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Volumn 10, Issue 8, 2014, Pages

EBNA3C Augments Pim-1 Mediated Phosphorylation and Degradation of p21 to Promote B-Cell Proliferation

Author keywords

[No Author keywords available]

Indexed keywords

EPSTEIN BARR VIRUS ANTIGEN; EPSTEIN BARR VIRUS NUCLEAR ANTIGEN 3C; ETOPOSIDE; PROTEIN KINASE PIM 1; PROTEIN P21; PROTEIN P53; UNCLASSIFIED DRUG; EBNA-3C, EPSTEIN-BARR VIRUS;

EID: 84928044072     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004304     Document Type: Article
Times cited : (43)

References (102)
  • 1
    • 0014596168 scopus 로고
    • Antibodies to Epstein-Barr virus in Burkitt's lymphoma and control groups
    • Henle G, Henle W, Clifford P, Diehl V, Kafuko GW, et al. (1969) Antibodies to Epstein-Barr virus in Burkitt's lymphoma and control groups. J Natl Cancer Inst 43: 1147–1157.
    • (1969) J Natl Cancer Inst , vol.43 , pp. 1147-1157
    • Henle, G.1    Henle, W.2    Clifford, P.3    Diehl, V.4    Kafuko, G.W.5
  • 2
    • 0034774343 scopus 로고    scopus 로고
    • Demonstration of Epstein-Barr virus in odontogenic and nonodontogenic tumors by the polymerase chain reaction (PCR)
    • Jang HS, Cho JO, Yoon CY, Kim HJ, Park JC, (2001) Demonstration of Epstein-Barr virus in odontogenic and nonodontogenic tumors by the polymerase chain reaction (PCR). J Oral Pathol Med 30: 603–610.
    • (2001) J Oral Pathol Med , vol.30 , pp. 603-610
    • Jang, H.S.1    Cho, J.O.2    Yoon, C.Y.3    Kim, H.J.4    Park, J.C.5
  • 3
    • 0036435166 scopus 로고    scopus 로고
    • Epstein-Barr virus in the pathogenesis of NPC
    • Raab-Traub N, (2002) Epstein-Barr virus in the pathogenesis of NPC. Semin Cancer Biol 12: 431–441.
    • (2002) Semin Cancer Biol , vol.12 , pp. 431-441
    • Raab-Traub, N.1
  • 5
    • 79955537371 scopus 로고    scopus 로고
    • Epstein-Barr Virus-related post-transplant lymphoproliferative disorders: pathogenetic insights for targeted therapy
    • Nourse JP, Jones K, Gandhi MK, Epstein-Barr Virus-related post-transplant lymphoproliferative disorders: pathogenetic insights for targeted therapy. Am J Transplant 11: 888–895.
    • Am J Transplant , vol.11 , pp. 888-895
    • Nourse, J.P.1    Jones, K.2    Gandhi, M.K.3
  • 6
    • 0033995792 scopus 로고    scopus 로고
    • Epstein-barr virus-associated malignancies: epidemiologic patterns and etiologic implications
    • Hsu JL, Glaser SL, (2000) Epstein-barr virus-associated malignancies: epidemiologic patterns and etiologic implications. Crit Rev Oncol Hematol 34: 27–53.
    • (2000) Crit Rev Oncol Hematol , vol.34 , pp. 27-53
    • Hsu, J.L.1    Glaser, S.L.2
  • 7
    • 0032873895 scopus 로고    scopus 로고
    • Virus-associated lymphomas
    • Cesarman E, Mesri EA, (1999) Virus-associated lymphomas. Curr Opin Oncol 11: 322–332.
    • (1999) Curr Opin Oncol , vol.11 , pp. 322-332
    • Cesarman, E.1    Mesri, E.A.2
  • 9
    • 0014125725 scopus 로고
    • Herpes-type virus and chromosome marker in normal leukocytes after growth with irradiated Burkitt cells
    • Henle W, Diehl V, Kohn G, Zur Hausen H, Henle G, (1967) Herpes-type virus and chromosome marker in normal leukocytes after growth with irradiated Burkitt cells. Science 157: 1064–1065.
    • (1967) Science , vol.157 , pp. 1064-1065
    • Henle, W.1    Diehl, V.2    Kohn, G.3    Zur Hausen, H.4    Henle, G.5
  • 10
    • 0033770573 scopus 로고    scopus 로고
    • The expression and function of Epstein-Barr virus encoded latent genes
    • Young LS, Dawson CW, Eliopoulos AG, (2000) The expression and function of Epstein-Barr virus encoded latent genes. Mol Pathol 53: 238–247.
    • (2000) Mol Pathol , vol.53 , pp. 238-247
    • Young, L.S.1    Dawson, C.W.2    Eliopoulos, A.G.3
  • 11
    • 67650899059 scopus 로고    scopus 로고
    • Epstein-barr virus latency in B cells leads to epigenetic repression and CpG methylation of the tumour suppressor gene Bim
    • Paschos K, Smith P, Anderton E, Middeldorp JM, White RE, et al. (2009) Epstein-barr virus latency in B cells leads to epigenetic repression and CpG methylation of the tumour suppressor gene Bim. PLoS Pathog 5: e1000492.
    • (2009) PLoS Pathog , vol.5 , pp. e1000492
    • Paschos, K.1    Smith, P.2    Anderton, E.3    Middeldorp, J.M.4    White, R.E.5
  • 12
    • 78651099289 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C regulated genes in lymphoblastoid cell lines
    • Zhao B, Mar JC, Maruo S, Lee S, Gewurz BE, et al. Epstein-Barr virus nuclear antigen 3C regulated genes in lymphoblastoid cell lines. Proc Natl Acad Sci U S A 108: 337–342.
    • Proc Natl Acad Sci U S A , vol.108 , pp. 337-342
    • Zhao, B.1    Mar, J.C.2    Maruo, S.3    Lee, S.4    Gewurz, B.E.5
  • 13
    • 79952170344 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigens 3C and 3A maintain lymphoblastoid cell growth by repressing p16INK4A and p14ARF expression
    • Maruo S, Zhao B, Johannsen E, Kieff E, Zou J, et al. Epstein-Barr virus nuclear antigens 3C and 3A maintain lymphoblastoid cell growth by repressing p16INK4A and p14ARF expression. Proc Natl Acad Sci U S A 108: 1919–1924.
    • Proc Natl Acad Sci U S A , vol.108 , pp. 1919-1924
    • Maruo, S.1    Zhao, B.2    Johannsen, E.3    Kieff, E.4    Zou, J.5
  • 14
    • 0036511237 scopus 로고    scopus 로고
    • The Epstein Barr nuclear antigen EBNA3C regulates transcription, cell transformation and cell migration
    • Subramanian C, Knight JS, Robertson ES, (2002) The Epstein Barr nuclear antigen EBNA3C regulates transcription, cell transformation and cell migration. Front Biosci 7: d704–716.
    • (2002) Front Biosci , vol.7 , pp. d704-716
    • Subramanian, C.1    Knight, J.S.2    Robertson, E.S.3
  • 15
    • 0029990265 scopus 로고    scopus 로고
    • The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa)
    • Robertson ES, Lin J, Kieff E, (1996) The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa). J Virol 70: 3068–3074.
    • (1996) J Virol , vol.70 , pp. 3068-3074
    • Robertson, E.S.1    Lin, J.2    Kieff, E.3
  • 16
    • 0028342725 scopus 로고
    • Epstein-Barr virus nuclear antigen EBNA3C/6 expression maintains the level of latent membrane protein 1 in G1-arrested cells
    • Allday MJ, Farrell PJ, (1994) Epstein-Barr virus nuclear antigen EBNA3C/6 expression maintains the level of latent membrane protein 1 in G1-arrested cells. J Virol 68: 3491–3498.
    • (1994) J Virol , vol.68 , pp. 3491-3498
    • Allday, M.J.1    Farrell, P.J.2
  • 17
    • 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, (2003) 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 77: 4261–4272.
    • (2003) J Virol , vol.77 , pp. 4261-4272
    • Knight, J.S.1    Lan, K.2    Subramanian, C.3    Robertson, E.S.4
  • 18
    • 0036337847 scopus 로고    scopus 로고
    • The metastatic suppressor Nm23-H1 interacts with EBNA3C at sequences located between the glutamine- and proline-rich domains and can cooperate in activation of transcription
    • Subramanian C, Robertson ES, (2002) The metastatic suppressor Nm23-H1 interacts with EBNA3C at sequences located between the glutamine- and proline-rich domains and can cooperate in activation of transcription. J Virol 76: 8702–8709.
    • (2002) J Virol , vol.76 , pp. 8702-8709
    • Subramanian, C.1    Robertson, E.S.2
  • 19
    • 84855265398 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C stabilizes Gemin3 to block p53-mediated apoptosis
    • Cai Q, Guo Y, Xiao B, Banerjee S, Saha A, et al. Epstein-Barr virus nuclear antigen 3C stabilizes Gemin3 to block p53-mediated apoptosis. PLoS Pathog 7: e1002418.
    • PLoS Pathog , vol.7 , pp. e1002418
    • Cai, Q.1    Guo, Y.2    Xiao, B.3    Banerjee, S.4    Saha, A.5
  • 20
    • 41949101446 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C interacts with and enhances the stability of the c-Myc oncoprotein
    • Bajaj BG, Murakami M, Cai Q, Verma SC, Lan K, et al. (2008) Epstein-Barr virus nuclear antigen 3C interacts with and enhances the stability of the c-Myc oncoprotein. J Virol 82: 4082–4090.
    • (2008) J Virol , vol.82 , pp. 4082-4090
    • Bajaj, B.G.1    Murakami, M.2    Cai, Q.3    Verma, S.C.4    Lan, K.5
  • 21
    • 67349118372 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C targets p53 and modulates its transcriptional and apoptotic activities
    • Yi F, Saha A, Murakami M, Kumar P, Knight JS, et al. (2009) Epstein-Barr virus nuclear antigen 3C targets p53 and modulates its transcriptional and apoptotic activities. Virology 388: 236–247.
    • (2009) Virology , vol.388 , pp. 236-247
    • Yi, F.1    Saha, A.2    Murakami, M.3    Kumar, P.4    Knight, J.S.5
  • 22
    • 79952209417 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C facilitates G1-S transition by stabilizing and enhancing the function of cyclin D1
    • Saha A, Halder S, Upadhyay SK, Lu J, Kumar P, et al. Epstein-Barr virus nuclear antigen 3C facilitates G1-S transition by stabilizing and enhancing the function of cyclin D1. PLoS Pathog 7: e1001275.
    • PLoS Pathog , vol.7 , pp. e1001275
    • Saha, A.1    Halder, S.2    Upadhyay, S.K.3    Lu, J.4    Kumar, P.5
  • 23
    • 77953180976 scopus 로고    scopus 로고
    • PIM serine/threonine kinases in the pathogenesis and therapy of hematologic malignancies and solid cancers
    • Brault L, Gasser C, Bracher F, Huber K, Knapp S, et al. PIM serine/threonine kinases in the pathogenesis and therapy of hematologic malignancies and solid cancers. Haematologica 95: 1004–1015.
    • Haematologica , vol.95 , pp. 1004-1015
    • Brault, L.1    Gasser, C.2    Bracher, F.3    Huber, K.4    Knapp, S.5
  • 24
    • 61749092591 scopus 로고    scopus 로고
    • PIM-1-specific mAb suppresses human and mouse tumor growth by decreasing PIM-1 levels, reducing Akt phosphorylation, and activating apoptosis
    • Hu XF, Li J, Vandervalk S, Wang Z, Magnuson NS, et al. (2009) PIM-1-specific mAb suppresses human and mouse tumor growth by decreasing PIM-1 levels, reducing Akt phosphorylation, and activating apoptosis. J Clin Invest 119: 362–375.
    • (2009) J Clin Invest , vol.119 , pp. 362-375
    • Hu, X.F.1    Li, J.2    Vandervalk, S.3    Wang, Z.4    Magnuson, N.S.5
  • 25
    • 34249747880 scopus 로고    scopus 로고
    • Evidence that the Pim1 kinase gene is a direct target of HOXA9
    • Hu YL, Passegue E, Fong S, Largman C, Lawrence HJ, (2007) Evidence that the Pim1 kinase gene is a direct target of HOXA9. Blood 109: 4732–4738.
    • (2007) Blood , vol.109 , pp. 4732-4738
    • Hu, Y.L.1    Passegue, E.2    Fong, S.3    Largman, C.4    Lawrence, H.J.5
  • 26
    • 0024408829 scopus 로고
    • The human protooncogene product p33pim is expressed during fetal hematopoiesis and in diverse leukemias
    • Amson R, Sigaux F, Przedborski S, Flandrin G, Givol D, et al. (1989) The human protooncogene product p33pim is expressed during fetal hematopoiesis and in diverse leukemias. Proc Natl Acad Sci U S A 86: 8857–8861.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 8857-8861
    • Amson, R.1    Sigaux, F.2    Przedborski, S.3    Flandrin, G.4    Givol, D.5
  • 27
    • 36849037512 scopus 로고    scopus 로고
    • Pim-1 regulates cardiomyocyte survival downstream of Akt
    • Muraski JA, Rota M, Misao Y, Fransioli J, Cottage C, et al. (2007) Pim-1 regulates cardiomyocyte survival downstream of Akt. Nat Med 13: 1467–1475.
    • (2007) Nat Med , vol.13 , pp. 1467-1475
    • Muraski, J.A.1    Rota, M.2    Misao, Y.3    Fransioli, J.4    Cottage, C.5
  • 28
    • 0034708236 scopus 로고    scopus 로고
    • Developmental expression of pim kinases suggests functions also outside of the hematopoietic system
    • Eichmann A, Yuan L, Breant C, Alitalo K, Koskinen PJ, (2000) Developmental expression of pim kinases suggests functions also outside of the hematopoietic system. Oncogene 19: 1215–1224.
    • (2000) Oncogene , vol.19 , pp. 1215-1224
    • Eichmann, A.1    Yuan, L.2    Breant, C.3    Alitalo, K.4    Koskinen, P.J.5
  • 30
    • 0027497115 scopus 로고
    • Expression of a Pim-1 transgene accelerates lymphoproliferation and inhibits apoptosis in lpr/lpr mice
    • Moroy T, Grzeschiczek A, Petzold S, Hartmann KU, (1993) Expression of a Pim-1 transgene accelerates lymphoproliferation and inhibits apoptosis in lpr/lpr mice. Proc Natl Acad Sci U S A 90: 10734–10738.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10734-10738
    • Moroy, T.1    Grzeschiczek, A.2    Petzold, S.3    Hartmann, K.U.4
  • 31
    • 0026019439 scopus 로고
    • The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG
    • Saris CJ, Domen J, Berns A, (1991) The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG. EMBO J 10: 655–664.
    • (1991) EMBO J , vol.10 , pp. 655-664
    • Saris, C.J.1    Domen, J.2    Berns, A.3
  • 32
    • 0030932844 scopus 로고    scopus 로고
    • Identification of the autophosphorylation sites of the Xenopus laevis Pim-1 proto-oncogene-encoded protein kinase
    • Palaty CK, Kalmar G, Tai G, Oh S, Amankawa L, et al. (1997) Identification of the autophosphorylation sites of the Xenopus laevis Pim-1 proto-oncogene-encoded protein kinase. J Biol Chem 272: 10514–10521.
    • (1997) J Biol Chem , vol.272 , pp. 10514-10521
    • Palaty, C.K.1    Kalmar, G.2    Tai, G.3    Oh, S.4    Amankawa, L.5
  • 33
    • 0030632044 scopus 로고    scopus 로고
    • Phosphorylation site substrate specificity determinants for the Pim-1 protooncogene-encoded protein kinase
    • Palaty CK, Clark-Lewis I, Leung D, Pelech SL, (1997) Phosphorylation site substrate specificity determinants for the Pim-1 protooncogene-encoded protein kinase. Biochem Cell Biol 75: 153–162.
    • (1997) Biochem Cell Biol , vol.75 , pp. 153-162
    • Palaty, C.K.1    Clark-Lewis, I.2    Leung, D.3    Pelech, S.L.4
  • 35
    • 0037121534 scopus 로고    scopus 로고
    • Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1 kinase
    • Wang Z, Bhattacharya N, Mixter PF, Wei W, Sedivy J, et al. (2002) Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1 kinase. Biochim Biophys Acta 1593: 45–55.
    • (2002) Biochim Biophys Acta , vol.1593 , pp. 45-55
    • Wang, Z.1    Bhattacharya, N.2    Mixter, P.F.3    Wei, W.4    Sedivy, J.5
  • 36
    • 34548670994 scopus 로고    scopus 로고
    • Pim-1 kinase-dependent phosphorylation of p21Cip1/WAF1 regulates its stability and cellular localization in H1299 cells
    • Zhang Y, Wang Z, Magnuson NS, (2007) Pim-1 kinase-dependent phosphorylation of p21Cip1/WAF1 regulates its stability and cellular localization in H1299 cells. Mol Cancer Res 5: 909–922.
    • (2007) Mol Cancer Res , vol.5 , pp. 909-922
    • Zhang, Y.1    Wang, Z.2    Magnuson, N.S.3
  • 37
    • 0033603454 scopus 로고    scopus 로고
    • Physical and functional interactions between Pim-1 kinase and Cdc25A phosphatase. Implications for the Pim-1-mediated activation of the c-Myc signaling pathway
    • Mochizuki T, Kitanaka C, Noguchi K, Muramatsu T, Asai A, et al. (1999) Physical and functional interactions between Pim-1 kinase and Cdc25A phosphatase. Implications for the Pim-1-mediated activation of the c-Myc signaling pathway. J Biol Chem 274: 18659–18666.
    • (1999) J Biol Chem , vol.274 , pp. 18659-18666
    • Mochizuki, T.1    Kitanaka, C.2    Noguchi, K.3    Muramatsu, T.4    Asai, A.5
  • 38
    • 0035370441 scopus 로고    scopus 로고
    • Pim-1 negatively regulates the activity of PTP-U2S phosphatase and influences terminal differentiation and apoptosis of monoblastoid leukemia cells
    • Wang Z, Bhattacharya N, Meyer MK, Seimiya H, Tsuruo T, et al. (2001) Pim-1 negatively regulates the activity of PTP-U2S phosphatase and influences terminal differentiation and apoptosis of monoblastoid leukemia cells. Arch Biochem Biophys 390: 9–18.
    • (2001) Arch Biochem Biophys , vol.390 , pp. 9-18
    • Wang, Z.1    Bhattacharya, N.2    Meyer, M.K.3    Seimiya, H.4    Tsuruo, T.5
  • 40
    • 9144225473 scopus 로고    scopus 로고
    • The oncogenic serine/threonine kinase Pim-1 phosphorylates and inhibits the activity of Cdc25C-associated kinase 1 (C-TAK1): a novel role for Pim-1 at the G2/M cell cycle checkpoint
    • Bachmann M, Hennemann H, Xing PX, Hoffmann I, Moroy T, (2004) The oncogenic serine/threonine kinase Pim-1 phosphorylates and inhibits the activity of Cdc25C-associated kinase 1 (C-TAK1): a novel role for Pim-1 at the G2/M cell cycle checkpoint. J Biol Chem 279: 48319–48328.
    • (2004) J Biol Chem , vol.279 , pp. 48319-48328
    • Bachmann, M.1    Hennemann, H.2    Xing, P.X.3    Hoffmann, I.4    Moroy, T.5
  • 41
    • 29244464759 scopus 로고    scopus 로고
    • The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C
    • Bachmann M, Kosan C, Xing PX, Montenarh M, Hoffmann I, et al. (2006) The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C. Int J Biochem Cell Biol 38: 430–443.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 430-443
    • Bachmann, M.1    Kosan, C.2    Xing, P.X.3    Montenarh, M.4    Hoffmann, I.5
  • 42
    • 0034721081 scopus 로고    scopus 로고
    • Pim-1 kinase protects hematopoietic FDC cells from genotoxin-induced death
    • Pircher TJ, Zhao S, Geiger JN, Joneja B, Wojchowski DM, (2000) Pim-1 kinase protects hematopoietic FDC cells from genotoxin-induced death. Oncogene 19: 3684–3692.
    • (2000) Oncogene , vol.19 , pp. 3684-3692
    • Pircher, T.J.1    Zhao, S.2    Geiger, J.N.3    Joneja, B.4    Wojchowski, D.M.5
  • 43
    • 33745886845 scopus 로고    scopus 로고
    • KSHV encoded LANA upregulates Pim-1 and is a substrate for its kinase activity
    • Bajaj BG, Verma SC, Lan K, Cotter MA, Woodman ZL, et al. (2006) KSHV encoded LANA upregulates Pim-1 and is a substrate for its kinase activity. Virology 351: 18–28.
    • (2006) Virology , vol.351 , pp. 18-28
    • Bajaj, B.G.1    Verma, S.C.2    Lan, K.3    Cotter, M.A.4    Woodman, Z.L.5
  • 44
    • 77956546771 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 increases chemo-resistance of cancer cells via cytoplasmic sequestration of Pim-1
    • Kim JH, Kim WS, Yun Y, Park C, Epstein-Barr virus latent membrane protein 1 increases chemo-resistance of cancer cells via cytoplasmic sequestration of Pim-1. Cell Signal 22: 1858–1863.
    • Cell Signal , vol.22 , pp. 1858-1863
    • Kim, J.H.1    Kim, W.S.2    Yun, Y.3    Park, C.4
  • 45
    • 13844266003 scopus 로고    scopus 로고
    • Pim kinases are upregulated during Epstein-Barr virus infection and enhance EBNA2 activity
    • Rainio EM, Ahlfors H, Carter KL, Ruuska M, Matikainen S, et al. (2005) Pim kinases are upregulated during Epstein-Barr virus infection and enhance EBNA2 activity. Virology 333: 201–206.
    • (2005) Virology , vol.333 , pp. 201-206
    • Rainio, E.M.1    Ahlfors, H.2    Carter, K.L.3    Ruuska, M.4    Matikainen, S.5
  • 46
    • 84861206434 scopus 로고    scopus 로고
    • E2F1 mediated apoptosis induced by the DNA damage response is blocked by EBV nuclear antigen 3C in lymphoblastoid cells
    • Saha A, Lu J, Morizur L, Upadhyay SK, Aj MP, et al. E2F1 mediated apoptosis induced by the DNA damage response is blocked by EBV nuclear antigen 3C in lymphoblastoid cells. PLoS Pathog 8: e1002573.
    • PLoS Pathog , vol.8 , pp. e1002573
    • Saha, A.1    Lu, J.2    Morizur, L.3    Upadhyay, S.K.4    Aj, M.P.5
  • 47
    • 0028226729 scopus 로고
    • Precipitation of the Epstein-Barr virus protein EBNA 2 by an EBNA 3c-specific monoclonal antibody
    • Maunders MJ, Petti L, Rowe M, (1994) Precipitation of the Epstein-Barr virus protein EBNA 2 by an EBNA 3c-specific monoclonal antibody. J Gen Virol 75 (Pt 4): 769–778.
    • (1994) J Gen Virol , vol.75 , pp. 769-778
    • Maunders, M.J.1    Petti, L.2    Rowe, M.3
  • 48
    • 67650498487 scopus 로고    scopus 로고
    • Pim-1 kinase expression predicts radiation response in squamocellular carcinoma of head and neck and is under the control of epidermal growth factor receptor
    • Peltola K, Hollmen M, Maula SM, Rainio E, Ristamaki R, et al. (2009) Pim-1 kinase expression predicts radiation response in squamocellular carcinoma of head and neck and is under the control of epidermal growth factor receptor. Neoplasia 11: 629–636.
    • (2009) Neoplasia , vol.11 , pp. 629-636
    • Peltola, K.1    Hollmen, M.2    Maula, S.M.3    Rainio, E.4    Ristamaki, R.5
  • 50
    • 66149106996 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C augments Mdm2-mediated p53 ubiquitination and degradation by deubiquitinating Mdm2
    • Saha A, Murakami M, Kumar P, Bajaj B, Sims K, et al. (2009) Epstein-Barr virus nuclear antigen 3C augments Mdm2-mediated p53 ubiquitination and degradation by deubiquitinating Mdm2. J Virol 83: 4652–4669.
    • (2009) J Virol , vol.83 , pp. 4652-4669
    • Saha, A.1    Murakami, M.2    Kumar, P.3    Bajaj, B.4    Sims, K.5
  • 51
    • 84878507873 scopus 로고    scopus 로고
    • The EBV Latent Antigen 3C Inhibits Apoptosis through Targeted Regulation of Interferon Regulatory Factors 4 and 8
    • Banerjee S, Lu J, Cai Q, Saha A, Jha HC, et al. The EBV Latent Antigen 3C Inhibits Apoptosis through Targeted Regulation of Interferon Regulatory Factors 4 and 8. PLoS Pathog 9: e1003314.
    • PLoS Pathog , vol.9 , pp. e1003314
    • Banerjee, S.1    Lu, J.2    Cai, Q.3    Saha, A.4    Jha, H.C.5
  • 52
    • 29444438631 scopus 로고    scopus 로고
    • Epstein-Barr virus latent antigen 3C can mediate the degradation of the retinoblastoma protein through an SCF cellular ubiquitin ligase
    • Knight JS, Sharma N, Robertson ES, (2005) Epstein-Barr virus latent antigen 3C can mediate the degradation of the retinoblastoma protein through an SCF cellular ubiquitin ligase. Proc Natl Acad Sci U S A 102: 18562–18566.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18562-18566
    • Knight, J.S.1    Sharma, N.2    Robertson, E.S.3
  • 53
    • 57049101684 scopus 로고    scopus 로고
    • Ki67 and PIM1 expression predict outcome in mantle cell lymphoma treated with high dose therapy, stem cell transplantation and rituximab: a Cancer and Leukemia Group B 59909 correlative science study
    • Hsi ED, Jung SH, Lai R, Johnson JL, Cook JR, et al. (2008) Ki67 and PIM1 expression predict outcome in mantle cell lymphoma treated with high dose therapy, stem cell transplantation and rituximab: a Cancer and Leukemia Group B 59909 correlative science study. Leuk Lymphoma 49: 2081–2090.
    • (2008) Leuk Lymphoma , vol.49 , pp. 2081-2090
    • Hsi, E.D.1    Jung, S.H.2    Lai, R.3    Johnson, J.L.4    Cook, J.R.5
  • 54
    • 30344470789 scopus 로고    scopus 로고
    • Transcript profiling in peripheral T-cell lymphoma, not otherwise specified, and diffuse large B-cell lymphoma identifies distinct tumor profile signatures
    • Mahadevan D, Spier C, Della Croce K, Miller S, George B, et al. (2005) Transcript profiling in peripheral T-cell lymphoma, not otherwise specified, and diffuse large B-cell lymphoma identifies distinct tumor profile signatures. Mol Cancer Ther 4: 1867–1879.
    • (2005) Mol Cancer Ther , vol.4 , pp. 1867-1879
    • Mahadevan, D.1    Spier, C.2    Della Croce, K.3    Miller, S.4    George, B.5
  • 55
    • 3343007095 scopus 로고    scopus 로고
    • Pim-1 kinase promotes inactivation of the pro-apoptotic Bad protein by phosphorylating it on the Ser112 gatekeeper site
    • Aho TL, Sandholm J, Peltola KJ, Mankonen HP, Lilly M, et al. (2004) Pim-1 kinase promotes inactivation of the pro-apoptotic Bad protein by phosphorylating it on the Ser112 gatekeeper site. FEBS Lett 571: 43–49.
    • (2004) FEBS Lett , vol.571 , pp. 43-49
    • Aho, T.L.1    Sandholm, J.2    Peltola, K.J.3    Mankonen, H.P.4    Lilly, M.5
  • 56
  • 57
    • 0037083465 scopus 로고    scopus 로고
    • Cutting edge: Transcriptional activity of NFATc1 is enhanced by the Pim-1 kinase
    • Rainio EM, Sandholm J, Koskinen PJ, (2002) Cutting edge: Transcriptional activity of NFATc1 is enhanced by the Pim-1 kinase. J Immunol 168: 1524–1527.
    • (2002) J Immunol , vol.168 , pp. 1524-1527
    • Rainio, E.M.1    Sandholm, J.2    Koskinen, P.J.3
  • 58
    • 0033959911 scopus 로고    scopus 로고
    • Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1)
    • Koike N, Maita H, Taira T, Ariga H, Iguchi-Ariga SM, (2000) Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1). FEBS Lett 467: 17–21.
    • (2000) FEBS Lett , vol.467 , pp. 17-21
    • Koike, N.1    Maita, H.2    Taira, T.3    Ariga, H.4    Iguchi-Ariga, S.M.5
  • 59
    • 0033869162 scopus 로고    scopus 로고
    • PAP-1, a novel target protein of phosphorylation by pim-1 kinase
    • Maita H, Harada Y, Nagakubo D, Kitaura H, Ikeda M, et al. (2000) PAP-1, a novel target protein of phosphorylation by pim-1 kinase. Eur J Biochem 267: 5168–5178.
    • (2000) Eur J Biochem , vol.267 , pp. 5168-5178
    • Maita, H.1    Harada, Y.2    Nagakubo, D.3    Kitaura, H.4    Ikeda, M.5
  • 60
    • 0035754569 scopus 로고    scopus 로고
    • Pim-1: a serine/threonine kinase with a role in cell survival, proliferation, differentiation and tumorigenesis
    • Wang Z, Bhattacharya N, Weaver M, Petersen K, Meyer M, et al. (2001) Pim-1: a serine/threonine kinase with a role in cell survival, proliferation, differentiation and tumorigenesis. J Vet Sci 2: 167–179.
    • (2001) J Vet Sci , vol.2 , pp. 167-179
    • Wang, Z.1    Bhattacharya, N.2    Weaver, M.3    Petersen, K.4    Meyer, M.5
  • 61
    • 67649424560 scopus 로고    scopus 로고
    • p21 in cancer: intricate networks and multiple activities
    • Abbas T, Dutta A, (2009) p21 in cancer: intricate networks and multiple activities. Nat Rev Cancer 9: 400–414.
    • (2009) Nat Rev Cancer , vol.9 , pp. 400-414
    • Abbas, T.1    Dutta, A.2
  • 63
    • 34547174700 scopus 로고    scopus 로고
    • APC/C(Cdc20) controls the ubiquitin-mediated degradation of p21 in prometaphase
    • Amador V, Ge S, Santamaria PG, Guardavaccaro D, Pagano M, (2007) APC/C(Cdc20) controls the ubiquitin-mediated degradation of p21 in prometaphase. Mol Cell 27: 462–473.
    • (2007) Mol Cell , vol.27 , pp. 462-473
    • Amador, V.1    Ge, S.2    Santamaria, P.G.3    Guardavaccaro, D.4    Pagano, M.5
  • 64
    • 0034738420 scopus 로고    scopus 로고
    • p21(WAF1/Cip1): more than a break to the cell cycle
    • Dotto GP, (2000) p21(WAF1/Cip1): more than a break to the cell cycle? Biochim Biophys Acta 1471: M43–56.
    • (2000) Biochim Biophys Acta , vol.1471 , pp. M43-56
    • Dotto, G.P.1
  • 65
    • 0037304898 scopus 로고    scopus 로고
    • New roles for p21 and p27 cell-cycle inhibitors: a function for each cell compartment
    • Coqueret O, (2003) New roles for p21 and p27 cell-cycle inhibitors: a function for each cell compartment? Trends Cell Biol 13: 65–70.
    • (2003) Trends Cell Biol , vol.13 , pp. 65-70
    • Coqueret, O.1
  • 66
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: positive and negative regulators of G1-phase progression
    • Sherr CJ, Roberts JM, (1999) CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev 13: 1501–1512.
    • (1999) Genes Dev , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 67
    • 38849187293 scopus 로고    scopus 로고
    • CDK inhibitors: cell cycle regulators and beyond
    • Besson A, Dowdy SF, Roberts JM, (2008) CDK inhibitors: cell cycle regulators and beyond. Dev Cell 14: 159–169.
    • (2008) Dev Cell , vol.14 , pp. 159-169
    • Besson, A.1    Dowdy, S.F.2    Roberts, J.M.3
  • 69
    • 84860423643 scopus 로고    scopus 로고
    • Pim1 kinase is required to maintain tumorigenicity in MYC-expressing prostate cancer cells
    • Wang J, Anderson PD, Luo W, Gius D, Roh M, et al. Pim1 kinase is required to maintain tumorigenicity in MYC-expressing prostate cancer cells. Oncogene 31: 1794–1803.
    • Oncogene , vol.31 , pp. 1794-1803
    • Wang, J.1    Anderson, P.D.2    Luo, W.3    Gius, D.4    Roh, M.5
  • 70
    • 33746886979 scopus 로고    scopus 로고
    • Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy
    • Fulda S, Debatin KM, (2006) Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene 25: 4798–4811.
    • (2006) Oncogene , vol.25 , pp. 4798-4811
    • Fulda, S.1    Debatin, K.M.2
  • 71
    • 8844263797 scopus 로고    scopus 로고
    • Targeting apoptosis pathways in cancer therapy
    • Fulda S, Debatin KM, (2004) Targeting apoptosis pathways in cancer therapy. Curr Cancer Drug Targets 4: 569–576.
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 569-576
    • Fulda, S.1    Debatin, K.M.2
  • 72
    • 20144384882 scopus 로고    scopus 로고
    • Lost in transcription: p21 repression, mechanisms, and consequences
    • Gartel AL, Radhakrishnan SK, (2005) Lost in transcription: p21 repression, mechanisms, and consequences. Cancer Res 65: 3980–3985.
    • (2005) Cancer Res , vol.65 , pp. 3980-3985
    • Gartel, A.L.1    Radhakrishnan, S.K.2
  • 73
    • 84871989736 scopus 로고    scopus 로고
    • E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation
    • Zhi X, Zhao D, Wang Z, Zhou Z, Wang C, et al. E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation. Cancer Res 73: 385–394.
    • Cancer Res , vol.73 , pp. 385-394
    • Zhi, X.1    Zhao, D.2    Wang, Z.3    Zhou, Z.4    Wang, C.5
  • 74
    • 0021233675 scopus 로고
    • Murine leukemia virus-induced T-cell lymphomagenesis: integration of proviruses in a distinct chromosomal region
    • Cuypers HT, Selten G, Quint W, Zijlstra M, Maandag ER, et al. (1984) Murine leukemia virus-induced T-cell lymphomagenesis: integration of proviruses in a distinct chromosomal region. Cell 37: 141–150.
    • (1984) Cell , vol.37 , pp. 141-150
    • Cuypers, H.T.1    Selten, G.2    Quint, W.3    Zijlstra, M.4    Maandag, E.R.5
  • 76
    • 0345268731 scopus 로고    scopus 로고
    • Pim-1 protein kinase is nuclear in Burkitt's lymphoma: nuclear localization is necessary for its biologic effects
    • Ionov Y, Le X, Tunquist BJ, Sweetenham J, Sachs T, et al. (2003) Pim-1 protein kinase is nuclear in Burkitt's lymphoma: nuclear localization is necessary for its biologic effects. Anticancer Res 23: 167–178.
    • (2003) Anticancer Res , vol.23 , pp. 167-178
    • Ionov, Y.1    Le, X.2    Tunquist, B.J.3    Sweetenham, J.4    Sachs, T.5
  • 77
    • 18244397943 scopus 로고    scopus 로고
    • Distinct types of primary cutaneous large B-cell lymphoma identified by gene expression profiling
    • Hoefnagel JJ, Dijkman R, Basso K, Jansen PM, Hallermann C, et al. (2005) Distinct types of primary cutaneous large B-cell lymphoma identified by gene expression profiling. Blood 105: 3671–3678.
    • (2005) Blood , vol.105 , pp. 3671-3678
    • Hoefnagel, J.J.1    Dijkman, R.2    Basso, K.3    Jansen, P.M.4    Hallermann, C.5
  • 78
    • 4344622788 scopus 로고    scopus 로고
    • Growth and survival mechanisms associated with perineural invasion in prostate cancer
    • Ayala GE, Dai H, Ittmann M, Li R, Powell M, et al. (2004) Growth and survival mechanisms associated with perineural invasion in prostate cancer. Cancer Res 64: 6082–6090.
    • (2004) Cancer Res , vol.64 , pp. 6082-6090
    • Ayala, G.E.1    Dai, H.2    Ittmann, M.3    Li, R.4    Powell, M.5
  • 79
  • 80
    • 78649746843 scopus 로고    scopus 로고
    • Extensive co-operation between the Epstein-Barr virus EBNA3 proteins in the manipulation of host gene expression and epigenetic chromatin modification
    • White RE, Groves IJ, Turro E, Yee J, Kremmer E, et al. Extensive co-operation between the Epstein-Barr virus EBNA3 proteins in the manipulation of host gene expression and epigenetic chromatin modification. PLoS One 5: e13979.
    • PLoS One , vol.5 , pp. e13979
    • White, R.E.1    Groves, I.J.2    Turro, E.3    Yee, J.4    Kremmer, E.5
  • 81
    • 77954664053 scopus 로고    scopus 로고
    • Epigenetic repression of p16(INK4A) by latent Epstein-Barr virus requires the interaction of EBNA3A and EBNA3C with CtBP
    • Skalska L, White RE, Franz M, Ruhmann M, Allday MJ, Epigenetic repression of p16(INK4A) by latent Epstein-Barr virus requires the interaction of EBNA3A and EBNA3C with CtBP. PLoS Pathog 6: e1000951.
    • PLoS Pathog , vol.6 , pp. e1000951
    • Skalska, L.1    White, R.E.2    Franz, M.3    Ruhmann, M.4    Allday, M.J.5
  • 82
    • 34648834046 scopus 로고    scopus 로고
    • Epstein-Barr virus latent nuclear antigens can induce metastasis in a nude mouse model
    • Kaul R, Murakami M, Choudhuri T, Robertson ES, (2007) Epstein-Barr virus latent nuclear antigens can induce metastasis in a nude mouse model. J Virol 81: 10352–10361.
    • (2007) J Virol , vol.81 , pp. 10352-10361
    • Kaul, R.1    Murakami, M.2    Choudhuri, T.3    Robertson, E.S.4
  • 83
    • 8644275515 scopus 로고    scopus 로고
    • A cyclin-binding motif within the amino-terminal homology domain of EBNA3C binds cyclin A and modulates cyclin A-dependent kinase activity in Epstein-Barr virus-infected cells
    • Knight JS, Sharma N, Kalman DE, Robertson ES, (2004) A cyclin-binding motif within the amino-terminal homology domain of EBNA3C binds cyclin A and modulates cyclin A-dependent kinase activity in Epstein-Barr virus-infected cells. J Virol 78: 12857–12867.
    • (2004) J Virol , vol.78 , pp. 12857-12867
    • Knight, J.S.1    Sharma, N.2    Kalman, D.E.3    Robertson, E.S.4
  • 85
    • 17144410021 scopus 로고    scopus 로고
    • Pim-1 kinase stability is regulated by heat shock proteins and the ubiquitin-proteasome pathway
    • Shay KP, Wang Z, Xing PX, McKenzie IF, Magnuson NS, (2005) Pim-1 kinase stability is regulated by heat shock proteins and the ubiquitin-proteasome pathway. Mol Cancer Res 3: 170–181.
    • (2005) Mol Cancer Res , vol.3 , pp. 170-181
    • Shay, K.P.1    Wang, Z.2    Xing, P.X.3    McKenzie, I.F.4    Magnuson, N.S.5
  • 86
    • 84874716795 scopus 로고    scopus 로고
    • Impact of EBV essential nuclear protein EBNA-3C on B-cell proliferation and apoptosis
    • Saha A, Robertson ES, Impact of EBV essential nuclear protein EBNA-3C on B-cell proliferation and apoptosis. Future Microbiol 8: 323–352.
    • Future Microbiol , vol.8 , pp. 323-352
    • Saha, A.1    Robertson, E.S.2
  • 87
    • 14044257866 scopus 로고    scopus 로고
    • SCFSkp2 complex targeted by Epstein-Barr virus essential nuclear antigen
    • Knight JS, Sharma N, Robertson ES, (2005) SCFSkp2 complex targeted by Epstein-Barr virus essential nuclear antigen. Mol Cell Biol 25: 1749–1763.
    • (2005) Mol Cell Biol , vol.25 , pp. 1749-1763
    • Knight, J.S.1    Sharma, N.2    Robertson, E.S.3
  • 88
    • 18144395736 scopus 로고    scopus 로고
    • Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells
    • Touitou R, O'Nions J, Heaney J, Allday MJ, (2005) Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells. J Gen Virol 86: 1269–1277.
    • (2005) J Gen Virol , vol.86 , pp. 1269-1277
    • Touitou, R.1    O'Nions, J.2    Heaney, J.3    Allday, M.J.4
  • 89
    • 84895482605 scopus 로고    scopus 로고
    • Epstein-Barr virus essential antigen EBNA3C attenuates H2AX expression
    • Jha HCAJM, Saha A, Banerjee S, Lu J, et al. Epstein-Barr virus essential antigen EBNA3C attenuates H2AX expression. J Virol 88: 3776–3788.
    • J Virol , vol.88 , pp. 3776-3788
    • Jha, H.C.A.J.M.1    Saha, A.2    Banerjee, S.3    Lu, J.4
  • 91
    • 0021767931 scopus 로고
    • Involvement of c-myc in MuLV-induced T cell lymphomas in mice: frequency and mechanisms of activation
    • Selten G, Cuypers HT, Zijlstra M, Melief C, Berns A, (1984) Involvement of c-myc in MuLV-induced T cell lymphomas in mice: frequency and mechanisms of activation. EMBO J 3: 3215–3222.
    • (1984) EMBO J , vol.3 , pp. 3215-3222
    • Selten, G.1    Cuypers, H.T.2    Zijlstra, M.3    Melief, C.4    Berns, A.5
  • 92
    • 26444448463 scopus 로고    scopus 로고
    • The survival kinases Akt and Pim as potential pharmacological targets
    • Amaravadi R, Thompson CB, (2005) The survival kinases Akt and Pim as potential pharmacological targets. J Clin Invest 115: 2618–2624.
    • (2005) J Clin Invest , vol.115 , pp. 2618-2624
    • Amaravadi, R.1    Thompson, C.B.2
  • 93
    • 0033602033 scopus 로고    scopus 로고
    • Two posttranscriptional pathways that regulate p21(Cip1/Waf1/Sdi1) are identified by HPV16-E6 interaction and correlate with life span and cellular senescence
    • Burkhart BA, Alcorta DA, Chiao C, Isaacs JS, Barrett JC, (1999) Two posttranscriptional pathways that regulate p21(Cip1/Waf1/Sdi1) are identified by HPV16-E6 interaction and correlate with life span and cellular senescence. Exp Cell Res 247: 168–175.
    • (1999) Exp Cell Res , vol.247 , pp. 168-175
    • Burkhart, B.A.1    Alcorta, D.A.2    Chiao, C.3    Isaacs, J.S.4    Barrett, J.C.5
  • 94
    • 33644747700 scopus 로고    scopus 로고
    • Phosphorylation of the cyclin-dependent kinase inhibitor p21Cip1 on serine 130 is essential for viral cyclin-mediated bypass of a p21Cip1-imposed G1 arrest
    • Jarviluoma A, Child ES, Sarek G, Sirimongkolkasem P, Peters G, et al. (2006) Phosphorylation of the cyclin-dependent kinase inhibitor p21Cip1 on serine 130 is essential for viral cyclin-mediated bypass of a p21Cip1-imposed G1 arrest. Mol Cell Biol 26: 2430–2440.
    • (2006) Mol Cell Biol , vol.26 , pp. 2430-2440
    • Jarviluoma, A.1    Child, E.S.2    Sarek, G.3    Sirimongkolkasem, P.4    Peters, G.5
  • 95
    • 0242636464 scopus 로고    scopus 로고
    • Epstein-Barr virus can inhibit genotoxin-induced G1 arrest downstream of p53 by preventing the inactivation of CDK2
    • O'Nions J, Allday MJ, (2003) Epstein-Barr virus can inhibit genotoxin-induced G1 arrest downstream of p53 by preventing the inactivation of CDK2. Oncogene 22: 7181–7191.
    • (2003) Oncogene , vol.22 , pp. 7181-7191
    • O'Nions, J.1    Allday, M.J.2
  • 96
    • 0037080197 scopus 로고    scopus 로고
    • CD40 signaling in B cells regulates the expression of the Pim-1 kinase via the NF-kappa B pathway
    • Zhu N, Ramirez LM, Lee RL, Magnuson NS, Bishop GA, et al. (2002) CD40 signaling in B cells regulates the expression of the Pim-1 kinase via the NF-kappa B pathway. J Immunol 168: 744–754.
    • (2002) J Immunol , vol.168 , pp. 744-754
    • Zhu, N.1    Ramirez, L.M.2    Lee, R.L.3    Magnuson, N.S.4    Bishop, G.A.5
  • 97
    • 67651113831 scopus 로고    scopus 로고
    • Pim-1 plays a pivotal role in hypoxia-induced chemoresistance
    • Chen J, Kobayashi M, Darmanin S, Qiao Y, Gully C, et al. (2009) Pim-1 plays a pivotal role in hypoxia-induced chemoresistance. Oncogene 28: 2581–2592.
    • (2009) Oncogene , vol.28 , pp. 2581-2592
    • Chen, J.1    Kobayashi, M.2    Darmanin, S.3    Qiao, Y.4    Gully, C.5
  • 99
    • 67650421846 scopus 로고    scopus 로고
    • Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus (KSHV) upregulates survivin expression in KSHV-Associated B-lymphoma cells and contributes to their proliferation
    • Lu J, Verma SC, Murakami M, Cai Q, Kumar P, et al. (2009) Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus (KSHV) upregulates survivin expression in KSHV-Associated B-lymphoma cells and contributes to their proliferation. J Virol 83: 7129–7141.
    • (2009) J Virol , vol.83 , pp. 7129-7141
    • Lu, J.1    Verma, S.C.2    Murakami, M.3    Cai, Q.4    Kumar, P.5
  • 100
    • 70349694198 scopus 로고    scopus 로고
    • Early events associated with infection of Epstein-Barr virus infection of primary B-cells
    • Halder S, Murakami M, Verma SC, Kumar P, Yi F, et al. (2009) Early events associated with infection of Epstein-Barr virus infection of primary B-cells. PLoS One 4: e7214.
    • (2009) PLoS One , vol.4 , pp. e7214
    • Halder, S.1    Murakami, M.2    Verma, S.C.3    Kumar, P.4    Yi, F.5
  • 101
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 102
    • 13544268345 scopus 로고    scopus 로고
    • Pim-1 is up-regulated by constitutively activated FLT3 and plays a role in FLT3-mediated cell survival
    • Kim KT, Baird K, Ahn JY, Meltzer P, Lilly M, et al. (2005) Pim-1 is up-regulated by constitutively activated FLT3 and plays a role in FLT3-mediated cell survival. Blood 105: 1759–1767.
    • (2005) Blood , vol.105 , pp. 1759-1767
    • Kim, K.T.1    Baird, K.2    Ahn, J.Y.3    Meltzer, P.4    Lilly, M.5


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