메뉴 건너뛰기




Volumn 1803, Issue 7, 2010, Pages 777-785

Herpesviruses: Hijacking the Ras signaling pathway

Author keywords

Cancer; EBV; HCMV; Herpesvirus; HHV6; HHV7; HHV8; HSV 1; HSV 2; Ras; VZV

Indexed keywords

GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR; PHOSPHATIDYLINOSITOL 3 KINASE; RAF PROTEIN; RAL PROTEIN; RAS PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 77953479971     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.03.007     Document Type: Review
Times cited : (30)

References (144)
  • 2
    • 0029022018 scopus 로고
    • Mutations of ras genes in human tumors
    • Kiaris H., Spandidos D.A. Mutations of ras genes in human tumors. Int. J. Oncol. 1995, 7:413-421.
    • (1995) Int. J. Oncol. , vol.7 , pp. 413-421
    • Kiaris, H.1    Spandidos, D.A.2
  • 3
    • 0037805547 scopus 로고    scopus 로고
    • RAS oncogenes: the first 30years
    • Malumbres M., Barbacid M. RAS oncogenes: the first 30years. Nat. Rev. Cancer 2003, 3:459-465.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 459-465
    • Malumbres, M.1    Barbacid, M.2
  • 4
    • 0032507881 scopus 로고    scopus 로고
    • Transcriptional regulation of the c-H-ras1 gene by the P53 protein is implicated in the development of human endometrial and ovarian tumours
    • Zachos G., Spandidos D.A. Transcriptional regulation of the c-H-ras1 gene by the P53 protein is implicated in the development of human endometrial and ovarian tumours. Oncogene 1998, 16:3013-3017.
    • (1998) Oncogene , vol.16 , pp. 3013-3017
    • Zachos, G.1    Spandidos, D.A.2
  • 5
    • 0037075886 scopus 로고    scopus 로고
    • GTPase activating proteins: critical regulators of intracellular signaling
    • Donovan S., Shannon K.M., Bollag G. GTPase activating proteins: critical regulators of intracellular signaling. Biochim. Biophys. Acta 2002, 1602:23-45.
    • (2002) Biochim. Biophys. Acta , vol.1602 , pp. 23-45
    • Donovan, S.1    Shannon, K.M.2    Bollag, G.3
  • 6
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski M.S., McCormick F. Proteins regulating Ras and its relatives. Nature 1993, 366:643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 8
    • 22744445886 scopus 로고    scopus 로고
    • Signaling interplay in Ras superfamily function
    • Mitin N., Rossman K.L., Der C.J. Signaling interplay in Ras superfamily function. Curr. Biol. 2005, 15:R563-574.
    • (2005) Curr. Biol. , vol.15
    • Mitin, N.1    Rossman, K.L.2    Der, C.J.3
  • 9
    • 7444245100 scopus 로고    scopus 로고
    • Renewing the conspiracy theory debate: does Raf function alone to mediate Ras oncogenesis?
    • Repasky G.A., Chenette E.J., Der C.J. Renewing the conspiracy theory debate: does Raf function alone to mediate Ras oncogenesis?. Trends Cell Biol. 2004, 14:639-647.
    • (2004) Trends Cell Biol. , vol.14 , pp. 639-647
    • Repasky, G.A.1    Chenette, E.J.2    Der, C.J.3
  • 10
    • 0027337519 scopus 로고
    • Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase
    • Moodie S.A., Willumsen B.M., Weber M.J., Wolfman A. Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 1993, 260:1658-1661.
    • (1993) Science , vol.260 , pp. 1658-1661
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 11
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne P.H., Viciana P.R., Downward J. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 1993, 364:352-355.
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Viciana, P.R.2    Downward, J.3
  • 13
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson G.L., Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 2002, 298:1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 14
    • 33646413672 scopus 로고    scopus 로고
    • The global health burden of infection-associated cancers in the year 2002
    • Parkin D.M. The global health burden of infection-associated cancers in the year 2002. Int. J. Cancer 2006, 118:3030-3044.
    • (2006) Int. J. Cancer , vol.118 , pp. 3030-3044
    • Parkin, D.M.1
  • 15
    • 0030198856 scopus 로고    scopus 로고
    • A cytokine profile of normal and malignant ovary
    • Burke F., Relf M., Negus R., Balkwill F. A cytokine profile of normal and malignant ovary. Cytokine 1996, 8:578-585.
    • (1996) Cytokine , vol.8 , pp. 578-585
    • Burke, F.1    Relf, M.2    Negus, R.3    Balkwill, F.4
  • 17
    • 0035451363 scopus 로고    scopus 로고
    • Molecular mechanisms underlying chemopreventive activities of anti-inflammatory phytochemicals: down-regulation of COX-2 and iNOS through suppression of NF-kappa B activation
    • Surh Y.J., Chun K.S., Cha H.H., Han S.S., Keum Y.S., Park K.K., Lee S.S. Molecular mechanisms underlying chemopreventive activities of anti-inflammatory phytochemicals: down-regulation of COX-2 and iNOS through suppression of NF-kappa B activation. Mutat. Res. 2001, 480-481:243-268.
    • (2001) Mutat. Res. , pp. 243-268
    • Surh, Y.J.1    Chun, K.S.2    Cha, H.H.3    Han, S.S.4    Keum, Y.S.5    Park, K.K.6    Lee, S.S.7
  • 18
    • 34248141100 scopus 로고    scopus 로고
    • A cytokine-mediated link between innate immunity, inflammation, and cancer
    • Lin W.W., Karin M. A cytokine-mediated link between innate immunity, inflammation, and cancer. J. Clin. Invest. 2007, 117:1175-1183.
    • (2007) J. Clin. Invest. , vol.117 , pp. 1175-1183
    • Lin, W.W.1    Karin, M.2
  • 19
    • 19244370055 scopus 로고    scopus 로고
    • Mechanisms of human cytomegalovirus persistence and latency
    • Jarvis M.A., Nelson J.A. Mechanisms of human cytomegalovirus persistence and latency. Front Biosci. 2002, 7:d1575-1582.
    • (2002) Front Biosci. , vol.7
    • Jarvis, M.A.1    Nelson, J.A.2
  • 20
    • 0035082504 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 promoter activity during latency establishment, maintenance, and reactivation in primary dorsal root neurons in vitro
    • Arthur J.L., Scarpini C.G., Connor V., Lachmann R.H., Tolkovsky A.M., Efstathiou S. Herpes simplex virus type 1 promoter activity during latency establishment, maintenance, and reactivation in primary dorsal root neurons in vitro. J. Virol. 2001, 75:3885-3895.
    • (2001) J. Virol. , vol.75 , pp. 3885-3895
    • Arthur, J.L.1    Scarpini, C.G.2    Connor, V.3    Lachmann, R.H.4    Tolkovsky, A.M.5    Efstathiou, S.6
  • 21
    • 0026074818 scopus 로고
    • Cooperation between oncogenes
    • Hunter T. Cooperation between oncogenes. Cell 1991, 64:249-270.
    • (1991) Cell , vol.64 , pp. 249-270
    • Hunter, T.1
  • 22
    • 0027179117 scopus 로고
    • Multiple steps in carcinogenesis involving alterations of multiple tumor suppressor genes
    • Yokota J., Sugimura T. Multiple steps in carcinogenesis involving alterations of multiple tumor suppressor genes. FASEB J. 1993, 7:920-925.
    • (1993) FASEB J. , vol.7 , pp. 920-925
    • Yokota, J.1    Sugimura, T.2
  • 23
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett R.D., Chelbi-Alix M.K. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 2007, 89:819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 24
    • 33845985638 scopus 로고    scopus 로고
    • Apoptosis during herpes simplex virus infection
    • Nguyen M.L., Blaho J.A. Apoptosis during herpes simplex virus infection. Adv. Virus Res. 2007, 69:67-97.
    • (2007) Adv. Virus Res. , vol.69 , pp. 67-97
    • Nguyen, M.L.1    Blaho, J.A.2
  • 26
    • 0035527523 scopus 로고    scopus 로고
    • Early shutoff of host protein synthesis in cells infected with herpes simplex viruses
    • Matis J., Kudelova M. Early shutoff of host protein synthesis in cells infected with herpes simplex viruses. Acta Virol. 2001, 45:269-277.
    • (2001) Acta Virol. , vol.45 , pp. 269-277
    • Matis, J.1    Kudelova, M.2
  • 28
    • 0000871794 scopus 로고    scopus 로고
    • Replicating oncolytic viruses: an overview
    • Kirn D.H. Replicating oncolytic viruses: an overview. Expert Opin. Investig. Drugs 1996, 5:753-762.
    • (1996) Expert Opin. Investig. Drugs , vol.5 , pp. 753-762
    • Kirn, D.H.1
  • 29
    • 2442492953 scopus 로고    scopus 로고
    • Infection with oncolytic herpes simplex virus-1 induces apoptosis in neighboring human cancer cells: a potential target to increase anticancer activity
    • Stanziale S.F., Petrowsky H., Adusumilli P.S., Ben-Porat L., Gonen M., Fong Y. Infection with oncolytic herpes simplex virus-1 induces apoptosis in neighboring human cancer cells: a potential target to increase anticancer activity. Clin. Cancer Res. 2004, 10:3225-3232.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3225-3232
    • Stanziale, S.F.1    Petrowsky, H.2    Adusumilli, P.S.3    Ben-Porat, L.4    Gonen, M.5    Fong, Y.6
  • 31
    • 0034789535 scopus 로고    scopus 로고
    • Virus-cell interactions regulating induction of tumor necrosis factor alpha production in macrophages infected with herpes simplex virus
    • Paludan S.R., Mogensen S.C. Virus-cell interactions regulating induction of tumor necrosis factor alpha production in macrophages infected with herpes simplex virus. J. Virol. 2001, 75:10170-10178.
    • (2001) J. Virol. , vol.75 , pp. 10170-10178
    • Paludan, S.R.1    Mogensen, S.C.2
  • 32
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • Everett R.D., Rechter S., Papior P., Tavalai N., Stamminger T., Orr A. PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 2006, 80:7995-8005.
    • (2006) J. Virol. , vol.80 , pp. 7995-8005
    • Everett, R.D.1    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 33
    • 0033230617 scopus 로고    scopus 로고
    • PKR; a sentinel kinase for cellular stress
    • Williams B.R. PKR; a sentinel kinase for cellular stress. Oncogene 1999, 18:6112-6120.
    • (1999) Oncogene , vol.18 , pp. 6112-6120
    • Williams, B.R.1
  • 34
    • 0031017382 scopus 로고    scopus 로고
    • The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • He B., Gross M., Roizman B. The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl. Acad Sci. U.S.A. 1997, 94:843-848.
    • (1997) Proc. Natl. Acad Sci. U.S.A. , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 35
    • 33644609471 scopus 로고    scopus 로고
    • PKR-dependent autophagic degradation of herpes simplex virus type 1
    • Talloczy Z., Virgin H.W.t., Levine B. PKR-dependent autophagic degradation of herpes simplex virus type 1. Autophagy 2006, 2:24-29.
    • (2006) Autophagy , vol.2 , pp. 24-29
    • Talloczy, Z.1    Virgin, H.2    Levine, B.3
  • 36
    • 0029819341 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 latency-associated transcript promoter is activated through Ras and Raf by nerve growth factor and sodium butyrate in PC12 cells
    • Schaffer P.A. The herpes simplex virus type 1 latency-associated transcript promoter is activated through Ras and Raf by nerve growth factor and sodium butyrate in PC12 cells. J. Virol. 1996, 70:7424-7432.
    • (1996) J. Virol. , vol.70 , pp. 7424-7432
    • Schaffer, P.A.1
  • 37
    • 0029819341 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 latency-associated transcript promoter is activated through Ras and Raf by nerve growth factor and sodium butyrate in PC12 cells
    • Frazier D.P., Cox D., Godshalk E.M., Schaffer P.A. The herpes simplex virus type 1 latency-associated transcript promoter is activated through Ras and Raf by nerve growth factor and sodium butyrate in PC12 cells. J. Virol. 1996, 70:7424-7432.
    • (1996) J. Virol. , vol.70 , pp. 7424-7432
    • Frazier, D.P.1    Cox, D.2    Godshalk, E.M.3    Schaffer, P.A.4
  • 38
    • 34548644394 scopus 로고    scopus 로고
    • The herpes simplex virus type 2 gene ICP10PK protects from apoptosis caused by nerve growth factor deprivation through inhibition of caspase-3 activation and XIAP up-regulation
    • Wales S.Q., Li B., Laing J.M., Aurelian L. The herpes simplex virus type 2 gene ICP10PK protects from apoptosis caused by nerve growth factor deprivation through inhibition of caspase-3 activation and XIAP up-regulation. J. Neurochem. 2007, 103:365-379.
    • (2007) J. Neurochem. , vol.103 , pp. 365-379
    • Wales, S.Q.1    Li, B.2    Laing, J.M.3    Aurelian, L.4
  • 39
    • 0032978709 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 regulatory protein ICP27 is required for the prevention of apoptosis in infected human cells
    • Aubert M.B.J.A. The herpes simplex virus type 1 regulatory protein ICP27 is required for the prevention of apoptosis in infected human cells. J. Virol. 1999, 73:2803-2813.
    • (1999) J. Virol. , vol.73 , pp. 2803-2813
    • Aubert, M.B.J.A.1
  • 40
    • 0032758642 scopus 로고    scopus 로고
    • Induction and prevention of apoptosis in human Hep-2 cells by herpes simplex virus type 1
    • Aubert M., O'Toole J., Blaho J.A. Induction and prevention of apoptosis in human Hep-2 cells by herpes simplex virus type 1. J. Virol. 1999, 73:10359-10370.
    • (1999) J. Virol. , vol.73 , pp. 10359-10370
    • Aubert, M.1    O'Toole, J.2    Blaho, J.A.3
  • 41
    • 33750946811 scopus 로고    scopus 로고
    • Herpes simplex virus genes Us3, Us5, and Us12 differentially regulate cytotoxic T lymphocyte-induced cytotoxicity
    • Aubert M., Krantz E.M., Jerome K.R. Herpes simplex virus genes Us3, Us5, and Us12 differentially regulate cytotoxic T lymphocyte-induced cytotoxicity. Viral Immunol. 2006, 19:391-408.
    • (2006) Viral Immunol. , vol.19 , pp. 391-408
    • Aubert, M.1    Krantz, E.M.2    Jerome, K.R.3
  • 42
    • 59649115408 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 ICP27 induces p38 mitogen-activated protein kinase signaling and apoptosis in HeLa cells
    • Gillis P.A., Okagaki L.H., Rice S.A. Herpes simplex virus type 1 ICP27 induces p38 mitogen-activated protein kinase signaling and apoptosis in HeLa cells. J. Virol. 2009, 83:1767-1777.
    • (2009) J. Virol. , vol.83 , pp. 1767-1777
    • Gillis, P.A.1    Okagaki, L.H.2    Rice, S.A.3
  • 43
    • 33845776528 scopus 로고    scopus 로고
    • Herpes simplex virus blocks apoptosis by precluding mitochondrial cytochrome c release independent of caspase activation in infected human epithelial cells
    • Aubert M., Pomeranz L.E., Blaho J.A. Herpes simplex virus blocks apoptosis by precluding mitochondrial cytochrome c release independent of caspase activation in infected human epithelial cells. Apoptosis 2007, 12:19-35.
    • (2007) Apoptosis , vol.12 , pp. 19-35
    • Aubert, M.1    Pomeranz, L.E.2    Blaho, J.A.3
  • 44
    • 0035120486 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 blocks the apoptotic host cell defense mechanisms that target Bcl-2 and manipulates activation of p38 mitogen-activated protein kinase to improve viral replication
    • Zachos G., Koffa M., Preston C.M., Clements J.B., Conner J. Herpes simplex virus type 1 blocks the apoptotic host cell defense mechanisms that target Bcl-2 and manipulates activation of p38 mitogen-activated protein kinase to improve viral replication. J. Virol. 2001, 75:2710-2728.
    • (2001) J. Virol. , vol.75 , pp. 2710-2728
    • Zachos, G.1    Koffa, M.2    Preston, C.M.3    Clements, J.B.4    Conner, J.5
  • 46
    • 0028220357 scopus 로고
    • The transmembrane domain of the large subunit of HSV-2 ribonucleotide reductase (ICP10) is required for protein kinase activity and transformation-related signaling pathways that result in ras activation
    • Smith C.C., Luo J.H., Hunter J.C., Ordonez J.V., Aurelian L. The transmembrane domain of the large subunit of HSV-2 ribonucleotide reductase (ICP10) is required for protein kinase activity and transformation-related signaling pathways that result in ras activation. Virology 1994, 200:598-612.
    • (1994) Virology , vol.200 , pp. 598-612
    • Smith, C.C.1    Luo, J.H.2    Hunter, J.C.3    Ordonez, J.V.4    Aurelian, L.5
  • 47
    • 0033766284 scopus 로고    scopus 로고
    • Ras-GAP binding and phosphorylation by herpes simplex virus type 2 RR1 PK (ICP10) and activation of the Ras/MEK/MAPK mitogenic pathway are required for timely onset of virus growth
    • Smith C.C., Nelson J., Aurelian L., Gober M., Goswami B.B. Ras-GAP binding and phosphorylation by herpes simplex virus type 2 RR1 PK (ICP10) and activation of the Ras/MEK/MAPK mitogenic pathway are required for timely onset of virus growth. J. Virol. 2000, 74:10417-10429.
    • (2000) J. Virol. , vol.74 , pp. 10417-10429
    • Smith, C.C.1    Nelson, J.2    Aurelian, L.3    Gober, M.4    Goswami, B.B.5
  • 48
    • 0036145517 scopus 로고    scopus 로고
    • The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway
    • Perkins D., Pereira E.F., Gober M., Yarowsky P.J., Aurelian L. The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway. J. Virol. 2002, 76:1435-1449.
    • (2002) J. Virol. , vol.76 , pp. 1435-1449
    • Perkins, D.1    Pereira, E.F.2    Gober, M.3    Yarowsky, P.J.4    Aurelian, L.5
  • 50
    • 0029063175 scopus 로고
    • Activated H-ras rescues E1A-induced apoptosis and cooperates with E1A to overcome p53-dependent growth arrest
    • Lin H.J., Eviner V., Prendergast G.C., White E. Activated H-ras rescues E1A-induced apoptosis and cooperates with E1A to overcome p53-dependent growth arrest. Mol. Cell. Biol. 1995, 15:4536-4544.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4536-4544
    • Lin, H.J.1    Eviner, V.2    Prendergast, G.C.3    White, E.4
  • 51
    • 0032793067 scopus 로고    scopus 로고
    • B-Raf inhibits programmed cell death downstream of cytochrome c release from mitochondria by activating the MEK/Erk pathway
    • Erhardt P., Schremser E.J., Cooper G.M. B-Raf inhibits programmed cell death downstream of cytochrome c release from mitochondria by activating the MEK/Erk pathway. Mol. Cell. Biol. 1999, 19:5308-5315.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5308-5315
    • Erhardt, P.1    Schremser, E.J.2    Cooper, G.M.3
  • 52
    • 21344437335 scopus 로고    scopus 로고
    • The herpes simplex virus type 2 protein ICP10PK: a master of versatility
    • Smith C.C. The herpes simplex virus type 2 protein ICP10PK: a master of versatility. Front Biosci. 2005, 10:2820-2831.
    • (2005) Front Biosci. , vol.10 , pp. 2820-2831
    • Smith, C.C.1
  • 53
    • 41949096891 scopus 로고    scopus 로고
    • Oncolytic virotherapy: molecular targets in tumor-selective replication and carrier cell-mediated delivery of oncolytic viruses
    • Guo Z.S., Thorne S.H., Bartlett D.L. Oncolytic virotherapy: molecular targets in tumor-selective replication and carrier cell-mediated delivery of oncolytic viruses. Biochim. Biophys. Acta 2008, 1785:217-231.
    • (2008) Biochim. Biophys. Acta , vol.1785 , pp. 217-231
    • Guo, Z.S.1    Thorne, S.H.2    Bartlett, D.L.3
  • 54
    • 28844444483 scopus 로고    scopus 로고
    • Recent progress in the battle between oncolytic viruses and tumours
    • Parato K.A., Senger D., Forsyth P.A., Bell J.C. Recent progress in the battle between oncolytic viruses and tumours. Nat. Rev. Cancer 2005, 5:965-976.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 965-976
    • Parato, K.A.1    Senger, D.2    Forsyth, P.A.3    Bell, J.C.4
  • 55
    • 33645889955 scopus 로고    scopus 로고
    • A mutant type 2 herpes simplex virus deleted for the protein kinase domain of the ICP10 gene is a potent oncolytic virus
    • Fu X., Tao L., Cai R., Prigge J., Zhang X. A mutant type 2 herpes simplex virus deleted for the protein kinase domain of the ICP10 gene is a potent oncolytic virus. Mol. Ther. 2006, 13:882-890.
    • (2006) Mol. Ther. , vol.13 , pp. 882-890
    • Fu, X.1    Tao, L.2    Cai, R.3    Prigge, J.4    Zhang, X.5
  • 58
    • 34447262594 scopus 로고    scopus 로고
    • Antitumor effects of two newly constructed oncolytic herpes simplex viruses against renal cell carcinoma
    • Fu X., Nakamori M., Tao L., Amato R., Zhang X. Antitumor effects of two newly constructed oncolytic herpes simplex viruses against renal cell carcinoma. Int. J. Oncol. 2007, 30:1561-1567.
    • (2007) Int. J. Oncol. , vol.30 , pp. 1561-1567
    • Fu, X.1    Nakamori, M.2    Tao, L.3    Amato, R.4    Zhang, X.5
  • 59
    • 34047177961 scopus 로고    scopus 로고
    • Induction of strong antitumor immunity by an HSV-2-based oncolytic virus in a murine mammary tumor model
    • Li H., Dutuor A., Fu X., Zhang X. Induction of strong antitumor immunity by an HSV-2-based oncolytic virus in a murine mammary tumor model. J. Gene. Med. 2007, 9:161-169.
    • (2007) J. Gene. Med. , vol.9 , pp. 161-169
    • Li, H.1    Dutuor, A.2    Fu, X.3    Zhang, X.4
  • 60
    • 33846288312 scopus 로고    scopus 로고
    • Virotherapy with a type 2 herpes simplex virus-derived oncolytic virus induces potent antitumor immunity against neuroblastoma
    • Li H., Dutuor A., Tao L., Fu X., Zhang X. Virotherapy with a type 2 herpes simplex virus-derived oncolytic virus induces potent antitumor immunity against neuroblastoma. Clin. Cancer Res. 2007, 13:316-322.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 316-322
    • Li, H.1    Dutuor, A.2    Tao, L.3    Fu, X.4    Zhang, X.5
  • 61
    • 33744818147 scopus 로고    scopus 로고
    • Effective treatment of pancreatic cancer xenografts with a conditionally replicating virus derived from type 2 herpes simplex virus
    • Fu X., Tao L., Li M., Fisher W.E., Zhang X. Effective treatment of pancreatic cancer xenografts with a conditionally replicating virus derived from type 2 herpes simplex virus. Clin. Cancer Res. 2006, 12:3152-3157.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 3152-3157
    • Fu, X.1    Tao, L.2    Li, M.3    Fisher, W.E.4    Zhang, X.5
  • 62
    • 0031684594 scopus 로고    scopus 로고
    • The PK domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is required for immediate-early gene expression and virus growth
    • Smith C.C., Peng T., Kulka M., Aurelian L. The PK domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is required for immediate-early gene expression and virus growth. J. Virol. 1998, 72:9131-9141.
    • (1998) J. Virol. , vol.72 , pp. 9131-9141
    • Smith, C.C.1    Peng, T.2    Kulka, M.3    Aurelian, L.4
  • 63
    • 68349144521 scopus 로고    scopus 로고
    • Utilizing ras signaling pathway to direct selective replication of herpes simplex virus-1
    • Pan W., Bodempudi V., Esfandyari T., Farassati F. Utilizing ras signaling pathway to direct selective replication of herpes simplex virus-1. PLoS ONE 2009, 4:e6514.
    • (2009) PLoS ONE , vol.4
    • Pan, W.1    Bodempudi, V.2    Esfandyari, T.3    Farassati, F.4
  • 64
    • 0028106296 scopus 로고
    • Intracellular transport of newly synthesized varicella-zoster virus: final envelopment in the trans-Golgi network
    • Gershon A.A., Sherman D.L., Zhu Z., Gabel C.A., Ambron R.T., Gershon M.D. Intracellular transport of newly synthesized varicella-zoster virus: final envelopment in the trans-Golgi network. J. Virol. 1994, 68:6372-6390.
    • (1994) J. Virol. , vol.68 , pp. 6372-6390
    • Gershon, A.A.1    Sherman, D.L.2    Zhu, Z.3    Gabel, C.A.4    Ambron, R.T.5    Gershon, M.D.6
  • 65
    • 0029973942 scopus 로고    scopus 로고
    • Varicella: historical perspective and clinical overview
    • Weller T.H. Varicella: historical perspective and clinical overview. J. Infect. Dis. 1996, 174(Suppl 3):S306-309.
    • (1996) J. Infect. Dis. , vol.174 , Issue.SUPPL. 3
    • Weller, T.H.1
  • 66
    • 0037377567 scopus 로고    scopus 로고
    • Pathophysiological roles of interleukin-8/CXCL8 in pulmonary diseases
    • Mukaida N. Pathophysiological roles of interleukin-8/CXCL8 in pulmonary diseases. Am. J. Physiol. Lung Cell Mol. Physiol. 2003, 284:L566-577.
    • (2003) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.284
    • Mukaida, N.1
  • 67
    • 44449174131 scopus 로고    scopus 로고
    • Varicella-zoster virus infection induces the secretion of interleukin-8
    • Desloges N., Schubert C., Wolff M.H., Rahaus M. Varicella-zoster virus infection induces the secretion of interleukin-8. Med. Microbiol. Immunol. 2008, 197:277-284.
    • (2008) Med. Microbiol. Immunol. , vol.197 , pp. 277-284
    • Desloges, N.1    Schubert, C.2    Wolff, M.H.3    Rahaus, M.4
  • 68
    • 33645538526 scopus 로고    scopus 로고
    • Varicella-zoster virus influences the activities of components and targets of the ERK signalling pathway
    • Rahaus M., Desloges N., Wolff M.H. Varicella-zoster virus influences the activities of components and targets of the ERK signalling pathway. J. Gen. Virol. 2006, 87:749-758.
    • (2006) J. Gen. Virol. , vol.87 , pp. 749-758
    • Rahaus, M.1    Desloges, N.2    Wolff, M.H.3
  • 70
    • 9944256120 scopus 로고    scopus 로고
    • Replication of varicella-zoster virus is influenced by the levels of JNK/SAPK and p38/MAPK activation
    • Rahaus M., Desloges N., Wolff M.H. Replication of varicella-zoster virus is influenced by the levels of JNK/SAPK and p38/MAPK activation. J Gen Virol 2004, 85:3529-3540.
    • (2004) J Gen Virol , vol.85 , pp. 3529-3540
    • Rahaus, M.1    Desloges, N.2    Wolff, M.H.3
  • 71
    • 36049031893 scopus 로고    scopus 로고
    • Deletion in open reading frame 49 of varicella-zoster virus reduces virus growth in human malignant melanoma cells but not in human embryonic fibroblasts
    • Sadaoka T., Yoshii H., Imazawa T., Yamanishi K., Mori Y. Deletion in open reading frame 49 of varicella-zoster virus reduces virus growth in human malignant melanoma cells but not in human embryonic fibroblasts. J. Virol. 2007, 81:12654-12665.
    • (2007) J. Virol. , vol.81 , pp. 12654-12665
    • Sadaoka, T.1    Yoshii, H.2    Imazawa, T.3    Yamanishi, K.4    Mori, Y.5
  • 72
    • 20044390558 scopus 로고    scopus 로고
    • ORF61 protein of Varicella-zoster virus influences JNK/SAPK and p38/MAPK phosphorylation
    • Rahaus M., Desloges N., Wolff M.H. ORF61 protein of Varicella-zoster virus influences JNK/SAPK and p38/MAPK phosphorylation. J. Med. Virol. 2005, 76:424-433.
    • (2005) J. Med. Virol. , vol.76 , pp. 424-433
    • Rahaus, M.1    Desloges, N.2    Wolff, M.H.3
  • 73
    • 0029743306 scopus 로고    scopus 로고
    • Human cytomegalovirus latent gene expression in granulocyte-macrophage progenitors in culture and in seropositive individuals
    • Kondo K., Xu J., Mocarski E.S. Human cytomegalovirus latent gene expression in granulocyte-macrophage progenitors in culture and in seropositive individuals. Proc. Natl Acad. Sci. USA 1996, 93:11137-11142.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11137-11142
    • Kondo, K.1    Xu, J.2    Mocarski, E.S.3
  • 74
    • 0036065383 scopus 로고    scopus 로고
    • Latency and reactivation of human cytomegalovirus
    • Sissons J.G., Bain M., Wills M.R. Latency and reactivation of human cytomegalovirus. J. Infect. 2002, 44:73-77.
    • (2002) J. Infect. , vol.44 , pp. 73-77
    • Sissons, J.G.1    Bain, M.2    Wills, M.R.3
  • 75
    • 0142075696 scopus 로고    scopus 로고
    • Models of HCMV latency and reactivation
    • Streblow D.N., Nelson J.A. Models of HCMV latency and reactivation. Trends Microbiol. 2003, 11:293-295.
    • (2003) Trends Microbiol. , vol.11 , pp. 293-295
    • Streblow, D.N.1    Nelson, J.A.2
  • 76
    • 0035502444 scopus 로고    scopus 로고
    • Cytomegalovirus (CMV) resistance to antivirals
    • Drew W.L., Paya C.V., Emery V. Cytomegalovirus (CMV) resistance to antivirals. Am. J. Transplant. 2001, 1:307-312.
    • (2001) Am. J. Transplant. , vol.1 , pp. 307-312
    • Drew, W.L.1    Paya, C.V.2    Emery, V.3
  • 77
    • 0032771737 scopus 로고    scopus 로고
    • Human cytomegalovirus and human herpesvirus 6 genes that transform and transactivate
    • Doniger J., Muralidhar S., Rosenthal L.J. Human cytomegalovirus and human herpesvirus 6 genes that transform and transactivate. Clin. Microbiol. Rev. 1999, 12:367-382.
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 367-382
    • Doniger, J.1    Muralidhar, S.2    Rosenthal, L.J.3
  • 78
    • 0030513082 scopus 로고    scopus 로고
    • Modulatory effects of human cytomegalovirus infection on malignant properties of cancer cells
    • Cinatl J., Cinatl J., Vogel J.U., Rabenau H., Kornhuber B., Doerr H.W. Modulatory effects of human cytomegalovirus infection on malignant properties of cancer cells. Intervirology 1996, 39:259-269.
    • (1996) Intervirology , vol.39 , pp. 259-269
    • Cinatl, J.1    Cinatl, J.2    Vogel, J.U.3    Rabenau, H.4    Kornhuber, B.5    Doerr, H.W.6
  • 80
    • 38849124313 scopus 로고    scopus 로고
    • Modulation of oncogenic phenotype in human glioma cells by cytomegalovirus IE1-mediated mitogenicity
    • Cobbs C.S., Soroceanu L., Denham S., Zhang W., Kraus M.H. Modulation of oncogenic phenotype in human glioma cells by cytomegalovirus IE1-mediated mitogenicity. Cancer Res. 2008, 68:724-730.
    • (2008) Cancer Res. , vol.68 , pp. 724-730
    • Cobbs, C.S.1    Soroceanu, L.2    Denham, S.3    Zhang, W.4    Kraus, M.H.5
  • 81
    • 0037121233 scopus 로고    scopus 로고
    • Specific localisation of human cytomegalovirus nucleic acids and proteins in human colorectal cancer
    • Harkins L., Volk A.L., Samanta M., Mikolaenko I., Britt W.J., Bland K.I., Cobbs C.S. Specific localisation of human cytomegalovirus nucleic acids and proteins in human colorectal cancer. Lancet 2002, 360:1557-1563.
    • (2002) Lancet , vol.360 , pp. 1557-1563
    • Harkins, L.1    Volk, A.L.2    Samanta, M.3    Mikolaenko, I.4    Britt, W.J.5    Bland, K.I.6    Cobbs, C.S.7
  • 82
    • 0036651552 scopus 로고    scopus 로고
    • Human cytomegalovirus in neoplastic cells of Epstein-Barr virus negative Hodgkin's disease
    • Huang G., Yan Q., Wang Z., Chen X., Zhang X., Guo Y., Li J.J. Human cytomegalovirus in neoplastic cells of Epstein-Barr virus negative Hodgkin's disease. Int. J. Oncol. 2002, 21:31-36.
    • (2002) Int. J. Oncol. , vol.21 , pp. 31-36
    • Huang, G.1    Yan, Q.2    Wang, Z.3    Chen, X.4    Zhang, X.5    Guo, Y.6    Li, J.J.7
  • 84
    • 0033987130 scopus 로고    scopus 로고
    • Human cytomegalovirus infects Caco-2 intestinal epithelial cells basolaterally regardless of the differentiation state
    • Esclatine A., Lemullois M., Servin A.L., Quero A.M., Geniteau-Legendre M. Human cytomegalovirus infects Caco-2 intestinal epithelial cells basolaterally regardless of the differentiation state. J. Virol. 2000, 74:513-517.
    • (2000) J. Virol. , vol.74 , pp. 513-517
    • Esclatine, A.1    Lemullois, M.2    Servin, A.L.3    Quero, A.M.4    Geniteau-Legendre, M.5
  • 85
    • 39149136486 scopus 로고    scopus 로고
    • Sensitive detection of human cytomegalovirus in tumors and peripheral blood of patients diagnosed with glioblastoma
    • Mitchell D.A., Xie W., Schmittling R., Learn C., Friedman A., McLendon R.E., Sampson J.H. Sensitive detection of human cytomegalovirus in tumors and peripheral blood of patients diagnosed with glioblastoma. Neuro. Oncol. 2008, 10:10-18.
    • (2008) Neuro. Oncol. , vol.10 , pp. 10-18
    • Mitchell, D.A.1    Xie, W.2    Schmittling, R.3    Learn, C.4    Friedman, A.5    McLendon, R.E.6    Sampson, J.H.7
  • 86
    • 0742304301 scopus 로고    scopus 로고
    • Molecular mechanisms of the modulatory effects of HCMV infection in tumor cell biology
    • Cinatl J., Scholz M., Kotchetkov R., Vogel J.U., Doerr H.W. Molecular mechanisms of the modulatory effects of HCMV infection in tumor cell biology. Trends Mol. Med. 2004, 10:19-23.
    • (2004) Trends Mol. Med. , vol.10 , pp. 19-23
    • Cinatl, J.1    Scholz, M.2    Kotchetkov, R.3    Vogel, J.U.4    Doerr, H.W.5
  • 87
    • 18844442068 scopus 로고    scopus 로고
    • Integrin alphavbeta3 is a coreceptor for human cytomegalovirus
    • Wang X., Huang D.Y., Huong S.M., Huang E.S. Integrin alphavbeta3 is a coreceptor for human cytomegalovirus. Nat. Med. 2005, 11:515-521.
    • (2005) Nat. Med. , vol.11 , pp. 515-521
    • Wang, X.1    Huang, D.Y.2    Huong, S.M.3    Huang, E.S.4
  • 88
    • 7444256550 scopus 로고    scopus 로고
    • Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain
    • Feire A.L., Koss H., Compton T. Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain. Proc. Natl Acad. Sci. USA 2004, 101:15470-15475.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15470-15475
    • Feire, A.L.1    Koss, H.2    Compton, T.3
  • 89
    • 0042265526 scopus 로고    scopus 로고
    • Epidermal growth factor receptor is a cellular receptor for human cytomegalovirus
    • Wang X., Huong S.M., Chiu M.L., Raab-Traub N., Huang E.S. Epidermal growth factor receptor is a cellular receptor for human cytomegalovirus. Nature 2003, 424:456-461.
    • (2003) Nature , vol.424 , pp. 456-461
    • Wang, X.1    Huong, S.M.2    Chiu, M.L.3    Raab-Traub, N.4    Huang, E.S.5
  • 90
    • 36348935041 scopus 로고    scopus 로고
    • Human cytomegalovirus induces cellular tyrosine kinase signaling and promotes glioma cell invasiveness
    • Cobbs C.S., Soroceanu L., Denham S., Zhang W., Britt W.J., Pieper R., Kraus M.H. Human cytomegalovirus induces cellular tyrosine kinase signaling and promotes glioma cell invasiveness. J. Neurooncol. 2007, 85:271-280.
    • (2007) J. Neurooncol. , vol.85 , pp. 271-280
    • Cobbs, C.S.1    Soroceanu, L.2    Denham, S.3    Zhang, W.4    Britt, W.J.5    Pieper, R.6    Kraus, M.H.7
  • 91
    • 34249950142 scopus 로고    scopus 로고
    • Epidermal growth factor receptor is not required for human cytomegalovirus entry or signaling
    • Isaacson M.K., Feire A.L., Compton T. Epidermal growth factor receptor is not required for human cytomegalovirus entry or signaling. J. Virol. 2007, 81:6241-6247.
    • (2007) J. Virol. , vol.81 , pp. 6241-6247
    • Isaacson, M.K.1    Feire, A.L.2    Compton, T.3
  • 92
    • 52149090536 scopus 로고    scopus 로고
    • Platelet-derived growth factor-alpha receptor activation is required for human cytomegalovirus infection
    • Soroceanu L., Akhavan A., Cobbs C.S. Platelet-derived growth factor-alpha receptor activation is required for human cytomegalovirus infection. Nature 2008, 455:391-395.
    • (2008) Nature , vol.455 , pp. 391-395
    • Soroceanu, L.1    Akhavan, A.2    Cobbs, C.S.3
  • 93
    • 20444411876 scopus 로고    scopus 로고
    • HCMV infection of human vascular smooth muscle cells leads to enhanced expression of functionally intact PDGF beta-receptor
    • Reinhardt B., Mertens T., Mayr-Beyrle U., Frank H., Luske A., Schierling K., Waltenberger J. HCMV infection of human vascular smooth muscle cells leads to enhanced expression of functionally intact PDGF beta-receptor. Cardiovasc. Res. 2005, 67:151-160.
    • (2005) Cardiovasc. Res. , vol.67 , pp. 151-160
    • Reinhardt, B.1    Mertens, T.2    Mayr-Beyrle, U.3    Frank, H.4    Luske, A.5    Schierling, K.6    Waltenberger, J.7
  • 94
    • 0033599510 scopus 로고    scopus 로고
    • The immediate early gene products of human cytomegalovirus increase vascular smooth muscle cell migration, proliferation, and expression of PDGF beta-receptor
    • Zhou Y.F., Yu Z.X., Wanishsawad C., Shou M., Epstein S.E. The immediate early gene products of human cytomegalovirus increase vascular smooth muscle cell migration, proliferation, and expression of PDGF beta-receptor. Biochem. Biophys. Res. Commun. 1999, 256:608-613.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 608-613
    • Zhou, Y.F.1    Yu, Z.X.2    Wanishsawad, C.3    Shou, M.4    Epstein, S.E.5
  • 95
    • 0032931994 scopus 로고    scopus 로고
    • Engagement of the cellular receptor for glycoprotein B of human cytomegalovirus activates the interferon-responsive pathway
    • Boyle K.A., Pietropaolo R.L., Compton T. Engagement of the cellular receptor for glycoprotein B of human cytomegalovirus activates the interferon-responsive pathway. Mol. Cell. Biol. 1999, 19:3607-3613.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3607-3613
    • Boyle, K.A.1    Pietropaolo, R.L.2    Compton, T.3
  • 96
    • 4544302236 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-dependent regulation of integrin-mediated signaling and cell cycle entry in epithelial cells
    • Bill H.M., Knudsen B., Moores S.L., Muthuswamy S.K., Rao V.R., Brugge J.S., Miranti C.K. Epidermal growth factor receptor-dependent regulation of integrin-mediated signaling and cell cycle entry in epithelial cells. Mol. Cell. Biol. 2004, 24:8586-8599.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8586-8599
    • Bill, H.M.1    Knudsen, B.2    Moores, S.L.3    Muthuswamy, S.K.4    Rao, V.R.5    Brugge, J.S.6    Miranti, C.K.7
  • 97
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human
    • Widmann C., Gibson S., Jarpe M.B., Johnson G.L. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 1999, 79:143-180.
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 98
    • 0030994219 scopus 로고    scopus 로고
    • The human cytomegalovirus UL55 (gB) and UL75 (gH) glycoprotein ligands initiate the rapid activation of Sp1 and NF-kappaB during infection
    • Yurochko A.D., Hwang E.S., Rasmussen L., Keay S., Pereira L., Huang E.S. The human cytomegalovirus UL55 (gB) and UL75 (gH) glycoprotein ligands initiate the rapid activation of Sp1 and NF-kappaB during infection. J. Virol. 1997, 71:5051-5059.
    • (1997) J. Virol. , vol.71 , pp. 5051-5059
    • Yurochko, A.D.1    Hwang, E.S.2    Rasmussen, L.3    Keay, S.4    Pereira, L.5    Huang, E.S.6
  • 99
    • 0033561760 scopus 로고    scopus 로고
    • Human cytomegalovirus binding to human monocytes induces immunoregulatory gene expression
    • Yurochko A.D., Huang E.S. Human cytomegalovirus binding to human monocytes induces immunoregulatory gene expression. J. Immunol. 1999, 162:4806-4816.
    • (1999) J. Immunol. , vol.162 , pp. 4806-4816
    • Yurochko, A.D.1    Huang, E.S.2
  • 100
    • 0024498076 scopus 로고
    • Expression of oncogenic ras in human teratocarcinoma cells induces partial differentiation and permissiveness for human cytomegalovirus infection
    • Shelbourn S.L., Sissons J.G., Sinclair J.H. Expression of oncogenic ras in human teratocarcinoma cells induces partial differentiation and permissiveness for human cytomegalovirus infection. J. Gen. Virol. 1989, 70(Pt 2):367-374.
    • (1989) J. Gen. Virol. , vol.70 , Issue.PART 2 , pp. 367-374
    • Shelbourn, S.L.1    Sissons, J.G.2    Sinclair, J.H.3
  • 101
    • 0035112558 scopus 로고    scopus 로고
    • The role of MKK1/2 kinase activity in human cytomegalovirus infection
    • Johnson R.A., Ma X.L., Yurochko A.D., Huang E.S. The role of MKK1/2 kinase activity in human cytomegalovirus infection. J. Gen. Virol. 2001, 82:493-497.
    • (2001) J. Gen. Virol. , vol.82 , pp. 493-497
    • Johnson, R.A.1    Ma, X.L.2    Yurochko, A.D.3    Huang, E.S.4
  • 102
    • 0031707104 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activity is sustained early during human cytomegalovirus infection
    • Rodems S.M., Spector D.H. Extracellular signal-regulated kinase activity is sustained early during human cytomegalovirus infection. J. Virol. 1998, 72:9173-9180.
    • (1998) J. Virol. , vol.72 , pp. 9173-9180
    • Rodems, S.M.1    Spector, D.H.2
  • 103
    • 58249118272 scopus 로고    scopus 로고
    • The story of human cytomegalovirus and cancer: increasing evidence and open questions
    • Michaelis M., Doerr H.W., Cinatl J. The story of human cytomegalovirus and cancer: increasing evidence and open questions. Neoplasia 2009, 11:1-9.
    • (2009) Neoplasia , vol.11 , pp. 1-9
    • Michaelis, M.1    Doerr, H.W.2    Cinatl, J.3
  • 111
    • 0030952950 scopus 로고    scopus 로고
    • Cell lines containing and expressing the human herpesvirus 6A ts gene are protected from both H-ras and BPV-1 transformation
    • Araujo J.C., Doniger J., Stoppler H., Sadaie M.R., Rosenthal L.J. Cell lines containing and expressing the human herpesvirus 6A ts gene are protected from both H-ras and BPV-1 transformation. Oncogene 1997, 14:937-943.
    • (1997) Oncogene , vol.14 , pp. 937-943
    • Araujo, J.C.1    Doniger, J.2    Stoppler, H.3    Sadaie, M.R.4    Rosenthal, L.J.5
  • 112
    • 0029075125 scopus 로고
    • Human herpesvirus 6A ts suppresses both transformation by H-ras and transcription by the H-ras and human immunodeficiency virus type 1 promoters
    • Araujo J.C., Doniger J., Kashanchi F., Hermonat P.L., Thompson J., Rosenthal L.J. Human herpesvirus 6A ts suppresses both transformation by H-ras and transcription by the H-ras and human immunodeficiency virus type 1 promoters. J. Virol. 1995, 69:4933-4940.
    • (1995) J. Virol. , vol.69 , pp. 4933-4940
    • Araujo, J.C.1    Doniger, J.2    Kashanchi, F.3    Hermonat, P.L.4    Thompson, J.5    Rosenthal, L.J.6
  • 114
    • 19444387952 scopus 로고    scopus 로고
    • Human herpesvirus type 6 and type 1 infection increases susceptibility to nonmelanoma skin tumors
    • Leite J.L., Stolf H.O., Reis N.A., Ward L.S. Human herpesvirus type 6 and type 1 infection increases susceptibility to nonmelanoma skin tumors. Cancer Lett. 2005, 224:213-219.
    • (2005) Cancer Lett. , vol.224 , pp. 213-219
    • Leite, J.L.1    Stolf, H.O.2    Reis, N.A.3    Ward, L.S.4
  • 115
    • 72949087815 scopus 로고    scopus 로고
    • Human tumor-associated viruses and new insights into the molecular mechanisms of cancer
    • Martin D., Gutkind J.S. Human tumor-associated viruses and new insights into the molecular mechanisms of cancer. Oncogene 2008, 27(Suppl 2):S31-42.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 2
    • Martin, D.1    Gutkind, J.S.2
  • 118
    • 0034136934 scopus 로고    scopus 로고
    • Epstein-Barr virus-associated diseases in humans
    • Kawa K. Epstein-Barr virus-associated diseases in humans. Int. J. Hematol. 2000, 71:108-117.
    • (2000) Int. J. Hematol. , vol.71 , pp. 108-117
    • Kawa, K.1
  • 119
    • 0033610075 scopus 로고    scopus 로고
    • A model for persistent infection with Epstein-Barr virus: the stealth virus of human B cells
    • Thorley-Lawson D.A., Babcock G.J. A model for persistent infection with Epstein-Barr virus: the stealth virus of human B cells. Life Sci. 1999, 65:1433-1453.
    • (1999) Life Sci. , vol.65 , pp. 1433-1453
    • Thorley-Lawson, D.A.1    Babcock, G.J.2
  • 120
    • 0033696976 scopus 로고    scopus 로고
    • The expression pattern of Epstein-Barr virus latent genes in vivo is dependent upon the differentiation stage of the infected B cell
    • Babcock G.J., Hochberg D., Thorley-Lawson A.D. The expression pattern of Epstein-Barr virus latent genes in vivo is dependent upon the differentiation stage of the infected B cell. Immunity 2000, 13:497-506.
    • (2000) Immunity , vol.13 , pp. 497-506
    • Babcock, G.J.1    Hochberg, D.2    Thorley-Lawson, A.D.3
  • 121
    • 0034710968 scopus 로고    scopus 로고
    • Tonsillar memory B cells, latently infected with Epstein-Barr virus, express the restricted pattern of latent genes previously found only in Epstein-Barr virus-associated tumors
    • Babcock G.J., Thorley-Lawson D.A. Tonsillar memory B cells, latently infected with Epstein-Barr virus, express the restricted pattern of latent genes previously found only in Epstein-Barr virus-associated tumors. Proc. Natl. Acad Sci. USA 2000, 97:12250-12255.
    • (2000) Proc. Natl. Acad Sci. USA , vol.97 , pp. 12250-12255
    • Babcock, G.J.1    Thorley-Lawson, D.A.2
  • 123
    • 0023409797 scopus 로고
    • Differences in B cell growth phenotype reflect novel patterns of Epstein-Barr virus latent gene expression in Burkitt's lymphoma cells
    • Rowe M., Rowe D.T., Gregory C.D., Young L.S., Farrell P.J., Rupani H., Rickinson A.B. Differences in B cell growth phenotype reflect novel patterns of Epstein-Barr virus latent gene expression in Burkitt's lymphoma cells. EMBO J. 1987, 6:2743-2751.
    • (1987) EMBO J. , vol.6 , pp. 2743-2751
    • Rowe, M.1    Rowe, D.T.2    Gregory, C.D.3    Young, L.S.4    Farrell, P.J.5    Rupani, H.6    Rickinson, A.B.7
  • 124
    • 0027252547 scopus 로고
    • Transcripts from the Epstein-Barr virus BamHI A fragment are detectable in all three forms of virus latency
    • Brooks L.A., Lear A.L., Young L.S., Rickinson A.B. Transcripts from the Epstein-Barr virus BamHI A fragment are detectable in all three forms of virus latency. J. Virol. 1993, 67:3182-3190.
    • (1993) J. Virol. , vol.67 , pp. 3182-3190
    • Brooks, L.A.1    Lear, A.L.2    Young, L.S.3    Rickinson, A.B.4
  • 125
    • 9644279753 scopus 로고    scopus 로고
    • Epstein-Barr virus (EBV) LMP2A mediates B-lymphocyte survival through constitutive activation of the Ras/PI3K/Akt pathway
    • Portis T., Longnecker R. Epstein-Barr virus (EBV) LMP2A mediates B-lymphocyte survival through constitutive activation of the Ras/PI3K/Akt pathway. Oncogene 2004, 23:8619-8628.
    • (2004) Oncogene , vol.23 , pp. 8619-8628
    • Portis, T.1    Longnecker, R.2
  • 126
    • 34548156449 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 2A mediates transformation through constitutive activation of the Ras/PI3-K/Akt Pathway
    • Fukuda M., Longnecker R. Epstein-Barr virus latent membrane protein 2A mediates transformation through constitutive activation of the Ras/PI3-K/Akt Pathway. J. Virol. 2007, 81:9299-9306.
    • (2007) J. Virol. , vol.81 , pp. 9299-9306
    • Fukuda, M.1    Longnecker, R.2
  • 127
  • 128
    • 61349106613 scopus 로고    scopus 로고
    • Tumor-derived variants of Epstein-Barr virus latent membrane protein 1 induce sustained Erk activation and c-Fos
    • Vaysberg M., Hatton O., Lambert S.L., Snow A.L., Wong B., Krams S.M., Martinez O.M. Tumor-derived variants of Epstein-Barr virus latent membrane protein 1 induce sustained Erk activation and c-Fos. J. Biol. Chem. 2008, 283:36573-36585.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36573-36585
    • Vaysberg, M.1    Hatton, O.2    Lambert, S.L.3    Snow, A.L.4    Wong, B.5    Krams, S.M.6    Martinez, O.M.7
  • 129
    • 0032484473 scopus 로고    scopus 로고
    • Activation of a ras-MAPK-dependent pathway by Epstein-Barr virus latent membrane protein 1 is essential for cellular transformation
    • Roberts M.L., Cooper N.R. Activation of a ras-MAPK-dependent pathway by Epstein-Barr virus latent membrane protein 1 is essential for cellular transformation. Virology 1998, 240:93-99.
    • (1998) Virology , vol.240 , pp. 93-99
    • Roberts, M.L.1    Cooper, N.R.2
  • 130
    • 41149159605 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded LMP1 regulates epithelial cell motility and invasion via the ERK-MAPK pathway
    • Dawson C.W., Laverick L., Morris M.A., Tramoutanis G., Young L.S. Epstein-Barr virus-encoded LMP1 regulates epithelial cell motility and invasion via the ERK-MAPK pathway. J Virol 2008, 82:3654-3664.
    • (2008) J Virol , vol.82 , pp. 3654-3664
    • Dawson, C.W.1    Laverick, L.2    Morris, M.A.3    Tramoutanis, G.4    Young, L.S.5
  • 131
    • 33646161719 scopus 로고    scopus 로고
    • Regulation of intracellular signalling by the terminal membrane proteins of members of the Gammaherpesvirinae
    • Brinkmann M.M., Schulz T.F. Regulation of intracellular signalling by the terminal membrane proteins of members of the Gammaherpesvirinae. J. Gen. Virol. 2006, 87:1047-1074.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1047-1074
    • Brinkmann, M.M.1    Schulz, T.F.2
  • 132
  • 133
    • 0029974841 scopus 로고    scopus 로고
    • Primary effusion lymphoma: a distinct clinicopathologic entity associated with the Kaposi's sarcoma-associated herpes virus
    • Nador R.G., Cesarman E., Chadburn A., Dawson D.B., Ansari M.Q., Sald J., Knowles D.M. Primary effusion lymphoma: a distinct clinicopathologic entity associated with the Kaposi's sarcoma-associated herpes virus. Blood 1996, 88:645-656.
    • (1996) Blood , vol.88 , pp. 645-656
    • Nador, R.G.1    Cesarman, E.2    Chadburn, A.3    Dawson, D.B.4    Ansari, M.Q.5    Sald, J.6    Knowles, D.M.7
  • 135
    • 0036008473 scopus 로고    scopus 로고
    • Integrin alpha3beta1 (CD 49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) entry into the target cells
    • Akula S.M., Pramod N.P., Wang F.Z., Chandran B. Integrin alpha3beta1 (CD 49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) entry into the target cells. Cell 2002, 108:407-419.
    • (2002) Cell , vol.108 , pp. 407-419
    • Akula, S.M.1    Pramod, N.P.2    Wang, F.Z.3    Chandran, B.4
  • 136
    • 0034969241 scopus 로고    scopus 로고
    • Immunoreceptor tyrosine-based activation motif-dependent signaling by Kaposi's sarcoma-associated herpesvirus K1 protein: effects on lytic viral replication
    • Lagunoff M., Lukac D.M., Ganem D. Immunoreceptor tyrosine-based activation motif-dependent signaling by Kaposi's sarcoma-associated herpesvirus K1 protein: effects on lytic viral replication. J. Virol. 2001, 75:5891-5898.
    • (2001) J. Virol. , vol.75 , pp. 5891-5898
    • Lagunoff, M.1    Lukac, D.M.2    Ganem, D.3
  • 138
    • 38049070690 scopus 로고    scopus 로고
    • Reactivation of Kaposi's sarcoma-associated herpesvirus from latency requires MEK/ERK, JNK and p38 multiple mitogen-activated protein kinase pathways
    • Xie J., Ajibade A.O., Ye F., Kuhne K., Gao S.J. Reactivation of Kaposi's sarcoma-associated herpesvirus from latency requires MEK/ERK, JNK and p38 multiple mitogen-activated protein kinase pathways. Virology 2008, 371:139-154.
    • (2008) Virology , vol.371 , pp. 139-154
    • Xie, J.1    Ajibade, A.O.2    Ye, F.3    Kuhne, K.4    Gao, S.J.5
  • 139
    • 14744270253 scopus 로고    scopus 로고
    • A Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50 deletion mutant is defective for reactivation of latent virus and DNA replication
    • Xu Y., AuCoin D.P., Huete A.R., Cei S.A., Hanson L.J., Pari G.S. A Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50 deletion mutant is defective for reactivation of latent virus and DNA replication. J Virol 2005, 79:3479-3487.
    • (2005) J Virol , vol.79 , pp. 3479-3487
    • Xu, Y.1    AuCoin, D.P.2    Huete, A.R.3    Cei, S.A.4    Hanson, L.J.5    Pari, G.S.6
  • 140
    • 0032567394 scopus 로고    scopus 로고
    • Reactivation of Kaposi's sarcoma-associated herpesvirus infection from latency by expression of the ORF 50 transactivator, a homolog of the EBV R protein
    • Lukac D.M., Renne R., Kirshner J.R., Ganem D. Reactivation of Kaposi's sarcoma-associated herpesvirus infection from latency by expression of the ORF 50 transactivator, a homolog of the EBV R protein. Virology 1998, 252:304-312.
    • (1998) Virology , vol.252 , pp. 304-312
    • Lukac, D.M.1    Renne, R.2    Kirshner, J.R.3    Ganem, D.4
  • 141
    • 0032167919 scopus 로고    scopus 로고
    • A viral gene that activates lytic cycle expression of Kaposi's sarcoma-associated herpesvirus
    • Sun R., Lin S.F., Gradoville L., Yuan Y., Zhu F., Miller G. A viral gene that activates lytic cycle expression of Kaposi's sarcoma-associated herpesvirus. Proc. Natl. Acad Sci. USA 1998, 95:10866-10871.
    • (1998) Proc. Natl. Acad Sci. USA , vol.95 , pp. 10866-10871
    • Sun, R.1    Lin, S.F.2    Gradoville, L.3    Yuan, Y.4    Zhu, F.5    Miller, G.6
  • 142
    • 33646747652 scopus 로고    scopus 로고
    • Modulation of Kaposi's sarcoma-associated herpesvirus infection and replication by MEK/ERK, JNK, and p38 multiple mitogen-activated protein kinase pathways during primary infection
    • Pan H., Xie J., Ye F., Gao S.J. Modulation of Kaposi's sarcoma-associated herpesvirus infection and replication by MEK/ERK, JNK, and p38 multiple mitogen-activated protein kinase pathways during primary infection. J. Virol. 2006, 80:5371-5382.
    • (2006) J. Virol. , vol.80 , pp. 5371-5382
    • Pan, H.1    Xie, J.2    Ye, F.3    Gao, S.J.4
  • 144
    • 0033782793 scopus 로고    scopus 로고
    • The latent nuclear antigen of Kaposi sarcoma-associated herpesvirus targets the retinoblastoma-E2F pathway and with the oncogene Hras transforms primary rat cells
    • Radkov S.A., Kellam P., Boshoff C. The latent nuclear antigen of Kaposi sarcoma-associated herpesvirus targets the retinoblastoma-E2F pathway and with the oncogene Hras transforms primary rat cells. Nat. Med. 2000, 6:1121-1127.
    • (2000) Nat. Med. , vol.6 , pp. 1121-1127
    • Radkov, S.A.1    Kellam, P.2    Boshoff, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.