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Volumn 36, Issue 4, 2008, Pages 625-628

Regulation of transcription by the Epstein-Barr virus nuclear antigen EBNA 2

Author keywords

C terminal domain phosphorylation (CTD phosphorylation); Cyclin dependent kinase 9 (CDK9); Elongation; Epstein Barr nuclear antigen 2 (EBNA 2); Epstein Barr virus (EBV); Transcription

Indexed keywords

ANDROGEN RECEPTOR; ANTIVIRUS AGENT; AROMATIC HYDROCARBON RECEPTOR; CD20 ANTIBODY; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN A; CYCLIN DEPENDENT KINASE 1; CYCLIN DEPENDENT KINASE 7; CYCLIN DEPENDENT KINASE 8; CYCLIN DEPENDENT KINASE 9; CYCLIN T1; E1A PROTEIN; EPSTEIN BARR VIRUS ANTIGEN 2; FLAVOPIRIDOL; HISTONE ACETYLTRANSFERASE PCAF; HISTONE H3; HISTONE H4; IMMUNOGLOBULIN J RECOMBINATION SIGNAL SEQUENCE BINDING PROTEIN; LATENT MEMBRANE PROTEIN 1; NUCLEAR RECEPTOR NUR77; POSITIVE TRANSCRIPTION ELONGATION FACTOR B; PROTEIN P300; PROTEIN P62; PROTEIN VP16; RNA POLYMERASE; TATA BINDING PROTEIN ASSOCIATED FACTOR; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR IIB; TRANSCRIPTION FACTOR PU 1; UNINDEXED DRUG; XERODERMA PIGMENTOSUM GROUP D PROTEIN;

EID: 49349115992     PISSN: 03005127     EISSN: None     Source Type: Journal    
DOI: 10.1042/BST0360625     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0033008462 scopus 로고    scopus 로고
    • Genetic evidence that EBNA-1 is needed for efficient, stable latent infection by Epstein-Barr virus
    • Lee, M.A., Diamond, M.E. and Yates, J.L. (1999) Genetic evidence that EBNA-1 is needed for efficient, stable latent infection by Epstein-Barr virus, J. Virol. 73, 2974-2982
    • (1999) J. Virol , vol.73 , pp. 2974-2982
    • Lee, M.A.1    Diamond, M.E.2    Yates, J.L.3
  • 2
    • 0022373077 scopus 로고
    • Transformation by Epstein-Barr virus requires DNA sequences in the region of BarnHI fragments Y and H
    • Skare, J., Farley, J, Strominger, J.L., Fresen, K.O., Cho, M.S. and zur Hausen, H. (1985) Transformation by Epstein-Barr virus requires DNA sequences in the region of BarnHI fragments Y and H. J. Virol. 55, 286-297
    • (1985) J. Virol , vol.55 , pp. 286-297
    • Skare, J.1    Farley, J.2    Strominger, J.L.3    Fresen, K.O.4    Cho, M.S.5    zur Hausen, H.6
  • 3
    • 0024317091 scopus 로고
    • Elpstein-Barr, virus nuclear protein 2 is a key determinant of lymphocyte transformation
    • Cohen, J.I., Wang, F., Mannick, J. and Kieff, E. (1989) Elpstein-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
  • 4
    • 0027479649 scopus 로고
    • Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation
    • Tomkinson, B., Robertson, E. and Kieff, E. (1993) Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation. J. Virol. 67, 2014-2025
    • (1993) J. Virol , vol.67 , pp. 2014-2025
    • Tomkinson, B.1    Robertson, E.2    Kieff, E.3
  • 5
    • 0028171081 scopus 로고
    • The human Jκ recombination signal sequence-binding protein (RBP-Jκ) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements
    • Waltzer, L., Logeat, F., Brou, C., Israel, A., Sergeant, A. and Manet, E. (1994) The human Jκ recombination signal sequence-binding protein (RBP-Jκ) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements. EMBO J. 13, 5633-5638
    • (1994) EMBO J , vol.13 , pp. 5633-5638
    • Waltzer, L.1    Logeat, F.2    Brou, C.3    Israel, A.4    Sergeant, A.5    Manet, E.6
  • 6
    • 0028124316 scopus 로고
    • The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the Jκ recombination signal binding protein
    • Grossman, S.R., Johannsen, E., Tong, X., Yalamanchili, R. and Kieff, E. (1994) The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the Jκ recombination signal binding protein. Proc. Natl. Acad. Sci. U.S.A. 91, 7568-7572
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 7568-7572
    • Grossman, S.R.1    Johannsen, E.2    Tong, X.3    Yalamanchili, R.4    Kieff, E.5
  • 7
    • 0028063483 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-Jκ, the homologue of Drosophilo Suppressor of Hairless
    • Zimber-Strobl, U., Strobl, L.J., Meitinger, C., Hinrichs, R., Sakai, T., Furukawa, T., Honjo, T. and Bornkamm, G.W. (1994) Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-Jκ, the homologue of Drosophilo 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
  • 8
    • 0028133036 scopus 로고
    • Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein
    • Henkel, T., Ling, P.D., Hayward, S.D. and Peterson, M.G. (1994) Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein Jκ. Science 265, 92-95
    • (1994) Jκ. Science , vol.265 , pp. 92-95
    • Henkel, T.1    Ling, P.D.2    Hayward, S.D.3    Peterson, M.G.4
  • 9
    • 0028924018 scopus 로고
    • Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by Jκ and PU. 1
    • Johannsen, E., Koh, E., Mosialos, G., Tong, X., Kieff, E. and Grossman, S.R. (1995) Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by Jκ and PU. 1. J. Virol. 69, 253-262
    • (1995) J. Virol , vol.69 , pp. 253-262
    • Johannsen, E.1    Koh, E.2    Mosialos, G.3    Tong, X.4    Kieff, E.5    Grossman, S.R.6
  • 10
    • 0025285021 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1
    • Wang, F., Tsang, S.F., Kurilla, M.G., Cohen, J.I. and Kieff, E. (1990) Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1. J. Virol. 64, 3407-3416
    • (1990) J. Virol , vol.64 , pp. 3407-3416
    • Wang, F.1    Tsang, S.F.2    Kurilla, M.G.3    Cohen, J.I.4    Kieff, E.5
  • 11
    • 0025274390 scopus 로고
    • Epstein-Barr virus nuclear antigen 2 induces expression of the virus-encoded latent membrane protein
    • Abbot, S.D., Rowe, M., Cadwallader, K., Ricksten, A., Gordon J, Wang, F., Rymo, L. and Rickinson, A.B. (1990) Epstein-Barr virus nuclear antigen 2 induces expression of the virus-encoded latent membrane protein. J. Virol. 64, 2126-2134
    • (1990) J. Virol , vol.64 , pp. 2126-2134
    • Abbot, S.D.1    Rowe, M.2    Cadwallader, K.3    Ricksten, A.4    Gordon, J.5    Wang, F.6    Rymo, L.7    Rickinson, A.B.8
  • 12
    • 0026086344 scopus 로고
    • An Epstein-Barr virus nuclear protein 2 domain essential for transformation is a direct transcriptional activator
    • Cohen, J.I. and Kieff, E. (1991) An Epstein-Barr virus nuclear protein 2 domain essential for transformation is a direct transcriptional activator. J. Virol. 65, 5880-5985
    • (1991) J. Virol , vol.65 , pp. 5880-5985
    • Cohen, J.I.1    Kieff, E.2
  • 13
    • 0026645980 scopus 로고
    • A region of herpes simplex virus VP16 can substitute for a transforming domain of Epstein-Barr virus nuclear protein 2
    • Cohen, J.I. (1992) A region of herpes simplex virus VP16 can substitute for a transforming domain of Epstein-Barr virus nuclear protein 2. Proc. Natl. Acad. Sci. U.S.A. 89, 8030-8034
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 8030-8034
    • Cohen, J.I.1
  • 14
    • 0029131021 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE
    • Tong, X., Drapkin, R., Yalamanchili, R., Mosialos, G. and Kieff, E. (1995) The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. Mol. Cell. Biol. 15, 4735-4744
    • (1995) Mol. Cell. Biol , vol.15 , pp. 4735-4744
    • Tong, X.1    Drapkin, R.2    Yalamanchili, R.3    Mosialos, G.4    Kieff, E.5
  • 15
    • 0028897411 scopus 로고
    • The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2
    • Tong, X., Drapkin, R., Reinberg, D. and Kieff, E. (1995) The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2. Proc. Natl. Acad. Sci. U.S.A. 92, 3259-3263
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 3259-3263
    • Tong, X.1    Drapkin, R.2    Reinberg, D.3    Kieff, E.4
  • 16
    • 0028924735 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein
    • Tong, X., Wang, F., Thut, C.J. and Kieff, E. (1995) The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein. J. Virol. 69, 585-588
    • (1995) J. Virol , vol.69 , pp. 585-588
    • Tong, X.1    Wang, F.2    Thut, C.J.3    Kieff, E.4
  • 17
    • 0034602777 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter
    • Wang, L., Grossman, S.R. and Kieff, E. (2000) Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter. Proc. Natl. Acad. Sci. U.S.A. 97, 430-435
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 430-435
    • Wang, L.1    Grossman, S.R.2    Kieff, E.3
  • 18
    • 0029841216 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1
    • Wu, D.Y., Kalpana, G.V., Goff, S.P. and Schubach, W,H. (1996) Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1. J. Virol. 70, 6020-6028
    • (1996) J. Virol , vol.70 , pp. 6020-6028
    • Wu, D.Y.1    Kalpana, G.V.2    Goff, S.P.3    Schubach, W.H.4
  • 19
    • 0038758749 scopus 로고    scopus 로고
    • Differential hyperacetylation of histones H3 and H4 upon promoter-specific recruitment of EBNA2 in Epstein-Barr virus chromatin
    • Alazafd, N., Gruffat, H., Hiriart, E., Sergeant, A. and Manet, E. (2003) Differential hyperacetylation of histones H3 and H4 upon promoter-specific recruitment of EBNA2 in Epstein-Barr virus chromatin. J. Virol. 77, 8166-8172
    • (2003) J. Virol , vol.77 , pp. 8166-8172
    • Alazafd, N.1    Gruffat, H.2    Hiriart, E.3    Sergeant, A.4    Manet, E.5
  • 20
    • 32444441332 scopus 로고    scopus 로고
    • cdc2/cyclin B1-dependent phosphorylation of EBNA2 at Ser243 regulates its function in mitosis
    • Yue, W., Shackelford, J. and Pagano, J.S. (2006) cdc2/cyclin B1-dependent phosphorylation of EBNA2 at Ser243 regulates its function in mitosis. J. Virol. 80, 2045-2050
    • (2006) J. Virol , vol.80 , pp. 2045-2050
    • Yue, W.1    Shackelford, J.2    Pagano, J.S.3
  • 21
    • 1842510003 scopus 로고    scopus 로고
    • Mitosis-specific hyperphosphorylation of Epstein-Barr virus nuclear antigen 2 suppresses its function
    • Yue, W., Davenport, M.G., Shackelford, J. and Pagano, J.S. (2004) Mitosis-specific hyperphosphorylation of Epstein-Barr virus nuclear antigen 2 suppresses its function. J. Virol. 78, 3542-3552
    • (2004) J. Virol , vol.78 , pp. 3542-3552
    • Yue, W.1    Davenport, M.G.2    Shackelford, J.3    Pagano, J.S.4
  • 22
    • 0141815505 scopus 로고    scopus 로고
    • Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation
    • Palancade, B. and Bensaude, O. (2003) Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation. Eur. J. Biochem. 270, 3859-3870
    • (2003) Eur. J. Biochem , vol.270 , pp. 3859-3870
    • Palancade, B.1    Bensaude, O.2
  • 23
    • 0035971078 scopus 로고    scopus 로고
    • Androgen receptor interacts with the positive elongation factor P-TEFb and enhances the efficiency of transcriptional elongation
    • Lee, D.K., Duan, H.O. and Chang, C. (2001) Androgen receptor interacts with the positive elongation factor P-TEFb and enhances the efficiency of transcriptional elongation. J. Biol. Chem. 276, 9978-9984
    • (2001) J. Biol. Chem , vol.276 , pp. 9978-9984
    • Lee, D.K.1    Duan, H.O.2    Chang, C.3
  • 24
    • 0242498382 scopus 로고    scopus 로고
    • Interactions between the aryl hydrocarbon receptor and P-TEFb: Sequential recruitment of transcription factors and differential phosphorylation of C-terminal domain of RNA polymerase II at cyp1a1 promoter
    • Tian, Y., Ke, S., Chen, M. and Sheng, T. (2003) Interactions between the aryl hydrocarbon receptor and P-TEFb: sequential recruitment of transcription factors and differential phosphorylation of C-terminal domain of RNA polymerase II at cyp1a1 promoter. J. Biol. Chem. 278, 44041-44048
    • (2003) J. Biol. Chem , vol.278 , pp. 44041-44048
    • Tian, Y.1    Ke, S.2    Chen, M.3    Sheng, T.4
  • 25
    • 0037131186 scopus 로고    scopus 로고
    • Myc recruits P-TEFb to mediate the final step in the transcriptional activation of the cad promoter
    • Eberhardy, S.R. and Farnham, P.J. (2002) Myc recruits P-TEFb to mediate the final step in the transcriptional activation of the cad promoter. J. Biol. Chem. 277, 40156-40162
    • (2002) J. Biol. Chem , vol.277 , pp. 40156-40162
    • Eberhardy, S.R.1    Farnham, P.J.2
  • 26
    • 0029841835 scopus 로고    scopus 로고
    • Viral transactivators E1A and VP16 interact with a large complex that is associated with CTD kinase activity and contains CDK8
    • Gold, M.O., Tassan, J.P., Nigg, E.A., Rice, A.P. and Herrmann, C.H. (1996) Viral transactivators E1A and VP16 interact with a large complex that is associated with CTD kinase activity and contains CDK8. Nucleic Acids Res. 24, 3771-3777
    • (1996) Nucleic Acids Res , vol.24 , pp. 3771-3777
    • Gold, M.O.1    Tassan, J.P.2    Nigg, E.A.3    Rice, A.P.4    Herrmann, C.H.5
  • 27
    • 0033618442 scopus 로고    scopus 로고
    • Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation
    • Isel, C. and Karn, J. (1999) Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation. J. Mol. Biol. 290, 929-941
    • (1999) J. Mol. Biol , vol.290 , pp. 929-941
    • Isel, C.1    Karn, J.2
  • 29
    • 33645017891 scopus 로고    scopus 로고
    • EBV EBNA 2 stimulates CDK9-dependent transcription and RNA polymefase II phosphorylation on serine 5
    • Bark-Jones, S.J., Webb, H.M. and West, MJ. (2006) EBV EBNA 2 stimulates CDK9-dependent transcription and RNA polymefase II phosphorylation on serine 5. Oncogene 25, 1775-1785
    • (2006) Oncogene , vol.25 , pp. 1775-1785
    • Bark-Jones, S.J.1    Webb, H.M.2    West, M.J.3
  • 30
    • 0036275982 scopus 로고    scopus 로고
    • Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation
    • Kim, Y.K., Bourgeois, C.F., Isel, C., Churcher, M.J. and Karn, J. (2002) Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation. Mol. Cell. Biol. 22, 4622-4637
    • (2002) Mol. Cell. Biol , vol.22 , pp. 4622-4637
    • Kim, Y.K.1    Bourgeois, C.F.2    Isel, C.3    Churcher, M.J.4    Karn, J.5
  • 31
    • 0033920260 scopus 로고    scopus 로고
    • Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription
    • Zhou, M., Halanski, M.A., Radonovich, M.F., Kashanchi, F., Peng, J., Price, D.H. and Brady, J.N. (2000) Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription. Mol. Cell. Biol. 20, 5077-5086
    • (2000) Mol. Cell. Biol , vol.20 , pp. 5077-5086
    • Zhou, M.1    Halanski, M.A.2    Radonovich, M.F.3    Kashanchi, F.4    Peng, J.5    Price, D.H.6    Brady, J.N.7
  • 32
    • 0035815612 scopus 로고    scopus 로고
    • Three RNA polymerase II carboxyl-terminal domain kinases display distinct substrate preferences
    • Ramanathan, Y., Rajpara, S.M., Reza, S.M., Lees, E., Shuman, S., Mathews, M.B. and Pe'ery, T. (2001) Three RNA polymerase II carboxyl-terminal domain kinases display distinct substrate preferences. J. Biol. Chem. 276, 10913-10920
    • (2001) J. Biol. Chem , vol.276 , pp. 10913-10920
    • Ramanathan, Y.1    Rajpara, S.M.2    Reza, S.M.3    Lees, E.4    Shuman, S.5    Mathews, M.B.6    Pe'ery, T.7
  • 33
    • 0025890062 scopus 로고
    • Early events in Epstein-Barr virus infection of human B lymphocytes
    • Alfieri, C., Birkenbach, M. and Kieff, E. (1991) Early events in Epstein-Barr virus infection of human B lymphocytes. Virology 181, 595-608
    • (1991) Virology , vol.181 , pp. 595-608
    • Alfieri, C.1    Birkenbach, M.2    Kieff, E.3
  • 34
    • 0024345877 scopus 로고
    • Epstein-Barr virus latent gene expression during the initiation of B cell immortalization
    • Allday, M.J., Crawford, D.H. and Griffin, B.E. (1989) Epstein-Barr virus latent gene expression during the initiation of B cell immortalization. J. Gen. Virol. 70, 1755-1764
    • (1989) J. Gen. Virol , vol.70 , pp. 1755-1764
    • Allday, M.J.1    Crawford, D.H.2    Griffin, B.E.3
  • 35
    • 0032488238 scopus 로고    scopus 로고
    • Characterisation of regulatory sequences at the Epstein-Barr virus BamHI W promoter
    • Bell, A., Skinner, J., Kirby, H. and Rickinson, A. (1998) Characterisation of regulatory sequences at the Epstein-Barr virus BamHI W promoter. Virology 252, 149-161
    • (1998) Virology , vol.252 , pp. 149-161
    • Bell, A.1    Skinner, J.2    Kirby, H.3    Rickinson, A.4
  • 37
    • 0035055595 scopus 로고    scopus 로고
    • Mechanisms of action of flavopiridol
    • Sedlacek, H.H. (2001) Mechanisms of action of flavopiridol. Crit. Rev. Oncol. Hematol. 38, 139-170
    • (2001) Crit. Rev. Oncol. Hematol , vol.38 , pp. 139-170
    • Sedlacek, H.H.1
  • 38
    • 0035943710 scopus 로고    scopus 로고
    • Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo
    • Chao, S.H. and Price, D.H. (2001) Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo. J. Biol. Chem. 276, 31793-31799
    • (2001) J. Biol. Chem , vol.276 , pp. 31793-31799
    • Chao, S.H.1    Price, D.H.2
  • 39
    • 0038754616 scopus 로고    scopus 로고
    • Flavopiridol-induced apoptosis is mediated through up-regulation of E2F1 and repression of Mcl-1
    • Ma, Y., Cress, W.D. and Haura, E.B. (2003) Flavopiridol-induced apoptosis is mediated through up-regulation of E2F1 and repression of Mcl-1. Mol. Cancer Ther. 2, 73-81
    • (2003) Mol. Cancer Ther , vol.2 , pp. 73-81
    • Ma, Y.1    Cress, W.D.2    Haura, E.B.3
  • 42
    • 0031958598 scopus 로고    scopus 로고
    • PITALRE, the catalytic subunit of TAK, is required for human immunodeficiency virus Tat transactivation in vivo
    • Gold, M.O., Yang, X., Herrmann, C.H. and Rice, A.P. (1998) PITALRE, the catalytic subunit of TAK, is required for human immunodeficiency virus Tat transactivation in vivo. J. Virol. 72, 4448-4453
    • (1998) J. Virol , vol.72 , pp. 4448-4453
    • Gold, M.O.1    Yang, X.2    Herrmann, C.H.3    Rice, A.P.4
  • 44
    • 0037395811 scopus 로고    scopus 로고
    • Amelioration of nephropathy in mice expressing HIV-1 genes by the cyclin-dependent kinase inhibitor flavopiridol
    • Nelson, P.J., D'Agati, V.D., Gries, J.M., Suarez, J.R. and Gelman, I.H. (2003) Amelioration of nephropathy in mice expressing HIV-1 genes by the cyclin-dependent kinase inhibitor flavopiridol. J. Antimicrob. Chemother. 51, 921-929
    • (2003) J. Antimicrob. Chemother , vol.51 , pp. 921-929
    • Nelson, P.J.1    D'Agati, V.D.2    Gries, J.M.3    Suarez, J.R.4    Gelman, I.H.5
  • 45
    • 33645340322 scopus 로고    scopus 로고
    • Management of patients with post-transplant lymphoproliferative disorder: The role of rituximab
    • Svoboda, J., Kotloff, R. and Tsai, D.E. (2006) Management of patients with post-transplant lymphoproliferative disorder: the role of rituximab. Transpl. Int. 19, 259-269
    • (2006) Transpl. Int , vol.19 , pp. 259-269
    • Svoboda, J.1    Kotloff, R.2    Tsai, D.E.3
  • 47
    • 7644227541 scopus 로고    scopus 로고
    • EBNA2 is required for protection of latently Epstein-Barr virus-infected B cells against specific apoptotic stimuli
    • Lee, J.M., Lee, K.H., Farrell, C.J., Ling, P.D., Kempkes, B., Park, J.H. and Hayward, S.D. (2004) EBNA2 is required for protection of latently Epstein-Barr virus-infected B cells against specific apoptotic stimuli. J. Virol. 78, 12694-12697
    • (2004) J. Virol , vol.78 , pp. 12694-12697
    • Lee, J.M.1    Lee, K.H.2    Farrell, C.J.3    Ling, P.D.4    Kempkes, B.5    Park, J.H.6    Hayward, S.D.7
  • 49
    • 1842585027 scopus 로고    scopus 로고
    • Inhibition of Epstein-Barr virus-induced growth proliferation by a nuclear antigen EBNA2-TAT peptide
    • Farrell, C.J., Lee, J.M., Shin, E.C., Cebrat, M., Cole, P.A. and Hayward, S.D. (2004) Inhibition of Epstein-Barr virus-induced growth proliferation by a nuclear antigen EBNA2-TAT peptide. Proc. Natl. Acad. Sci. U.S.A. 101, 4625-4630
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 4625-4630
    • Farrell, C.J.1    Lee, J.M.2    Shin, E.C.3    Cebrat, M.4    Cole, P.A.5    Hayward, S.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.