메뉴 건너뛰기




Volumn 84, Issue 6, 2010, Pages 2787-2797

The p38 signaling pathway upregulates expression of the Epstein-Barr virus LMP1 oncogene

Author keywords

[No Author keywords available]

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ACTIVATING TRANSCRIPTION FACTOR 1; CELL PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; ESTROGEN; LATENT MEMBRANE PROTEIN 1; SMALL INTERFERING RNA; SYNAPTOPHYSIN; TRICHOSTATIN A; VIRUS PROTEIN;

EID: 77649135016     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01052-09     Document Type: Article
Times cited : (18)

References (65)
  • 1
    • 85176695445 scopus 로고    scopus 로고
    • Alessi, D. R., A. Cuenda, P. Cohen, D. T. Dudley, and A. R. Saltiel. 1995. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:27489-27494.
    • Alessi, D. R., A. Cuenda, P. Cohen, D. T. Dudley, and A. R. Saltiel. 1995. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:27489-27494.
  • 2
    • 33749044616 scopus 로고    scopus 로고
    • Analysis of Epstein-Barr virus latent gene expression in endemic Burkitt's lymphoma and nasopharyngeal carcinoma tumour cells by using quantitative real-time PCR assays
    • Bell, A. I., K. Groves, G. L. Kelly, D. Croom-Carter, E. Hui, A. T. Chan, and A. B. Rickinson. 2006. Analysis of Epstein-Barr virus latent gene expression in endemic Burkitt's lymphoma and nasopharyngeal carcinoma tumour cells by using quantitative real-time PCR assays. J. Gen. Virol. 87:2885-2890.
    • (2006) J. Gen. Virol , vol.87 , pp. 2885-2890
    • Bell, A.I.1    Groves, K.2    Kelly, G.L.3    Croom-Carter, D.4    Hui, E.5    Chan, A.T.6    Rickinson, A.B.7
  • 3
    • 61449188280 scopus 로고    scopus 로고
    • Cyclical expression of EBV latent membrane protein 1 in EBV-transformed B cells underpins heterogeneity of epitope presentation and CD8+ T cell recognition
    • Brooks, J. M., S. P. Lee, A. M. Leese, W. A. Thomas, M. Rowe, and A. B. Rickinson. 2009. Cyclical expression of EBV latent membrane protein 1 in EBV-transformed B cells underpins heterogeneity of epitope presentation and CD8+ T cell recognition. J. Immunol. 182:1919-1928.
    • (2009) J. Immunol , vol.182 , pp. 1919-1928
    • Brooks, J.M.1    Lee, S.P.2    Leese, A.M.3    Thomas, W.A.4    Rowe, M.5    Rickinson, A.B.6
  • 4
    • 77649091478 scopus 로고    scopus 로고
    • Cahir-McFarland, E., and E. Kieff. 2005. Epstein-Barr Virus latent infection membrane protein 1, p. 553-570. In E. S. Robertson (ed.), Epstein-Barr virus. Caister Academic Press, Norwich, England.
    • Cahir-McFarland, E., and E. Kieff. 2005. Epstein-Barr Virus latent infection membrane protein 1, p. 553-570. In E. S. Robertson (ed.), Epstein-Barr virus. Caister Academic Press, Norwich, England.
  • 5
    • 0035123574 scopus 로고    scopus 로고
    • Linkage between STAT regulation and Epstein-Barr virus gene expression in tumors
    • Chen, H., J. M. Lee, Y. Zong, M. Borowitz, M. H. Ng, R. F. Ambinder, and S. D. Hayward. 2001. Linkage between STAT regulation and Epstein-Barr virus gene expression in tumors. J. Virol. 75:2929-2937.
    • (2001) J. Virol , vol.75 , pp. 2929-2937
    • Chen, H.1    Lee, J.M.2    Zong, Y.3    Borowitz, M.4    Ng, M.H.5    Ambinder, R.F.6    Hayward, S.D.7
  • 6
    • 0025248571 scopus 로고
    • Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino) ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells
    • Chijiwa, T., A. Mishima, M. Hagiwara, M. Sano, K. Hayashi, T. Inoue, K. Naito, T. Toshioka, and H. Hidaka. 1990. Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino) ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells. J. Biol. Chem. 265:5267-5272.
    • (1990) J. Biol. Chem , vol.265 , pp. 5267-5272
    • Chijiwa, T.1    Mishima, A.2    Hagiwara, M.3    Sano, M.4    Hayashi, K.5    Inoue, T.6    Naito, K.7    Toshioka, T.8    Hidaka, H.9
  • 7
    • 0024317091 scopus 로고
    • Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation
    • Cohen, J. I., F. Wang, J. Mannick, and E. Kieff. 1989. Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation. Proc. Natl. Acad. Sci. U. S. A. 86:9558-9562.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , pp. 9558-9562
    • Cohen, J.I.1    Wang, F.2    Mannick, J.3    Kieff, E.4
  • 8
    • 0032193226 scopus 로고    scopus 로고
    • p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes
    • Craxton, A., G. Shu, J. D. Graves, J. Saklatvala, E. G. Krebs, and E. A. Clark. 1998. p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes. J. Immunol. 161:3225-3236.
    • (1998) J. Immunol , vol.161 , pp. 3225-3236
    • Craxton, A.1    Shu, G.2    Graves, J.D.3    Saklatvala, J.4    Krebs, E.G.5    Clark, E.A.6
  • 9
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda, A., J. Rouse, Y. N. Doza, R. Meier, P. Cohen, T. F. Gallagher, P. R. Young, and J. C. Lee. 1995. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 364:229-233.
    • (1995) FEBS Lett , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 10
    • 34547154349 scopus 로고    scopus 로고
    • p38 MAP-kinases pathway regulation, function and role in human diseases
    • Cuenda, A., and S. Rousseau. 2007. p38 MAP-kinases pathway regulation, function and role in human diseases. Biochim. Biophys. Acta 1773:1358-1375.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1358-1375
    • Cuenda, A.1    Rousseau, S.2
  • 11
    • 0008899310 scopus 로고
    • U2 region of Epstein-Barr virus DNA may encode Epstein-Barr nuclear antigen 2
    • Dambaugh, T., K. Hennessy, L. Chamnankit, and E. Kieff. 1984. U2 region of Epstein-Barr virus DNA may encode Epstein-Barr nuclear antigen 2. Proc. Natl. Acad. Sci. U. S. A. 81:7632-7636.
    • (1984) Proc. Natl. Acad. Sci. U. S. A , vol.81 , pp. 7632-7636
    • Dambaugh, T.1    Hennessy, K.2    Chamnankit, L.3    Kieff, E.4
  • 12
    • 0037423201 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 (LMP1) activates the phosphatidylinositol 3-kinase/Akt pathway to promote cell survival and induce actin filament remodeling
    • Dawson, C. W., G. Tramountanis, A. G. Eliopoulos, and L. S. Young. 2003. Epstein-Barr virus latent membrane protein 1 (LMP1) activates the phosphatidylinositol 3-kinase/Akt pathway to promote cell survival and induce actin filament remodeling. J. Biol. Chem. 278:3694-3704.
    • (2003) J. Biol. Chem , vol.278 , pp. 3694-3704
    • Dawson, C.W.1    Tramountanis, G.2    Eliopoulos, A.G.3    Young, L.S.4
  • 13
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak, M., A. D. Clifton, L. M. Lucocq, and D. R. Alessi. 1998. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 17:4426-4441.
    • (1998) EMBO J , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 14
  • 15
    • 0037052968 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 5 inhibits pre-mRNA cleavage and polyadenylation
    • Dufva, M., J. Flodin, A. Nerstedt, U. Ruetschi, and L. Rymo. 2002. Epstein-Barr virus nuclear antigen 5 inhibits pre-mRNA cleavage and polyadenylation. Nucleic Acids Res. 30:2131-2143.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2131-2143
    • Dufva, M.1    Flodin, J.2    Nerstedt, A.3    Ruetschi, U.4    Rymo, L.5
  • 16
    • 0033523115 scopus 로고    scopus 로고
    • Activation of the p38 mitogen-activated protein kinase pathway by Epstein-Barr virus-encoded latent membrane protein 1 coregulates interleukin-6 and interleukin-8 production
    • Eliopoulos, A. G., N. J. Gallagher, S. M. Blake, C. W. Dawson, and L. S. Young. 1999. Activation of the p38 mitogen-activated protein kinase pathway by Epstein-Barr virus-encoded latent membrane protein 1 coregulates interleukin-6 and interleukin-8 production. J. Biol. Chem. 274:16085- 16096.
    • (1999) J. Biol. Chem , vol.274 , pp. 16085-16096
    • Eliopoulos, A.G.1    Gallagher, N.J.2    Blake, S.M.3    Dawson, C.W.4    Young, L.S.5
  • 17
    • 0028593659 scopus 로고
    • Response to cAMP levels of the Epstein-Barr virus EBNA2-inducible LMP1 oncogene and EBNA2 inhibition of a PP1-like activity
    • Fahraeus, R., L. Palmqvist, A. Nerdstedt, S. Farzad, L. Rymo, and S. Lain. 1994. Response to cAMP levels of the Epstein-Barr virus EBNA2-inducible LMP1 oncogene and EBNA2 inhibition of a PP1-like activity. EMBO J. 13:6041-6051.
    • (1994) EMBO J , vol.13 , pp. 6041-6051
    • Fahraeus, R.1    Palmqvist, L.2    Nerdstedt, A.3    Farzad, S.4    Rymo, L.5    Lain, S.6
  • 18
    • 0030245723 scopus 로고    scopus 로고
    • Cytostatic effect of Epstein-Barr virus latent membrane protein-1 analyzed using tetracycline-regulated expression in B cell lines
    • Floettmann, J. E., K. Ward, A. B. Rickinson, and M. Rowe. 1996. Cytostatic effect of Epstein-Barr virus latent membrane protein-1 analyzed using tetracycline-regulated expression in B cell lines. Virology 223:29-40.
    • (1996) Virology , vol.223 , pp. 29-40
    • Floettmann, J.E.1    Ward, K.2    Rickinson, A.B.3    Rowe, M.4
  • 19
    • 0032578559 scopus 로고    scopus 로고
    • The activation state of p38 mitogen-activated protein kinase determines the efficiency of ATP competition for pyridinylimidazole inhibitor binding
    • Frantz, B., T. Klatt, M. Pang, J. Parsons, A. Rolando, H. Williams, M. J. Tocci, S. J. O'Keefe, and E. A. O'Neill. 1998. The activation state of p38 mitogen-activated protein kinase determines the efficiency of ATP competition for pyridinylimidazole inhibitor binding. Biochemistry 37:13846-13853.
    • (1998) Biochemistry , vol.37 , pp. 13846-13853
    • Frantz, B.1    Klatt, T.2    Pang, M.3    Parsons, J.4    Rolando, A.5    Williams, H.6    Tocci, M.J.7    O'Keefe, S.J.8    O'Neill, E.A.9
  • 20
    • 0037223402 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts
    • Frevel, M. A., T. Bakheet, A. M. Silva, J. G. Hissong, K. S. Khabar, and B. R. Williams. 2003. p38 mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts. Mol. Cell. Biol. 23:425-436.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 425-436
    • Frevel, M.A.1    Bakheet, T.2    Silva, A.M.3    Hissong, J.G.4    Khabar, K.S.5    Williams, B.R.6
  • 22
    • 0025816554 scopus 로고
    • Biochemical characterization of Epstein-Barr virus nuclear antigen 2A
    • Grasser, F. A., P. Haiss, S. Gottel, and N. Mueller-Lantzsch. 1991. Biochemical characterization of Epstein-Barr virus nuclear antigen 2A. J. Virol. 65:3779-3788.
    • (1991) J. Virol , vol.65 , pp. 3779-3788
    • Grasser, F.A.1    Haiss, P.2    Gottel, S.3    Mueller-Lantzsch, N.4
  • 23
    • 0023762901 scopus 로고
    • Downregulation of cell adhesion molecules LFA-3 and ICAM-1 in Epstein-Barr virus-positive Burkitt's lymphoma underlies tumor cell escape from virus-specific T cell surveillance
    • Gregory, C. D., R. J. Murray, C. F. Edwards, and A. B. Rickinson. 1988. Downregulation of cell adhesion molecules LFA-3 and ICAM-1 in Epstein-Barr virus-positive Burkitt's lymphoma underlies tumor cell escape from virus-specific T cell surveillance. J. Exp. Med. 167:1811-1824.
    • (1988) J. Exp. Med , vol.167 , pp. 1811-1824
    • Gregory, C.D.1    Murray, R.J.2    Edwards, C.F.3    Rickinson, A.B.4
  • 24
    • 0028124316 scopus 로고    scopus 로고
    • Grossman, S. R., E. Johannsen, X. Tong, R. Yalamanchili, and E. Kieff. 1994. The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein. Proc. Natl. Acad. Sci. U. S. A. 91:7568-7572.
    • Grossman, S. R., E. Johannsen, X. Tong, R. Yalamanchili, and E. Kieff. 1994. The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein. Proc. Natl. Acad. Sci. U. S. A. 91:7568-7572.
  • 25
    • 0028133036 scopus 로고    scopus 로고
    • Henkel, T., P. D. Ling, S. D. Hayward, and M. G. Peterson. 1994. Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science 265:92-95.
    • Henkel, T., P. D. Ling, S. D. Hayward, and M. G. Peterson. 1994. Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science 265:92-95.
  • 26
    • 0032444348 scopus 로고    scopus 로고
    • Inducible and constitutive transcription factors in the mammalian nervous system: Control of gene expression by Jun, Fos and Krox, and CREB/ATF proteins
    • Herdegen, T., and J. D. Leah. 1998. Inducible and constitutive transcription factors in the mammalian nervous system: control of gene expression by Jun, Fos and Krox, and CREB/ATF proteins. Brain Res. Brain Res. Rev. 28:370-490.
    • (1998) Brain Res. Brain Res. Rev , vol.28 , pp. 370-490
    • Herdegen, T.1    Leah, J.D.2
  • 28
    • 34347366409 scopus 로고    scopus 로고
    • Activity of the LMP1 gene promoter in Epstein-Barr virus-transformed cell lines is modulated by sequence variations in the promoter-proximal CRE site
    • Jansson, A., P. Johansson, S. Li, and L. Rymo. 2007. Activity of the LMP1 gene promoter in Epstein-Barr virus-transformed cell lines is modulated by sequence variations in the promoter-proximal CRE site. J. Gen. Virol. 88:1887-1894.
    • (2007) J. Gen. Virol , vol.88 , pp. 1887-1894
    • Jansson, A.1    Johansson, P.2    Li, S.3    Rymo, L.4
  • 29
    • 34447620156 scopus 로고    scopus 로고
    • Role of a consensus AP-2 regulatory sequence within the Epstein-Barr virus LMP1 promoter in EBNA2 mediated transactivation
    • Jansson, A., P. Johansson, W. Yang, L. Palmqvist, A. Sjoblom-Hallen, and L. Rymo. 2007. Role of a consensus AP-2 regulatory sequence within the Epstein-Barr virus LMP1 promoter in EBNA2 mediated transactivation. Virus Genes 35:203-214.
    • (2007) Virus Genes , vol.35 , pp. 203-214
    • Jansson, A.1    Johansson, P.2    Yang, W.3    Palmqvist, L.4    Sjoblom-Hallen, A.5    Rymo, L.6
  • 30
    • 0028924018 scopus 로고    scopus 로고
    • Johannsen, E., E. Koh, G. Mosialos, X. Tong, E. Kieff, and S. R. Grossman. 1995. Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by J kappa and PU. 1. J. Virol. 69:253-262.
    • Johannsen, E., E. Koh, G. Mosialos, X. Tong, E. Kieff, and S. R. Grossman. 1995. Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by J kappa and PU. 1. J. Virol. 69:253-262.
  • 31
    • 59749098067 scopus 로고    scopus 로고
    • Nuclear factor-kappaB binds to the Epstein-Barr virus LMP1 promoter and upregulates its expression
    • Johansson, P., A. Jansson, U. Ruetschi, and L. Rymo. 2009. Nuclear factor-kappaB binds to the Epstein-Barr virus LMP1 promoter and upregulates its expression. J. Virol. 83:1393-1401.
    • (2009) J. Virol , vol.83 , pp. 1393-1401
    • Johansson, P.1    Jansson, A.2    Ruetschi, U.3    Rymo, L.4
  • 32
    • 0032923696 scopus 로고    scopus 로고
    • The proto-oncogene c-myc is a direct target gene of Epstein-Barr virus nuclear antigen 2
    • Kaiser, C., G. Laux, D. Eick, N. Jochner, G. W. Bornkamm, and B. Kempkes. 1999. The proto-oncogene c-myc is a direct target gene of Epstein-Barr virus nuclear antigen 2. J. Virol. 73:4481-4484.
    • (1999) J. Virol , vol.73 , pp. 4481-4484
    • Kaiser, C.1    Laux, G.2    Eick, D.3    Jochner, N.4    Bornkamm, G.W.5    Kempkes, B.6
  • 33
    • 0034624703 scopus 로고    scopus 로고
    • The amino-terminus and membrane-spanning domains of LMP-1 inhibit cell proliferation
    • Kaykas, A., and B. Sugden. 2000. The amino-terminus and membrane-spanning domains of LMP-1 inhibit cell proliferation. Oncogene 19:1400-1410.
    • (2000) Oncogene , vol.19 , pp. 1400-1410
    • Kaykas, A.1    Sugden, B.2
  • 34
    • 0029561039 scopus 로고
    • Epstein-Barr virus nuclear antigen 2-estrogen receptor fusion proteins transactivate viral and cellular genes and interact with RBP-J kappa in a conditional fashion
    • Kempkes, B., M. Pawlita, U. Zimber-Strobl, G. Eissner, G. Laux, and G. W. Bornkamm. 1995. Epstein-Barr virus nuclear antigen 2-estrogen receptor fusion proteins transactivate viral and cellular genes and interact with RBP-J kappa in a conditional fashion. Virology 214:675-679.
    • (1995) Virology , vol.214 , pp. 675-679
    • Kempkes, B.1    Pawlita, M.2    Zimber-Strobl, U.3    Eissner, G.4    Laux, G.5    Bornkamm, G.W.6
  • 36
    • 0000942112 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • D. M. Knipe and P. M. Howley ed, 4th ed. Lippincott-Raven Publishers, Philadelphia, PA
    • Kieff, E., and A. B. Rickinson. 2001. Epstein-Barr virus and its replication, p. 2511-2574. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 4th ed. Lippincott-Raven Publishers, Philadelphia, PA.
    • (2001) Fields virology , pp. 2511-2574
    • Kieff, E.1    Rickinson, A.B.2
  • 37
    • 0842347778 scopus 로고    scopus 로고
    • High physiological levels of LMP1 result in phosphorylation of eIF2 alpha in Epstein-Barr virus-infected cells
    • Lam, N., M. L. Sandberg, and B. Sugden. 2004. High physiological levels of LMP1 result in phosphorylation of eIF2 alpha in Epstein-Barr virus-infected cells. J. Virol. 78:1657-1664.
    • (2004) J. Virol , vol.78 , pp. 1657-1664
    • Lam, N.1    Sandberg, M.L.2    Sugden, B.3
  • 38
    • 0019314499 scopus 로고
    • 5,6-Dichloro-1-beta-ribofuranosylbenzimidazole enhances premature termination of late transcription of simian virus 40 DNA
    • Laub, O., E. B. Jakobovits, and Y. Aloni. 1980. 5,6-Dichloro-1-beta-ribofuranosylbenzimidazole enhances premature termination of late transcription of simian virus 40 DNA. Proc. Natl. Acad. Sci. U. S. A. 77:3297-3301.
    • (1980) Proc. Natl. Acad. Sci. U. S. A , vol.77 , pp. 3297-3301
    • Laub, O.1    Jakobovits, E.B.2    Aloni, Y.3
  • 39
    • 42949162045 scopus 로고    scopus 로고
    • The latent membrane protein 1 oncogene modifies B-cell physiology by regulating autophagy
    • Lee, D. Y., and B. Sugden. 2008. The latent membrane protein 1 oncogene modifies B-cell physiology by regulating autophagy. Oncogene 27:2833-2842.
    • (2008) Oncogene , vol.27 , pp. 2833-2842
    • Lee, D.Y.1    Sugden, B.2
  • 40
    • 41349088623 scopus 로고    scopus 로고
    • The LMP1 oncogene of EBV activates PERK and the unfolded protein response to drive its own synthesis
    • Lee, D. Y., and B. Sugden. 2008. The LMP1 oncogene of EBV activates PERK and the unfolded protein response to drive its own synthesis. Blood 111:2280-2289.
    • (2008) Blood , vol.111 , pp. 2280-2289
    • Lee, D.Y.1    Sugden, B.2
  • 41
    • 0027358873 scopus 로고
    • The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein
    • Ling, P. D., D. R. Rawlins, and S. D. Hayward. 1993. The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein. Proc. Natl. Acad. Sci. U. S. A. 90:9237-9241.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 9237-9241
    • Ling, P.D.1    Rawlins, D.R.2    Hayward, S.D.3
  • 44
    • 0035430282 scopus 로고    scopus 로고
    • Transcriptional regulation by the phosphorylation-dependent factor CREB
    • Mayr, B., and M. Montminy. 2001. Transcriptional regulation by the phosphorylation-dependent factor CREB. Nat. Rev. Mol. Cell Biol. 2:599-609.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 599-609
    • Mayr, B.1    Montminy, M.2
  • 45
    • 33745240363 scopus 로고    scopus 로고
    • The Epstein-Barr virus oncoprotein LMP1 inhibits the activity of viral or cellular promoters without inducing cytostasis
    • Narbonnet, S., and B. Mariame. 2006. The Epstein-Barr virus oncoprotein LMP1 inhibits the activity of viral or cellular promoters without inducing cytostasis. Virology 350:381-393.
    • (2006) Virology , vol.350 , pp. 381-393
    • Narbonnet, S.1    Mariame, B.2
  • 46
    • 33847661809 scopus 로고    scopus 로고
    • Protocol for the fast chromatin immunoprecipitation (ChIP) method
    • Nelson, J. D., O. Denisenko, and K. Bomsztyk. 2006. Protocol for the fast chromatin immunoprecipitation (ChIP) method. Nat. Protoc. 1:179-185.
    • (2006) Nat. Protoc , vol.1 , pp. 179-185
    • Nelson, J.D.1    Denisenko, O.2    Bomsztyk, K.3
  • 47
    • 0041387416 scopus 로고    scopus 로고
    • Interferon regulatory factor 7 regulates expression of Epstein-Barr virus latent membrane protein 1: A regulatory circuit
    • Ning, S., A. M. Hahn, L. E. Huye, and J. S. Pagano. 2003. Interferon regulatory factor 7 regulates expression of Epstein-Barr virus latent membrane protein 1: a regulatory circuit. J. Virol. 77:9359-9368.
    • (2003) J. Virol , vol.77 , pp. 9359-9368
    • Ning, S.1    Hahn, A.M.2    Huye, L.E.3    Pagano, J.S.4
  • 48
    • 22544477984 scopus 로고    scopus 로고
    • Interferon regulatory factor 5 represses expression of the Epstein-Barr virus oncoprotein LMP1: Braking of the IRF7/LMP1 regulatory circuit
    • Ning, S., L. E. Huye, and J. S. Pagano. 2005. Interferon regulatory factor 5 represses expression of the Epstein-Barr virus oncoprotein LMP1: braking of the IRF7/LMP1 regulatory circuit. J. Virol. 79:11671-11676.
    • (2005) J. Virol , vol.79 , pp. 11671-11676
    • Ning, S.1    Huye, L.E.2    Pagano, J.S.3
  • 49
    • 0024394417 scopus 로고
    • Staurosporine, K-252 and UCN-01: Potent but nonspecific inhibitors of protein kinases
    • Ruegg, U. T., and G. M. Burgess. 1989. Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases. Trends Pharmacol. Sci. 10:218-220.
    • (1989) Trends Pharmacol. Sci , vol.10 , pp. 218-220
    • Ruegg, U.T.1    Burgess, G.M.2
  • 50
    • 0025255258 scopus 로고
    • Transcription of the Epstein-Barr virus genome during latency in growth-transformed lymphocytes
    • Sample, J., and E. Kieff. 1990. Transcription of the Epstein-Barr virus genome during latency in growth-transformed lymphocytes. J. Virol. 64:1667-1674.
    • (1990) J. Virol , vol.64 , pp. 1667-1674
    • Sample, J.1    Kieff, E.2
  • 51
    • 0033809589 scopus 로고    scopus 로고
    • Latent membrane protein 1 of Epstein-Barr virus inhibits as well as stimulates gene expression
    • Sandberg, M. L., A. Kaykas, and B. Sugden. 2000. Latent membrane protein 1 of Epstein-Barr virus inhibits as well as stimulates gene expression. J. Virol. 74:9755-9761.
    • (2000) J. Virol , vol.74 , pp. 9755-9761
    • Sandberg, M.L.1    Kaykas, A.2    Sugden, B.3
  • 52
    • 0028803804 scopus 로고
    • PU box-binding transcription factors and a POU domain protein cooperate in the Epstein-Barr virus (EBV) nuclear antigen 2-induced transactivation of the EBV latent membrane protein 1 promoter
    • Sjoblom, A., A. Jansson, W. Yang, S. Lain, T. Nilsson, and L. Rymo. 1995. PU box-binding transcription factors and a POU domain protein cooperate in the Epstein-Barr virus (EBV) nuclear antigen 2-induced transactivation of the EBV latent membrane protein 1 promoter. J. Gen. Virol. 76(Part 11): 2679-2692.
    • (1995) J. Gen. Virol , vol.76 , Issue.PART 11 , pp. 2679-2692
    • Sjoblom, A.1    Jansson, A.2    Yang, W.3    Lain, S.4    Nilsson, T.5    Rymo, L.6
  • 53
    • 2642706679 scopus 로고    scopus 로고
    • An ATF/CRE element mediates both EBNA2-dependent and EBNA2-independent activation of the Epstein-Barr virus LMP1 gene promoter
    • Sjoblom, A., W. Yang, L. Palmqvist, A. Jansson, and L. Rymo. 1998. An ATF/CRE element mediates both EBNA2-dependent and EBNA2-independent activation of the Epstein-Barr virus LMP1 gene promoter. J. Virol. 72:1365-1376.
    • (1998) J. Virol , vol.72 , pp. 1365-1376
    • Sjoblom, A.1    Yang, W.2    Palmqvist, L.3    Jansson, A.4    Rymo, L.5
  • 54
    • 0033044134 scopus 로고    scopus 로고
    • Silencing of the Epstein-Barr virus latent membrane protein 1 gene by the Max-Mad1-mSin3A modulator of chromatin structure
    • Sjoblom-Hallen, A., W. Yang, A. Jansson, and L. Rymo. 1999. Silencing of the Epstein-Barr virus latent membrane protein 1 gene by the Max-Mad1-mSin3A modulator of chromatin structure. J. Virol. 73:2983-2993.
    • (1999) J. Virol , vol.73 , pp. 2983-2993
    • Sjoblom-Hallen, A.1    Yang, W.2    Jansson, A.3    Rymo, L.4
  • 55
    • 84934436278 scopus 로고    scopus 로고
    • LMP1 TRAfficking activates growth and survival pathways
    • Soni, V., E. Cahir-McFarland, and E. Kieff. 2007. LMP1 TRAfficking activates growth and survival pathways. Adv. Exp. Med. Biol. 597:173-187.
    • (2007) Adv. Exp. Med. Biol , vol.597 , pp. 173-187
    • Soni, V.1    Cahir-McFarland, E.2    Kieff, E.3
  • 56
    • 0029790656 scopus 로고    scopus 로고
    • FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2
    • Tan, Y., J. Rouse, A. Zhang, S. Cariati, P. Cohen, and M. J. Comb. 1996. FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2. EMBO J. 15:4629-4642.
    • (1996) EMBO J , vol.15 , pp. 4629-4642
    • Tan, Y.1    Rouse, J.2    Zhang, A.3    Cariati, S.4    Cohen, P.5    Comb, M.J.6
  • 57
    • 33744484523 scopus 로고    scopus 로고
    • Epstein-Barr virus (EBV) and its associated human cancers-genetics, epigenetics, pathobiology and novel therapeutics
    • Tao, Q., L. S. Young, C. B. Woodman, and P. G. Murray. 2006. Epstein-Barr virus (EBV) and its associated human cancers-genetics, epigenetics, pathobiology and novel therapeutics. Front. Biosci. 11:2672-2713.
    • (2006) Front. Biosci , vol.11 , pp. 2672-2713
    • Tao, Q.1    Young, L.S.2    Woodman, C.B.3    Murray, P.G.4
  • 58
    • 23244448471 scopus 로고    scopus 로고
    • EBV the prototypical human tumor virus-just how bad is it?
    • Thorley-Lawson, D. A. 2005. EBV the prototypical human tumor virus-just how bad is it? J. Allergy Clin. Immunol. 116:251-261.
    • (2005) J. Allergy Clin. Immunol , vol.116 , pp. 251-261
    • Thorley-Lawson, D.A.1
  • 59
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways
    • Tibbles, L. A., and J. R. Woodgett. 1999. The stress-activated protein kinase pathways. Cell. Mol. Life Sci. 55:1230-1254.
    • (1999) Cell. Mol. Life Sci , vol.55 , pp. 1230-1254
    • Tibbles, L.A.1    Woodgett, J.R.2
  • 61
    • 0028171081 scopus 로고    scopus 로고
    • Waltzer, L., F. Logeat, C. Brou, A. Israel, A. Sergeant, and E. Manet. 1994. The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements. EMBO J. 13:5633-5638.
    • Waltzer, L., F. Logeat, C. Brou, A. Israel, A. Sergeant, and E. Manet. 1994. The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements. EMBO J. 13:5633-5638.
  • 62
    • 34547196977 scopus 로고    scopus 로고
    • Regulation of gene transcription by mitogen-activated protein kinase signaling pathways
    • Whitmarsh, A. J. 2007. Regulation of gene transcription by mitogen-activated protein kinase signaling pathways. Biochim. Biophys. Acta 1773:1285-1298.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1285-1298
    • Whitmarsh, A.J.1
  • 63
    • 34347347786 scopus 로고    scopus 로고
    • EBNA2 transcription regulation in EBV latency
    • E. S. Robertson ed, Caister Academic Press, Norwich, England
    • Zetterberg, H., and L. Rymo. 2005. EBNA2 transcription regulation in EBV latency, p. 439-462. In E. S. Robertson (ed.), Epstein-Barr virus. Caister Academic Press, Norwich, England.
    • (2005) Epstein-Barr virus , pp. 439-462
    • Zetterberg, H.1    Rymo, L.2
  • 64
    • 0032968832 scopus 로고    scopus 로고
    • Relative levels of EBNA1 gene transcripts from the C/W, F and Q promoters in Epstein-Barr virus-transformed lymphoid cells in latent and lytic stages of infection
    • Zetterberg, H., M. Stenglein, A. Jansson, A. Ricksten, and L. Rymo. 1999. Relative levels of EBNA1 gene transcripts from the C/W, F and Q promoters in Epstein-Barr virus-transformed lymphoid cells in latent and lytic stages of infection. J. Gen. Virol. 80(Part 2):457-466.
    • (1999) J. Gen. Virol , vol.80 , Issue.PART 2 , pp. 457-466
    • Zetterberg, H.1    Stenglein, M.2    Jansson, A.3    Ricksten, A.4    Rymo, L.5
  • 65
    • 0028063483 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless
    • Zimber-Strobl, U., L. J. Strobl, C. Meitinger, R. Hinrichs, T. Sakai, T. Furukawa, T. Honjo, and G. W. Bornkamm. 1994. Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless. EMBO J. 13:4973-4982.
    • (1994) EMBO J , vol.13 , pp. 4973-4982
    • Zimber-Strobl, U.1    Strobl, L.J.2    Meitinger, C.3    Hinrichs, R.4    Sakai, T.5    Furukawa, T.6    Honjo, T.7    Bornkamm, G.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.