메뉴 건너뛰기




Volumn 84, Issue 9, 2010, Pages 4383-4394

Sumoylation of the Epstein-Barr virus BZLF1 protein inhibits its transcriptional activity and is regulated by the virus-encoded protein kinase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; IMMEDIATE EARLY PROTEIN BZLF1; PROTEIN KINASE; SUMO 1 PROTEIN; SUMO 2 PROTEIN; THREONINE;

EID: 77950811209     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02369-09     Document Type: Article
Times cited : (50)

References (78)
  • 1
    • 24344466952 scopus 로고    scopus 로고
    • Effects of SUMO-1 upon Epstein-Barr virus BZLF1 function and BMRF1 expression
    • Adamson, A. L. 2005. Effects of SUMO-1 upon Epstein-Barr virus BZLF1 function and BMRF1 expression. Biochem. Biophys. Res. Commun. 336:22-28.
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 22-28
    • Adamson, A.L.1
  • 2
    • 0035124377 scopus 로고    scopus 로고
    • Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies
    • Adamson, A. L., and S. Kenney. 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
  • 3
    • 0032506210 scopus 로고    scopus 로고
    • Rescue of the Epstein-Barr virus BZLF1 mutant, Z(S186A), early gene activation defect by the BRLF1 gene product
    • Adamson, A. L., and S. C. Kenney. 1998. Rescue of the Epstein-Barr virus BZLF1 mutant, Z(S186A), early gene activation defect by the BRLF1 gene product. Virology 251:187-197.
    • (1998) Virology , vol.251 , pp. 187-197
    • Adamson, A.L.1    Kenney, S.C.2
  • 4
    • 0035082279 scopus 로고    scopus 로고
    • Evaluation of interactions of human cytomegalovirus immediate-early IE2 regulatory protein with small ubiquitin-like modifiers and their conjugation enzyme Ubc9
    • Ahn, J. H., Y. Xu, W. J. Jang, M. J. Matunis, and G. S. Hayward. 2001. Evaluation of interactions of human cytomegalovirus immediate-early IE2 regulatory protein with small ubiquitin-like modifiers and their conjugation enzyme Ubc9. J. Virol. 75:3859-3872.
    • (2001) J. Virol. , vol.75 , pp. 3859-3872
    • Ahn, J.H.1    Xu, Y.2    Jang, W.J.3    Matunis, M.J.4    Hayward, G.S.5
  • 6
    • 67849088972 scopus 로고    scopus 로고
    • Epstein-Barr virus protein kinase BGLF4 interacts with viral transactivator BZLF1 and regulates its transactivation activity
    • Asai, R., A. Kato, and Y. Kawaguchi. 2009. Epstein-Barr virus protein kinase BGLF4 interacts with viral transactivator BZLF1 and regulates its transactivation activity. J. Gen. Virol. 90:1575-1581.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1575-1581
    • Asai, R.1    Kato, A.2    Kawaguchi, Y.3
  • 7
    • 19544380887 scopus 로고    scopus 로고
    • Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization
    • Beech, S. J., K. J. Lethbridge, N. Killick, N. McGlincy, and K. N. Leppard. 2005. Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization. Exp. Cell Res. 307:109-117.
    • (2005) Exp. Cell Res. , vol.307 , pp. 109-117
    • Beech, S.J.1    Lethbridge, K.J.2    Killick, N.3    McGlincy, N.4    Leppard, K.N.5
  • 8
    • 19944397140 scopus 로고    scopus 로고
    • BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186
    • Bhende, P. M., W. T. Seaman, H. J. Delecluse, and S. C. Kenney. 2005. BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186. J. Virol. 79:7338-7348.
    • (2005) J. Virol. , vol.79 , pp. 7338-7348
    • Bhende, P.M.1    Seaman, W.T.2    Delecluse, H.J.3    Kenney, S.C.4
  • 9
    • 6944244957 scopus 로고    scopus 로고
    • The EBV lytic switch protein, Z, preferentially binds to and activates the methylated viral genome
    • Bhende, P. M., W. T. Seaman, H. J. Delecluse, and S. C. Kenney. 2004. The EBV lytic switch protein, Z, preferentially binds to and activates the methylated viral genome. Nat. Genet. 36:1099-1104.
    • (2004) Nat. Genet. , vol.36 , pp. 1099-1104
    • Bhende, P.M.1    Seaman, W.T.2    Delecluse, H.J.3    Kenney, S.C.4
  • 10
    • 50149091508 scopus 로고    scopus 로고
    • The Epstein-Barr virus LF2 protein inhibits viral replication
    • Calderwood, M. A., A. M. Holthaus, and E. Johannsen. 2008. The Epstein-Barr virus LF2 protein inhibits viral replication. J. Virol. 82:8509-8519.
    • (2008) J. Virol. , vol.82 , pp. 8509-8519
    • Calderwood, M.A.1    Holthaus, A.M.2    Johannsen, E.3
  • 11
    • 0030011018 scopus 로고    scopus 로고
    • 1 cell cycle arrest through induction of cyclin-dependent kinase inhibitors
    • Cayrol, C., and E. K. Flemington. 1996. The Epstein-Barr virus bZIP transcription factor Zta causes G0/G1 cell cycle arrest through induction of cyclin-dependent kinase inhibitors. EMBO J. 15:2748-2759. (Pubitemid 26176252)
    • (1996) EMBO Journal , vol.15 , Issue.11 , pp. 2748-2759
    • Cayrol, C.1    Flemington, E.K.2
  • 13
    • 0025290086 scopus 로고
    • The Epstein-Barr virus Zta transactivator: A member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif
    • Chang, Y. N., D. L. Dong, G. S. Hayward, and S. D. Hayward. 1990. The Epstein-Barr virus Zta transactivator: a member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif. J. Virol. 64:3358-3369.
    • (1990) J. Virol. , vol.64 , pp. 3358-3369
    • Chang, Y.N.1    Dong, D.L.2    Hayward, G.S.3    Hayward, S.D.4
  • 14
    • 0034011617 scopus 로고    scopus 로고
    • A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro
    • Chen, M. R., S. J. Chang, H. Huang, and J. Y. Chen. 2000. A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro. J. Virol. 74:3093-3104.
    • (2000) J. Virol. , vol.74 , pp. 3093-3104
    • Chen, M.R.1    Chang, S.J.2    Huang, H.3    Chen, J.Y.4
  • 15
    • 0023036072 scopus 로고
    • Both Epstein-Barr virus (EBV)-encoded trans-acting factors, EB1 and EB2, are required to activate transcription from an EBV early promoter
    • Chevallier-Greco, A., E. Manet, P. Chavrier, C. Mosnier, J. Daillie, and A. Sergeant. 1986. Both Epstein-Barr virus (EBV)-encoded trans-acting factors, EB1 and EB2, are required to activate transcription from an EBV early promoter. EMBO J. 5:3243-3249.
    • (1986) EMBO J. , vol.5 , pp. 3243-3249
    • Chevallier-Greco, A.1    Manet, E.2    Chavrier, P.3    Mosnier, C.4    Daillie, J.5    Sergeant, A.6
  • 16
    • 0023503201 scopus 로고
    • Polymorphic proteins encoded within BZLF1 of defective and standard Epstein-Barr viruses disrupt latency
    • Countryman, J., H. Jenson, R. Seibl, H. Wolf, and G. Miller. 1987. Polymorphic proteins encoded within BZLF1 of defective and standard Epstein-Barr viruses disrupt latency. J. Virol. 61:3672-3679. (Pubitemid 18011461)
    • (1987) Journal of Virology , vol.61 , Issue.12 , pp. 3672-3679
    • Countryman, J.1    Jenson, H.2    Seibl, R.3    Wolf, H.4    Miller, G.5
  • 17
    • 1642457437 scopus 로고
    • Activation of expression of latent Epstein-Barr herpesvirus after gene transfer with a small cloned subfragment of heterogeneous viral DNA
    • Countryman, J., and G. Miller. 1985. Activation of expression of latent Epstein-Barr herpesvirus after gene transfer with a small cloned subfragment of heterogeneous viral DNA. Proc. Natl. Acad. Sci. USA 82:4085-4089.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4085-4089
    • Countryman, J.1    Miller, G.2
  • 18
    • 0034974152 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BRLF1 induces the lytic form of viral replication through a mechanism involving phosphatidylinositol-3 kinase activation
    • Darr, C. D., A. Mauser, and S. Kenney. 2001. Epstein-Barr virus immediate-early protein BRLF1 induces the lytic form of viral replication through a mechanism involving phosphatidylinositol-3 kinase activation. J. Virol. 75:6135-6142.
    • (2001) J. Virol. , vol.75 , pp. 6135-6142
    • Darr, C.D.1    Mauser, A.2    Kenney, S.3
  • 20
  • 22
    • 3142726432 scopus 로고    scopus 로고
    • Phosphorylation of Epstein-Barr virus ZEBRA protein at its casein kinase 2 sites mediates its ability to repress activation of a viral lytic cycle late gene by Rta
    • El-Guindy, A. S., and G. Miller. 2004. Phosphorylation of Epstein-Barr virus ZEBRA protein at its casein kinase 2 sites mediates its ability to repress activation of a viral lytic cycle late gene by Rta. J. Virol. 78:7634-7644.
    • (2004) J. Virol. , vol.78 , pp. 7634-7644
    • El-Guindy, A.S.1    Miller, G.2
  • 23
    • 33645642986 scopus 로고    scopus 로고
    • Identification of constitutive phosphorylation sites on the Epstein-Barr virus ZEBRA protein
    • El-Guindy, A. S., S. Y. Paek, J. Countryman, and G. Miller. 2006. Identification of constitutive phosphorylation sites on the Epstein-Barr virus ZEBRA protein. J. Biol. Chem. 281:3085-3095.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3085-3095
    • El-Guindy, A.S.1    Paek, S.Y.2    Countryman, J.3    Miller, G.4
  • 24
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • Everett, R. D., and M. K. Chelbi-Alix. 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
  • 25
    • 0024469056 scopus 로고
    • Epstein-Barr virus BZLF1 trans-activator specifically binds to a consensus AP-1 site and is related to c-fos
    • Farrell, P. J., D. T. Rowe, C. M. Rooney, and T. Kouzarides. 1989. Epstein-Barr virus BZLF1 trans-activator specifically binds to a consensus AP-1 site and is related to c-fos. EMBO J. 8:127-132.
    • (1989) EMBO J. , vol.8 , pp. 127-132
    • Farrell, P.J.1    Rowe, D.T.2    Rooney, C.M.3    Kouzarides, T.4
  • 26
    • 0034660443 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators
    • Feederle, R., M. Kost, M. Baumann, A. Janz, E. Drouet, W. Hammerschmidt, and H. J. Delecluse. 2000. The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators. EMBO J. 19:3080-3089. (Pubitemid 30386778)
    • (2000) EMBO Journal , vol.19 , Issue.12 , pp. 3080-3089
    • Feederle, R.1    Kost, M.2    Baumann, M.3    Janz, A.4    Drouet, E.5    Hammerschmidt, W.6    Delecluse, H.-J.7
  • 27
    • 35348896613 scopus 로고    scopus 로고
    • ZEB1 and c-Jun levels contribute to the establishment of highly lytic Epstein-Barr virus infection in gastric AGS cells
    • Feng, W. H., R. J. Kraus, S. J. Dickerson, H. J. Lim, R. J. Jones, X. Yu, J. E. Mertz, and S. C. Kenney. 2007. ZEB1 and c-Jun levels contribute to the establishment of highly lytic Epstein-Barr virus infection in gastric AGS cells. J. Virol. 81:10113-10122.
    • (2007) J. Virol. , vol.81 , pp. 10113-10122
    • Feng, W.H.1    Kraus, R.J.2    Dickerson, S.J.3    Lim, H.J.4    Jones, R.J.5    Yu, X.6    Mertz, J.E.7    Kenney, S.C.8
  • 28
    • 0025214570 scopus 로고
    • Autoregulation of Epstein-Barr virus putative lytic switch gene BZLF1
    • Flemington, E., and S. H. Speck. 1990. Autoregulation of Epstein-Barr virus putative lytic switch gene BZLF1. J. Virol. 64:1227-1232. (Pubitemid 20087761)
    • (1990) Journal of Virology , vol.64 , Issue.3 , pp. 1227-1232
    • Flemington, E.1    Speck, S.H.2
  • 29
    • 0025604607 scopus 로고
    • Evidence for coiled-coil dimer formation by an Epstein-Barr virus transactivator that lacks a heptad repeat of leucine residues
    • Flemington, E., and S. H. Speck. 1990. Evidence for coiled-coil dimer formation by an Epstein-Barr virus transactivator that lacks a heptad repeat of leucine residues. Proc. Natl. Acad. Sci. USA 87:9459-9463.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9459-9463
    • Flemington, E.1    Speck, S.H.2
  • 31
    • 7644240606 scopus 로고    scopus 로고
    • Expression and localization of the Epstein-Barr virus-encoded protein kinase
    • DOI 10.1128/JVI.78.22.12140-12146.2004
    • Gershburg, E., M. Marschall, K. Hong, and J. S. Pagano. 2004. Expression and localization of the Epstein-Barr virus-encoded protein kinase. J. Virol. 78:12140-12146. (Pubitemid 39458733)
    • (2004) Journal of Virology , vol.78 , Issue.22 , pp. 12140-12146
    • Gershburg, E.1    Marschall, M.2    Hong, K.3    Pagano, J.S.4
  • 32
    • 0036143222 scopus 로고    scopus 로고
    • Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the L-riboside benzimidazole 1263W94
    • Gershburg, E., and J. S. Pagano. 2002. Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the L-riboside benzimidazole 1263W94. J. Virol. 76:998-1003. (Pubitemid 34070632)
    • (2002) Journal of Virology , vol.76 , Issue.3 , pp. 998-1003
    • Gershburg, E.1    Pagano, J.S.2
  • 33
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman, C. M., L. F. Moffat, and B. H. Howard. 1982. Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol. Cell. Biol. 2:1044-1051.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 1044-1051
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 34
    • 0025666546 scopus 로고
    • The enhancer factor R of Epstein-Barr virus (EBV) is a sequence-specific DNA binding protein
    • Gruffat, H., E. Manet, A. Rigolet, and A. Sergeant. 1990. The enhancer factor R of Epstein-Barr virus (EBV) is a sequence-specific DNA binding protein. Nucleic Acids Res. 18:6835-6843. (Pubitemid 120006065)
    • (1990) Nucleic Acids Research , vol.18 , Issue.23 , pp. 6835-6843
    • Gruffat, H.1    Manet, E.2    Rigolet, A.3    Sergeant, A.4
  • 35
    • 0025286703 scopus 로고
    • Use of an immobilized enzyme and specific antibodies to analyse the accessibility and role of histone tails in chromatin structure
    • Hacques, M. F., S. Muller, G. De Murcia, M. H. Van Regenmortel, and C. Marion. 1990. Use of an immobilized enzyme and specific antibodies to analyse the accessibility and role of histone tails in chromatin structure. Biochem. Biophys. Res. Commun. 168:637-643.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 637-643
    • Hacques, M.F.1    Muller, S.2    De Murcia, G.3    Van Regenmortel, M.H.4    Marion, C.5
  • 36
    • 0023698910 scopus 로고
    • Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus
    • DOI 10.1016/0092-8674(88)90028-1
    • Hammerschmidt, W., and B. Sugden. 1988. Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus. Cell 55:427-433. (Pubitemid 18261432)
    • (1988) Cell , vol.55 , Issue.3 , pp. 427-433
    • Hammerschmidt, W.1    Sugden, B.2
  • 37
    • 0023889721 scopus 로고
    • A new Epstein-Barr virus transactivator, R, induces expression of a cytoplasmic early antigen
    • Hardwick, J. M., P. M. Lieberman, and S. D. Hayward. 1988. A new Epstein-Barr virus transactivator, R, induces expression of a cytoplasmic early antigen. J. Virol. 62:2274-2284.
    • (1988) J. Virol. , vol.62 , pp. 2274-2284
    • Hardwick, J.M.1    Lieberman, P.M.2    Hayward, S.D.3
  • 38
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R. T. 2005. SUMO: a history of modification. Mol. Cell 18:1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 39
    • 67649170780 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic cycle activator Zta interacts with methylated ZRE in the promoter of host target gene egr1
    • Heather, J., K. Flower, S. Isaac, and A. J. Sinclair. 2009. The Epstein-Barr virus lytic cycle activator Zta interacts with methylated ZRE in the promoter of host target gene egr1. J. Gen. Virol. 90:1450-1454.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1450-1454
    • Heather, J.1    Flower, K.2    Isaac, S.3    Sinclair, A.J.4
  • 40
    • 0343340071 scopus 로고    scopus 로고
    • Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b
    • DOI 10.1128/JVI.74.6.2510-2524.2000
    • Hofmann, H., S. Floss, and T. Stamminger. 2000. Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b. J. Virol. 74:2510-2524. (Pubitemid 30117560)
    • (2000) Journal of Virology , vol.74 , Issue.6 , pp. 2510-2524
    • Hofmann, H.1    Floss, S.2    Stamminger, T.3
  • 41
    • 2342520167 scopus 로고    scopus 로고
    • The BRRF1 early gene of Epstein-Barr virus encodes a transcription factor that enhances induction of lytic infection by BRLF1
    • Hong, G. K., H. J. Delecluse, H. Gruffat, T. E. Morrison, W. H. Feng, A. Sergeant, and S. C. Kenney. 2004. The BRRF1 early gene of Epstein-Barr virus encodes a transcription factor that enhances induction of lytic infection by BRLF1. J. Virol. 78:4983-4992.
    • (2004) J. Virol. , vol.78 , pp. 4983-4992
    • Hong, G.K.1    Delecluse, H.J.2    Gruffat, H.3    Morrison, T.E.4    Feng, W.H.5    Sergeant, A.6    Kenney, S.C.7
  • 42
    • 22544486295 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K-bZIP represses gene transcription via SUMO modification
    • DOI 10.1128/JVI.79.15.9912-9925.2005
    • Izumiya, Y., T. J. Ellison, E. T. Yeh, J. U. Jung, P. A. Luciw, and H. J. Kung. 2005. Kaposi's sarcoma-associated herpesvirus K-bZIP represses gene transcription via SUMO modification. J. Virol. 79:9912-9925. (Pubitemid 41022333)
    • (2005) Journal of Virology , vol.79 , Issue.15 , pp. 9912-9925
    • Izumiya, Y.1    Ellison, T.J.2    Yeh, E.T.H.3    Jung, J.U.4    Luciw, P.A.5    Kung, H.-J.6
  • 43
    • 33846629003 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-encoded protein kinase and its interaction with K-bZIP
    • DOI 10.1128/JVI.01473-06
    • Izumiya, Y., C. Izumiya, A. Van Geelen, D. H. Wang, K. S. Lam, P. A. Luciw, and H. J. Kung. 2007. Kaposi's sarcoma-associated herpesvirus-encoded protein kinase and its interaction with K-bZIP. J. Virol. 81:1072-1082. (Pubitemid 46170756)
    • (2007) Journal of Virology , vol.81 , Issue.3 , pp. 1072-1082
    • Izumiya, Y.1    Izumiya, C.2    Van Geelen, A.3    Wang, D.-H.4    Lam, K.S.5    Luciw, P.A.6    Kung, H.-J.7
  • 44
    • 49349094196 scopus 로고    scopus 로고
    • The reversal of epigenetic silencing of the EBV genome is regulated by viral bZIP protein
    • Karlsson, Q. H., C. Schelcher, E. Verrall, C. Petosa, and A. J. Sinclair. 2008. The reversal of epigenetic silencing of the EBV genome is regulated by viral bZIP protein. Biochem. Soc. Trans. 36:637-639.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 637-639
    • Karlsson, Q.H.1    Schelcher, C.2    Verrall, E.3    Petosa, C.4    Sinclair, A.J.5
  • 45
    • 0024550905 scopus 로고
    • The Epstein-Barr virus (EBV) BZLF1 immediate-early gene product differentially affects latent versus productive EBV promoters
    • Kenney, S., J. Kamine, E. Holley-Guthrie, J. C. Lin, E. C. Mar, and J. Pagano. 1989. The Epstein-Barr virus (EBV) BZLF1 immediate-early gene product differentially affects latent versus productive EBV promoters. J. Virol. 63:1729-1736. (Pubitemid 19085987)
    • (1989) Journal of Virology , vol.63 , Issue.4 , pp. 1729-1736
    • Kenney, S.1    Kamine, J.2    Holley-Guthrie, E.H.3    Lin, J.-C.4    Mar, E.-C.5    Pagano, J.6
  • 46
    • 34250010253 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • 5th ed. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Kieff, E., and A. B. Rickinson. 2007. Epstein-Barr virus and its replication, p. 2603-2654. Fields virology, 5th ed. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields Virology , pp. 2603-2654
    • Kieff, E.1    Rickinson, A.B.2
  • 47
    • 11144245265 scopus 로고    scopus 로고
    • Terminal differentiation into plasma cells initiates the replicative cycle of Epstein-Barr virus in vivo
    • Laichalk, L. L., and D. A. Thorley-Lawson. 2005. Terminal differentiation into plasma cells initiates the replicative cycle of Epstein-Barr virus in vivo. J. Virol. 79:1296-1307.
    • (2005) J. Virol. , vol.79 , pp. 1296-1307
    • Laichalk, L.L.1    Thorley-Lawson, D.A.2
  • 48
    • 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., D. J. Kim, J. M. Lee, C. Y. Choi, B. Y. Ahn, G. S. Hayward, and J. H. Ahn. 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
  • 49
    • 0034881576 scopus 로고    scopus 로고
    • Interaction with the Epstein-Barr virus helicase targets Zta to DNA replication compartments
    • DOI 10.1128/JVI.75.18.8792-8802.2001
    • Liao, G., F. Y. Wu, and S. D. Hayward. 2001. Interaction with the Epstein-Barr virus helicase targets Zta to DNA replication compartments. J. Virol. 75:8792-8802. (Pubitemid 32768983)
    • (2001) Journal of Virology , vol.75 , Issue.18 , pp. 8792-8802
    • Liao, G.1    Wu, F.Y.2    Hayward, S.D.3
  • 50
    • 0025311439 scopus 로고
    • In vitro transcriptional activation, dimerization, and DNA-binding specificity of the Epstein-Barr virus Zta protein
    • Lieberman, P. M., and A. J. Berk. 1990. In vitro transcriptional activation, dimerization, and DNA-binding specificity of the Epstein-Barr virus Zta protein. J. Virol. 64:2560-2568.
    • (1990) J. Virol. , vol.64 , pp. 2560-2568
    • Lieberman, P.M.1    Berk, A.J.2
  • 51
    • 0025255970 scopus 로고
    • The zta transactivator involved in induction of lytic cycle gene expression in Epstein-Barr virus-infected lymphocytes binds to both AP-1 and ZRE sites in target promoter and enhancer regions
    • Lieberman, P. M., J. M. Hardwick, J. Sample, G. S. Hayward, and S. D. Hayward. 1990. The zta transactivator involved in induction of lytic cycle gene expression in Epstein-Barr virus-infected lymphocytes binds to both AP-1 and ZRE sites in target promoter and enhancer regions. J. Virol. 64:1143-1155.
    • (1990) J. Virol. , vol.64 , pp. 1143-1155
    • Lieberman, P.M.1    Hardwick, J.M.2    Sample, J.3    Hayward, G.S.4    Hayward, S.D.5
  • 52
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., C. Delphin, T. Guan, L. Gerace, and F. Melchior. 1997. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88:97-107. (Pubitemid 27180334)
    • (1997) Cell , vol.88 , Issue.1 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 53
    • 0036255961 scopus 로고    scopus 로고
    • Direct targeting of human cytomegalovirus protein kinase pUL97 by kinase inhibitors is a novel principle for antiviral therapy
    • Marschall, M., M. Stein-Gerlach, M. Freitag, R. Kupfer, M. van den Bogaard, and T. Stamminger. 2002. Direct targeting of human cytomegalovirus protein kinase pUL97 by kinase inhibitors is a novel principle for antiviral therapy. J. Gen. Virol. 83:1013-1023.
    • (2002) J. Gen. Virol. , vol.83 , pp. 1013-1023
    • Marschall, M.1    Stein-Gerlach, M.2    Freitag, M.3    Kupfer, R.4    Van Den Bogaard, M.5    Stamminger, T.6
  • 54
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M. J., E. Coutavas, and G. Blobel. 1996. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 55
    • 63149115965 scopus 로고    scopus 로고
    • Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation
    • McDonald, C. M., C. Petosa, and P. J. Farrell. 2009. Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation. J. Virol. 83:3397-3401.
    • (2009) J. Virol. , vol.83 , pp. 3397-3401
    • McDonald, C.M.1    Petosa, C.2    Farrell, P.J.3
  • 56
    • 0141856355 scopus 로고    scopus 로고
    • The gammaherpesvirus 68 latency-associated nuclear antigen homolog is critical for the establishment of splenic latency
    • Moorman, N. J., D. O. Willer, and S. H. Speck. 2003. The gammaherpesvirus 68 latency-associated nuclear antigen homolog is critical for the establishment of splenic latency. J. Virol. 77:10295-10303.
    • (2003) J. Virol. , vol.77 , pp. 10295-10303
    • Moorman, N.J.1    Willer, D.O.2    Speck, S.H.3
  • 57
    • 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
    • Müller, S., and A. Dejean. 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. (Pubitemid 29246776)
    • (1999) Journal of Virology , vol.73 , Issue.6 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 58
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • DOI 10.1093/emboj/17.1.61
    • Müller, S., M. J. Matunis, and A. Dejean. 1998. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17:61-70. (Pubitemid 28041048)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 59
    • 0037069336 scopus 로고    scopus 로고
    • Glycoprotein gp110 of Epstein-Barr virus determines viral tropism and efficiency of infection
    • Neuhierl, B., R. Feederle, W. Hammerschmidt, and H. J. Delecluse. 2002. Glycoprotein gp110 of Epstein-Barr virus determines viral tropism and efficiency of infection. Proc. Natl. Acad. Sci. USA 99:15036-15041.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15036-15041
    • Neuhierl, B.1    Feederle, R.2    Hammerschmidt, W.3    Delecluse, H.J.4
  • 60
    • 3142732205 scopus 로고    scopus 로고
    • SUMOylation of the human cytomegalovirus 72-kilodalton IE1 protein facilitates expression of the 86-kilodalton IE2 protein and promotes viral replication
    • DOI 10.1128/JVI.78.14.7803-7812.2004
    • Nevels, M., W. Brune, and T. Shenk. 2004. SUMOylation of the human cytomegalovirus 72-kilodalton IE1 protein facilitates expression of the 86-kilodalton IE2 protein and promotes viral replication. J. Virol. 78:7803-7812. (Pubitemid 38915926)
    • (2004) Journal of Virology , vol.78 , Issue.14 , pp. 7803-7812
    • Nevels, M.1    Brune, W.2    Shenk, T.3
  • 61
    • 65849402960 scopus 로고    scopus 로고
    • SUMOylation of DRIL1 directs its transcriptional activity towards leukocyte lineage-specific genes
    • Prieur, A., K. Nacerddine, M. van Lohuizen, and D. S. Peeper. 2009. SUMOylation of DRIL1 directs its transcriptional activity towards leukocyte lineage-specific genes. PLoS One 4:e5542.
    • (2009) PLoS One , vol.4
    • Prieur, A.1    Nacerddine, K.2    Van Lohuizen, M.3    Peeper, D.S.4
  • 62
    • 0031694397 scopus 로고    scopus 로고
    • The Epstein-Barr virus Rta protein activates lytic cycle genes and can disrupt latency in B lymphocytes
    • Ragoczy, T., L. Heston, and G. Miller. 1998. The Epstein-Barr virus Rta protein activates lytic cycle genes and can disrupt latency in B lymphocytes. J. Virol. 72:7978-7984. (Pubitemid 28421790)
    • (1998) Journal of Virology , vol.72 , Issue.10 , pp. 7978-7984
    • Ragoczy, T.1    Heston, L.2    Miller, G.3
  • 63
    • 0030971868 scopus 로고    scopus 로고
    • Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix
    • Reyes, J. C., C. Muchardt, and M. Yaniv. 1997. Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J. Cell Biol. 137:263-274.
    • (1997) J. Cell Biol. , vol.137 , pp. 263-274
    • Reyes, J.C.1    Muchardt, C.2    Yaniv, M.3
  • 64
    • 34249064632 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Rickinson, A. B., and E. Kieff. 2006. Epstein-Barr virus, p. 2655-2700. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2006) Fields Virology , pp. 2655-2700
    • Rickinson, A.B.1    Kieff, E.2
  • 65
    • 0024379416 scopus 로고
    • The spliced BZLF1 gene of Epstein-Barr virus (EBV) transactivates an early EBV promoter and induces the virus productive cycle
    • Rooney, C. M., D. T. Rowe, T. Ragot, and P. J. Farrell. 1989. The spliced BZLF1 gene of Epstein-Barr virus (EBV) transactivates an early EBV promoter and induces the virus productive cycle. J. Virol. 63:3109-3116.
    • (1989) J. Virol. , vol.63 , pp. 3109-3116
    • Rooney, C.M.1    Rowe, D.T.2    Ragot, T.3    Farrell, P.J.4
  • 66
    • 0029861946 scopus 로고    scopus 로고
    • A replication function associated with the activation domain of the Epstein-Barr virus Zta transactivator
    • Sarisky, R. T., Z. Gao, P. M. Lieberman, E. D. Fixman, G. S. Hayward, and S. D. Hayward. 1996. A replication function associated with the activation domain of the Epstein-Barr virus Zta transactivator. J. Virol. 70:8340-8347.
    • (1996) J. Virol. , vol.70 , pp. 8340-8347
    • Sarisky, R.T.1    Gao, Z.2    Lieberman, P.M.3    Fixman, E.D.4    Hayward, G.S.5    Hayward, S.D.6
  • 67
    • 0027282974 scopus 로고
    • A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus
    • Schepers, A., D. Pich, and W. Hammerschmidt. 1993. A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus. EMBO J. 12:3921-3929. (Pubitemid 23282768)
    • (1993) EMBO Journal , vol.12 , Issue.10 , pp. 3921-3929
    • Schepers, A.1    Pich, D.2    Hammerschmidt, W.3
  • 68
    • 0027207953 scopus 로고
    • Cis-Acting elements in the lytic origin of DNA replication of Epstein- Barr virus
    • Schepers, A., D. Pich, J. Mankertz, and W. Hammerschmidt. 1993. cis-acting elements in the lytic origin of DNA replication of Epstein-Barr virus. J. Virol. 67:4237-4245. (Pubitemid 23180750)
    • (1993) Journal of Virology , vol.67 , Issue.7 , pp. 4237-4245
    • Schepers, A.1    Pich, D.2    Mankertz, J.3    Hammerschmidt, W.4
  • 69
    • 0032798391 scopus 로고    scopus 로고
    • Construction and transposon mutagenesis in Escherichia coli of a full-length infectious clone of pseudorabies virus, an alphaherpesvirus
    • Smith, G. A., and L. W. Enquist. 1999. Construction and transposon mutagenesis in Escherichia coli of a full-length infectious clone of pseudorabies virus, an alphaherpesvirus. J. Virol. 73:6405-6414.
    • (1999) J. Virol. , vol.73 , pp. 6405-6414
    • Smith, G.A.1    Enquist, L.W.2
  • 70
    • 0022646563 scopus 로고
    • Trans Activation of the latent Epstein-Barr virus (EBV) genome after transfection of the EBV DNA fragment
    • Takada, K., N. Shimizu, S. Sakuma, and Y. Ono. 1986. Trans-activation of the latent Epstein-Barr virus (EBV) genome after transfection of the EBV DNA fragment. J. Virol. 57:1016-1022. (Pubitemid 16143985)
    • (1986) Journal of Virology , vol.57 , Issue.3 , pp. 1016-1022
    • Takada, K.1    Shimizu, N.2    Sakuma, S.3    Ono, Y.4
  • 72
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • Yeh, E. T., L. Gong, and T. Kamitani. 2000. Ubiquitin-like proteins: new wines in new bottles. Gene 248:1-14.
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 73
    • 37849038673 scopus 로고    scopus 로고
    • ZEB1 regulates the latent-lytic switch in infection by Epstein-Barr virus
    • Yu, X., Z. Wang, and J. E. Mertz. 2007. ZEB1 regulates the latent-lytic switch in infection by Epstein-Barr virus. PLoS Pathog. 3:e194.
    • (2007) PLoS Pathog. , vol.3
    • Yu, X.1    Wang, Z.2    Mertz, J.E.3
  • 74
    • 0029830047 scopus 로고    scopus 로고
    • Epstein-Barr viral latency is disrupted by the immediate-early BRLF1 protein through a cell-specific mechanism
    • Zalani, S., E. Holley-Guthrie, and S. Kenney. 1996. Epstein-Barr viral latency is disrupted by the immediate-early BRLF1 protein through a cell-specific mechanism. Proc. Natl. Acad. Sci. USA 93:9194-9199.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9194-9199
    • Zalani, S.1    Holley-Guthrie, E.2    Kenney, S.3
  • 75
    • 0028268278 scopus 로고
    • Functional and physical interaction between p53 and BZLF1: Implications for Epstein-Barr virus latency
    • Zhang, Q., D. Gutsch, and S. Kenney. 1994. Functional and physical interaction between p53 and BZLF1: implications for Epstein-Barr virus latency. Mol. Cell. Biol. 14:1929-1938.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1929-1938
    • Zhang, Q.1    Gutsch, D.2    Kenney, S.3
  • 76
    • 0029931715 scopus 로고    scopus 로고
    • Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: Effects on EBV transcription and lytic replication
    • Zhang, Q., Y. Hong, D. Dorsky, E. Holley-Guthrie, S. Zalani, N. A. Elshiekh, A. Kiehl, T. Le, and S. Kenney. 1996. Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: effects on EBV transcription and lytic replication. J. Virol. 70:5131-5142. (Pubitemid 26240684)
    • (1996) Journal of Virology , vol.70 , Issue.8 , pp. 5131-5142
    • Zhang, Q.1    Hong, Y.2    Dorsky, D.3    Holley-Guthrie, E.4    Zalani, S.5    Elshiekh, N.A.6    Kiehl, A.7    Le, T.8    Kenney, S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.