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110
    • Stow ND, Stow EC. 1986. Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110. J. Gen. Virol. 67:2571-2585.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2571-2585
    • Stow, N.D.1    Stow, E.C.2
  • 52
    • 0018337950 scopus 로고
    • Control of herpes simplex virus type 1 mRNA synthesis in cells infected with wild-type virus or the temperature-sensitive mutant tsK
    • Preston CM. 1979. Control of herpes simplex virus type 1 mRNA synthesis in cells infected with wild-type virus or the temperature-sensitive mutant tsK. J. Virol. 29:275-284.
    • (1979) J. Virol. , vol.29 , pp. 275-284
    • Preston, C.M.1
  • 53
    • 0030801241 scopus 로고    scopus 로고
    • Repression of gene expression upon infection of cells with herpes simplex virus type 1 mutants impaired for immediate-early protein synthesis
    • Preston CM, Nicholl MJ. 1997. Repression of gene expression upon infection of cells with herpes simplex virus type 1 mutants impaired for immediate-early protein synthesis. J. Virol. 71:7807-7813.
    • (1997) J. Virol. , vol.71 , pp. 7807-7813
    • Preston, C.M.1    Nicholl, M.J.2
  • 54
    • 0842347715 scopus 로고    scopus 로고
    • Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0
    • Everett RD, Boutell C, Orr A. 2004. Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0. J. Virol. 78:1763-1774.
    • (2004) J. Virol. , vol.78 , pp. 1763-1774
    • Everett, R.D.1    Boutell, C.2    Orr, A.3
  • 55
    • 79955541111 scopus 로고    scopus 로고
    • Interaction of the human cytomegalovirus particle with the host cell induces hypoxiainducible factor 1 alpha
    • McFarlane S, Nicholl MJ, Sutherland JS, Preston CM. 2011. Interaction of the human cytomegalovirus particle with the host cell induces hypoxiainducible factor 1 alpha. Virology 414:83-90.
    • (2011) Virology , vol.414 , pp. 83-90
    • McFarlane, S.1    Nicholl, M.J.2    Sutherland, J.S.3    Preston, C.M.4
  • 57
    • 0029045486 scopus 로고
    • Quiescent viral genomes in human fibroblasts after infection with herpes simplex virus type 1 Vmw65 mutants
    • Jamieson DR, Robinson LH, Daksis JI, Nicholl MJ, Preston CM. 1995. Quiescent viral genomes in human fibroblasts after infection with herpes simplex virus type 1 Vmw65 mutants. J. Gen. Virol. 76:1417-1431.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1417-1431
    • Jamieson, D.R.1    Robinson, L.H.2    Daksis, J.I.3    Nicholl, M.J.4    Preston, C.M.5
  • 58
    • 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 HH, Szostecki C, Schroder P, Matschl U, Jensen K, Luders C, Will H, Sternsdorf T. 1999. Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif. J. Cell Sci. 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
  • 60
    • 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
    • Everett RD, Sourvinos G, Leiper C, Clements JB, Orr A. 2004. 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. 78:1903-1917.
    • (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
  • 62
    • 0029102140 scopus 로고
    • An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1
    • Yao F, Schaffer PA. 1995. An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1. J. Virol. 69:6249-6258.
    • (1995) J. Virol. , vol.69 , pp. 6249-6258
    • Yao, F.1    Schaffer, P.A.2
  • 63
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMOtargeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • Boutell C, Cuchet-Lourenco D, Vanni E, Orr A, Glass M, McFarlane S, Everett RD. 2011. A viral ubiquitin ligase has substrate preferential SUMOtargeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS Pathog. 7:e1002245. doi:10.1371/journal.ppat.1002245.
    • (2011) PLoS Pathog , vol.7
    • Boutell, C.1    Cuchet-Lourenco, D.2    Vanni, E.3    Orr, A.4    Glass, M.5    McFarlane, S.6    Everett, R.D.7
  • 65
    • 79959848568 scopus 로고    scopus 로고
    • The intrinsic antiviral defense to incoming HSV-1 genomes includes specificDNArepair proteins and is counteracted by the viral protein ICP0
    • Lilley CE, Chaurushiya MS, Boutell C, Everett RD, Weitzman MD. 2011. The intrinsic antiviral defense to incoming HSV-1 genomes includes specificDNArepair proteins and is counteracted by the viral protein ICP0. PLoS Pathog. 7:e1002084. doi:10.1371/journal.ppat.1002084.
    • (2011) PLoS Pathog , vol.7
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Everett, R.D.4    Weitzman, M.D.5
  • 67
    • 35448980849 scopus 로고    scopus 로고
    • Reactivation of expression from quiescent herpes simplex virus type 1 genomes in the absence of immediate-early protein ICP0
    • Preston CM. 2007. Reactivation of expression from quiescent herpes simplex virus type 1 genomes in the absence of immediate-early protein ICP0. J. Virol. 81:11781-11789.
    • (2007) J. Virol. , vol.81 , pp. 11781-11789
    • Preston, C.M.1
  • 68
    • 10644281037 scopus 로고    scopus 로고
    • Human cytomegalovirus tegument protein pp71 directs long-term gene expression from quiescent herpes simplex virus genomes
    • Preston CM, Nicholl MJ. 2005. Human cytomegalovirus tegument protein pp71 directs long-term gene expression from quiescent herpes simplex virus genomes. J. Virol. 79:525-535.
    • (2005) J. Virol. , vol.79 , pp. 525-535
    • Preston, C.M.1    Nicholl, M.J.2
  • 69
    • 57349108706 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection
    • Lukashchuk V, McFarlane S, Everett RD, Preston CM. 2008. Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection. J. Virol. 82: 12543-12554.
    • (2008) J. Virol. , vol.82 , pp. 12543-12554
    • Lukashchuk, V.1    McFarlane, S.2    Everett, R.D.3    Preston, C.M.4
  • 70
    • 0030912888 scopus 로고    scopus 로고
    • The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PMLassociated nuclear bodies at very early times in infected permissive cells
    • Ahn JH, Hayward GS. 1997. The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PMLassociated nuclear bodies at very early times in infected permissive cells. J. Virol. 71:4599-4613.
    • (1997) J. Virol. , vol.71 , pp. 4599-4613
    • Ahn, J.H.1    Hayward, G.S.2
  • 71
    • 2642574870 scopus 로고    scopus 로고
    • Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells
    • Lee HR, Kim DJ, Lee JM, Choi CY, Ahn BY, Hayward GS, Ahn JH. 2004. Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells. J. Virol. 78: 6527-6542.
    • (2004) 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
  • 72
    • 0035124377 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies
    • Adamson AL, Kenney S. 2001. Epstein-Barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies. J. Virol. 75:2388-2399.
    • (2001) J. Virol. , vol.75 , pp. 2388-2399
    • Adamson, A.L.1    Kenney, S.2
  • 73
    • 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 PM, Maul GG. 2000. Lytic but not latent replication of Epstein-Barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins. J. Virol. 74:11800-11810.
    • (2000) J. Virol. , vol.74 , pp. 11800-11810
    • Bell, P.1    Lieberman, P.M.2    Maul, G.G.3
  • 74
    • 49149094503 scopus 로고    scopus 로고
    • Murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PML and is essential for production of infectious virus
    • Ling PD, Tan J, Sewatanon J, Peng R. 2008. Murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PML and is essential for production of infectious virus. J. Virol. 82:8000-8012.
    • (2008) J. Virol. , vol.82 , pp. 8000-8012
    • Ling, P.D.1    Tan, J.2    Sewatanon, J.3    Peng, R.4
  • 75
    • 84861303373 scopus 로고    scopus 로고
    • Herpesvirus saimiri antagonizes nuclear domain 10-instituted intrinsic immunity via an ORF3-mediated selective degradation of cellular protein Sp100
    • Full F, Reuter N, Zielke K, Stamminger T, Ensser A. 2012. Herpesvirus saimiri antagonizes nuclear domain 10-instituted intrinsic immunity via an ORF3-mediated selective degradation of cellular protein Sp100. J. Virol. 86:3541-3553.
    • (2012) J. Virol. , vol.86 , pp. 3541-3553
    • Full, F.1    Reuter, N.2    Zielke, K.3    Stamminger, T.4    Ensser, A.5
  • 76
    • 84869025216 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation
    • Cuchet-Lourenco D, Vanni E, Glass M, Orr A, Everett RD. 2012. Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation. J. Virol. 86:11209-11222.
    • (2012) J. Virol. , vol.86 , pp. 11209-11222
    • Cuchet-Lourenco, D.1    Vanni, E.2    Glass, M.3    Orr, A.4    Everett, R.D.5
  • 77
    • 0032534802 scopus 로고    scopus 로고
    • A viral activator of gene expression functions via the ubiquitin-proteasome pathway
    • Everett RD, Orr A, Preston CM. 1998. A viral activator of gene expression functions via the ubiquitin-proteasome pathway. EMBO J. 17:7161-7169.
    • (1998) EMBO J , vol.17 , pp. 7161-7169
    • Everett, R.D.1    Orr, A.2    Preston, C.M.3
  • 78
    • 80052341054 scopus 로고    scopus 로고
    • Disruption of PML nuclear bodies is mediated by ORF61 SUMOinteracting motifs and required for varicella-zoster virus pathogenesis in skin
    • Wang L, Oliver SL, Sommer M, Rajamani J, Reichelt M, Arvin AM. 2011. Disruption of PML nuclear bodies is mediated by ORF61 SUMOinteracting motifs and required for varicella-zoster virus pathogenesis in skin. PLoS Pathog. 7:e1002157. doi:10.1371/journal.ppat.1002157.
    • (2011) PLoS Pathog , vol.7
    • Wang, L.1    Oliver, S.L.2    Sommer, M.3    Rajamani, J.4    Reichelt, M.5    Arvin, A.M.6
  • 79
    • 35148893559 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts
    • Everett RD, Murray J, Orr A, Preston CM. 2007. Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts. J. Virol. 81:10991-11004.
    • (2007) J. Virol. , vol.81 , pp. 10991-11004
    • Everett, R.D.1    Murray, J.2    Orr, A.3    Preston, C.M.4
  • 80
    • 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
    • Catez F, Picard C, Held K, Gross S, Rousseau A, Theil D, Sawtell N, Labetoulle M, Lomonte P. 2012. HSV-1 genome subnuclear positioning and associations with host-cell PML-NBs and centromeres regulate LAT locus transcription during latency in neurons. PLoS Pathog. 8:e1002852. doi:10.1371/journal.ppat.1002852.
    • (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
  • 81
    • 80054057670 scopus 로고    scopus 로고
    • Severe viral infections and primary immunodeficiencies
    • Dropulic LK, Cohen JI. 2011. Severe viral infections and primary immunodeficiencies. Clin. Infect. Dis. 53:897-909.
    • (2011) Clin. Infect. Dis. , vol.53 , pp. 897-909
    • Dropulic, L.K.1    Cohen, J.I.2
  • 82
    • 80054773903 scopus 로고    scopus 로고
    • Human herpes virus 8 in solid organ transplantation
    • Ariza-Heredia EJ, Razonable RR. 2011. Human herpes virus 8 in solid organ transplantation. Transplantation 92:837-844.
    • (2011) Transplantation , vol.92 , pp. 837-844
    • Ariza-Heredia, E.J.1    Razonable, R.R.2
  • 84
    • 80054064328 scopus 로고    scopus 로고
    • Slipping and sliding: frameshift mutations in herpes simplex virus thymidine kinase and drug-resistance
    • Griffiths A. 2011. Slipping and sliding: frameshift mutations in herpes simplex virus thymidine kinase and drug-resistance. Drug Resist. Updat. 14:251-259.
    • (2011) Drug Resist. Updat. , vol.14 , pp. 251-259
    • Griffiths, A.1
  • 85
    • 77954541853 scopus 로고    scopus 로고
    • Cytomegalovirus infection/disease after hematopoietic stem cell transplantation
    • Mori T, Kato J. 2010. Cytomegalovirus infection/disease after hematopoietic stem cell transplantation. Int. J. Hematol. 91:588-595.
    • (2010) Int. J. Hematol. , vol.91 , pp. 588-595
    • Mori, T.1    Kato, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.