메뉴 건너뛰기




Volumn 29, Issue 1-2, 1998, Pages 81-92

The tumor necrosis factor signaling complex: Choosing a path toward cell death or cell proliferation

Author keywords

Apoptosis; Death domain; Lymphotoxin; Proliferation; TNF; TRAF

Indexed keywords

TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0031833240     PISSN: 10428194     EISSN: None     Source Type: Journal    
DOI: 10.3109/10428199809058384     Document Type: Review
Times cited : (34)

References (94)
  • 2
    • 0029075329 scopus 로고
    • Tumor necrosis factor ligand superfamily: Involvement in the pathology of malignant lymphomas
    • Gruss, H. J. and Dower, S. K. (1995). Tumor necrosis factor ligand superfamily: involvement in the pathology of malignant lymphomas. Blood, 85, 3378-3404.
    • (1995) Blood , vol.85 , pp. 3378-3404
    • Gruss, H.J.1    Dower, S.K.2
  • 4
    • 0029900295 scopus 로고    scopus 로고
    • The tumor necrosis factor ligand and receptor families
    • Bazzoni, F. and Beutler, B. (1996). The tumor necrosis factor ligand and receptor families. New England Journal of Medicine, 334, 1717-1725.
    • (1996) New England Journal of Medicine , vol.334 , pp. 1717-1725
    • Bazzoni, F.1    Beutler, B.2
  • 5
    • 0028990332 scopus 로고
    • Mechanisms of action of the tumor necrosis factor and lymphotoxin ligand-receptor system
    • Warzocha, K., Bienvenu, J., Coiffier, B. and Salles, G. (1995) Mechanisms of action of the tumor necrosis factor and lymphotoxin ligand-receptor system. European Cytokine Network, 6, 83-96.
    • (1995) European Cytokine Network , vol.6 , pp. 83-96
    • Warzocha, K.1    Bienvenu, J.2    Coiffier, B.3    Salles, G.4
  • 8
    • 0023637999 scopus 로고
    • Enhancement of human B-cell proliferation and differentiation by tumor necrosis factor alpha and interleukin-1
    • Jelinek, D. F. and Lipsky, P. E. (1987) Enhancement of human B-cell proliferation and differentiation by tumor necrosis factor alpha and interleukin-1. Journal of Immunology, 139, 2970-2975.
    • (1987) Journal of Immunology , vol.139 , pp. 2970-2975
    • Jelinek, D.F.1    Lipsky, P.E.2
  • 10
  • 11
    • 0026446156 scopus 로고
    • GM-CSF and TNF-α cooperate in the generation of dendritic Langerhans cells
    • Caux, C., Dezutter-Dambuyant, C., Schmitt, D. and Banchereau, J. (1992) GM-CSF and TNF-α cooperate in the generation of dendritic Langerhans cells. Nature, 360, 258-261.
    • (1992) Nature , vol.360 , pp. 258-261
    • Caux, C.1    Dezutter-Dambuyant, C.2    Schmitt, D.3    Banchereau, J.4
  • 12
    • 0027287507 scopus 로고
    • Membrane tumour necrosis factor-α is involved in the polyclonal B-cell activation induced by HIV-infected human T-cells
    • Macchia, D., Almerigogna, F., Parronchi, P., Ravina, A., Maggi, E. and Romagnani, S. (1993). Membrane tumour necrosis factor-α is involved in the polyclonal B-cell activation induced by HIV-infected human T-cells. Nature, 363, 464-466.
    • (1993) Nature , vol.363 , pp. 464-466
    • Macchia, D.1    Almerigogna, F.2    Parronchi, P.3    Ravina, A.4    Maggi, E.5    Romagnani, S.6
  • 14
    • 0027485202 scopus 로고
    • TNF alpha acts in synergy with GM-CSF to induce proliferation of acute myeloid leukemia cells by upregulation the GM-CSF receptor and GM-CSF gene expression
    • Brailly, H., Pebusque, M. J., Tabilio, A. and Mannoni, P. (1993). TNF alpha acts in synergy with GM-CSF to induce proliferation of acute myeloid leukemia cells by upregulation the GM-CSF receptor and GM-CSF gene expression. Leukemia, 7, 1557-1563.
    • (1993) Leukemia , vol.7 , pp. 1557-1563
    • Brailly, H.1    Pebusque, M.J.2    Tabilio, A.3    Mannoni, P.4
  • 17
    • 0023521629 scopus 로고
    • Lymphotoxin is an important T-cell derived growth factor for human B-cells
    • Kehrl, J. H., Alvarez-Mon, M., Delsing, G. A. and Fauci, A. S. (1987). Lymphotoxin is an important T-cell derived growth factor for human B-cells. Science, 238, 1144-1148.
    • (1987) Science , vol.238 , pp. 1144-1148
    • Kehrl, J.H.1    Alvarez-Mon, M.2    Delsing, G.A.3    Fauci, A.S.4
  • 18
    • 0030050618 scopus 로고    scopus 로고
    • T cell receptor-dependent cell death of T-cell hybridomas mediated by the CD30 cytoplasmic domain in association with tumor necrosis factor receptor-associated factors
    • Lee, S. Y., Park, C. G. and Choi, Y. (1996). T cell receptor-dependent cell death of T-cell hybridomas mediated by the CD30 cytoplasmic domain in association with tumor necrosis factor receptor-associated factors. Journal of Experimental Medicine, 183, 669-674.
    • (1996) Journal of Experimental Medicine , vol.183 , pp. 669-674
    • Lee, S.Y.1    Park, C.G.2    Choi, Y.3
  • 19
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
    • Smith, C. A., Farrah, T. and Goodwin, R. G. (1994). The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell, 76, 959-962.
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 21
    • 0026803051 scopus 로고
    • Lymphotoxin is expressed as a heteromeric complex with a distinct 33 kDa glycoprotein on the surface of an activated human T-cell hybridoma
    • Androlewicz, M. J., Browning, J. L. and Ware, C. F. (1992). Lymphotoxin is expressed as a heteromeric complex with a distinct 33 kDa glycoprotein on the surface of an activated human T-cell hybridoma. Journal of Biological Chemistry, 267, 2542-2547.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 2542-2547
    • Androlewicz, M.J.1    Browning, J.L.2    Ware, C.F.3
  • 22
    • 0024281428 scopus 로고
    • A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: Ramifications for the complex physiology of TNF
    • Kriegler, M., Perez, C. C., DeFay, K., Albert, I. and Lu, D. (1988). A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell, 53, 45-53.
    • (1988) Cell , vol.53 , pp. 45-53
    • Kriegler, M.1    Perez, C.C.2    DeFay, K.3    Albert, I.4    Lu, D.5
  • 28
    • 0025789089 scopus 로고
    • Lymphotoxin and an associated 33 kDa glycoprotein are expressed on the surface of an activated human T-cell hybridoma
    • Browning, J. L., Androlewicz, M. J. and Ware, C. F. (1991). Lymphotoxin and an associated 33 kDa glycoprotein are expressed on the surface of an activated human T-cell hybridoma. Journal of Immunology, 147, 1230-1237.
    • (1991) Journal of Immunology , vol.147 , pp. 1230-1237
    • Browning, J.L.1    Androlewicz, M.J.2    Ware, C.F.3
  • 30
    • 0025269050 scopus 로고
    • Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor
    • Loetscher, H., Pan, Y. C. E., Lahm, H. W., Gentz, R., Brockhaus, M., Tabuchi, H. and Lesslauer, W. (1990). Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor. Cell, 61, 351-359.
    • (1990) Cell , vol.61 , pp. 351-359
    • Loetscher, H.1    Pan, Y.C.E.2    Lahm, H.W.3    Gentz, R.4    Brockhaus, M.5    Tabuchi, H.6    Lesslauer, W.7
  • 34
    • 0024448122 scopus 로고
    • Two different cell types have different major receptors for human tumor necrosis factor (TNFα)
    • Hohmann, H. P., Remy, R. and Brochaus, M. (1989). Two different cell types have different major receptors for human tumor necrosis factor (TNFα). Journal of Biological Chemistry, 264, 14927-14934.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 14927-14934
    • Hohmann, H.P.1    Remy, R.2    Brochaus, M.3
  • 36
    • 0027211801 scopus 로고
    • Construction and evaluation of a hcDNA library of human 12p transcribed sequences derived from a somatic cell hybrid
    • Baens, M., Chaffanet, M., Cassiman, J. J., Van den Berghe, H. and Marynen, P. (1993). Construction and evaluation of a hcDNA library of human 12p transcribed sequences derived from a somatic cell hybrid. Genomics, 16, 214-218.
    • (1993) Genomics , vol.16 , pp. 214-218
    • Baens, M.1    Chaffanet, M.2    Cassiman, J.J.3    Van Den Berghe, H.4    Marynen, P.5
  • 38
    • 0026744103 scopus 로고
    • Tumor necrosis factor receptor signaling. A dominant negative mutation supresses the activation of the 55-kDa tumor necrosis factor receptor
    • Tartaglia, L. A. and Goeddel, D. V. (1992). Tumor necrosis factor receptor signaling. A dominant negative mutation supresses the activation of the 55-kDa tumor necrosis factor receptor. Journal of Biological Chemistry, 267, 4304-4307.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 4304-4307
    • Tartaglia, L.A.1    Goeddel, D.V.2
  • 39
    • 0027281373 scopus 로고
    • A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen
    • Itoh, N. and Nagata, S. (1993). A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen. Journal of Biological Chemistry, 268, 10932-10937.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 10932-10937
    • Itoh, N.1    Nagata, S.2
  • 40
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia, L. A., Ayres, T. M., Wong, G. H. W. and Goeddel, D. V. (1993). A novel domain within the 55 kd TNF receptor signals cell death. Cell, 73, 845-853.
    • (1993) Cell , vol.73 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.W.3    Goeddel, D.V.4
  • 41
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75kDa tumor necrosis factor receptor
    • Rothe, M., Wong, S. C., Henzel, W. J. and Goeddel, D. V. (1994). A novel family of putative signal transducers associated with the cytoplasmic domain of the 75kDa tumor necrosis factor receptor. Cell, 78, 681-692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 42
  • 43
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-κB by TNF receptor2 and CD40
    • Rothe, M., Sarma, V., Dixit, V. M. and Goeddel, D. V. (1995). TRAF2-mediated activation of NF-κB by TNF receptor2 and CD40. Science, 269, 1424-1427.
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 46
    • 0029761275 scopus 로고    scopus 로고
    • TRAF6 is a signal transducer for interleukin-1
    • Cao, Z., Xiong, J., Takeuchi, M., Kurama, T. and Goeddel, D. V. (1996). TRAF6 is a signal transducer for interleukin-1. Nature, 383, 443-446.
    • (1996) Nature , vol.383 , pp. 443-446
    • Cao, Z.1    Xiong, J.2    Takeuchi, M.3    Kurama, T.4    Goeddel, D.V.5
  • 48
    • 0030063533 scopus 로고    scopus 로고
    • Soluble cytokine receptors
    • Heaney, M. L. and Golde, D. W. (1996). Soluble cytokine receptors. Blood, 87, 847-857.
    • (1996) Blood , vol.87 , pp. 847-857
    • Heaney, M.L.1    Golde, D.W.2
  • 49
    • 0026009871 scopus 로고
    • Increased serum levels of soluble receptors for tumour necrosis factor in cancer patients
    • Aderka, D., Engelmann, H., Hornik, V., Skornick, Y., Levo, Y., Wallach, D. and Kushtar, G. (1991). Increased serum levels of soluble receptors for tumour necrosis factor in cancer patients. Cancer Research, 51, 5602-5609.
    • (1991) Cancer Research , vol.51 , pp. 5602-5609
    • Aderka, D.1    Engelmann, H.2    Hornik, V.3    Skornick, Y.4    Levo, Y.5    Wallach, D.6    Kushtar, G.7
  • 50
    • 0026741275 scopus 로고
    • Tumor necrosis factor soluble receptors circulate during experimental and clinical inflammation and can protect against excessive tumor necrosis factor α in vitro and in vivo
    • Van Zee, K. J., Kohno, T., Fischer, E., Rock, C. S., Moldawer, L. L. and Lowry, S. F. (1992). Tumor necrosis factor soluble receptors circulate during experimental and clinical inflammation and can protect against excessive tumor necrosis factor α in vitro and in vivo. Proceedings of the National Academy of Science USA, 89, 4845-4849.
    • (1992) Proceedings of the National Academy of Science USA , vol.89 , pp. 4845-4849
    • Van Zee, K.J.1    Kohno, T.2    Fischer, E.3    Rock, C.S.4    Moldawer, L.L.5    Lowry, S.F.6
  • 51
    • 0026595122 scopus 로고
    • Inhibition of ligand binding and antiproliferative effects of tumor necrosis factor and lymphotoxin by soluble forms of recombinant p60 and p80 receptors
    • Higuchi, M. and Aggarwal, B. B. (1992). Inhibition of ligand binding and antiproliferative effects of tumor necrosis factor and lymphotoxin by soluble forms of recombinant p60 and p80 receptors. Biochemical Biophysical Research Communications, 182, 638-643.
    • (1992) Biochemical Biophysical Research Communications , vol.182 , pp. 638-643
    • Higuchi, M.1    Aggarwal, B.B.2
  • 53
    • 0027245985 scopus 로고
    • Influence of nephrectomy on tumor necrosis factor clearance in murine model
    • Bemelmans, M. H. A., Gouma, D. J. and Buurman, W. A. (1993). Influence of nephrectomy on tumor necrosis factor clearance in murine model. Journal of Immunology, 150, 2007-2017.
    • (1993) Journal of Immunology , vol.150 , pp. 2007-2017
    • Bemelmans, M.H.A.1    Gouma, D.J.2    Buurman, W.A.3
  • 54
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation
    • Banner, D. W., D'Arcy, A., Janes, W., Gentz, R., Schoenfeld, H. J., Broger, C., Loetscher, H. and Lesslauer, W. (1993). Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: implications for TNF receptor activation. Cell, 73, 431-445.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.J.5    Broger, C.6    Loetscher, H.7    Lesslauer, W.8
  • 56
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. (1995). Dimerization of cell surface receptors in signal transduction. Cell, 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 57
    • 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, M. P., Mett, I. L., Varfolomeev, E. E., Chumakov, I., Shemer-Avni, Y., Camonis, J. H. and Wallach, D. (1995). 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. Journal of Biological Chemistry, 270, 387-391.
    • (1995) Journal of Biological Chemistry , 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
  • 58
    • 0027301244 scopus 로고
    • Ligand passing: The 75-kDa tumor necrosis factor (TNF) receptor recruits TNF for signaling by the 55-kDa TNF receptor
    • Tartaglia, L. A., Pennica, D. and Goeddel, D. V. (1993). Ligand passing: the 75-kDa tumor necrosis factor (TNF) receptor recruits TNF for signaling by the 55-kDa TNF receptor. Journal of Biological Chemistry, 268, 18542-18548.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 18542-18548
    • Tartaglia, L.A.1    Pennica, D.2    Goeddel, D.V.3
  • 59
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A. M., O'Rourke, K., Tewari, M., Dixit, V. M. (1995). FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell, 81, 505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 60
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu, H., Xiong, J. and Goeddel, D. V. (1995). The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell, 81, 495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 61
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger, B. Z., Leder, P., Lee, T. H., Kim, E. and Seed, B. (1995). RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell, 81, 513-523.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 62
    • 0028223847 scopus 로고
    • Generalized lymphoproliferative disease in mice, caused by a point mutation in the Fas ligand
    • Takahashi, T., Tanaka, M., Brannan, C. I., Jenkins, N. A., Copeland, N. G., Suda, T. and Nagata, S. (1994). Generalized lymphoproliferative disease in mice, caused by a point mutation in the Fas ligand. Cell, 76, 969-976.
    • (1994) Cell , vol.76 , pp. 969-976
    • Takahashi, T.1    Tanaka, M.2    Brannan, C.I.3    Jenkins, N.A.4    Copeland, N.G.5    Suda, T.6    Nagata, S.7
  • 63
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- And TNF receptor-induced cell death
    • Boldin, M. P., Goncharov, T. M., Goltsev, Y. V. and Wallach, D. (1996). Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell, 85, 803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 68
    • 0028873964 scopus 로고
    • Fas- And tumor necrosis factor-induced apoptosis is inhibited by the poxvirus Crma gene product
    • Tewari, M. and Dixit, V. M. (1995). Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus Crma gene product. Journal of Biological Chemistry, 270, 3255-3260.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 3255-3260
    • Tewari, M.1    Dixit, V.M.2
  • 70
    • 0023926860 scopus 로고
    • Sensitization and densitization to lethal effects of tumor necrosis factor and IL-1
    • Wallach, D., Holtmann, H., Engelmann, H. and Nophar, Y. (1988). Sensitization and densitization to lethal effects of tumor necrosis factor and IL-1. Journal of Immunology, 140, 2994-2999.
    • (1988) Journal of Immunology , vol.140 , pp. 2994-2999
    • Wallach, D.1    Holtmann, H.2    Engelmann, H.3    Nophar, Y.4
  • 71
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle, P. A. and Baltimore, D. (1996). NF-κB: ten years after. Cell, 87, 13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 72
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB
    • Beg, A. A., Sha, W. C., Bronson, R. T., Ghosh, S. and Baltimore, D. (1995). Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB. Nature, 376, 167-170.
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Ghosh, S.4    Baltimore, D.5
  • 73
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-β-induced cell death
    • Beg, A. A. and Baltimore, D. (1996). An essential role for NF-κB in preventing TNF-β-induced cell death. Science, 274, 782-784.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 74
    • 0029858387 scopus 로고    scopus 로고
    • TNF-and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB
    • Wang, C. Y., Mayo, M. W. and Baldwin, A. S. (1996). TNF-and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB. Science, 274, 784-787.
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin, A.S.3
  • 76
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death
    • Liu, Z. G., Hsu, H., Goeddel, D. V. and Karin, M. (1996). Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell, 87, 565-567.
    • (1996) Cell , vol.87 , pp. 565-567
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 77
    • 0029786304 scopus 로고    scopus 로고
    • Anatomy of TRAF2. Distinct domains for nucelar factor-κB activation and association with tumor necrosis factor signaling proteins
    • Takeuchi, M., Rothe, M. and Goeddel, Goeddel, D. V. (1996). Anatomy of TRAF2. Distinct domains for nucelar factor-κB activation and association with tumor necrosis factor signaling proteins. Journal of Biological Chemistry, 271, 19935-19942.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 19935-19942
    • Takeuchi, M.1    Rothe, M.2    Goeddel3    Goeddel, D.V.4
  • 78
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor1 signal transduction pathways
    • Hsu, H., Shu, H. B., Pan, M. G. and Goeddel, D. V. (1996). TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor1 signal transduction pathways. Cell, 84, 299-308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 79
    • 0029898073 scopus 로고    scopus 로고
    • The CD95 (APO-1/Fas) receptor activates NF-kappaB independently of its cytotoxic function
    • Ponton, A., Clement, M. V. and Stamenkovic, I. (1996). The CD95 (APO-1/Fas) receptor activates NF-kappaB independently of its cytotoxic function. Journal of Biological Chemistry, 271, 8991-8995.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 8991-8995
    • Ponton, A.1    Clement, M.V.2    Stamenkovic, I.3
  • 80
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1
    • Malinin, N. L., Boldin, M. P., Kovalenko, A. V. and Wallach, D. (1997). MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature, 385, 540-544.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 81
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger, R. and Krebs, E. G. (1995). The MAPK signaling cascade. FASEB Journal, 9, 726-735.
    • (1995) FASEB Journal , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 82
    • 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, H. B., Baichwal, V. and Goeddel, D. V. (1996). TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity, 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
  • 83
    • 0031013545 scopus 로고    scopus 로고
    • Activation of SAPK/JNK by TNF receptor 1 through a noncytotoxic TRAF2-dependent pathway
    • Natoli, G., Costanzo, A., Ianni, A., Templeton, D. J., Woodgett, J. R., Balsano, C. and Levrero, M. (1997). Activation of SAPK/JNK by TNF receptor 1 through a noncytotoxic TRAF2-dependent pathway. Science, 275, 200-203.
    • (1997) Science , vol.275 , pp. 200-203
    • Natoli, G.1    Costanzo, A.2    Ianni, A.3    Templeton, D.J.4    Woodgett, J.R.5    Balsano, C.6    Levrero, M.7
  • 84
    • 0027499132 scopus 로고
    • Pelle encodes a protein kinase required to establish dorsoventral polarity in the Drosophila embryo
    • Shelton, C. A. and Wasserman, S. A. (1993). Pelle encodes a protein kinase required to establish dorsoventral polarity in the Drosophila embryo. Cell, 72, 515-525.
    • (1993) Cell , vol.72 , pp. 515-525
    • Shelton, C.A.1    Wasserman, S.A.2
  • 85
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos, G., Birkenbach, M., Yalamanchili, R., VanArsdale, T., Ware, C. and Kieff, E. (1995). The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell, 80, 389-399.
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1    Birkenbach, M.2    Yalamanchili, R.3    VanArsdale, T.4    Ware, C.5    Kieff, E.6
  • 86
    • 0027939679 scopus 로고
    • Upregulation of bcl-2 by the Epstein-Barr virus latent membrane protein LMP1: A B-cell specific response that is delayed relative to NF-kappa B activation and to induction of cell surface markers
    • Rowe, M., Peng-Pilon, M., Huen, D. S., Hardy, R., Croom-Carter, D., Lundgren, E. and Rickinson, A. B. (1994). Upregulation of bcl-2 by the Epstein-Barr virus latent membrane protein LMP1: a B-cell specific response that is delayed relative to NF-kappa B activation and to induction of cell surface markers. Journal of Virology, 68, 5602-5612.
    • (1994) Journal of Virology , vol.68 , pp. 5602-5612
    • Rowe, M.1    Peng-Pilon, M.2    Huen, D.S.3    Hardy, R.4    Croom-Carter, D.5    Lundgren, E.6    Rickinson, A.B.7
  • 87
    • 0029583176 scopus 로고
    • Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death
    • Hay, B. A., Wassarman, D. A. and Rubin, G. M. (1995). Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death. Cell, 83, 1253-1262.
    • (1995) Cell , vol.83 , pp. 1253-1262
    • Hay, B.A.1    Wassarman, D.A.2    Rubin, G.M.3
  • 88
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculovirus inhibitor of apoptosis proteins
    • Rothe, M., Pan, M. G., Henzel, W. J., Ayres, T. M. and Goeddel, D. V. (1995). The TNFR2-TRAF signaling complex contains two novel proteins related to baculovirus inhibitor of apoptosis proteins. Cell, 83, 1243-1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 91
    • 0028233935 scopus 로고
    • Differential sensitivity of normal and Ha-ras-transformed C3H mouse embryo fibroblasts to tumor necrosis factor: Induction of bcl-2, c-myc, and manganese superoxide dismutase in resistant cells
    • Fernandez, A., Marin, M. C., McDonnell, T. and Ananthaswamy, H. N. (1994). Differential sensitivity of normal and Ha-ras-transformed C3H mouse embryo fibroblasts to tumor necrosis factor: induction of bcl-2, c-myc, and manganese superoxide dismutase in resistant cells. Oncogene, 9, 2009-2017.
    • (1994) Oncogene , vol.9 , pp. 2009-2017
    • Fernandez, A.1    Marin, M.C.2    McDonnell, T.3    Ananthaswamy, H.N.4
  • 92
    • 0027513548 scopus 로고
    • Expression of bcl-2 proten enhances the survival of mouse fibrosarcoid cells to tumor necrosis factor-mediated cytotoxicity
    • Hennet, T., Bertoni, G., Richter, C. and Peterhans, E. (1993). Expression of bcl-2 proten enhances the survival of mouse fibrosarcoid cells to tumor necrosis factor-mediated cytotoxicity. Cancer Research, 53, 1456-1460.
    • (1993) Cancer Research , vol.53 , pp. 1456-1460
    • Hennet, T.1    Bertoni, G.2    Richter, C.3    Peterhans, E.4
  • 93
    • 0027161158 scopus 로고
    • Effect of bcl-2 on Fas antigen-mediated cell death
    • Itoh, N., Tsujimoto, Y. and Nagata, S. (1993). Effect of bcl-2 on Fas antigen-mediated cell death. Journal of Immunology, 151, 621-627.
    • (1993) Journal of Immunology , vol.151 , pp. 621-627
    • Itoh, N.1    Tsujimoto, Y.2    Nagata, S.3
  • 94
    • 0028017574 scopus 로고
    • Differential expression of bcl-2 and susceptibility to anti-Fas-mediated cell death in peripheral blood lymphocytes, monocytes, and neutrophils
    • Iwai, K., Miyawaki, T., Takizawa, T., Konno, A., Ohta, K., Yachie, A., Seki, H. and Taniguchi, N. (1994). Differential expression of bcl-2 and susceptibility to anti-Fas-mediated cell death in peripheral blood lymphocytes, monocytes, and neutrophils. Blood, 84, 1201-1208.
    • (1994) Blood , vol.84 , pp. 1201-1208
    • Iwai, K.1    Miyawaki, T.2    Takizawa, T.3    Konno, A.4    Ohta, K.5    Yachie, A.6    Seki, H.7    Taniguchi, N.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.