메뉴 건너뛰기




Volumn 27, Issue 5, 2007, Pages 365-376

Herpes simplex virus blocks fas-mediated apoptosis independent of viral activation of NF-κB in human epithelial HEp-2 cells

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXIMIDE; FAS ANTIBODY; FAS ANTIGEN; FAS LIGAND; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 34249706794     PISSN: 10799907     EISSN: None     Source Type: Journal    
DOI: 10.1089/jir.2006.0143     Document Type: Article
Times cited : (11)

References (62)
  • 2
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell 1997;88:355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 3
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
    • Smith CA, Farrah T, Goodwin RG. The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell 1994;76:959-962.
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 4
    • 0029026548 scopus 로고    scopus 로고
    • Chinnaiyan AM. O'Rourke K, Tewari M, Dixit VM. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995;81:505-512.
    • Chinnaiyan AM. O'Rourke K, Tewari M, Dixit VM. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995;81:505-512.
  • 5
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia LA, Ayres TM, Wong GH, Goeddel DV. A novel domain within the 55 kd TNF receptor signals cell death. Cell 1993;74:845-853.
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 6
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 1996;4:387-396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 7
    • 0030934465 scopus 로고    scopus 로고
    • Fas-associated death domain protein interleukin-1 beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling
    • Vincenz C, Dixit VM. Fas-associated death domain protein interleukin-1 beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling. J. Biol. Chem. 1997;272:6578-6583.
    • (1997) J. Biol. Chem , vol.272 , pp. 6578-6583
    • Vincenz, C.1    Dixit, V.M.2
  • 8
    • 15844412409 scopus 로고    scopus 로고
    • Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J, Scaffidi C, Bretz JD, Zhang M, Gentz R, Mann M, Krammer PH, Peter ME, Dixit VM. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996;85:817-827.
    • Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J, Scaffidi C, Bretz JD, Zhang M, Gentz R, Mann M, Krammer PH, Peter ME, Dixit VM. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996;85:817-827.
  • 9
    • 0028985261 scopus 로고
    • Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects
    • Boldin MP, Mett IL, Varfolomeev EE, Chumakov I, Shemer-Avni Y, Camonis JH, Wallach D. Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects. J. Biol. Chem. 1995;270:387-391.
    • (1995) J. Biol. Chem , vol.270 , pp. 387-391
    • Boldin, M.P.1    Mett, I.L.2    Varfolomeev, E.E.3    Chumakov, I.4    Shemer-Avni, Y.5    Camonis, J.H.6    Wallach, D.7
  • 11
    • 0002204915 scopus 로고
    • Definition and incidence of apoptosis: An historical perspective
    • Tomei LD, Cope FO, eds, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Kerr FR, Harmon BV. Definition and incidence of apoptosis: an historical perspective. In: Tomei LD, Cope FO, eds. Apoptosis: The Molecular Basis of Cell Death. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1991:5-29.
    • (1991) Apoptosis: The Molecular Basis of Cell Death , pp. 5-29
    • Kerr, F.R.1    Harmon, B.V.2
  • 12
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 1972;26:239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 13
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • Knipe DM, Howley PM, eds, 4th ed. Philadelphia, PA: Lippineott-Raven
    • Roizman B, Knipe DM. Herpes simplex viruses and their replication. In: Knipe DM, Howley PM, eds. Virology, 4th ed. Philadelphia, PA: Lippineott-Raven, 2001:2399-2459.
    • (2001) Virology , pp. 2399-2459
    • Roizman, B.1    Knipe, D.M.2
  • 16
    • 0038678185 scopus 로고    scopus 로고
    • NF-kappaB is required for apoptosis prevention during herpes simplex virus type 1 infection
    • Goodkin ML, Ting AT, Blaho JA. NF-kappaB is required for apoptosis prevention during herpes simplex virus type 1 infection. J. Virol. 2003;77:7261-7280.
    • (2003) J. Virol , vol.77 , pp. 7261-7280
    • Goodkin, M.L.1    Ting, A.T.2    Blaho, J.A.3
  • 17
    • 0035800780 scopus 로고    scopus 로고
    • Activation of I kappa b kinase by herpes simplex virus type 1. A novel target for antiherpetic therapy
    • Amici C, Belardo G, Rossi A, Santoro MG. Activation of I kappa b kinase by herpes simplex virus type 1. A novel target for antiherpetic therapy. J. Biol. Chem. 2001;276:28759-28766.
    • (2001) J. Biol. Chem , vol.276 , pp. 28759-28766
    • Amici, C.1    Belardo, G.2    Rossi, A.3    Santoro, M.G.4
  • 18
    • 0032129268 scopus 로고    scopus 로고
    • Herpes simplex type 1 induction of persistent NF-kappa B nuclear translocation increases the efficiency of virus replication
    • Patel A, Hanson J, McLean TI, Hilton M, Miller WE, Bachenheimer SL. Herpes simplex type 1 induction of persistent NF-kappa B nuclear translocation increases the efficiency of virus replication. Virology 1998;247:212-222.
    • (1998) Virology , vol.247 , pp. 212-222
    • Patel, A.1    Hanson, J.2    McLean, T.I.3    Hilton, M.4    Miller, W.E.5    Bachenheimer, S.L.6
  • 19
    • 10044241988 scopus 로고    scopus 로고
    • Efficient replication by herpes simplex virus type I involves activation of the IkappaB kinase-IkappaB-p65 pathway
    • Gregory D, Hargett D, Holmes D, Money E, Bachenheimer SL. Efficient replication by herpes simplex virus type I involves activation of the IkappaB kinase-IkappaB-p65 pathway. J. Virol. 2004;78:13582-13590.
    • (2004) J. Virol , vol.78 , pp. 13582-13590
    • Gregory, D.1    Hargett, D.2    Holmes, D.3    Money, E.4    Bachenheimer, S.L.5
  • 21
    • 0037168545 scopus 로고    scopus 로고
    • The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene
    • Taddeo B, Esclatine A, Roizman B. The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene. Proc. Natl. Acad. Sci. USA 2002;99:17031-17036.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 17031-17036
    • Taddeo, B.1    Esclatine, A.2    Roizman, B.3
  • 22
    • 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 JA. 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
  • 23
    • 0032584081 scopus 로고    scopus 로고
    • Herpes simplex virus 1 induces and blocks apoptosis at multiple steps during infection and protects cells from exogenous inducers in a cell type-dependent manner
    • Galvan V, Roizman B. Herpes simplex virus 1 induces and blocks apoptosis at multiple steps during infection and protects cells from exogenous inducers in a cell type-dependent manner. Proc. Natl. Acad. Sci. USA 1998;95:3931-3936.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3931-3936
    • Galvan, V.1    Roizman, B.2
  • 24
    • 0031975191 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 renders infected cells resistant to cylotoxic T-lymphocyte-induced apoptosis
    • Jerome KR, Tait JF, Koelle DM, Corey L. Herpes simplex virus type 1 renders infected cells resistant to cylotoxic T-lymphocyte-induced apoptosis. J. Virol. 1998;72:436-441.
    • (1998) J. Virol , vol.72 , pp. 436-441
    • Jerome, K.R.1    Tait, J.F.2    Koelle, D.M.3    Corey, L.4
  • 25
    • 0031041895 scopus 로고    scopus 로고
    • Suppression of apoptotic DNA fragmentation in herpes simplex virus type 1-infected cells
    • Koyama AH, Miwa Y. Suppression of apoptotic DNA fragmentation in herpes simplex virus type 1-infected cells. J. Virol. 1997;71:2567-2571.
    • (1997) J. Virol , vol.71 , pp. 2567-2571
    • Koyama, A.H.1    Miwa, Y.2
  • 26
    • 0035163815 scopus 로고    scopus 로고
    • Accumulation of herpes simplex virus type 1 early and leaky-late proteins correlates with apoptosis prevention in infected human HEp-2 cells
    • Aubert M, Rice SA, Blaho JA. Accumulation of herpes simplex virus type 1 early and leaky-late proteins correlates with apoptosis prevention in infected human HEp-2 cells. J. Virol. 2001;75:1013-1030.
    • (2001) J. Virol , vol.75 , pp. 1013-1030
    • Aubert, M.1    Rice, S.A.2    Blaho, J.A.3
  • 27
    • 0141997719 scopus 로고    scopus 로고
    • Apoptosis prevention as a mechanism of immune evasion
    • Aubert M, Jerome KR. Apoptosis prevention as a mechanism of immune evasion. Int. Rev. Immunol. 2003;22:361-371.
    • (2003) Int. Rev. Immunol , vol.22 , pp. 361-371
    • Aubert, M.1    Jerome, K.R.2
  • 28
    • 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, Blaho JA. 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.1    Blaho, J.A.2
  • 29
    • 0034468747 scopus 로고    scopus 로고
    • Zhou G, Galvan V, Campadelli-Fiume G, Roizman B. Glycoprotein D or J delivered in trans blocks apoptosis in SK-N-SH cells induced by a herpes simplex virus 1 mutant lacking intact genes expressing both glycoproteins. J. Virol. 2000;74:11782-11791.
    • Zhou G, Galvan V, Campadelli-Fiume G, Roizman B. Glycoprotein D or J delivered in trans blocks apoptosis in SK-N-SH cells induced by a herpes simplex virus 1 mutant lacking intact genes expressing both glycoproteins. J. Virol. 2000;74:11782-11791.
  • 30
    • 0037334581 scopus 로고    scopus 로고
    • The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectinl
    • Zhou G, Avitabile E, Campadelli-Fiume G, Roizman B. The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectinl. J. Virol. 2003;77:3759-3767.
    • (2003) J. Virol , vol.77 , pp. 3759-3767
    • Zhou, G.1    Avitabile, E.2    Campadelli-Fiume, G.3    Roizman, B.4
  • 31
    • 0030671324 scopus 로고    scopus 로고
    • Induction of apoptosis by herpes simplex virus type 1
    • Koyama AH, Adachi A. Induction of apoptosis by herpes simplex virus type 1. J. Gen. Virol. 1997;78:2909-2912.
    • (1997) J. Gen. Virol , vol.78 , pp. 2909-2912
    • Koyama, A.H.1    Adachi, A.2
  • 32
    • 0346365298 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early gene expression is required for the induction of apoptosis in human epithelial HEp-2 cells
    • Sanfilippo CM, Chirimuuta FN, Blaho JA. Herpes simplex virus type 1 immediate-early gene expression is required for the induction of apoptosis in human epithelial HEp-2 cells. J. Virol. 2004; 78:224-239.
    • (2004) J. Virol , vol.78 , pp. 224-239
    • Sanfilippo, C.M.1    Chirimuuta, F.N.2    Blaho, J.A.3
  • 33
    • 0023708697 scopus 로고
    • Re-evaluation of HeLa, HeLa S3, and HEp-2 karyotypes
    • Chen TR. Re-evaluation of HeLa, HeLa S3, and HEp-2 karyotypes. Cytogenet. Cell Genet. 1988;48:19-24.
    • (1988) Cytogenet. Cell Genet , vol.48 , pp. 19-24
    • Chen, T.R.1
  • 34
    • 18844426293 scopus 로고    scopus 로고
    • African green monkey kidney Vero cells require de novo protein synthesis for efficient herpes simplex virus 1-dependent apoptosis
    • Nguyen ML, Kraft RM, Blaho JA. African green monkey kidney Vero cells require de novo protein synthesis for efficient herpes simplex virus 1-dependent apoptosis. Virology 2005;336:274-290.
    • (2005) Virology , vol.336 , pp. 274-290
    • Nguyen, M.L.1    Kraft, R.M.2    Blaho, J.A.3
  • 35
    • 0014286962 scopus 로고
    • Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells
    • Ejercito PM, Kieff ED, Roizman B. Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells. J. Gen. Virol. 1968;2:357-364.
    • (1968) J. Gen. Virol , vol.2 , pp. 357-364
    • Ejercito, P.M.1    Kieff, E.D.2    Roizman, B.3
  • 38
    • 0032775897 scopus 로고    scopus 로고
    • Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection
    • Pomeranz LE, Blaho JA. Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection. J. Virol. 1999;73:6769-6781.
    • (1999) J. Virol , vol.73 , pp. 6769-6781
    • Pomeranz, L.E.1    Blaho, J.A.2
  • 40
    • 0033879526 scopus 로고    scopus 로고
    • Bcl-2 does not inhibit cell death induced by the physiological Fas ligand: Implications for the existence of type I and type II cells
    • Huang DC, Tschopp J, Strasser A. Bcl-2 does not inhibit cell death induced by the physiological Fas ligand: implications for the existence of type I and type II cells. Cell Death Differ. 2000; 7:754-755.
    • (2000) Cell Death Differ , vol.7 , pp. 754-755
    • Huang, D.C.1    Tschopp, J.2    Strasser, A.3
  • 41
    • 0037185002 scopus 로고    scopus 로고
    • A novel signaling mechanism for soluble CD95 ligand. Synergy with anti-CD95 monoclonal antibodies for apoptosis and NF-kappaB nuclear translocation
    • Xiao S, Jodo S, Sung SS, Marshak-Rothstein A, Ju ST. A novel signaling mechanism for soluble CD95 ligand. Synergy with anti-CD95 monoclonal antibodies for apoptosis and NF-kappaB nuclear translocation. J. Biol. Chem. 2002;277:50907-50913.
    • (2002) J. Biol. Chem , vol.277 , pp. 50907-50913
    • Xiao, S.1    Jodo, S.2    Sung, S.S.3    Marshak-Rothstein, A.4    Ju, S.T.5
  • 42
    • 0028782762 scopus 로고
    • Apoptosis regulated by a death factor and its receptor: Fas ligand and Fas
    • Nagata S. Apoptosis regulated by a death factor and its receptor: Fas ligand and Fas. Philos. Trans. R. Soc. Lond. B Biol. Sci. 1994; 345:281-287.
    • (1994) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.345 , pp. 281-287
    • Nagata, S.1
  • 43
    • 0037347576 scopus 로고    scopus 로고
    • Inhibition of nuclear translocation of transcription factor nuclear factor-kappa B induces FAS- as well as tumour necrosis factor-alpha-mediated apoptosis through downregulation of a conserved family of inhibitor of apoptosis 1
    • Imanishi T, Hano T, Takarada S, Nishio I. Inhibition of nuclear translocation of transcription factor nuclear factor-kappa B induces FAS- as well as tumour necrosis factor-alpha-mediated apoptosis through downregulation of a conserved family of inhibitor of apoptosis 1. Clin. Exp. Pharmacol. Physiol. 2003;30:133-139.
    • (2003) Clin. Exp. Pharmacol. Physiol , vol.30 , pp. 133-139
    • Imanishi, T.1    Hano, T.2    Takarada, S.3    Nishio, I.4
  • 44
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • Ghosh S, Karin M. Missing pieces in the NF-kappaB puzzle. Cell 2002;109(Suppl):S81-96.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Ghosh, S.1    Karin, M.2
  • 45
    • 0034731365 scopus 로고    scopus 로고
    • Dynamic shuttling of nuclear factor kappa B between the nucleus and cytoplasm as a consequence of inhibitor dissociation
    • Carlotti F, Dower SK, Qwarnstrom EE. Dynamic shuttling of nuclear factor kappa B between the nucleus and cytoplasm as a consequence of inhibitor dissociation. J Biol. Chem. 2000;275:41028-41034.
    • (2000) J Biol. Chem , vol.275 , pp. 41028-41034
    • Carlotti, F.1    Dower, S.K.2    Qwarnstrom, E.E.3
  • 46
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kappaB in preventing TNF-alpha-induced cell death
    • Beg AA, Baltimore D. An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 1996;274:782-784.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 47
    • 0034812986 scopus 로고    scopus 로고
    • Modulation of apoptosis during herpes simplex virus infection in human cells
    • Aubert M, Blaho JA. Modulation of apoptosis during herpes simplex virus infection in human cells. Microbes Infect. 2001;10: 859-866.
    • (2001) Microbes Infect , vol.10 , pp. 859-866
    • Aubert, M.1    Blaho, J.A.2
  • 48
    • 0027207242 scopus 로고
    • Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of I kappa B alpha: A mechanism for NF-kappa B activation
    • Beg AA, Finco TS, Nantermet PV, Baldwin AS Jr. Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of I kappa B alpha: a mechanism for NF-kappa B activation. Mol. Cell. Biol. 1993;13:3301-3310.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 3301-3310
    • Beg, A.A.1    Finco, T.S.2    Nantermet, P.V.3    Baldwin Jr., A.S.4
  • 49
    • 0025266685 scopus 로고
    • Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B
    • Ghosh S, Baltimore D. Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature 1990;344:678-682.
    • (1990) Nature , vol.344 , pp. 678-682
    • Ghosh, S.1    Baltimore, D.2
  • 50
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity
    • Chen ZJ, Parent L, Maniatis T. Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. Cell 1996;84:853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 51
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-kappaB transcription factors
    • Pahl HL. Activators and target genes of Rel/NF-kappaB transcription factors. Oncogene 1999;18:6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 52
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and C-IAP2 to suppress caspase-8 activation
    • Wang CY, Mayo MW, Korneluk RG, Goeddel DV, Baldwin AS Jr. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and C-IAP2 to suppress caspase-8 activation. Science 1998;281:1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin Jr., A.S.5
  • 53
    • 0022499725 scopus 로고
    • Induction of beta 2-interferon by tumor necrosis factor: A homeostatic mechanism in the control of cell proliferation
    • Kohase M, Henriksen-DeStefano D, May LT, Vilcek J, Sehgal PB. Induction of beta 2-interferon by tumor necrosis factor: a homeostatic mechanism in the control of cell proliferation. Cell 1986; 45:659-666.
    • (1986) Cell , vol.45 , pp. 659-666
    • Kohase, M.1    Henriksen-DeStefano, D.2    May, L.T.3    Vilcek, J.4    Sehgal, P.B.5
  • 54
    • 0028929371 scopus 로고
    • Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation
    • Brockman JA, Scherer DC, McKinsey TA, et al. Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation. Mol. Cell. Biol. 1985;15: 2809-2818.
    • (1985) Mol. Cell. Biol , vol.15 , pp. 2809-2818
    • Brockman, J.A.1    Scherer, D.C.2    McKinsey, T.A.3
  • 55
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis
    • Ting AT, Pimentel-Muinos FX, Seed B. RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis. EMBO J. 1996;15:6189-6196.
    • (1996) EMBO J , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muinos, F.X.2    Seed, B.3
  • 56
    • 0033396491 scopus 로고    scopus 로고
    • Fas ligand-induced apoptosis
    • Nagata S. Fas ligand-induced apoptosis. Annu. Rev. Genet. 1999; 33:29-55.
    • (1999) Annu. Rev. Genet , vol.33 , pp. 29-55
    • Nagata, S.1
  • 57
    • 0029898073 scopus 로고    scopus 로고
    • The CD95 (APO-1/Fas) receptor activates NF-kappaB independently of its cytotoxic function
    • Ponton A, Clement MV, Stamenkovic I. The CD95 (APO-1/Fas) receptor activates NF-kappaB independently of its cytotoxic function. J. Biol. Chem. 1996;271:8991-8995.
    • (1996) J. Biol. Chem , vol.271 , pp. 8991-8995
    • Ponton, A.1    Clement, M.V.2    Stamenkovic, I.3
  • 58
    • 0032032627 scopus 로고    scopus 로고
    • CD95 (Fas)-induced caspase-mediated proteolysis of NF-kappaB
    • Ravi R, Bedi A, Fuchs EJ. CD95 (Fas)-induced caspase-mediated proteolysis of NF-kappaB. Cancer Res. 1998;58:882-886.
    • (1998) Cancer Res , vol.58 , pp. 882-886
    • Ravi, R.1    Bedi, A.2    Fuchs, E.J.3
  • 60
    • 0033548603 scopus 로고    scopus 로고
    • Cycloheximide-induced T cell death is mediated by a Fas-associated death domain-dependent mechanism
    • Tang D, Lahti JM, Grenet J, Kidd VJ. Cycloheximide-induced T cell death is mediated by a Fas-associated death domain-dependent mechanism. J. Biol. Chem. 1999;274:7245-7252.
    • (1999) J. Biol. Chem , vol.274 , pp. 7245-7252
    • Tang, D.1    Lahti, J.M.2    Grenet, J.3    Kidd, V.J.4
  • 61
    • 27644443762 scopus 로고    scopus 로고
    • Herpes simplex virus 2 modulates apoptosis and stimulates NF-kappaB nuclear translocation during infection in human epithelial HEp-2 cells
    • Yedowitz JC, Blaho JA. Herpes simplex virus 2 modulates apoptosis and stimulates NF-kappaB nuclear translocation during infection in human epithelial HEp-2 cells. Virology 2005;342:297-310.
    • (2005) Virology , vol.342 , pp. 297-310
    • Yedowitz, J.C.1    Blaho, J.A.2
  • 62
    • 34249663387 scopus 로고    scopus 로고
    • Sanfilippo CM, Blaho JA. The induction of apoptosis by HSV-1. In: Sandri-Goldin RM, ed. Alpha Herpesvirus: Molecular and Cellular Biology. Norfolk, U.K.: Caister; 2006:219-238.
    • Sanfilippo CM, Blaho JA. The induction of apoptosis by HSV-1. In: Sandri-Goldin RM, ed. Alpha Herpesvirus: Molecular and Cellular Biology. Norfolk, U.K.: Caister; 2006:219-238.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.