메뉴 건너뛰기




Volumn 96, Issue 19, 2004, Pages 1447-1457

Selective efficacy of depsipeptide in a xenograft model of Epstein-Barr virus-positive lymphoproliferative disorder

Author keywords

[No Author keywords available]

Indexed keywords

BUTYRIC ACID; CASPASE 3; CASPASE INHIBITOR; DEPSIPEPTIDE; HISTONE DEACETYLASE INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LATENT MEMBRANE PROTEIN 1; TRICHOSTATIN A; ANTINEOPLASTIC AGENT; CASPASE; CYCLOPEPTIDE; EBV ASSOCIATED MEMBRANE ANTIGEN, EPSTEIN BARR VIRUS; EBV-ASSOCIATED MEMBRANE ANTIGEN, EPSTEIN-BARR VIRUS; ENZYME INHIBITOR; FR 901228; HISTONE DEACETYLASE; MATRIX PROTEIN; PROTEIN BCL 2; THYMIDINE;

EID: 6944240526     PISSN: 00278874     EISSN: None     Source Type: Journal    
DOI: 10.1093/jnci/djh271     Document Type: Article
Times cited : (30)

References (50)
  • 1
    • 0000942112 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • Fields BN, editor. 4th ed. New York (NY): Lippincott Williams & Wilkins
    • Rickinson AB, Kieff E. Epstein-Barr virus. In: Fields BN, editor. Fields' virology. Vol 1. 4th ed. New York (NY): Lippincott Williams & Wilkins; 2001. p. 2575-627.
    • (2001) Fields' Virology , vol.1 , pp. 2575-2627
    • Rickinson, A.B.1    Kieff, E.2
  • 2
    • 0000942112 scopus 로고    scopus 로고
    • Epstein-Barr virus and replication
    • Fields BN, editor. 4th ed. New York (NY): Lippincott Williams & Wilkins
    • Kieff E, Rickinson AB. Epstein-Barr virus and replication. In Fields BN, editor. Fields' virology. Vol 1. 4th ed. New York (NY): Lippincott Williams & Wilkins; 2001. p. 2511-73.
    • (2001) Fields' Virology , vol.1 , pp. 2511-2573
    • Kieff, E.1    Rickinson, A.B.2
  • 3
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone RW. Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discov 2002;1:287-99.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 4
    • 0036301281 scopus 로고    scopus 로고
    • Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms
    • Sandor V, Bakke S, Robey RW, Kang MH, Blagosklonny MV, Bender J, et al. Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms. Clin Cancer Res 2002;8:718-28.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 718-728
    • Sandor, V.1    Bakke, S.2    Robey, R.W.3    Kang, M.H.4    Blagosklonny, M.V.5    Bender, J.6
  • 5
    • 0035525781 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report
    • Piekarz RL, Robey R, Sandor V, Bakke S, Wilson WH, Dahmoush L, et al. Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: a case report. Blood 2001;98:2865-8.
    • (2001) Blood , vol.98 , pp. 2865-2868
    • Piekarz, R.L.1    Robey, R.2    Sandor, V.3    Bakke, S.4    Wilson, W.H.5    Dahmoush, L.6
  • 6
    • 0028307864 scopus 로고
    • Low-dose interleukin 2 prevents the development of Epstein-Barr virus (EBV)-associated lymphoproliferative disease in scid/scid mice reconstituted i.p. with EBV-seropositive human peripheral blood lymphocytes
    • Baiocchi RA, Caligiuri MA. Low-dose interleukin 2 prevents the development of Epstein-Barr virus (EBV)-associated lymphoproliferative disease in scid/scid mice reconstituted i.p. with EBV-seropositive human peripheral blood lymphocytes. Proc Natl Acad Sci U S A 1994;91:5577-81.
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 5577-5581
    • Baiocchi, R.A.1    Caligiuri, M.A.2
  • 7
    • 0027237666 scopus 로고
    • Selective long-term elimination of natural killer cells in vivo by an anti-interleukin 2 receptor beta chain monoclonal antibody in mice
    • Tanaka T, Kitamura F, Nagasaka Y, Kuida K, Suwa H, Miyasaka M. Selective long-term elimination of natural killer cells in vivo by an anti-interleukin 2 receptor beta chain monoclonal antibody in mice. J Exp Med 1993;178:1103-7.
    • (1993) J. Exp. Med. , vol.178 , pp. 1103-1107
    • Tanaka, T.1    Kitamura, F.2    Nagasaka, Y.3    Kuida, K.4    Suwa, H.5    Miyasaka, M.6
  • 8
    • 0033960792 scopus 로고    scopus 로고
    • A subnanogram API LC/MS/MS quantitation method for depsipeptide FR901228 and its preclinical pharmacokinetics
    • Li Z, Chan KK. A subnanogram API LC/MS/MS quantitation method for depsipeptide FR901228 and its preclinical pharmacokinetics. J Pharm Biomed Anal 2000;22:33-44.
    • (2000) J. Pharm. Biomed. Anal. , vol.22 , pp. 33-44
    • Li, Z.1    Chan, K.K.2
  • 9
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
    • Vermes I, Haanen C, Steffens-Nakken H, Reutelingsperger C. A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J Immunol Methods 1995;184:39-51.
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 10
    • 0035874522 scopus 로고    scopus 로고
    • Human natural killer cells: A unique innate immunoregulatory role for the CD56(bright) subset
    • Cooper MA, Fehniger TA, Turner SC, Chen KS, Ghaheri BA, Ghayur T, et al. Human natural killer cells: a unique innate immunoregulatory role for the CD56(bright) subset. Blood 2001;97:3146-51.
    • (2001) Blood , vol.97 , pp. 3146-3151
    • Cooper, M.A.1    Fehniger, T.A.2    Turner, S.C.3    Chen, K.S.4    Ghaheri, B.A.5    Ghayur, T.6
  • 11
    • 0028908918 scopus 로고
    • Lymphomagenesis in the SCID-hu mouse involves abundant production of human interleukin-10
    • Baiocchi RA, Ross ME, Tan JC, Chou CC, Sullivan L, Haldar S, et al. Lymphomagenesis in the SCID-hu mouse involves abundant production of human interleukin-10. Blood 1995;85:1063-74.
    • (1995) Blood , vol.85 , pp. 1063-1074
    • Baiocchi, R.A.1    Ross, M.E.2    Tan, J.C.3    Chou, C.C.4    Sullivan, L.5    Haldar, S.6
  • 12
    • 0028912155 scopus 로고
    • Functional consequences of APO-1/Fas (CD95) antigen expression by normal and neoplastic hematopoietic cells
    • Robertson MJ, Manley TJ, Pichert G., Cameron C, Cochran KJ, Levine H, et al. Functional consequences of APO-1/Fas (CD95) antigen expression by normal and neoplastic hematopoietic cells. Leuk Lymphoma 1995;17:51-61.
    • (1995) Leuk. Lymphoma , vol.17 , pp. 51-61
    • Robertson, M.J.1    Manley, T.J.2    Pichert, G.3    Cameron, C.4    Cochran, K.J.5    Levine, H.6
  • 13
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti I, Migliorati G, Pagliacci MC, Grignani F, Riccardi C. A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J Immunol Methods 1991;139:271-9.
    • (1991) J. Immunol. Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 15
    • 0037021658 scopus 로고    scopus 로고
    • Using cyclooxygenase-2 inhibitors as molecular platforms to develop a new class of apoptosis-inducing agents
    • Zhu J, Song X, Lin HP, Young DC, Yan S, Marquez VE, et al. Using cyclooxygenase-2 inhibitors as molecular platforms to develop a new class of apoptosis-inducing agents. J Natl Cancer Inst 2002;94:1745-57.
    • (2002) J. Natl. Cancer Inst. , vol.94 , pp. 1745-1757
    • Zhu, J.1    Song, X.2    Lin, H.P.3    Young, D.C.4    Yan, S.5    Marquez, V.E.6
  • 16
    • 0038494686 scopus 로고    scopus 로고
    • Depsipeptide (FR901228) induces histone acetylation and inhibition of histone deacetylase in chronic lymphocytic leukemia cells concurrent with activation of caspase 8-mediated apoptosis and down-regulation of c-FLIP protein
    • Aron JL, Parthun MR, Marcucci G, Kitada S, Mone AP, Davis ME, et al. Depsipeptide (FR901228) induces histone acetylation and inhibition of histone deacetylase in chronic lymphocytic leukemia cells concurrent with activation of caspase 8-mediated apoptosis and down-regulation of c-FLIP protein. Blood 2003;102:652-8.
    • (2003) Blood , vol.102 , pp. 652-658
    • Aron, J.L.1    Parthun, M.R.2    Marcucci, G.3    Kitada, S.4    Mone, A.P.5    Davis, M.E.6
  • 18
    • 0003440032 scopus 로고    scopus 로고
    • Survival analysis: Techniques for censored and truncated data
    • New York (NY): Springer
    • Klein JP, Moeschberger, ML. Survival analysis: techniques for censored and truncated data. New York (NY): Springer; 1997.
    • (1997)
    • Klein, J.P.1    Moeschberger, M.L.2
  • 19
    • 0026072991 scopus 로고
    • Activation of Epstein-Barr virus latent genes protects human B cells from death by apoptosis
    • Gregory CD, Dive C, Henderson S, Smith CA, Williams GT, Gordon J, et al. Activation of Epstein-Barr virus latent genes protects human B cells from death by apoptosis. Nature 1991;349:612-4.
    • (1991) Nature , vol.349 , pp. 612-614
    • Gregory, C.D.1    Dive, C.2    Henderson, S.3    Smith, C.A.4    Williams, G.T.5    Gordon, J.6
  • 20
    • 0025772343 scopus 로고
    • Induction of bcl-2 expression by Epstein-Barr virus latent membrane protein 1 protects infected B cells from programmed cell death
    • Henderson S, Rowe M, Gregory C, Croom-Carter D, Wang F, Longnecker R, et al. Induction of bcl-2 expression by Epstein-Barr virus latent membrane protein 1 protects infected B cells from programmed cell death. Cell 1991;65:1107-15.
    • (1991) Cell , vol.65 , pp. 1107-1115
    • Henderson, S.1    Rowe, M.2    Gregory, C.3    Croom-Carter, D.4    Wang, F.5    Longnecker, R.6
  • 21
    • 0029956392 scopus 로고    scopus 로고
    • Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: Role in NF-kappaB activation
    • Devergne O, Hatzivassiliou E, Izumi KM, Kaye KM, Kleijnen MF, Kieff E, et al. Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation. Mol Cell Biol 1996;16:7098-108.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 7098-7108
    • Devergne, O.1    Hatzivassiliou, E.2    Izumi, K.M.3    Kaye, K.M.4    Kleijnen, M.F.5    Kieff, E.6
  • 22
    • 0034667777 scopus 로고    scopus 로고
    • Activation of the BRLF1 promoter and lytic cycle of Epstein-Barr virus by histone acetylation
    • Chang L, Liu ST. Activation of the BRLF1 promoter and lytic cycle of Epstein-Barr virus by histone acetylation. Nucleic Acids Res 2000;28: 3918-25.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3918-3925
    • Chang, L.1    Liu, S.T.2
  • 23
    • 0033987840 scopus 로고    scopus 로고
    • Histone acetylation and reactivation of Epstein-Barr virus from latency
    • Jenkins PJ, Binne UK, Farrell PJ. Histone acetylation and reactivation of Epstein-Barr virus from latency. J Virol 2000;74:710-20.
    • (2000) J. Virol. , vol.74 , pp. 710-720
    • Jenkins, P.J.1    Binne, U.K.2    Farrell, P.J.3
  • 24
    • 0032991714 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription
    • Radkov S, Touitou R, Brehm A, Rowe M, West M, Kourzarides R, et al. Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription. J Virol 1999;73:5688-97.
    • (1999) J. Virol. , vol.73 , pp. 5688-5697
    • Radkov, S.1    Touitou, R.2    Brehm, A.3    Rowe, M.4    West, M.5    Kourzarides, R.6
  • 25
    • 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 SR, Kieff E. 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 2000;97: 430-5.
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , pp. 430-435
    • Wang, L.1    Grossman, S.R.2    Kieff, E.3
  • 26
    • 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, Yang W, Jansson A, Rymo L. Silencing of the Epstein-Barr virus latent membrane protein 1 gene by the Max-Mad1-mSin3A modulator of chromatin structure. J Virol 1999;73:2983-93.
    • (1999) J. Virol. , vol.73 , pp. 2983-2993
    • Sjoblom-Hallen, A.1    Yang, W.2    Jansson, A.3    Rymo, L.4
  • 27
    • 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 DY, Kalpana GV, Goff SP, Schubach WH. Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1. J Virol 1996;70:6020-8.
    • (1996) J. Virol. , vol.70 , pp. 6020-6028
    • Wu, D.Y.1    Kalpana, G.V.2    Goff, S.P.3    Schubach, W.H.4
  • 28
    • 0037378585 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C recruits histone deacetylase activity and associates with the corepressors mSin3A and NCoR in human B cell lines
    • Knight JS, Lan K, Subramanian C, Robertson ES. Epstein-Barr virus nuclear antigen 3C recruits histone deacetylase activity and associates with the corepressors mSin3A and NCoR in human B cell lines. J Virol 2003; 77:4261-72.
    • (2003) J. Virol. , vol.77 , pp. 4261-4272
    • Knight, J.S.1    Lan, K.2    Subramanian, C.3    Robertson, E.S.4
  • 29
    • 0035793596 scopus 로고    scopus 로고
    • Defining Ca(2+)/calmodulin-dependent protein kinase cascades in transcriptional regulation
    • Corcoran EE, Means AR. Defining Ca(2+)/calmodulin-dependent protein kinase cascades in transcriptional regulation. J Biol Chem 2002; 276:2975-8.
    • (2002) J. Biol. Chem. , vol.276 , pp. 2975-2978
    • Corcoran, E.E.1    Means, A.R.2
  • 30
    • 0034614611 scopus 로고    scopus 로고
    • Ca(2 +)-dependent gene expression mediated by MEF2 transcription factors
    • Blaeser F, Ho N, Prywes R, Chatila TA. Ca(2 +)-dependent gene expression mediated by MEF2 transcription factors. J Biol Chem 2000; 275:197-209.
    • (2000) J. Biol. Chem. , vol.275 , pp. 197-209
    • Blaeser, F.1    Ho, N.2    Prywes, R.3    Chatila, T.A.4
  • 31
    • 7244258185 scopus 로고    scopus 로고
    • Treatment of EBV-transformed B cell lines with depsipeptide results in the induction of a viral thymidine kinase and enhanced susceptibility to antiviral-induced apoptosis
    • Proceedings of the EORTC, NCI, and American Association for Cancer Research; Nov 2; Miami, FL
    • Baiocchi RA, Sekula T, Vourganti S, Nair V, Roychowdhury S, Parthun M, et al. Treatment of EBV-transformed B cell lines with depsipeptide results in the induction of a viral thymidine kinase and enhanced susceptibility to antiviral-induced apoptosis. Proceedings of the EORTC, NCI, and American Association for Cancer Research; 2001 Nov 2; Miami, FL.
    • (2001)
    • Baiocchi, R.A.1    Sekula, T.2    Vourganti, S.3    Nair, V.4    Roychowdhury, S.5    Parthun, M.6
  • 32
    • 0142123234 scopus 로고    scopus 로고
    • mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad
    • Pal S, Yun R, Datta A, Lacomis L, Erdjument-Bromage H, Kumar J, et al. mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad. Mol Cell Biol 2003;23:7475-87.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7475-7487
    • Pal, S.1    Yun, R.2    Datta, A.3    Lacomis, L.4    Erdjument-Bromage, H.5    Kumar, J.6
  • 33
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997;90:595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 34
    • 9144266953 scopus 로고    scopus 로고
    • Induction of PIG3 and NOXA through acetylation of p53 at 320 and 373 lysine residues as a mechanism for apoptotic cell death by histone deacetylase inhibitors
    • Terui T, Murakami K, Takimoto R, Takahashi M, Takada K, Murakami T, et al. Induction of PIG3 and NOXA through acetylation of p53 at 320 and 373 lysine residues as a mechanism for apoptotic cell death by histone deacetylase inhibitors. Cancer Res 2003;63:8948-54.
    • (2003) Cancer Res. , vol.63 , pp. 8948-8954
    • Terui, T.1    Murakami, K.2    Takimoto, R.3    Takahashi, M.4    Takada, K.5    Murakami, T.6
  • 35
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li M, Luo J, Brooks CL, Gu W. Acetylation of p53 inhibits its ubiquitination by Mdm2. J Biol Chem 2002;277:50607-11.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 38
    • 0036943615 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein-1 induction by histone deacetylase inhibitors mediates induction of intercellular adhesion molecule-1 expression and homotypic aggregation
    • Park JH, Faller DV. Epstein-Barr virus latent membrane protein-1 induction by histone deacetylase inhibitors mediates induction of intercellular adhesion molecule-1 expression and homotypic aggregation. Virology 2002;303:345-63.
    • (2002) Virology , vol.303 , pp. 345-363
    • Park, J.H.1    Faller, D.V.2
  • 39
    • 0034948735 scopus 로고    scopus 로고
    • Cytokine signaling and Epstein-Barr virus-mediated cell transformation
    • Mosialos G. Cytokine signaling and Epstein-Barr virus-mediated cell transformation. Cytokine Growth Factor Rev 2001;12:259-70.
    • (2001) Cytokine Growth Factor Rev. , vol.12 , pp. 259-270
    • Mosialos, G.1
  • 40
    • 0035195435 scopus 로고    scopus 로고
    • Antisense to the Epstein-Barr virus (EBV)-encoded latent membrane protein 1 (LMP-1) sensitizes EBV-immortalized B cells to transforming growth factor-beta and chemotherapeutic agents
    • Kenney JL, Guinness ME, Reiss M, Lacy J. Antisense to the Epstein-Barr virus (EBV)-encoded latent membrane protein 1 (LMP-1) sensitizes EBV-immortalized B cells to transforming growth factor-beta and chemotherapeutic agents. Int J Cancer 2001;91:89-98.
    • (2001) Int. J. Cancer , vol.91 , pp. 89-98
    • Kenney, J.L.1    Guinness, M.E.2    Reiss, M.3    Lacy, J.4
  • 41
    • 0038758749 scopus 로고    scopus 로고
    • Differential hyperacetylation of histones H3 and H4 upon promoter-specific recruitment of EBNA2 in Epstein-Barr virus chromatin
    • Alazard N, Gruffat H, Hiriart E, Sergeant A, Manet E. Differential hyperacetylation of histones H3 and H4 upon promoter-specific recruitment of EBNA2 in Epstein-Barr virus chromatin. J Virol 2003;77:8166-72.
    • (2003) J. Virol. , vol.77 , pp. 8166-8172
    • Alazard, N.1    Gruffat, H.2    Hiriart, E.3    Sergeant, A.4    Manet, E.5
  • 42
    • 0037378585 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C recruits histone deacetylase activity and associates with the corepressors mSin3A and NCoR in human B-cell lines
    • Knight JS, Lan K, Subramanian C, Robertson ES. Epstein-Barr virus nuclear antigen 3C recruits histone deacetylase activity and associates with the corepressors mSin3A and NCoR in human B-cell lines. J Virol 2003; 77:4261-72.
    • (2003) J. Virol. , vol.77 , pp. 4261-4272
    • Knight, J.S.1    Lan, K.2    Subramanian, C.3    Robertson, E.S.4
  • 43
    • 0033044134 scopus 로고    scopus 로고
    • Silencing of the Epstein-Barr virus latent membrane protein-1 gene by the Max-Mad-mSin3A modulator of chromatin structure
    • Sjoblom-Hallen A, Yang W, Jansson A, Rymo L. Silencing of the Epstein-Barr virus latent membrane protein-1 gene by the Max-Mad-mSin3A modulator of chromatin structure. J Virol 1999;73:2983-93.
    • (1999) J. Virol. , vol.73 , pp. 2983-2993
    • Sjoblom-Hallen, A.1    Yang, W.2    Jansson, A.3    Rymo, L.4
  • 44
    • 0029914174 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 blocks p53 mediated apoptosis through the induction of the A20 gene
    • Fries KL, Miller WE, Raab-Traub N. Epstein-Barr virus latent membrane protein 1 blocks p53 mediated apoptosis through the induction of the A20 gene. J Virol 1996;70:8653-9.
    • (1996) J. Virol. , vol.70 , pp. 8653-8659
    • Fries, K.L.1    Miller, W.E.2    Raab-Traub, N.3
  • 45
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: Roles in cell survival and oncogenesis
    • Cory S, Huang DC, Adams JM. The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 2003;22:8590-607.
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.M.3
  • 46
    • 0033596129 scopus 로고    scopus 로고
    • Epstein-Barr virus transformation: Involvement of latent membrane protein 1-mediated activation of NF-kappaB
    • Cahir McFarland ED, Izumi KM, Mosialos G. Epstein-Barr virus transformation: involvement of latent membrane protein 1-mediated activation of NF-kappaB. Oncogene 1999;18:6959-64.
    • (1999) Oncogene , vol.18 , pp. 6959-6964
    • Cahir McFarland, E.D.1    Izumi, K.M.2    Mosialos, G.3
  • 48
    • 0035504081 scopus 로고    scopus 로고
    • Transcriptional regulation of bcl-2by nuclear factor kB and its significance in prostate cancer
    • Catz SD, Johnson JL. Transcriptional regulation of bcl-2by nuclear factor kB and its significance in prostate cancer. Oncogene 2001;20:7342-51.
    • (2001) Oncogene , vol.20 , pp. 7342-7351
    • Catz, S.D.1    Johnson, J.L.2
  • 49
    • 0032588317 scopus 로고    scopus 로고
    • NF-kappaB induces expression of the Bcl2 homologue A1/BfL-1 to preferentially suppress chemotherapy-induced apoptosis
    • Wang CY, Guttridge DC, Mayo M, Baldwin AS. NF-kappaB induces expression of the Bcl2 homologue A1/BfL-1 to preferentially suppress chemotherapy-induced apoptosis. Mol Cell Biol 1999;19:5923-9.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5923-5929
    • Wang, C.Y.1    Guttridge, D.C.2    Mayo, M.3    Baldwin, A.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.