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Volumn 84, Issue 9, 2010, Pages 4524-4533

Simian virus 40 T/t antigens and lamin A/C small interfering RNA rescue the phenotype of an Epstein-Barr virus protein kinase (BGLF4) mutant

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; SERUM RESPONSE FACTOR; TRANSCRIPTION FACTOR ELK 1;

EID: 77950805340     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02456-09     Document Type: Article
Times cited : (19)

References (63)
  • 1
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., J. Cohn, L. Buhle, and L. Gerace. 1986. The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323:560-564. (Pubitemid 16025383)
    • (1986) Nature , vol.323 , Issue.6088 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 2
    • 27944448894 scopus 로고    scopus 로고
    • Involvement of PP2A in viral and cellular transformation
    • Arroyo, J. D., and W. C. Hahn. 2005. Involvement of PP2A in viral and cellular transformation. Oncogene 24:7746-7755.
    • (2005) Oncogene , vol.24 , pp. 7746-7755
    • Arroyo, J.D.1    Hahn, W.C.2
  • 3
    • 33646737238 scopus 로고    scopus 로고
    • Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1
    • DOI 10.1128/JVI.02674-05
    • Asai, R., A. Kato, K. Kato, M. Kanamori-Koyama, K. Sugimoto, T. Sairenji, Y. Nishiyama, and Y. Kawaguchi. 2006. Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1. J. Virol. 80:5125-5134. (Pubitemid 43752758)
    • (2006) Journal of Virology , vol.80 , Issue.11 , pp. 5125-5134
    • Asai, R.1    Kato, A.2    Kato, K.3    Kanamori-Koyama, M.4    Sugimoto, K.5    Sairenji, T.6    Nishiyama, Y.7    Kawaguchi, Y.8
  • 4
    • 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
  • 5
    • 0021337583 scopus 로고
    • Transformation by purified early genes of simian virus 40
    • Chang, L. S., M. M. Pater, N. I. Hutchinson, and G. di Mayorca. 1984. Transformation by purified early genes of simian virus 40. Virology 133:341-353. (Pubitemid 14138018)
    • (1984) Virology , vol.133 , Issue.2 , pp. 341-353
    • Chang, L.-S.1    Pater, M.M.2    Hutchinson, N.I.3    Di Mayorca, G.4
  • 6
    • 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
  • 7
    • 34249876632 scopus 로고    scopus 로고
    • Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40
    • Chen, Y., Y. Xu, Q. Bao, Y. Xing, Z. Li, Z. Lin, J. B. Stock, P. D. Jeffrey, and Y. Shi. 2007. Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40. Nat. Struct. Mol. Biol. 14:527-534.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 527-534
    • Chen, Y.1    Xu, Y.2    Bao, Q.3    Xing, Y.4    Li, Z.5    Lin, Z.6    Stock, J.B.7    Jeffrey, P.D.8    Shi, Y.9
  • 10
    • 70350289948 scopus 로고    scopus 로고
    • The Epstein-Barr Virus protein kinase BGLF4 and the exonuclease BGLF5 have opposite effects on the regulation of viral protein production
    • Feederle, R., A. M. Mehl-Lautscham, H. Bannert, and H. J. Delecluse. 2009. The Epstein-Barr Virus protein kinase BGLF4 and the exonuclease BGLF5 have opposite effects on the regulation of viral protein production. J. Virol. 83:10877-10891.
    • (2009) J. Virol. , vol.83 , pp. 10877-10891
    • Feederle, R.1    Mehl-Lautscham, A.M.2    Bannert, H.3    Delecluse, H.J.4
  • 11
    • 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
  • 12
    • 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
  • 13
    • 34248339596 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus
    • DOI 10.1128/JVI.02398-06
    • Gershburg, E., S. Raffa, M. R. Torrisi, and J. S. Pagano. 2007. Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus. J. Virol. 81:5407-5412. (Pubitemid 46744449)
    • (2007) Journal of Virology , vol.81 , Issue.10 , pp. 5407-5412
    • Gershburg, E.1    Raffa, S.2    Torrisi, M.R.3    Pagano, J.S.4
  • 16
    • 0029871773 scopus 로고    scopus 로고
    • BK virus large T antigen: Interactions with the retinoblastoma family of tumor suppressor proteins and effects on cellular growth control
    • Harris, K. F., J. B. Christensen, and M. J. Imperiale. 1996. BK virus large T antigen: interactions with the retinoblastoma family of tumor suppressor proteins and effects on cellular growth control. J. Virol. 70:2378-2386.
    • (1996) J. Virol. , vol.70 , pp. 2378-2386
    • Harris, K.F.1    Christensen, J.B.2    Imperiale, M.J.3
  • 17
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin a that prevent nuclear lamina disassembly in mitosis
    • DOI 10.1016/0092-8674(90)90470-Y
    • Heald, R., and F. McKeon. 1990. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 61:579-589. (Pubitemid 20169014)
    • (1990) Cell , vol.61 , Issue.4 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 18
    • 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
  • 19
    • 67650511701 scopus 로고    scopus 로고
    • Phosphorylation of p27Kip1 by Epstein-Barr virus protein kinase induces its degradation through SCFSkp2 ubiquitin ligase actions during viral lytic replication
    • Iwahori, S., T. Murata, A. Kudoh, Y. Sato, S. Nakayama, H. Isomura, T. Kanda, and T. Tsurumi. 2009. Phosphorylation of p27Kip1 by Epstein-Barr virus protein kinase induces its degradation through SCFSkp2 ubiquitin ligase actions during viral lytic replication. J. Biol. Chem. 284:18923-18931.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18923-18931
    • Iwahori, S.1    Murata, T.2    Kudoh, A.3    Sato, Y.4    Nakayama, S.5    Isomura, H.6    Kanda, T.7    Tsurumi, T.8
  • 21
    • 0021716296 scopus 로고
    • In vitro mutagenesis of a putative DNA binding domain of SV40 large-T
    • Kalderon, D., and A. E. Smith. 1984. In vitro mutagenesis of a putative DNA binding domain of SV40 large-T. Virology 139:109-137.
    • (1984) Virology , vol.139 , pp. 109-137
    • Kalderon, D.1    Smith, A.E.2
  • 22
    • 0028021165 scopus 로고
    • Comparison of heterotrimeric protein phosphatase 2A containing different B subunits
    • Kamibayashi, C., R. Estes, R. L. Lickteig, S. I. Yang, C. Craft, and M. C. Mumby. 1994. Comparison of heterotrimeric protein phosphatase 2A containing different B subunits. J. Biol. Chem. 269:20139-20148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20139-20148
    • Kamibayashi, C.1    Estes, R.2    Lickteig, R.L.3    Yang, S.I.4    Craft, C.5    Mumby, M.C.6
  • 23
    • 70349730029 scopus 로고    scopus 로고
    • Human papillomavirus 16 E7 inactivator of retinoblastoma family proteins complements human cytomegalovirus lacking UL97 protein kinase
    • Kamil, J. P., A. J. Human, I. Jurak, K. Munger, R. F. Kalejta, and D. M. Coen. 2009. Human papillomavirus 16 E7 inactivator of retinoblastoma family proteins complements human cytomegalovirus lacking UL97 protein kinase. Proc. Natl. Acad. Sci. U. S. A. 106:16823-16828.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16823-16828
    • Kamil, J.P.1    Human, A.J.2    Jurak, I.3    Munger, K.4    Kalejta, R.F.5    Coen, D.M.6
  • 24
    • 17144468445 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded protein kinase BGLF4 mediates hyperphosphorylation of cellular elongation factor 1δ (EF-1delta): EF-1delta is universally modified by conserved protein kinases of herpesviruses in mammalian cells
    • Kato, K., Y. Kawaguchi, M. Tanaka, M. Igarashi, A. Yokoyama, G. Matsuda, M. Kanamori, K. Nakajima, Y. Nishimura, M. Shimojima, H. T. Phung, E. Takahashi, and K. Hirai. 2001. Epstein-Barr virus-encoded protein kinase BGLF4 mediates hyperphosphorylation of cellular elongation factor 1δ (EF-1delta): EF-1delta is universally modified by conserved protein kinases of herpesviruses in mammalian cells. J. Gen. Virol. 82:1457-1463.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1457-1463
    • Kato, K.1    Kawaguchi, Y.2    Tanaka, M.3    Igarashi, M.4    Yokoyama, A.5    Matsuda, G.6    Kanamori, M.7    Nakajima, K.8    Nishimura, Y.9    Shimojima, M.10    Phung, H.T.11    Takahashi, E.12    Hirai, K.13
  • 25
    • 0348013196 scopus 로고    scopus 로고
    • Identification of protein kinases responsible for phosphorylation of Epstein-Barr virus nuclear antigen leader protein at serine-35, which regulates its coactivator function
    • Kato, K., A. Yokoyama, Y. Tohya, H. Akashi, Y. Nishiyama, and Y. Kawaguchi. 2003. Identification of protein kinases responsible for phosphorylation of Epstein-Barr virus nuclear antigen leader protein at serine-35, which regulates its coactivator function. J. Gen. Virol. 84:3381-3392.
    • (2003) J. Gen. Virol. , vol.84 , pp. 3381-3392
    • Kato, K.1    Yokoyama, A.2    Tohya, Y.3    Akashi, H.4    Nishiyama, Y.5    Kawaguchi, Y.6
  • 26
    • 0037319965 scopus 로고    scopus 로고
    • Conserved protein kinases encoded by herpesviruses and cellular protein kinase cdc2 target the same phosphorylation site in eukaryotic elongation factor 1δ
    • DOI 10.1128/JVI.77.4.2359-2368.2003
    • Kawaguchi, Y., K. Kato, M. Tanaka, M. Kanamori, Y. Nishiyama, and Y. Yamanashi. 2003. Conserved protein kinases encoded by herpesviruses and cellular protein kinase cdc2 target the same phosphorylation site in eukaryotic elongation factor 1δ. J. Virol. 77:2359-2368. (Pubitemid 36222759)
    • (2003) Journal of Virology , vol.77 , Issue.4 , pp. 2359-2368
    • Kawaguchi, Y.1    Kato, K.2    Tanaka, M.3    Kanamori, M.4    Nishiyama, Y.5    Yamanashi, Y.6
  • 27
    • 0035656133 scopus 로고    scopus 로고
    • Interaction of SV40 large T antigen with components of the nucleo/cytoskeleton
    • Klawitz, I., U. Preuss, and K. H. Scheidtmann. 2001. Interaction of SV40 large T antigen with components of the nucleo/cytoskeleton. Int. J. Oncol. 19:1325-1332.
    • (2001) Int. J. Oncol. , vol.19 , pp. 1325-1332
    • Klawitz, I.1    Preuss, U.2    Scheidtmann, K.H.3
  • 28
    • 0037225808 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress
    • Krosky, P. M., M. C. Baek, and D. M. Coen. 2003. The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress. J. Virol. 77:905-914.
    • (2003) J. Virol. , vol.77 , pp. 905-914
    • Krosky, P.M.1    Baek, M.C.2    Coen, D.M.3
  • 29
    • 33749463157 scopus 로고    scopus 로고
    • Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication
    • DOI 10.1128/JVI.00678-06
    • Kudoh, A., T. Daikoku, Y. Ishimi, Y. Kawaguchi, N. Shirata, S. Iwahori, H. Isomura, and T. Tsurumi. 2006. Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication. J. Virol. 80:10064-10072. (Pubitemid 44522600)
    • (2006) Journal of Virology , vol.80 , Issue.20 , pp. 10064-10072
    • Kudoh, A.1    Daikoku, T.2    Ishimi, Y.3    Kawaguchi, Y.4    Shirata, N.5    Iwahori, S.6    Isomura, H.7    Tsurumi, T.8
  • 30
    • 0022347752 scopus 로고
    • Simian virus 40 replication in adenovirus-transformed human cells antagonizes gene expression
    • DOI 10.1038/317169a0
    • Lebkowski, J. S., S. Clancy, and M. P. Calos. 1985. Simian virus 40 replication in adenovirus-transformed human cells antagonizes gene expression. Nature 317:169-171. (Pubitemid 16243135)
    • (1985) Nature , vol.317 , Issue.6033 , pp. 169-171
    • Lebkowski, J.S.1    Clancy, S.2    Calos, M.P.3
  • 31
    • 34248354361 scopus 로고    scopus 로고
    • Epstein-Barr virus BGLF4 kinase induces premature chromosome condensation through activation of condensin and topoisomerase II
    • Lee, C. P., J. Y. Chen, J. T. Wang, K. Kimura, A. Takemoto, C. C. Lu, and M. R. Chen. 2007. Epstein-Barr virus BGLF4 kinase induces premature chromosome condensation through activation of condensin and topoisomerase II. J. Virol. 81:5166-5180.
    • (2007) J. Virol. , vol.81 , pp. 5166-5180
    • Lee, C.P.1    Chen, J.Y.2    Wang, J.T.3    Kimura, K.4    Takemoto, A.5    Lu, C.C.6    Chen, M.R.7
  • 32
    • 56449106108 scopus 로고    scopus 로고
    • Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production
    • Lee, C. P., Y. H. Huang, S. F. Lin, Y. Chang, Y. H. Chang, K. Takada, and M. R. Chen. 2008. Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production. J. Virol. 82:11913-11926.
    • (2008) J. Virol. , vol.82 , pp. 11913-11926
    • Lee, C.P.1    Huang, Y.H.2    Lin, S.F.3    Chang, Y.4    Chang, Y.H.5    Takada, K.6    Chen, M.R.7
  • 33
    • 0027976913 scopus 로고
    • The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein
    • Mancini, M. A., B. Shan, J. A. Nickerson, S. Penman, and W. H. Lee. 1994. The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein. Proc. Natl. Acad. Sci. U. S. A. 91:418-422.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 418-422
    • Mancini, M.A.1    Shan, B.2    Nickerson, J.A.3    Penman, S.4    Lee, W.H.5
  • 34
    • 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
  • 35
    • 77950850768 scopus 로고    scopus 로고
    • The Epstein-Barr virus (EBV)-encoded protein kinase, EBV-PK, but not the thymidine kinase (EBV-TK), is required for ganciclovir and acyclovir inhibition of lytic viral replication
    • Meng, Q., S. R. Hagemeier, J. D. Fingeroth, E. Gershberg, J. S. Pagano, and S. C. Kenney. 2010. The Epstein-Barr virus (EBV)-encoded protein kinase, EBV-PK, but not the thymidine kinase (EBV-TK), is required for ganciclovir and acyclovir inhibition of lytic viral replication. J. Virol. 84:4534-4542.
    • (2010) J. Virol. , vol.84 , pp. 4534-4542
    • Meng, Q.1    Hagemeier, S.R.2    Fingeroth, J.D.3    Gershberg, E.4    Pagano, J.S.5    Kenney, S.C.6
  • 37
    • 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
  • 38
    • 5344249316 scopus 로고    scopus 로고
    • BZLF1, an Epstein-Barr virus immediate-early protein, induces p65 nuclear translocation while inhibiting p65 transcriptional function
    • Morrison, T. E., and S. C. Kenney. 2004. BZLF1, an Epstein-Barr virus immediate-early protein, induces p65 nuclear translocation while inhibiting p65 transcriptional function. Virology 328:219-232.
    • (2004) Virology , vol.328 , pp. 219-232
    • Morrison, T.E.1    Kenney, S.C.2
  • 39
    • 34249939914 scopus 로고    scopus 로고
    • S3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells
    • DOI 10.1128/JVI.00380-07
    • Mou, F., T. Forest, and J. D. Baines. 2007. US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells. J. Virol. 81:6459-6470. (Pubitemid 46878051)
    • (2007) Journal of Virology , vol.81 , Issue.12 , pp. 6459-6470
    • Mou, F.1    Forest, T.2    Baines, J.D.3
  • 40
    • 49149090155 scopus 로고    scopus 로고
    • Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane
    • Mou, F., E. G. Wills, R. Park, and J. D. Baines. 2008. Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane. J. Virol. 82:8094-8104.
    • (2008) J. Virol. , vol.82 , pp. 8094-8104
    • Mou, F.1    Wills, E.G.2    Park, R.3    Baines, J.D.4
  • 42
    • 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. U. S. A. 99:15036-15041.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15036-15041
    • Neuhierl, B.1    Feederle, R.2    Hammerschmidt, W.3    Delecluse, H.J.4
  • 43
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter, M., J. Nakagawa, M. Doree, J. C. Labbe, and E. A. Nigg. 1990. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61:591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 44
    • 0033046766 scopus 로고    scopus 로고
    • The simian virus 40 small-t and large-T antigens jointly regulate cell cycle reentry in human fibroblasts
    • Porras, A., S. Gaillard, and K. Rundell. 1999. The simian virus 40 small-t and large-T antigens jointly regulate cell cycle reentry in human fibroblasts. J. Virol. 73:3102-3107. (Pubitemid 29135700)
    • (1999) Journal of Virology , vol.73 , Issue.4 , pp. 3102-3107
    • Porras, A.1    Gaillard, S.2    Rundell, K.3
  • 45
    • 0022895276 scopus 로고
    • The structure of the termini of the Epstein-Barr virus as a marker of clonal cellular proliferation
    • Raab-Traub, N., and K. Flynn. 1986. The structure of the termini of the Epstein-Barr virus as a marker of clonal cellular proliferation. Cell 47:883-889. (Pubitemid 17005061)
    • (1986) Cell , vol.47 , Issue.6 , pp. 883-889
    • Raab-Traub, N.1    Flynn, K.2
  • 46
    • 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
  • 47
    • 33845366594 scopus 로고    scopus 로고
    • Analysis of the structure-activity relationship of four herpesviral UL97 subfamily protein kinases reveals partial but not full functional conservation
    • Romaker, D., V. Schregel, K. Maurer, S. Auerochs, A. Marzi, H. Sticht, and M. Marschall. 2006. Analysis of the structure-activity relationship of four herpesviral UL97 subfamily protein kinases reveals partial but not full functional conservation. J. Med. Chem. 49:7044-7053.
    • (2006) J. Med. Chem. , vol.49 , pp. 7044-7053
    • Romaker, D.1    Schregel, V.2    Maurer, K.3    Auerochs, S.4    Marzi, A.5    Sticht, H.6    Marschall, M.7
  • 48
    • 0035100119 scopus 로고    scopus 로고
    • The role of the SV40 ST antigen in cell growth promotion and transformation
    • Rundell, K., and R. Parakati. 2001. The role of the SV40 ST antigen in cell growth promotion and transformation. Semin. Cancer Biol. 11:5-13.
    • (2001) Semin. Cancer Biol. , vol.11 , pp. 5-13
    • Rundell, K.1    Parakati, R.2
  • 49
    • 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
  • 50
    • 26444466028 scopus 로고    scopus 로고
    • Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection
    • DOI 10.1128/JVI.79.20.12840-12851.2005
    • Simpson-Holley, M., R. C. Colgrove, G. Nalepa, J. W. Harper, and D. M. Knipe. 2005. Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection. J. Virol. 79:12840-12851. (Pubitemid 41433203)
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 12840-12851
    • Simpson-Holley, M.1    Colgrove, R.C.2    Nalepa, G.3    Harper, J.W.4    Knipe, D.M.5
  • 51
    • 0034712723 scopus 로고    scopus 로고
    • A self-recombining bacterial artificial chromosome and its application for analysis of herpesvirus pathogenesis
    • Smith, G. A., and L. W. Enquist. 2000. A self-recombining bacterial artificial chromosome and its application for analysis of herpesvirus pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 97:4873-4878.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4873-4878
    • Smith, G.A.1    Enquist, L.W.2
  • 53
    • 0018747167 scopus 로고
    • Nucleotide sequence analysis of viable deletion mutants lacking segments of the Simian virus 40 genome coding for small t antigen
    • Thimmappaya, B., and T. Shenk. 1979. Nucleotide sequence analysis of viable deletion mutants lacking segments of the simian virus 40 genome coding for small t antigen. J. Virol. 30:668-673. (Pubitemid 9194307)
    • (1979) Journal of Virology , vol.30 , Issue.3 , pp. 668-673
    • Thimmappaya, B.1    Shenk, T.2
  • 54
    • 59649113242 scopus 로고    scopus 로고
    • Epstein-Barr virus BGLF4 kinase suppresses the interferon regulatory factor 3 signaling pathway
    • Wang, J. T., S. L. Doong, S. C. Teng, C. P. Lee, C. H. Tsai, and M. R. Chen. 2009. Epstein-Barr virus BGLF4 kinase suppresses the interferon regulatory factor 3 signaling pathway. J. Virol. 83:1856-1869.
    • (2009) J. Virol. , vol.83 , pp. 1856-1869
    • Wang, J.T.1    Doong, S.L.2    Teng, S.C.3    Lee, C.P.4    Tsai, C.H.5    Chen, M.R.6
  • 55
    • 28044472990 scopus 로고    scopus 로고
    • Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles
    • Wang, J. T., P. W. Yang, C. P. Lee, C. H. Han, C. H. Tsai, and M. R. Chen. 2005. Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles. J. Gen. Virol. 86:3215-3225.
    • (2005) J. Gen. Virol. , vol.86 , pp. 3215-3225
    • Wang, J.T.1    Yang, P.W.2    Lee, C.P.3    Han, C.H.4    Tsai, C.H.5    Chen, M.R.6
  • 56
    • 0025285068 scopus 로고
    • Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C
    • DOI 10.1016/0092-8674(90)90469-U
    • Ward, G. E., and M. W. Kirschner. 1990. Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C. Cell 61:561-577. (Pubitemid 20169013)
    • (1990) Cell , vol.61 , Issue.4 , pp. 561-577
    • Ward, G.E.1    Kirschner, M.W.2
  • 58
    • 45549092198 scopus 로고    scopus 로고
    • Effect of phosphorylation on the transactivation activity of Epstein-Barr virus BMRF1, a major target of the viral BGLF4 kinase
    • Yang, P. W., S. S. Chang, C. H. Tsai, Y. H. Chao, and M. R. Chen. 2008. Effect of phosphorylation on the transactivation activity of Epstein-Barr virus BMRF1, a major target of the viral BGLF4 kinase. J. Gen. Virol. 89:884-895.
    • (2008) J. Gen. Virol. , vol.89 , pp. 884-895
    • Yang, P.W.1    Chang, S.S.2    Tsai, C.H.3    Chao, Y.H.4    Chen, M.R.5
  • 60
    • 0035035295 scopus 로고    scopus 로고
    • Identification of major phosphorylation sites of epstein-barr virus nuclear antigen leader protein (EBNA-LP): Ability of EBNA-LP to induce latent membrane protein 1 cooperatively with EBNA-2 is regulated by phosphorylation
    • DOI 10.1128/JVI.75.11.5119-5128.2001
    • Yokoyama, A., M. Tanaka, G. Matsuda, K. Kato, M. Kanamori, H. Kawasaki, H. Hirano, I. Kitabayashi, M. Ohki, K. Hirai, and Y. Kawaguchi. 2001. Identification of major phosphorylation sites of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP): ability of EBNA-LP to induce latent membrane protein 1 cooperatively with EBNA-2 is regulated by phosphorylation. J. Virol. 75:5119-5128. (Pubitemid 32448534)
    • (2001) Journal of Virology , vol.75 , Issue.11 , pp. 5119-5128
    • Yokoyama, A.1    Tanaka, M.2    Matsuda, G.3    Kato, K.4    Kanamori, M.5    Kawasaki, H.6    Hirano, H.7    Kitabayashi, I.8    Ohki, M.9    Hirai, K.10    Kawaguchi, Y.11
  • 61
    • 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
  • 62
    • 17444372050 scopus 로고    scopus 로고
    • Hyperphosphorylation of EBNA2 by Epstein-Barr virus protein kinase suppresses transactivation of the LMP1 promoter
    • DOI 10.1128/JVI.79.9.5880-5885.2005
    • Yue, W., E. Gershburg, and J. S. Pagano. 2005. Hyperphosphorylation of EBNA2 by Epstein-Barr virus protein kinase suppresses transactivation of the LMP1 promoter. J. Virol. 79:5880-5885. (Pubitemid 40548259)
    • (2005) Journal of Virology , vol.79 , Issue.9 , pp. 5880-5885
    • Yue, W.1    Gershburg, E.2    Pagano, J.S.3


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