메뉴 건너뛰기




Volumn 8, Issue 5, 2013, Pages

Heat Shock Protein 90 Inhibitors Repress Latent Membrane Protein 1 (LMP1) Expression and Proliferation of Epstein-Barr Virus-Positive Natural Killer Cell Lymphoma

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90 INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; JANUS KINASE; LATENT MEMBRANE PROTEIN 1; MITOGEN ACTIVATED PROTEIN KINASE; ONCOPROTEIN; PROTEIN KINASE B; RADICICOL; STAT PROTEIN; TANESPIMYCIN; TUMOR NECROSIS FACTOR RECEPTOR; ANTINEOPLASTIC AGENT; BENZOQUINONE DERIVATIVE; EBV-ASSOCIATED MEMBRANE ANTIGEN, EPSTEIN-BARR VIRUS; HEAT SHOCK PROTEIN 90; MACROCYCLIC LACTAM; MACROLIDE; MATRIX PROTEIN; MOLECULAR LIBRARY;

EID: 84877022289     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0063566     Document Type: Article
Times cited : (32)

References (48)
  • 1
    • 0035880226 scopus 로고    scopus 로고
    • Clinical and virologic characteristics of chronic active Epstein-Barr virus infection
    • Kimura H, Hoshino Y, Kanegane H, Tsuge I, Okamura T, et al. (2001) Clinical and virologic characteristics of chronic active Epstein-Barr virus infection. Blood 98: 280-286.
    • (2001) Blood , vol.98 , pp. 280-286
    • Kimura, H.1    Hoshino, Y.2    Kanegane, H.3    Tsuge, I.4    Okamura, T.5
  • 2
    • 0035892143 scopus 로고    scopus 로고
    • Mosquito allergy and Epstein-Barr virus-associated T/natural killer-cell lymphoproliferative disease
    • Kawa K, Okamura T, Yagi K, Takeuchi M, Nakayama M, et al. (2001) Mosquito allergy and Epstein-Barr virus-associated T/natural killer-cell lymphoproliferative disease. Blood 98: 3173-3174.
    • (2001) Blood , vol.98 , pp. 3173-3174
    • Kawa, K.1    Okamura, T.2    Yagi, K.3    Takeuchi, M.4    Nakayama, M.5
  • 3
    • 33746562435 scopus 로고    scopus 로고
    • Pathogenesis of chronic active Epstein-Barr virus infection: is this an infectious disease, lymphoproliferative disorder, or immunodeficiency?
    • Kimura H, (2006) Pathogenesis of chronic active Epstein-Barr virus infection: is this an infectious disease, lymphoproliferative disorder, or immunodeficiency? Rev Med Virol 16: 251-261.
    • (2006) Rev Med Virol , vol.16 , pp. 251-261
    • Kimura, H.1
  • 4
    • 84857788518 scopus 로고    scopus 로고
    • Deciphering the role of Epstein-Barr virus in the pathogenesis of T and NK cell lymphoproliferations
    • Fox CP, Shannon-Lowe C, Rowe M, (2011) Deciphering the role of Epstein-Barr virus in the pathogenesis of T and NK cell lymphoproliferations. Herpesviridae 2: 8.
    • (2011) Herpesviridae , vol.2 , pp. 8
    • Fox, C.P.1    Shannon-Lowe, C.2    Rowe, M.3
  • 5
    • 28544444488 scopus 로고    scopus 로고
    • Natural killer-cell malignancies: diagnosis and treatment
    • Kwong YL, (2005) Natural killer-cell malignancies: diagnosis and treatment. Leukemia 19: 2186-2194.
    • (2005) Leukemia , vol.19 , pp. 2186-2194
    • Kwong, Y.L.1
  • 6
    • 84934436278 scopus 로고    scopus 로고
    • LMP1 TRAFficking activates growth and survival pathways
    • Soni V, Cahir-McFarland E, Kieff E, (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
  • 7
    • 0037209628 scopus 로고    scopus 로고
    • CD40 and its viral mimic, LMP1: similar means to different ends
    • Lam N, Sugden B, (2003) CD40 and its viral mimic, LMP1: similar means to different ends. Cell Signal 15: 9-16.
    • (2003) Cell Signal , vol.15 , pp. 9-16
    • Lam, N.1    Sugden, B.2
  • 8
    • 37349127804 scopus 로고    scopus 로고
    • EBV latent membrane protein 1 activates Akt, NFkappaB, and Stat3 in B cell lymphomas
    • Shair KH, Bendt KM, Edwards RH, Bedford EC, Nielsen JN, et al. (2007) EBV latent membrane protein 1 activates Akt, NFkappaB, and Stat3 in B cell lymphomas. PLoS Pathog 3: e166.
    • (2007) PLoS Pathog , vol.3
    • Shair, K.H.1    Bendt, K.M.2    Edwards, R.H.3    Bedford, E.C.4    Nielsen, J.N.5
  • 9
    • 0032578485 scopus 로고    scopus 로고
    • Expression of the Epstein-Barr virus latent membrane protein 1 induces B cell lymphoma in transgenic mice
    • Kulwichit W, Edwards RH, Davenport EM, Baskar JF, Godfrey V, et al. (1998) Expression of the Epstein-Barr virus latent membrane protein 1 induces B cell lymphoma in transgenic mice. Proc Natl Acad Sci U S A 95: 11963-11968.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11963-11968
    • Kulwichit, W.1    Edwards, R.H.2    Davenport, E.M.3    Baskar, J.F.4    Godfrey, V.5
  • 10
    • 0037938602 scopus 로고    scopus 로고
    • LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments
    • Lam N, Sugden B, (2003) LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments. EMBO J 22: 3027-3038.
    • (2003) EMBO J , vol.22 , pp. 3027-3038
    • Lam, N.1    Sugden, B.2
  • 11
    • 20144374689 scopus 로고    scopus 로고
    • Latent membrane protein 1 of Epstein-Barr virus coordinately regulates proliferation with control of apoptosis
    • Dirmeier U, Hoffmann R, Kilger E, Schultheiss U, Briseno C, et al. (2005) Latent membrane protein 1 of Epstein-Barr virus coordinately regulates proliferation with control of apoptosis. Oncogene 24: 1711-1717.
    • (2005) Oncogene , vol.24 , pp. 1711-1717
    • Dirmeier, U.1    Hoffmann, R.2    Kilger, E.3    Schultheiss, U.4    Briseno, C.5
  • 12
    • 0032536860 scopus 로고    scopus 로고
    • Epstein-Barr virus-mediated B-cell proliferation is dependent upon latent membrane protein 1, which simulates an activated CD40 receptor
    • Kilger E, Kieser A, Baumann M, Hammerschmidt W, (1998) Epstein-Barr virus-mediated B-cell proliferation is dependent upon latent membrane protein 1, which simulates an activated CD40 receptor. EMBO J 17: 1700-1709.
    • (1998) EMBO J , vol.17 , pp. 1700-1709
    • Kilger, E.1    Kieser, A.2    Baumann, M.3    Hammerschmidt, W.4
  • 13
    • 0033522511 scopus 로고    scopus 로고
    • LMP1 signal transduction differs substantially from TNF receptor 1 signaling in the molecular functions of TRADD and TRAF2
    • Kieser A, Kaiser C, Hammerschmidt W, (1999) LMP1 signal transduction differs substantially from TNF receptor 1 signaling in the molecular functions of TRADD and TRAF2. EMBO J 18: 2511-2521.
    • (1999) EMBO J , vol.18 , pp. 2511-2521
    • Kieser, A.1    Kaiser, C.2    Hammerschmidt, W.3
  • 14
    • 0029037660 scopus 로고
    • Expression of LMP1 in epithelial cells leads to the activation of a select subset of NF-kappa B/Rel family proteins
    • Paine E, Scheinman RI, Baldwin AS Jr, Raab-Traub N, (1995) Expression of LMP1 in epithelial cells leads to the activation of a select subset of NF-kappa B/Rel family proteins. J Virol 69: 4572-4576.
    • (1995) J Virol , vol.69 , pp. 4572-4576
    • Paine, E.1    Scheinman, R.I.2    Baldwin Jr., A.S.3    Raab-Traub, N.4
  • 15
    • 0033536591 scopus 로고    scopus 로고
    • Mimicry of CD40 signals by Epstein-Barr virus LMP1 in B lymphocyte responses
    • Uchida J, Yasui T, Takaoka-Shichijo Y, Muraoka M, Kulwichit W, et al. (1999) Mimicry of CD40 signals by Epstein-Barr virus LMP1 in B lymphocyte responses. Science 286: 300-303.
    • (1999) Science , vol.286 , pp. 300-303
    • Uchida, J.1    Yasui, T.2    Takaoka-Shichijo, Y.3    Muraoka, M.4    Kulwichit, W.5
  • 16
    • 35348890981 scopus 로고    scopus 로고
    • Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress
    • Workman P, Burrows F, Neckers L, Rosen N, (2007) Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann N Y Acad Sci 1113: 202-216.
    • (2007) Ann N Y Acad Sci , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 17
    • 84855457952 scopus 로고    scopus 로고
    • Hsp90 molecular chaperone inhibitors: are we there yet?
    • Neckers L, Workman P, (2012) Hsp90 molecular chaperone inhibitors: are we there yet? Clin Cancer Res 18: 64-76.
    • (2012) Clin Cancer Res , vol.18 , pp. 64-76
    • Neckers, L.1    Workman, P.2
  • 18
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL, (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 19
    • 84857039457 scopus 로고    scopus 로고
    • Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers
    • Jhaveri K, Taldone T, Modi S, Chiosis G, (2012) Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers. Biochim Biophys Acta 1823: 742-755.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 742-755
    • Jhaveri, K.1    Taldone, T.2    Modi, S.3    Chiosis, G.4
  • 20
    • 84860557226 scopus 로고    scopus 로고
    • HSP90 inhibitors as therapy for multiple myeloma
    • Usmani SZ, Chiosis G, (2011) HSP90 inhibitors as therapy for multiple myeloma. Clin Lymphoma Myeloma Leuk 11Suppl 1: S77-81.
    • (2011) Clin Lymphoma Myeloma Leuk , vol.11
    • Usmani, S.Z.1    Chiosis, G.2
  • 21
    • 0035254641 scopus 로고    scopus 로고
    • Characterization of novel natural killer (NK)-cell and gammadelta T-cell lines established from primary lesions of nasal T/NK-cell lymphomas associated with the Epstein-Barr virus
    • Nagata H, Konno A, Kimura N, Zhang Y, Kimura M, et al. (2001) Characterization of novel natural killer (NK)-cell and gammadelta T-cell lines established from primary lesions of nasal T/NK-cell lymphomas associated with the Epstein-Barr virus. Blood 97: 708-713.
    • (2001) Blood , vol.97 , pp. 708-713
    • Nagata, H.1    Konno, A.2    Kimura, N.3    Zhang, Y.4    Kimura, M.5
  • 22
    • 0037495094 scopus 로고    scopus 로고
    • Common cytological and cytogenetic features of Epstein-Barr virus (EBV)-positive natural killer (NK) cells and cell lines derived from patients with nasal T/NK-cell lymphomas, chronic active EBV infection and hydroa vacciniforme-like eruptions
    • Zhang Y, Nagata H, Ikeuchi T, Mukai H, Oyoshi MK, et al. (2003) Common cytological and cytogenetic features of Epstein-Barr virus (EBV)-positive natural killer (NK) cells and cell lines derived from patients with nasal T/NK-cell lymphomas, chronic active EBV infection and hydroa vacciniforme-like eruptions. Br J Haematol 121: 805-814.
    • (2003) Br J Haematol , vol.121 , pp. 805-814
    • Zhang, Y.1    Nagata, H.2    Ikeuchi, T.3    Mukai, H.4    Oyoshi, M.K.5
  • 23
    • 0015539979 scopus 로고
    • Release of infectious Epstein-Barr virus by transformed marmoset leukocytes
    • Miller G, Lipman M, (1973) Release of infectious Epstein-Barr virus by transformed marmoset leukocytes. Proc Natl Acad Sci U S A 70: 190-194.
    • (1973) Proc Natl Acad Sci U S A , vol.70 , pp. 190-194
    • Miller, G.1    Lipman, M.2
  • 24
    • 84861313347 scopus 로고    scopus 로고
    • Epigenetic Histone Modification of Epstein-Barr Virus BZLF1 Promoter during Latency and Reactivation in Raji Cells
    • Murata T, Kondo Y, Sugimoto A, Kawashima D, Saito S, et al. (2012) Epigenetic Histone Modification of Epstein-Barr Virus BZLF1 Promoter during Latency and Reactivation in Raji Cells. J Virol 86: 4752-4761.
    • (2012) J Virol , vol.86 , pp. 4752-4761
    • Murata, T.1    Kondo, Y.2    Sugimoto, A.3    Kawashima, D.4    Saito, S.5
  • 25
    • 82755163018 scopus 로고    scopus 로고
    • Identification and characterization of CCAAT enhancer-binding protein (C/EBP) as a transcriptional activator for Epstein-Barr virus oncogene latent membrane protein 1
    • Noda C, Murata T, Kanda T, Yoshiyama H, Sugimoto A, et al. (2011) Identification and characterization of CCAAT enhancer-binding protein (C/EBP) as a transcriptional activator for Epstein-Barr virus oncogene latent membrane protein 1. J Biol Chem 286: 42524-42533.
    • (2011) J Biol Chem , vol.286 , pp. 42524-42533
    • Noda, C.1    Murata, T.2    Kanda, T.3    Yoshiyama, H.4    Sugimoto, A.5
  • 26
    • 48749085122 scopus 로고    scopus 로고
    • IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription
    • Kimura M, (2008) IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription. FEBS Lett 582: 2833-2837.
    • (2008) FEBS Lett , vol.582 , pp. 2833-2837
    • Kimura, M.1
  • 27
    • 35349010666 scopus 로고    scopus 로고
    • The heat-shock protein 90 inhibitor, geldanamycin, induces apoptotic cell death in Epstein-Barr virus-positive NK/T-cell lymphoma by Akt down-regulation
    • Jeon YK, Park CH, Kim KY, Li YC, Kim J, et al. (2007) The heat-shock protein 90 inhibitor, geldanamycin, induces apoptotic cell death in Epstein-Barr virus-positive NK/T-cell lymphoma by Akt down-regulation. J Pathol 213: 170-179.
    • (2007) J Pathol , vol.213 , pp. 170-179
    • Jeon, Y.K.1    Park, C.H.2    Kim, K.Y.3    Li, Y.C.4    Kim, J.5
  • 28
    • 77649261204 scopus 로고    scopus 로고
    • Hsp90 inhibitors block outgrowth of EBV-infected malignant cells in vitro and in vivo through an EBNA1-dependent mechanism
    • Sun X, Barlow EA, Ma S, Hagemeier SR, Duellman SJ, et al. (2010) Hsp90 inhibitors block outgrowth of EBV-infected malignant cells in vitro and in vivo through an EBNA1-dependent mechanism. Proc Natl Acad Sci U S A 107: 3146-3151.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 3146-3151
    • Sun, X.1    Barlow, E.A.2    Ma, S.3    Hagemeier, S.R.4    Duellman, S.J.5
  • 29
    • 80055085376 scopus 로고    scopus 로고
    • Novel mouse xenograft models reveal a critical role of CD4+ T cells in the proliferation of EBV-infected T and NK cells
    • Imadome K, Yajima M, Arai A, Nakazawa A, Kawano F, et al. (2011) Novel mouse xenograft models reveal a critical role of CD4+ T cells in the proliferation of EBV-infected T and NK cells. PLoS Pathog 7: e1002326.
    • (2011) PLoS Pathog , vol.7
    • Imadome, K.1    Yajima, M.2    Arai, A.3    Nakazawa, A.4    Kawano, F.5
  • 30
    • 0028924018 scopus 로고
    • Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by J kappa and PU.1
    • Johannsen E, Koh E, Mosialos G, Tong X, Kieff E, et al. (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.
    • (1995) J Virol , vol.69 , pp. 253-262
    • Johannsen, E.1    Koh, E.2    Mosialos, G.3    Tong, X.4    Kieff, E.5
  • 31
    • 0028004111 scopus 로고
    • The Spi-1/PU.1 and Spi-B ets family transcription factors and the recombination signal binding protein RBP-J kappa interact with an Epstein-Barr virus nuclear antigen 2 responsive cis-element
    • Laux G, Adam B, Strobl LJ, Moreau-Gachelin F, (1994) The Spi-1/PU.1 and Spi-B ets family transcription factors and the recombination signal binding protein RBP-J kappa interact with an Epstein-Barr virus nuclear antigen 2 responsive cis-element. EMBO J 13: 5624-5632.
    • (1994) EMBO J , vol.13 , pp. 5624-5632
    • Laux, G.1    Adam, B.2    Strobl, L.J.3    Moreau-Gachelin, F.4
  • 32
    • 0028124316 scopus 로고
    • The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein
    • Grossman SR, Johannsen E, Tong X, Yalamanchili R, Kieff E, (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.
    • (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
  • 33
    • 78650986640 scopus 로고    scopus 로고
    • STAT6 signaling pathway activated by the cytokines IL-4 and IL-13 induces expression of the Epstein-Barr virus-encoded protein LMP-1 in absence of EBNA-2: implications for the type II EBV latent gene expression in Hodgkin lymphoma
    • Kis LL, Gerasimcik N, Salamon D, Persson EK, Nagy N, et al. (2011) STAT6 signaling pathway activated by the cytokines IL-4 and IL-13 induces expression of the Epstein-Barr virus-encoded protein LMP-1 in absence of EBNA-2: implications for the type II EBV latent gene expression in Hodgkin lymphoma. Blood 117: 165-174.
    • (2011) Blood , vol.117 , pp. 165-174
    • Kis, L.L.1    Gerasimcik, N.2    Salamon, D.3    Persson, E.K.4    Nagy, N.5
  • 34
    • 76249098582 scopus 로고    scopus 로고
    • IL-21 imposes a type II EBV gene expression on type III and type I B cells by the repression of C- and activation of LMP-1-promoter
    • Kis LL, Salamon D, Persson EK, Nagy N, Scheeren FA, et al. (2010) IL-21 imposes a type II EBV gene expression on type III and type I B cells by the repression of C- and activation of LMP-1-promoter. Proc Natl Acad Sci U S A 107: 872-877.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 872-877
    • Kis, L.L.1    Salamon, D.2    Persson, E.K.3    Nagy, N.4    Scheeren, F.A.5
  • 35
    • 33645508895 scopus 로고    scopus 로고
    • IL-10 can induce the expression of EBV-encoded latent membrane protein-1 (LMP-1) in the absence of EBNA-2 in B lymphocytes and in Burkitt lymphoma- and NK lymphoma-derived cell lines
    • Kis LL, Takahara M, Nagy N, Klein G, Klein E, (2006) IL-10 can induce the expression of EBV-encoded latent membrane protein-1 (LMP-1) in the absence of EBNA-2 in B lymphocytes and in Burkitt lymphoma- and NK lymphoma-derived cell lines. Blood 107: 2928-2935.
    • (2006) Blood , vol.107 , pp. 2928-2935
    • Kis, L.L.1    Takahara, M.2    Nagy, N.3    Klein, G.4    Klein, E.5
  • 36
    • 41649104652 scopus 로고    scopus 로고
    • Interleukin-21 regulates expression of key Epstein-Barr virus oncoproteins, EBNA2 and LMP1, in infected human B cells
    • Konforte D, Simard N, Paige CJ, (2008) Interleukin-21 regulates expression of key Epstein-Barr virus oncoproteins, EBNA2 and LMP1, in infected human B cells. Virology 374: 100-113.
    • (2008) Virology , vol.374 , pp. 100-113
    • Konforte, D.1    Simard, N.2    Paige, C.J.3
  • 37
    • 0035123574 scopus 로고    scopus 로고
    • Linkage between STAT regulation and Epstein-Barr virus gene expression in tumors
    • Chen H, Lee JM, Zong Y, Borowitz M, Ng MH, et al. (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
  • 38
    • 0037378534 scopus 로고    scopus 로고
    • A positive autoregulatory loop of LMP1 expression and STAT activation in epithelial cells latently infected with Epstein-Barr virus
    • Chen H, Hutt-Fletcher L, Cao L, Hayward SD, (2003) A positive autoregulatory loop of LMP1 expression and STAT activation in epithelial cells latently infected with Epstein-Barr virus. J Virol 77: 4139-4148.
    • (2003) J Virol , vol.77 , pp. 4139-4148
    • Chen, H.1    Hutt-Fletcher, L.2    Cao, L.3    Hayward, S.D.4
  • 39
    • 77954406525 scopus 로고    scopus 로고
    • HSP90 is essential for Jak-STAT signaling in classical Hodgkin lymphoma cells
    • Schoof N, von Bonin F, Trumper L, Kube D, (2009) HSP90 is essential for Jak-STAT signaling in classical Hodgkin lymphoma cells. Cell Commun Signal 7: 17.
    • (2009) Cell Commun Signal , vol.7 , pp. 17
    • Schoof, N.1    von Bonin, F.2    Trumper, L.3    Kube, D.4
  • 40
    • 33751584842 scopus 로고    scopus 로고
    • Concomitant increase of LMP1 and CD25 (IL-2-receptor alpha) expression induced by IL-10 in the EBV-positive NK lines SNK6 and KAI3
    • Takahara M, Kis LL, Nagy N, Liu A, Harabuchi Y, et al. (2006) Concomitant increase of LMP1 and CD25 (IL-2-receptor alpha) expression induced by IL-10 in the EBV-positive NK lines SNK6 and KAI3. Int J Cancer 119: 2775-2783.
    • (2006) Int J Cancer , vol.119 , pp. 2775-2783
    • Takahara, M.1    Kis, L.L.2    Nagy, N.3    Liu, A.4    Harabuchi, Y.5
  • 41
    • 0036681795 scopus 로고    scopus 로고
    • A role for NF-kappa B activation in perforin expression of NK cells upon IL-2 receptor signaling
    • Zhou J, Zhang J, Lichtenheld MG, Meadows GG, (2002) A role for NF-kappa B activation in perforin expression of NK cells upon IL-2 receptor signaling. J Immunol 169: 1319-1325.
    • (2002) J Immunol , vol.169 , pp. 1319-1325
    • Zhou, J.1    Zhang, J.2    Lichtenheld, M.G.3    Meadows, G.G.4
  • 42
    • 0347951253 scopus 로고    scopus 로고
    • Additive interaction of oxaliplatin and 17-allylamino-17-demethoxygeldanamycin in colon cancer cell lines results from inhibition of nuclear factor kappaB signaling
    • Rakitina TV, Vasilevskaya IA, O'Dwyer PJ, (2003) Additive interaction of oxaliplatin and 17-allylamino-17-demethoxygeldanamycin in colon cancer cell lines results from inhibition of nuclear factor kappaB signaling. Cancer Res 63: 8600-8605.
    • (2003) Cancer Res , vol.63 , pp. 8600-8605
    • Rakitina, T.V.1    Vasilevskaya, I.A.2    O'Dwyer, P.J.3
  • 43
    • 31544470589 scopus 로고    scopus 로고
    • 17-allylamino-17-demethoxygeldanamycin synergistically potentiates tumor necrosis factor-induced lung cancer cell death by blocking the nuclear factor-kappaB pathway
    • Wang X, Ju W, Renouard J, Aden J, Belinsky SA, et al. (2006) 17-allylamino-17-demethoxygeldanamycin synergistically potentiates tumor necrosis factor-induced lung cancer cell death by blocking the nuclear factor-kappaB pathway. Cancer Res 66: 1089-1095.
    • (2006) Cancer Res , vol.66 , pp. 1089-1095
    • Wang, X.1    Ju, W.2    Renouard, J.3    Aden, J.4    Belinsky, S.A.5
  • 44
    • 0028171081 scopus 로고
    • The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements
    • Waltzer L, Logeat F, Brou C, Israel A, Sergeant A, et al. (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.
    • (1994) EMBO J , vol.13 , pp. 5633-5638
    • Waltzer, L.1    Logeat, F.2    Brou, C.3    Israel, A.4    Sergeant, A.5
  • 45
    • 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, Jansson A, Yang W, Lain S, Nilsson T, et al. (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 (Pt 11): 2679-2692.
    • (1995) J Gen Virol , vol.76 , Issue.Pt 11 , pp. 2679-2692
    • Sjoblom, A.1    Jansson, A.2    Yang, W.3    Lain, S.4    Nilsson, T.5
  • 46
    • 0028811194 scopus 로고
    • Domains of the Epstein-Barr virus nuclear antigen 2 (EBNA2) involved in the transactivation of the latent membrane protein 1 and the EBNA Cp promoters
    • Sjoblom A, Nerstedt A, Jansson A, Rymo L, (1995) Domains of the Epstein-Barr virus nuclear antigen 2 (EBNA2) involved in the transactivation of the latent membrane protein 1 and the EBNA Cp promoters. J Gen Virol 76 (Pt 11): 2669-2678.
    • (1995) J Gen Virol , vol.76 , Issue.Pt 11 , pp. 2669-2678
    • Sjoblom, A.1    Nerstedt, A.2    Jansson, A.3    Rymo, L.4
  • 47
    • 59649086503 scopus 로고    scopus 로고
    • SNX-2112, a selective Hsp90 inhibitor, potently inhibits tumor cell growth, angiogenesis, and osteoclastogenesis in multiple myeloma and other hematologic tumors by abrogating signaling via Akt and ERK
    • Okawa Y, Hideshima T, Steed P, Vallet S, Hall S, et al. (2009) SNX-2112, a selective Hsp90 inhibitor, potently inhibits tumor cell growth, angiogenesis, and osteoclastogenesis in multiple myeloma and other hematologic tumors by abrogating signaling via Akt and ERK. Blood 113: 846-855.
    • (2009) Blood , vol.113 , pp. 846-855
    • Okawa, Y.1    Hideshima, T.2    Steed, P.3    Vallet, S.4    Hall, S.5
  • 48
    • 76449118324 scopus 로고    scopus 로고
    • Radicicol-mediated inhibition of Bcr-Abl in K562 cells induced p38-MAPK dependent erythroid differentiation and PU.1 down-regulation
    • Morceau F, Buck I, Dicato M, Diederich M, (2008) Radicicol-mediated inhibition of Bcr-Abl in K562 cells induced p38-MAPK dependent erythroid differentiation and PU.1 down-regulation. Biofactors 34: 313-329.
    • (2008) Biofactors , vol.34 , pp. 313-329
    • Morceau, F.1    Buck, I.2    Dicato, M.3    Diederich, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.