메뉴 건너뛰기




Volumn 10, Issue 1, 2003, Pages 45-65

Tumor necrosis factor signaling

Author keywords

Apoptosis; IKK; immunity; JNK; Necrosis; NF B; TNF; TRAF2

Indexed keywords

CASPASE; CATHEPSIN B; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR ALPHA RECEPTOR; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND;

EID: 0037276438     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401189     Document Type: Review
Times cited : (2029)

References (337)
  • 1
    • 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, DeFay K et al. (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.2    DeFay, K.3
  • 2
    • 0030055168 scopus 로고    scopus 로고
    • Human pro-tumor necrosis factor is a homotrimer
    • Tang P, Hung M-C and Klostergaard J (1996) Human pro-tumor necrosis factor is a homotrimer. Biochemistry 35: 8216-8225
    • (1996) Biochemistry , vol.35 , pp. 8216-8225
    • Tang, P.1    Hung, M.-C.2    Klostergaard, J.3
  • 3
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black RA, Rauch CT, Kozlosky CJ et al. (1997) A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385: 729-733
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3
  • 4
    • 0001197832 scopus 로고
    • Emerging families of cytokines and receptors
    • Bazan JF (1993) Emerging families of cytokines and receptors. Curr. Biol. 3: 603-606
    • (1993) Curr. Biol. , vol.3 , pp. 603-606
    • Bazan, J.F.1
  • 5
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley RM, Killeen N and Lenardo MJ (2001) The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104: 487-501
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 7
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: Implications for TNF receptor activation
    • Banner DW, D'Arcy A, Janes W et al. (1993) Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta 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
  • 8
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    • Chan FK, Chun HJ, Zheng L et al. (2000) A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science 288: 2351-2354
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.1    Chun, H.J.2    Zheng, L.3
  • 9
    • 0028866022 scopus 로고
    • The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor
    • Grell M, Douni E, Wajant H et al. (1995) The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor. Cell 83: 793-802
    • (1995) Cell , vol.83 , pp. 793-802
    • Grell, M.1    Douni, E.2    Wajant, H.3
  • 10
    • 0031882913 scopus 로고    scopus 로고
    • The type 1 receptor (CD120a) is the high-affinity receptor for soluble tumor necrosis factor
    • Grell M, Wajant H, Zimmermann G and Scheurich P (1998) The type 1 receptor (CD120a) is the high-affinity receptor for soluble tumor necrosis factor. Proc. Natl. Acad. Sci. USA 95: 570-575
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 570-575
    • Grell, M.1    Wajant, H.2    Zimmermann, G.3    Scheurich, P.4
  • 11
    • 0026335446 scopus 로고
    • Soluble and cell surface receptors for tumor necrosis factor
    • Wallach D, Engelmann H, Nophar Y et al. (1991) Soluble and cell surface receptors for tumor necrosis factor. Agents Actions Suppl. 35: 51-57
    • (1991) Agents Actions Suppl. , vol.35 , pp. 51-57
    • Wallach, D.1    Engelmann, H.2    Nophar, Y.3
  • 12
    • 0035012652 scopus 로고    scopus 로고
    • Anti-tumor necrosis factor therapies
    • Taylor PC (2001) Anti-tumor necrosis factor therapies. Curr. Opin. Rheumatol. 13: 164-169
    • (2001) Curr. Opin. Rheumatol. , vol.13 , pp. 164-169
    • Taylor, P.C.1
  • 13
    • 0032846604 scopus 로고    scopus 로고
    • Cutting edge: A dominant negative form of TNF-alpha converting enzyme inhibits proTNF and TNFRII secretion
    • Solomon KA, Pesti N, Wu G and Newton RC (1999) Cutting edge: a dominant negative form of TNF-alpha converting enzyme inhibits proTNF and TNFRII secretion. J. Immunol. 163: 4105-4108
    • (1999) J. Immunol. , vol.163 , pp. 4105-4108
    • Solomon, K.A.1    Pesti, N.2    Wu, G.3    Newton, R.C.4
  • 14
    • 0033515520 scopus 로고    scopus 로고
    • Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes
    • McDermott MF, Aksentijevich I, Galon J et al. (1999) Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes. Cell 97: 133-144
    • (1999) Cell , vol.97 , pp. 133-144
    • McDermott, M.F.1    Aksentijevich, I.2    Galon, J.3
  • 15
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia LA, Ayres TM, Wong GH and Goeddel DV (1993) A novel domain within the 55 kd TNF receptor signals cell death. Cell 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
  • 17
    • 0032734462 scopus 로고    scopus 로고
    • TNF in the inflammatory response
    • Mannel DN and Echtenacher B (2000) TNF in the inflammatory response. Chem. Immunol. 74: 141-161
    • (2000) Chem. Immunol. , vol.74 , pp. 141-161
    • Mannel, D.N.1    Echtenacher, B.2
  • 18
    • 0022371461 scopus 로고
    • Identity of tumour necrosis factor and the macrophage-secreted factor cachectin
    • Beutler B, Greenwald D, Hulmes JD et al. (1985) Identity of tumour necrosis factor and the macrophage-secreted factor cachectin. Nature 316: 552-554
    • (1985) Nature , vol.316 , pp. 552-554
    • Beutler, B.1    Greenwald, D.2    Hulmes, J.D.3
  • 19
    • 0028864801 scopus 로고
    • Spontaneous inflammatory demyelinating disease in transgenic mice showing central nervous system-specific expression of tumor necrosis factor alpha
    • Probert L, Akassoglou K, Pasparakis M et al. (1995) Spontaneous inflammatory demyelinating disease in transgenic mice showing central nervous system-specific expression of tumor necrosis factor alpha. Proc. Natl. Acad. Sci. USA 92: 11294-11298
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11294-11298
    • Probert, L.1    Akassoglou, K.2    Pasparakis, M.3
  • 20
    • 0036548875 scopus 로고    scopus 로고
    • Neurodegenerative and neuroprotective effects of tumor necrosis factor (TNF) in retinal ischemia: Opposite roles of TNF receptor 1 and TNF receptor 2
    • Fontaine V, Mohand-Said S, Hanoteau N et al. (2002) Neurodegenerative and neuroprotective effects of tumor necrosis factor (TNF) in retinal ischemia: opposite roles of TNF receptor 1 and TNF receptor 2. J. Neurosci. 22: RC216
    • (2002) J. Neurosci. , vol.22
    • Fontaine, V.1    Mohand-Said, S.2    Hanoteau, N.3
  • 21
    • 0033103805 scopus 로고    scopus 로고
    • Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: Implications for joint and gut-associated immunopathologies
    • Kontoyiannis D, Pasparakis M, Pizarro TT et al. (1999) Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: implications for joint and gut-associated immunopathologies. Immunity 10: 387-398
    • (1999) Immunity , vol.10 , pp. 387-398
    • Kontoyiannis, D.1    Pasparakis, M.2    Pizarro, T.T.3
  • 22
    • 0031028140 scopus 로고    scopus 로고
    • Initiation of liver growth by tumor necrosis factor: Deficient liver regeneration in mice lacking type I tumor necrosis factor receptor
    • Yamada Y, Kirillova I, Peschon JJ and Fausto N (1997) Initiation of liver growth by tumor necrosis factor: deficient liver regeneration in mice lacking type I tumor necrosis factor receptor. Proc. Natl. Acad. Sci. USA 94: 1441-1446
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1441-1446
    • Yamada, Y.1    Kirillova, I.2    Peschon, J.J.3    Fausto, N.4
  • 23
    • 0031682110 scopus 로고    scopus 로고
    • Mechanisms of hepatic toxicity. I. TNF-induced liver injury
    • Bradham CA, Plumpe J, Manns MP et al. (1998) Mechanisms of hepatic toxicity. I. TNF-induced liver injury. Am. J. Physiol. 275: G387-G392
    • (1998) Am. J. Physiol. , vol.275
    • Bradham, C.A.1    Plumpe, J.2    Manns, M.P.3
  • 24
    • 0343674489 scopus 로고    scopus 로고
    • Reduction of chemokine levels and leukocyte traffic to joints by tumor necrosis factor alpha blockade in patients with rheumatoid arthritis
    • Taylor PC, Peters AM, Paleolog E et al. (2000) Reduction of chemokine levels and leukocyte traffic to joints by tumor necrosis factor alpha blockade in patients with rheumatoid arthritis. Arthritis Rheum. 43: 38-47
    • (2000) Arthritis Rheum. , vol.43 , pp. 38-47
    • Taylor, P.C.1    Peters, A.M.2    Paleolog, E.3
  • 25
    • 0034936964 scopus 로고    scopus 로고
    • Integrating anti-tumor necrosis factor therapy in inflammatory bowel disease: Current and future perspectives
    • Blam ME, Stein RB and Lichtenstein GR (2001) Integrating anti-tumor necrosis factor therapy in inflammatory bowel disease: current and future perspectives. Am. J. Gastroenterol. 96: 1977-1997
    • (2001) Am. J. Gastroenterol. , vol.96 , pp. 1977-1997
    • Blam, M.E.1    Stein, R.B.2    Lichtenstein, G.R.3
  • 26
    • 0031832783 scopus 로고    scopus 로고
    • Cytokine regulation of secondary lymphoid organ development
    • Chaplin DD and Fu Y (1998) Cytokine regulation of secondary lymphoid organ development. Curr. Opin. Immunol. 10: 289-297
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 289-297
    • Chaplin, D.D.1    Fu, Y.2
  • 27
    • 0032806023 scopus 로고    scopus 로고
    • Lymphoid neo-organogenesis: Lymphotoxin's role in inflammation and development
    • Ruddle NH (1999) Lymphoid neo-organogenesis: lymphotoxin's role in inflammation and development. Immunol. Res. 19: 119-125
    • (1999) Immunol. Res. , vol.19 , pp. 119-125
    • Ruddle, N.H.1
  • 28
    • 0345609037 scopus 로고    scopus 로고
    • Characterization of tumor necrosis factor-deficient mice
    • Marino MW, Dunn A, Grail D et al. (1997) Characterization of tumor necrosis factor-deficient mice. Proc. Natl. Acad. Sci. USA 194: 8093-8098
    • (1997) Proc. Natl. Acad. Sci. USA , vol.194 , pp. 8093-8098
    • Marino, M.W.1    Dunn, A.2    Grail, D.3
  • 29
    • 0028979703 scopus 로고
    • Tumor necrosis factor-alpha is required in the protective immune response against Mycobacterium tuberculosis in mice
    • Flynn JL, Goldstein MM, Chan J et al. (1995) Tumor necrosis factor-alpha is required in the protective immune response against Mycobacterium tuberculosis in mice. Immunity 2: 561-572
    • (1995) Immunity , vol.2 , pp. 561-572
    • Flynn, J.L.1    Goldstein, M.M.2    Chan, J.3
  • 30
    • 0028585950 scopus 로고
    • Phenotypic analysis of TNFR1-deficient mice and characterization of TNFR1-deficient fibroblasts in vitro
    • Rothe J, Mackay F, Bluethmann H et al. (1994) Phenotypic analysis of TNFR1-deficient mice and characterization of TNFR1-deficient fibroblasts in vitro. Circ. Shock 44: 51-56
    • (1994) Circ. Shock , vol.44 , pp. 51-56
    • Rothe, J.1    Mackay, F.2    Bluethmann, H.3
  • 31
    • 0029982872 scopus 로고    scopus 로고
    • Mice lacking the TNF receptor p55 fail to resolve lesions caused by infection with Leishmania major, but control parasite replication
    • Vieira LQ, Goldschmidt M, Nashleanas M et al. (1996) Mice lacking the TNF receptor p55 fail to resolve lesions caused by infection with Leishmania major, but control parasite replication. J. Immunol. 157: 827-835
    • (1996) J. Immunol. , vol.157 , pp. 827-835
    • Vieira, L.Q.1    Goldschmidt, M.2    Nashleanas, M.3
  • 32
    • 0033559125 scopus 로고    scopus 로고
    • Structural deficiencies in granuloma formation in TNF gene-targeted mice underlie the heightened susceptibility to aerosol Mycobacterium tuberculosis infection, which is not compensated for by lymphotoxin
    • Bean AG, Roach DR, Briscoe H et al. (1999) Structural deficiencies in granuloma formation in TNF gene-targeted mice underlie the heightened susceptibility to aerosol Mycobacterium tuberculosis infection, which is not compensated for by lymphotoxin. J. Immunol. 162: 3504-3511
    • (1999) J. Immunol. , vol.162 , pp. 3504-3511
    • Bean, A.G.1    Roach, D.R.2    Briscoe, H.3
  • 33
    • 0032055198 scopus 로고    scopus 로고
    • Crucial role of TNF receptor type 1 (p55), but not of TNF receptor type 2 (p75), in murine toxoplasmosis
    • Deckert-Schluter M, Bluethmann H, Rang A et al. (1998) Crucial role of TNF receptor type 1 (p55), but not of TNF receptor type 2 (p75), in murine toxoplasmosis. J. Immunol. 160: 3427-3436
    • (1998) J. Immunol. , vol.160 , pp. 3427-3436
    • Deckert-Schluter, M.1    Bluethmann, H.2    Rang, A.3
  • 34
    • 0034489595 scopus 로고    scopus 로고
    • Absence of the p55 Kd TNF-alpha receptor promotes survival in rabies virus acute encephalitis
    • Camelo S, Lafage M and Lafon M (2000) Absence of the p55 Kd TNF-alpha receptor promotes survival in rabies virus acute encephalitis. J. Neurovirol. 6: 507-518
    • (2000) J. Neurovirol. , vol.6 , pp. 507-518
    • Camelo, S.1    Lafage, M.2    Lafon, M.3
  • 35
    • 0033982986 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor p55-deficient mice respond to acute Yersinia enterocolitica infection with less apoptosis and more effective host resistance
    • Zhao YX, Lajoie G, Zhang H et al. (2000) Tumor necrosis factor receptor p55-deficient mice respond to acute Yersinia enterocolitica infection with less apoptosis and more effective host resistance. Infect. Immun. 68: 1243-1251
    • (2000) Infect. Immun. , vol.68 , pp. 1243-1251
    • Zhao, Y.X.1    Lajoie, G.2    Zhang, H.3
  • 36
    • 15644382222 scopus 로고    scopus 로고
    • Crucial role of tumor necrosis factor (TNF) receptor 2 and membrane- bound TNF in experimental cerebral malaria
    • Lucas R, Juillard P, Decoster E et al. (1997) Crucial role of tumor necrosis factor (TNF) receptor 2 and membrane- bound TNF in experimental cerebral malaria. Eur. J. Immunol. 27: 1719-1725
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1719-1725
    • Lucas, R.1    Juillard, P.2    Decoster, E.3
  • 37
    • 0032813516 scopus 로고    scopus 로고
    • On the role of tumor necrosis factor and receptors in models of multiorgan failure, rheumatoid arthritis, multiple sclerosis and inflammatory bowel disease
    • Kollias G, Douni E, Kassiotis G and Kontoyiannis D (1999) On the role of tumor necrosis factor and receptors in models of multiorgan failure, rheumatoid arthritis, multiple sclerosis and inflammatory bowel disease. Immunol. Rev. 169: 175-194
    • (1999) Immunol. Rev. , vol.169 , pp. 175-194
    • Kollias, G.1    Douni, E.2    Kassiotis, G.3    Kontoyiannis, D.4
  • 38
    • 0036157584 scopus 로고    scopus 로고
    • Exacerbation of Mycobacterium tuberculosis enteritis masquerading as Crohn's disease after treatment with a tumor necrosis factor-alpha inhibitor
    • Wagner TE, Huseby ES and Huseby JS (2002) Exacerbation of Mycobacterium tuberculosis enteritis masquerading as Crohn's disease after treatment with a tumor necrosis factor-alpha inhibitor. Am. J. Med. 112: 67-69
    • (2002) Am. J. Med. , vol.112 , pp. 67-69
    • Wagner, T.E.1    Huseby, E.S.2    Huseby, J.S.3
  • 39
    • 0024009890 scopus 로고
    • Tumor necrosis factor
    • Old LJ (1988) Tumor necrosis factor. Sci. Am. 258: 59-75
    • (1988) Sci. Am. , vol.258 , pp. 59-75
    • Old, L.J.1
  • 40
    • 0022382737 scopus 로고
    • Recombinant human tumor necrosis factor-alpha: Effects on proliferation of normal and transformed cells in vitro
    • Sugarman BJ, Aggarwal BB, Hass PE et al. (1985) Recombinant human tumor necrosis factor-alpha: effects on proliferation of normal and transformed cells in vitro. Science 230: 943-945
    • (1985) Science , vol.230 , pp. 943-945
    • Sugarman, B.J.1    Aggarwal, B.B.2    Hass, P.E.3
  • 41
    • 0027407938 scopus 로고
    • Mechanisms of rejection induced by tumor cell-targeted gene transfer of interleukin 2, interleukin 4, interleukin 7, tumor necrosis factor, or interferon gamma
    • Hock H, Dorsch M, Kunzendorf U et al. (1993) Mechanisms of rejection induced by tumor cell-targeted gene transfer of interleukin 2, interleukin 4, interleukin 7, tumor necrosis factor, or interferon gamma. Proc. Natl. Acad. Sci. USA 90: 2774-2778
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2774-2778
    • Hock, H.1    Dorsch, M.2    Kunzendorf, U.3
  • 42
    • 0035403040 scopus 로고    scopus 로고
    • Isolated limb perfusion for extremity soft-tissue sarcomas, in-transit metastases, and other unresectable tumors: Credits, debits, and future perspectives
    • Eggermont AM and ten Hagen TL (2001) Isolated limb perfusion for extremity soft-tissue sarcomas, in-transit metastases, and other unresectable tumors: credits, debits, and future perspectives. Curr. Oncol. Rep. 3: 359-367
    • (2001) Curr. Oncol. Rep. , vol.3 , pp. 359-367
    • Eggermont, A.M.1    ten Hagen, T.L.2
  • 43
    • 0040887215 scopus 로고    scopus 로고
    • Evidence for the involvement of endothelial cell integrin alphaVbeta3 in the disruption of the tumor vasculature induced by TNF and IFN-gamma
    • Ruegg C, Yilmaz A and Bieler G et al. (1998) Evidence for the involvement of endothelial cell integrin alphaVbeta3 in the disruption of the tumor vasculature induced by TNF and IFN-gamma. Nat. Med. 4: 408-414
    • (1998) Nat. Med. , vol.4 , pp. 408-414
    • Ruegg, C.1    Yilmaz, A.2    Bieler, G.3
  • 44
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • Baud V and Karin M (2001) Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol. 11: 372-377
    • (2001) Trends Cell Biol. , vol.11 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 45
    • 0028971289 scopus 로고
    • Rel/NF-kappa B/I kappa B family: Intimate tales of association and dissociation
    • Verma IM, Stevenson JK, Schwarz EM et al. (1995) Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation. Genes Dev. 9: 2723-2735
    • (1995) Genes Dev. , vol.9 , pp. 2723-2735
    • Verma, I.M.1    Stevenson, J.K.2    Schwarz, E.M.3
  • 46
    • 0034283837 scopus 로고    scopus 로고
    • The Rel/NF-kappa B family: Friend and foe
    • Perkins ND (2000) The Rel/NF-kappa B family: friend and foe. Trends Biochem. Sci. 25: 434-440
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 434-440
    • Perkins, N.D.1
  • 47
    • 0030685825 scopus 로고    scopus 로고
    • IKK-1 and IKK-2: Cytokine-activated IkappaB kinases essential for NF-kappaB activation
    • Mercurio F, Zhu H, Murray BW et al. (1997) IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation. Science 278: 860-866
    • (1997) Science , vol.278 , pp. 860-866
    • Mercurio, F.1    Zhu, H.2    Murray, B.W.3
  • 48
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB
    • DiDonato JA, Hayakawa M, Rothwarf DM et al. (1997) A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB. Nature 388: 548-554
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3
  • 49
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • Zandi E, Rothwarf DM, Delhase M et al. (1997) The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91: 243-252
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3
  • 50
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation
    • Yamaoka S, Courtois G, Bessia C et al. (1998) Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 93: 1231-1240
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3
  • 51
    • 0033514445 scopus 로고    scopus 로고
    • Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis
    • Li Y, Kang J, Friedman J et al. (1999) Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis. Proc. Natl. Acad. Sci. USA 96: 1042-1047
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1042-1047
    • Li, Y.1    Kang, J.2    Friedman, J.3
  • 52
    • 0032541657 scopus 로고    scopus 로고
    • IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex
    • Rothwarf DM, Zandi E, Natoli G and Karin M (1998) IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex. Nature 395: 297-300
    • (1998) Nature , vol.395 , pp. 297-300
    • Rothwarf, D.M.1    Zandi, E.2    Natoli, G.3    Karin, M.4
  • 53
    • 0034624810 scopus 로고    scopus 로고
    • Somatic mutagenesis studies of NF-kappa B signaling in human T cells: Evidence for an essential role of IKK gamma in NF-kappa B activation by T-cell costimulatory signals and HTLV-I Tax protein
    • Harhaj EW, Good L, Xiao G et al. (2000) Somatic mutagenesis studies of NF-kappa B signaling in human T cells: evidence for an essential role of IKK gamma in NF-kappa B activation by T-cell costimulatory signals and HTLV-I Tax protein. Oncogene 19: 1448-1456
    • (2000) Oncogene , vol.19 , pp. 1448-1456
    • Harhaj, E.W.1    Good, L.2    Xiao, G.3
  • 54
    • 0032589935 scopus 로고    scopus 로고
    • IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex
    • Mercurio F, Murray BW, Shevchenko A et al. (1999) IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex. Mol. Cell Biol. 19: 1526-1538
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1526-1538
    • Mercurio, F.1    Murray, B.W.2    Shevchenko, A.3
  • 55
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • Chen G, Cao P and Goeddel DV (2002) TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol. Cell 9: 401-410
    • (2002) Mol. Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 56
    • 0034175632 scopus 로고    scopus 로고
    • Severe liver degeneration and lack of NF-kappaB activation in NEMO/IKKgamma-deficient mice
    • Rudolph D, Yeh WC, Wakeham A et al. (2000) Severe liver degeneration and lack of NF-kappaB activation in NEMO/IKKgamma-deficient mice. Genes Dev. 14: 854-862
    • (2000) Genes Dev. , vol.14 , pp. 854-862
    • Rudolph, D.1    Yeh, W.C.2    Wakeham, A.3
  • 57
    • 0033638970 scopus 로고    scopus 로고
    • NEMO/IKK gamma-deficient mice model incontinentia pigmenti
    • Schmidt-Supprian M, Bloch W, Courtois G et al. (2000) NEMO/IKK gamma-deficient mice model incontinentia pigmenti. Mol. Cell 5: 981-992
    • (2000) Mol. Cell , vol.5 , pp. 981-992
    • Schmidt-Supprian, M.1    Bloch, W.2    Courtois, G.3
  • 58
    • 0033634663 scopus 로고    scopus 로고
    • Female mice heterozygous for IKK gamma/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti
    • Makris C, Godfrey VL, Krahn-Senftleben G et al. (2000) Female mice heterozygous for IKK gamma/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti. Mol. Cell 5: 969-979
    • (2000) Mol. Cell , vol.5 , pp. 969-979
    • Makris, C.1    Godfrey, V.L.2    Krahn-Senftleben, G.3
  • 59
    • 0033119952 scopus 로고    scopus 로고
    • Embryonic lethality, liver degeneration, and impaired NF-kappa B activation in IKK-beta-deficient mice
    • Tanaka M, Fuentes ME, Yamaguchi K et al. (1999) Embryonic lethality, liver degeneration, and impaired NF-kappa B activation in IKK-beta-deficient mice. Immunity 10: 421-429
    • (1999) Immunity , vol.10 , pp. 421-429
    • Tanaka, M.1    Fuentes, M.E.2    Yamaguchi, K.3
  • 60
    • 0033537739 scopus 로고    scopus 로고
    • Severe liver degeneration in mice lacking the IkappaB kinase 2 gene
    • Li Q, Van Antwerp D, Mercurio F et al. (1999) Severe liver degeneration in mice lacking the IkappaB kinase 2 gene. Science 284: 321-325
    • (1999) Science , vol.284 , pp. 321-325
    • Li, Q.1    Van Antwerp, D.2    Mercurio, F.3
  • 61
    • 0033537757 scopus 로고    scopus 로고
    • Limb and skin abnormalities in mice lacking IKKalpha
    • Takeda K, Takeuchi O, Tsujimura T et al. (1999) Limb and skin abnormalities in mice lacking IKKalpha. Science 284: 313-316
    • (1999) Science , vol.284 , pp. 313-316
    • Takeda, K.1    Takeuchi, O.2    Tsujimura, T.3
  • 62
    • 0033537767 scopus 로고    scopus 로고
    • Abnormal morphogenesis but intact IKK activation in mice lacking the IKKalpha subunit of IkappaB kinase
    • Hu Y, Baud V, Delhase M et al. (1999) Abnormal morphogenesis but intact IKK activation in mice lacking the IKKalpha subunit of IkappaB kinase. Science 284: 316-320
    • (1999) Science , vol.284 , pp. 316-320
    • Hu, Y.1    Baud, V.2    Delhase, M.3
  • 63
    • 0033563227 scopus 로고    scopus 로고
    • IKK1-deficient mice exhibit abnormal development of skin and skeleton
    • Li Q, Lu Q, Hwang JY et al. (1999) IKK1-deficient mice exhibit abnormal development of skin and skeleton. Genes Dev. 13: 1322-1328
    • (1999) Genes Dev. , vol.13 , pp. 1322-1328
    • Li, Q.1    Lu, Q.2    Hwang, J.Y.3
  • 64
    • 17944378526 scopus 로고    scopus 로고
    • Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway
    • Senftleben U, Cao Y, Xiao G et al. (2001) Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway. Science 293: 1495-1499
    • (2001) Science , vol.293 , pp. 1495-1499
    • Senftleben, U.1    Cao, Y.2    Xiao, G.3
  • 65
    • 0035803392 scopus 로고    scopus 로고
    • Retroviral oncoprotein Tax induces processing of NF-kappaB2/p100 in T cells: Evidence for the involvement of IKKalpha
    • Xiao G, Cvijic ME, Fong A et al. (2001) Retroviral oncoprotein Tax induces processing of NF-kappaB2/p100 in T cells: evidence for the involvement of IKKalpha. EMBO J. 20: 6805-6815
    • (2001) EMBO J. , vol.20 , pp. 6805-6815
    • Xiao, G.1    Cvijic, M.E.2    Fong, A.3
  • 66
    • 0034661272 scopus 로고    scopus 로고
    • Complete lack of NF-kappaB activity in IKK1 and IKK2 double-deficient mice: Additional defect in neurulation
    • Li Q, Estepa G, Memet S et al. (2000) Complete lack of NF-kappaB activity in IKK1 and IKK2 double-deficient mice: additional defect in neurulation. Genes Dev. 14: 1729-1733
    • (2000) Genes Dev. , vol.14 , pp. 1729-1733
    • Li, Q.1    Estepa, G.2    Memet, S.3
  • 67
    • 0033485542 scopus 로고    scopus 로고
    • NF-kappaB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase
    • Pomerantz JL and Baltimore D (1999) NF-kappaB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase. EMBO J. 18: 6694-6704
    • (1999) EMBO J. , vol.18 , pp. 6694-6704
    • Pomerantz, J.L.1    Baltimore, D.2
  • 68
    • 0034665047 scopus 로고    scopus 로고
    • Deficiency of T2K leads to apoptotic liver degeneration and impaired NF-kappaB-dependent gene transcription
    • Bonnard M, Mirtsos C, Suzuki S et al. (2000) Deficiency of T2K leads to apoptotic liver degeneration and impaired NF-kappaB-dependent gene transcription. EMBO J. 19: 4976-4985
    • (2000) EMBO J. , vol.19 , pp. 4976-4985
    • Bonnard, M.1    Mirtsos, C.2    Suzuki, S.3
  • 69
    • 0034643170 scopus 로고    scopus 로고
    • NAK is an IkappaB kinase-activating kinase
    • Tojima Y, Fujimoto A, Delhase M et al. (2000) NAK is an IkappaB kinase-activating kinase. Nature 404: 778-782
    • (2000) Nature , vol.404 , pp. 778-782
    • Tojima, Y.1    Fujimoto, A.2    Delhase, M.3
  • 70
    • 0033623848 scopus 로고    scopus 로고
    • IKKepsilon is part of a novel PMA-inducible IkappaB kinase complex
    • Peters RT, Liao SM and Maniatis T (2000) IKKepsilon is part of a novel PMA-inducible IkappaB kinase complex. Mol. Cell 5: 513-522
    • (2000) Mol. Cell , vol.5 , pp. 513-522
    • Peters, R.T.1    Liao, S.M.2    Maniatis, T.3
  • 71
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang Y, Woronicz JD, Liu W and Goeddel DV (1999) Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 283: 543-546
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 72
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF- kappa B activation
    • Hsu H, Xiong J and Goeddel DV (1995) The TNF receptor 1-associated protein TRADD signals cell death and NF- kappa B activation. Cell 81: 495-504
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 73
    • 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 et al. (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
  • 74
    • 0034982801 scopus 로고    scopus 로고
    • The TNF-receptor-associated factor family. Scaffold molecules for cytokine receptors, kinases and their regulators
    • Wajant H, Henkler F, Scheurich P (2001) The TNF-receptor-associated factor family. Scaffold molecules for cytokine receptors, kinases and their regulators. Cell Signal. 13: 389-400
    • (2001) Cell Signal , vol.13 , pp. 389-400
    • Wajant, H.1    Henkler, F.2    Scheurich, P.3
  • 75
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H, Shu HB, Pan MG and Goeddel DV (1996) TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 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
  • 76
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin A, Cook A, Lin Y et al. (2000) The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 12: 419-429
    • (2000) Immunity , vol.12 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3
  • 77
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation
    • Zhang SQ, Kovalenko A, Cantarella G and Wallach D (2000) Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation. Immunity 12: 301-311
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 78
    • 0035021123 scopus 로고    scopus 로고
    • The alpha and beta subunits of IkappaB kinase (IKK) mediate TRAF2- dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF
    • Davin A, Lin Y, Yamaoka S et al. (2001) The alpha and beta subunits of IkappaB kinase (IKK) mediate TRAF2- dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF. Mol. Cell Biol. 21: 3986-3994
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3986-3994
    • Davin, A.1    Lin, Y.2    Yamaoka, S.3
  • 79
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NE-kappaB but not Fas/APO-1-initiated apoptosis
    • Ting AT, Pimentel-Muinos FX and Seed B (1996) RIP mediates tumor necrosis factor receptor 1 activation of NE-kappaB but not Fas/APO-1-initiated apoptosis. EMBO J. 15: 6189-6196
    • (1996) EMBO J. , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muinos, F.X.2    Seed, B.3
  • 80
    • 0034922161 scopus 로고    scopus 로고
    • The essential role of MEKK3 in TNF-induced NF-kappaB activation
    • Yang J, Lin Y, Guo Z et al. (2001) The essential role of MEKK3 in TNF-induced NF-kappaB activation. Nat. Immunol. 2: 620-624
    • (2001) Nat. Immunol. , vol.2 , pp. 620-624
    • Yang, J.1    Lin, Y.2    Guo, Z.3
  • 81
    • 0033563101 scopus 로고    scopus 로고
    • Signaling by proinflammatory cytokines: Oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain
    • Baud V, Liu ZG, Bennett B et al. (1999) Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain. Genes Dev. 13: 1297-1308
    • (1999) Genes Dev. , vol.13 , pp. 1297-1308
    • Baud, V.1    Liu, Z.G.2    Bennett, B.3
  • 82
    • 0035920178 scopus 로고    scopus 로고
    • Role of receptor-interacting protein in tumor necrosis factor-alpha-dependent MEKK1 activation
    • Kim JW, Joe CO and Choi EJ (2001) Role of receptor-interacting protein in tumor necrosis factor-alpha-dependent MEKK1 activation. J. Biol. Chem. 276: 27064-27070
    • (2001) J. Biol. Chem. , vol.276 , pp. 27064-27070
    • Kim, J.W.1    Joe, C.O.2    Choi, E.J.3
  • 83
    • 0034625170 scopus 로고    scopus 로고
    • MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration
    • Xia Y, Makris C, Su B et al. (2000) MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration. Proc. Natl. Acad. Sci. USA 97: 5243-5248
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5243-5248
    • Xia, Y.1    Makris, C.2    Su, B.3
  • 84
    • 0034691062 scopus 로고    scopus 로고
    • MEK kinase 1 gene disruption alters cell migration and c-Jun NH2-terminal kinase regulation but does not cause a measurable defect in NF-kappa B activation
    • Yujiri T, Ware M, Widmann C et al. (2000) MEK kinase 1 gene disruption alters cell migration and c-Jun NH2-terminal kinase regulation but does not cause a measurable defect in NF-kappa B activation. Proc. Natl. Acad. Sci. USA 97: 7272-7277
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7272-7277
    • Yujiri, T.1    Ware, M.2    Widmann, C.3
  • 85
    • 0034599476 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL1-TRAF6 pathway
    • Sanz L, Diaz-Meco MT, Nakano H and Moscat J (2000) The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL1-TRAF6 pathway. EMBO J. 19: 1576-1586
    • (2000) EMBO J. , vol.19 , pp. 1576-1586
    • Sanz, L.1    Diaz-Meco, M.T.2    Nakano, H.3    Moscat, J.4
  • 86
    • 13944253118 scopus 로고    scopus 로고
    • Targeted disruption of the zetaPKC gene results in the impairment of the NF-kappaB pathway
    • Leitges M, Sanz L, Martin P et al. (2001) Targeted disruption of the zetaPKC gene results in the impairment of the NF-kappaB pathway. Mol. Cell 8: 771-780
    • (2001) Mol. Cell , vol.8 , pp. 771-780
    • Leitges, M.1    Sanz, L.2    Martin, P.3
  • 87
    • 0033531795 scopus 로고    scopus 로고
    • Regulation of NF-kappaB ReIA phosphorylation and transcriptional activity by p21(ras) and protein kinase Czeta in primary endothelial cells
    • Anrather J, Csizmadia V, Soares MP and Winkler H (1999) Regulation of NF-kappaB ReIA phosphorylation and transcriptional activity by p21(ras) and protein kinase Czeta in primary endothelial cells. J. Biol. Chem. 274: 13594-13603
    • (1999) J. Biol. Chem. , vol.274 , pp. 13594-13603
    • Anrather, J.1    Csizmadia, V.2    Soares, M.P.3    Winkler, H.4
  • 88
    • 0030991201 scopus 로고    scopus 로고
    • The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism
    • Zhong H, SuYang H, Erdjument-Bromage H et al. (1997) The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell 89: 413-424
    • (1997) Cell , vol.89 , pp. 413-424
    • Zhong, H.1    SuYang, H.2    Erdjument-Bromage, H.3
  • 89
    • 0032588389 scopus 로고    scopus 로고
    • Activation of IkappaB kinase beta by protein kinase C isoforms
    • Lallena MJ, Diaz-Meco MT, Bren G et al. (1999) Activation of IkappaB kinase beta by protein kinase C isoforms. Mol. Cell Biol. 19: 2180-2188
    • (1999) Mol. Cell Biol. , vol.19 , pp. 2180-2188
    • Lallena, M.J.1    Diaz-Meco, M.T.2    Bren, G.3
  • 90
    • 0033153320 scopus 로고    scopus 로고
    • The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation
    • Sanz L, Sanchez P, Lallena MJ et al. (1999) The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. EMBO J. 18: 3044-3053
    • (1999) EMBO J. , vol.18 , pp. 3044-3053
    • Sanz, L.1    Sanchez, P.2    Lallena, M.J.3
  • 91
    • 0034693133 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II
    • Wang D, Westerheide SD, Hanson JL and Baldwin AS (2000) Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II. J. Biol. Chem. 275: 32592-32597
    • (2000) J. Biol. Chem. , vol.275 , pp. 32592-32597
    • Wang, D.1    Westerheide, S.D.2    Hanson, J.L.3    Baldwin, A.S.4
  • 92
    • 0037039665 scopus 로고    scopus 로고
    • Distinct roles of the Ikappa B kinase alpha and beta subunits in liberating nuclear factor kappa B (NF-kappa B) from Ikappa B and in phosphorylating the p65 subunit of NF-kappa B
    • Sizemore N, Lerner N, Dombrowski N et al. (2002) Distinct roles of the Ikappa B kinase alpha and beta subunits in liberating nuclear factor kappa B (NF-kappa B) from Ikappa B and in phosphorylating the p65 subunit of NF-kappa B. J. Biol. Chem. 277: 3863-3869
    • (2002) J. Biol. Chem. , vol.277 , pp. 3863-3869
    • Sizemore, N.1    Lerner, N.2    Dombrowski, N.3
  • 93
    • 0033517189 scopus 로고    scopus 로고
    • NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes ON, Mayo LD, Gustin JA et al. (1999) NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 401: 82-85
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3
  • 94
    • 0033517190 scopus 로고    scopus 로고
    • NF-kappaB is a target of AKT in antiapoptotic PDGF signalling
    • Romashkova JA and Makarov SS (1999) NF-kappaB is a target of AKT in antiapoptotic PDGF signalling. Nature 401: 86-90
    • (1999) Nature , vol.401 , pp. 86-90
    • Romashkova, J.A.1    Makarov, S.S.2
  • 95
    • 0033617315 scopus 로고    scopus 로고
    • A novel pathway for tumor necrosis factor-alpha and ceramide signaling involving sequential activation of tyrosine kinase, p21(ras), and phosphatidylinositol 3-kinase
    • Hanna AN, Chan EY, Xu J et al. (1999) A novel pathway for tumor necrosis factor-alpha and ceramide signaling involving sequential activation of tyrosine kinase, p21(ras), and phosphatidylinositol 3-kinase. J. Biol. Chem. 274: 12722-12729
    • (1999) J. Biol. Chem. , vol.274 , pp. 12722-12729
    • Hanna, A.N.1    Chan, E.Y.2    Xu, J.3
  • 96
    • 0033588162 scopus 로고    scopus 로고
    • Roles of phosphatidylinositol 3-kinase and Rac in the nuclear signaling by tumor necrosis factor-alpha in rat-2 fibroblasts
    • Kim BC, Lee MN, Kim JY et al. (1999) Roles of phosphatidylinositol 3-kinase and Rac in the nuclear signaling by tumor necrosis factor-alpha in rat-2 fibroblasts. J. Biol. Chem. 274: 24372-24377
    • (1999) J. Biol. Chem. , vol.274 , pp. 24372-24377
    • Kim, B.C.1    Lee, M.N.2    Kim, J.Y.3
  • 97
    • 0034142254 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase as a mediator of TNF-induced NF-kappa B activation
    • Reddy SA, Huang JH and Liao WS (2000) Phosphatidylinositol 3-kinase as a mediator of TNF-induced NF-kappa B activation. J. Immunol. 164: 1355-1363
    • (2000) J. Immunol. , vol.164 , pp. 1355-1363
    • Reddy, S.A.1    Huang, J.H.2    Liao, W.S.3
  • 98
    • 0033516674 scopus 로고    scopus 로고
    • Tumor necrosis factor induces phosphorylation and translocation of BAD through a phosphatidylinositide-3-OH kinase-dependent pathway
    • Pastorino JG, Tafani M and Farber JL (1999) Tumor necrosis factor induces phosphorylation and translocation of BAD through a phosphatidylinositide-3-OH kinase-dependent pathway. J. Biol. Chem. 274: 19411-19416
    • (1999) J. Biol. Chem. , vol.274 , pp. 19411-19416
    • Pastorino, J.G.1    Tafani, M.2    Farber, J.L.3
  • 99
    • 0034667519 scopus 로고    scopus 로고
    • Phosphatidylcholine-specific phospholipase C and phospholipase D are respectively implicated in mitogen-activated protein kinase and nuclear factor kappaB activation in tumour-necrosis-factor-alpha-treated immature acute-myeloid-leukaemia cells
    • Plo I, Lautier D, Levade T et al. (2000) Phosphatidylcholine-specific phospholipase C and phospholipase D are respectively implicated in mitogen-activated protein kinase and nuclear factor kappaB activation in tumour-necrosis-factor-alpha-treated immature acute-myeloid-leukaemia cells. Biochem. J. 351: 459-467
    • (2000) Biochem. J. , vol.351 , pp. 459-467
    • Plo, I.1    Lautier, D.2    Levade, T.3
  • 100
    • 0035399943 scopus 로고    scopus 로고
    • TNF-alpha-induced sphingosine 1-phosphate inhibits apoptosis through a phosphatidylinositol 3-kinase/Akt pathway in human hepatocytes
    • Osawa Y, Banno Y, Nagaki M et al. (2001) TNF-alpha-induced sphingosine 1-phosphate inhibits apoptosis through a phosphatidylinositol 3-kinase/Akt pathway in human hepatocytes. J. Immunol. 167: 173-180
    • (2001) J. Immunol. , vol.167 , pp. 173-180
    • Osawa, Y.1    Banno, Y.2    Nagaki, M.3
  • 101
    • 0035844233 scopus 로고    scopus 로고
    • Regulation of nuclear factor kappa B transactivation. Implication of phosphatidylinositol 3-kinase and protein kinase C zeta in c-Rel activation by tumor necrosis factor alpha
    • Martin AG, San Antonio B and Fresno M (2001) Regulation of nuclear factor kappa B transactivation. Implication of phosphatidylinositol 3-kinase and protein kinase C zeta in c-Rel activation by tumor necrosis factor alpha. J. Biol. Chem. 276: 15840-15849
    • (2001) J. Biol. Chem. , vol.276 , pp. 15840-15849
    • Martin, A.G.1    San Antonio, B.2    Fresno, M.3
  • 102
    • 0037192829 scopus 로고    scopus 로고
    • PTEN blocks tumor necrosis factor-induced NF-kappa B-dependent transcription by inhibiting the transactivation potential of the p65 subunit
    • Mayo MW, Madrid LV, Westerheide SD at al. (2002) PTEN blocks tumor necrosis factor-induced NF-kappa B-dependent transcription by inhibiting the transactivation potential of the p65 subunit. J. Biol. Chem. 277: 11116-11125
    • (2002) J. Biol. Chem. , vol.277 , pp. 11116-11125
    • Mayo, M.W.1    Madrid, L.V.2    Westerheide, S.D.3
  • 103
    • 0035920131 scopus 로고    scopus 로고
    • The PTEN tumor suppressor protein inhibits tumor necrosis factor- induced nuclear factor kappa B activity
    • Gustin JA, Maehama T, Dixon JE and Donner DB. (2001) The PTEN tumor suppressor protein inhibits tumor necrosis factor- induced nuclear factor kappa B activity. J. Biol. Chem. 276: 27740-27744
    • (2001) J. Biol. Chem. , vol.276 , pp. 27740-27744
    • Gustin, J.A.1    Maehama, T.2    Dixon, J.E.3    Donner, D.B.4
  • 104
    • 0035379555 scopus 로고    scopus 로고
    • Akt stimulates the transactivation potential of the RelA/p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogen-activated protein kinase p38
    • Madrid LV, Mayo MW, Reuther JY and Baldwin Jr AS (2001) Akt stimulates the transactivation potential of the RelA/p65 Subunit of NF-kappa B through utilization of the Ikappa B kinase and activation of the mitogen-activated protein kinase p38. J. Biol. Chem. 276: 18934-18940
    • (2001) J. Biol. Chem. , vol.276 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin A.S., Jr.4
  • 105
    • 0035835481 scopus 로고    scopus 로고
    • Poly(APD-ribosyl)ation, a DNA damage-driven protein modification and regulator of genomic instability
    • Burkle A (2001) Poly(APD-ribosyl)ation, a DNA damage-driven protein modification and regulator of genomic instability. Cancer Lett. 163: 1-5
    • (2001) Cancer Lett. , vol.163 , pp. 1-5
    • Burkle, A.1
  • 106
    • 0344721492 scopus 로고    scopus 로고
    • Resistance to endotoxic shock as a consequence of defective NF-kappaB activation in poly (ADP-ribose) polymerase-1 deficient mice
    • Oliver FJ, Menissier-de Murcia J, Nacci C at al. (1999) Resistance to endotoxic shock as a consequence of defective NF-kappaB activation in poly (ADP-ribose) polymerase-1 deficient mice. EMBO J. 18: 4446-4454
    • (1999) EMBO J. , vol.18 , pp. 4446-4454
    • Oliver, F.J.1    Menissier-de Murcia, J.2    Nacci, C.3
  • 107
    • 0032863224 scopus 로고    scopus 로고
    • A role of poly (ADP-ribose) polymerase in NF-kappaB transcriptional activation
    • Hasse PO and Hottiger MO (1999) A role of poly (ADP-ribose) polymerase in NF-kappaB transcriptional activation. Biol. Chem. 380: 953-959
    • (1999) Biol. Chem. , vol.380 , pp. 953-959
    • Hasse, P.O.1    Hottiger, M.O.2
  • 108
    • 0035824647 scopus 로고    scopus 로고
    • The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function
    • Hassa PO, Covic M, Hasan S at al. (2001) The enzymatic and DNA binding activity of PARP-1 are not required for NF-kappa B coactivator function. J. Biol. Chem. 276: 45588-45597
    • (2001) J. Biol. Chem. , vol.276 , pp. 45588-45597
    • Hassa, P.O.1    Covic, M.2    Hasan, S.3
  • 109
    • 0035861675 scopus 로고    scopus 로고
    • The sequence-specific DNA binding of NF-kappa B is reversibly regulated by the automodification reaction of poly (ADP-ribose) polymerase 1
    • Chang WJ and Alvarez-Gonzalez R (2001) The sequence-specific DNA binding of NF-kappa B is reversibly regulated by the automodification reaction of poly (ADP-ribose) polymerase 1. J. Biol. Chem. 276: 47664-47670
    • (2001) J. Biol. Chem. , vol.276 , pp. 47664-47670
    • Chang, W.J.1    Alvarez-Gonzalez, R.2
  • 110
    • 0035202873 scopus 로고    scopus 로고
    • Regulation of microglial expression of integrins by poly(ADP-ribose) polymerase-1
    • Ullrich O, Diestel A, Eyupoglu IY, Nitsch R (2001) Regulation of microglial expression of integrins by poly(ADP-ribose) polymerase-1. Nat. Cell Biol. 3: 1035-1042
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1035-1042
    • Ullrich, O.1    Diestel, A.2    Eyupoglu, I.Y.3    Nitsch, R.4
  • 111
    • 0345628001 scopus 로고    scopus 로고
    • Inhibitors of ADP-ribosylation impair inducible nitric oxide synthase gene transcription through inhibition of NF kappa B activation
    • Le Page C, Sanceau J, Drapier JC, Wetzerbin J (1998) Inhibitors of ADP-ribosylation impair inducible nitric oxide synthase gene transcription through inhibition of NF kappa B activation. Biochem. Biophys. Res. Commun. 243: 451-457
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 451-457
    • Le Page, C.1    Sanceau, J.2    Drapier, J.C.3    Wetzerbin, J.4
  • 112
    • 0034654055 scopus 로고    scopus 로고
    • Evidence for regulation of NF-kappaB by poly(ADP-ribose) polymerase
    • Kameoka M, Ota K, Tetsuka T at al. (2000) Evidence for regulation of NF-kappaB by poly(ADP-ribose) polymerase. Biochem. J. 346: 641-649
    • (2000) Biochem. J. , vol.346 , pp. 641-649
    • Kameoka, M.1    Ota, K.2    Tetsuka, T.3
  • 113
    • 0037022627 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 dependence of stress-induced transcription factors and associated gene expression in glia
    • Ha HC, Hester LD, Snyder SH (2002) Poly(ADP-ribose) polymerase-1 dependence of stress-induced transcription factors and associated gene expression in glia. Proc. Natl. Acad. Sci. USA 99: 3270-3275
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3270-3275
    • Ha, H.C.1    Hester, L.D.2    Snyder, S.H.3
  • 114
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation
    • Hoeflich KP, Luo J, Rubie EA at al. (2000) Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation. Nature 406: 86-90
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoeflich, K.P.1    Luo, J.2    Rubie, E.A.3
  • 115
    • 0028351535 scopus 로고
    • TNF induces internalization of the p60 receptor and shedding of the p80 receptor
    • Higuchi M and Aggarwal BB (1994) TNF induces internalization of the p60 receptor and shedding of the p80 receptor. J. Immunol. 152: 3550-3558
    • (1994) J. Immunol. , vol.152 , pp. 3550-3558
    • Higuchi, M.1    Aggarwal, B.B.2
  • 116
    • 0023716003 scopus 로고
    • Endocytic pathway of recombinant murine tumor necrosis factor in L-929 cells
    • Mosselmans R, Hepbum A, Dumont JE at al. (1988) Endocytic pathway of recombinant murine tumor necrosis factor in L-929 cells. J. Immunol. 141: 3096-3100
    • (1988) J. Immunol. , vol.141 , pp. 3096-3100
    • Mosselmans, R.1    Hepbum, A.2    Dumont, J.E.3
  • 117
    • 0033538073 scopus 로고    scopus 로고
    • Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling
    • Schutze S, Machleidt T, Adam D at al. (1999) Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling. J. Biol. Chem. 274: 10203-10212
    • (1999) J. Biol. Chem. , vol.274 , pp. 10203-10212
    • Schutze, S.1    Machleidt, T.2    Adam, D.3
  • 118
    • 0028971291 scopus 로고
    • Constitutive NF-kappa B activation, enhanced granulopoiesis, and neonatal lethality in I kappa B alpha-deficient mice
    • Beg AA, Sha WC, Bronson RT and Baltimore D (1995) Constitutive NF-kappa B activation, enhanced granulopoiesis, and neonatal lethality in I kappa B alpha-deficient mice. Genes Dev. 9: 2736-2746
    • (1995) Genes Dev. , vol.9 , pp. 2736-2746
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Baltimore, D.4
  • 119
    • 0029073035 scopus 로고
    • Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis
    • Sarma V, Lin Z, Clark L at al. (1995) Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis. J. Biol. Chem. 270: 12343-12346
    • (1995) J. Biol. Chem. , vol.270 , pp. 12343-12346
    • Sarma, V.1    Lin, Z.2    Clark, L.3
  • 120
    • 0000564581 scopus 로고    scopus 로고
    • The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation
    • Song HY, Rothe M and Goeddel DV (1996) The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation. Proc. Natl. Acad. Sci. USA 93: 6721-6725
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6721-6725
    • Song, H.Y.1    Rothe, M.2    Goeddel, D.V.3
  • 121
    • 0034730713 scopus 로고    scopus 로고
    • Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice
    • Lee EG, Boone DL, Chai S at al. (2000) Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. Science 289: 2350-2354
    • (2000) Science , vol.289 , pp. 2350-2354
    • Lee, E.G.1    Boone, D.L.2    Chai, S.3
  • 122
    • 0035929684 scopus 로고    scopus 로고
    • A20 inhibits NF-kappa B activation downstream of multiple Map3 kinases and interacts with the I kappa B signalosome
    • Zetoune FS, Murthy AR, Shao Z at al. (2001) A20 inhibits NF-kappa B activation downstream of multiple Map3 kinases and interacts with the I kappa B signalosome. Cytokine 15: 282-298
    • (2001) Cytokine , vol.15 , pp. 282-298
    • Zetoune, F.S.1    Murthy, A.R.2    Shao, Z.3
  • 123
    • 0033612571 scopus 로고    scopus 로고
    • The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN
    • Heyninck K, De Valck D, Vanden Berghe W at al. (1999) The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN. J. Cell Biol. 145: 1471-1482
    • (1999) J. Cell Biol. , vol.145 , pp. 1471-1482
    • Heyninck, K.1    De Valck, D.2    Vanden Berghe, W.3
  • 124
    • 0030026698 scopus 로고    scopus 로고
    • A20 zinc finger protein inhibits TNF and IL1 signaling
    • Jaattela M, Mouritzen H, Elling F and Bastholm L (1996) A20 zinc finger protein inhibits TNF and IL1 signaling. J. Immunol. 156: 1166-1173
    • (1996) J. Immunol. , vol.156 , pp. 1166-1173
    • Jaattela, M.1    Mouritzen, H.2    Elling, F.3    Bastholm, L.4
  • 125
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation
    • Delhase M, Hayakawa M, Chen Y and Karin M (1999) Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation. Science 284: 309-313
    • (1999) Science , vol.284 , pp. 309-313
    • Delhase, M.1    Hayakawa, M.2    Chen, Y.3    Karin, M.4
  • 126
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian E and Karin M (2002) AP-1 as a regulator of cell life and death. Nat. Cell Biol. 4: 131-136
    • (2002) Nat. Cell Biol. , vol.4 , pp. 131-136
    • Shaulian, E.1    Karin, M.2
  • 127
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L and Karin M (2001) Mammalian MAP kinase signalling cascades. Nature 410: 37-40
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 128
    • 0024503589 scopus 로고
    • Prolonged activation of jun and collagenase genes by tumour necrosis factor-alpha
    • Brenner DA, O'Hara M, Angel P at al. (1989) Prolonged activation of jun and collagenase genes by tumour necrosis factor-alpha. Nature 337: 661-663
    • (1989) Nature , vol.337 , pp. 661-663
    • Brenner, D.A.1    O'Hara, M.2    Angel, P.3
  • 129
    • 0027157651 scopus 로고
    • Tumor necrosis factor-alpha induces expression of monocyte chemoattractant JE via fos and jun genes in clonal osteoblastic MC3T3-E1 cells
    • Hanazawa S, Takeshita A, Amano S at al. (1993) Tumor necrosis factor-alpha induces expression of monocyte chemoattractant JE via fos and jun genes in clonal osteoblastic MC3T3-E1 cells. J. Biol. Chem. 268: 9526-9532
    • (1993) J. Biol. Chem. , vol.268 , pp. 9526-9532
    • Hanazawa, S.1    Takeshita, A.2    Amano, S.3
  • 130
    • 0031252641 scopus 로고    scopus 로고
    • TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappa B and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways
    • Min W and Pober JS (1997) TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappa B and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways. J. Immunol. 159: 3508-3518
    • (1997) J. Immunol. , vol.159 , pp. 3508-3518
    • Min, W.1    Pober, J.S.2
  • 131
    • 0028518860 scopus 로고
    • Tumor necrosis factor-alpha induces c-jun during the regenerative response to liver injury
    • Diehl AM, Yin M, Fleckenstein J at al. (1994) Tumor necrosis factor-alpha induces c-jun during the regenerative response to liver injury. Am. J. Physiol. 267: G552-G561
    • (1994) Am. J. Physiol. , vol.267
    • Diehl, A.M.1    Yin, M.2    Fleckenstein, J.3
  • 132
    • 0031030599 scopus 로고    scopus 로고
    • Induction of early-immediate genes by tumor necrosis factor alpha contribute to liver repair following chemical-induced hepatotoxicity
    • Bruccoleri A, Gallucci R, Germolec DR at al. (1997) Induction of early-immediate genes by tumor necrosis factor alpha contribute to liver repair following chemical-induced hepatotoxicity. Hepatology 25: 133-141
    • (1997) Hepatology , vol.25 , pp. 133-141
    • Bruccoleri, A.1    Gallucci, R.2    Germolec, D.R.3
  • 133
    • 0031048067 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-induced activation of c-jun N-terminal kinase is mediated by TRAF2
    • Reinhard C, Shamoon B, Shyamala V and Williams LT (1997) Tumor necrosis factor alpha-induced activation of c-jun N-terminal kinase is mediated by TRAF2. EMBO J. 16: 1080-1092
    • (1997) EMBO J. , vol.16 , pp. 1080-1092
    • Reinhard, C.1    Shamoon, B.2    Shyamala, V.3    Williams, L.T.4
  • 134
    • 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 at al. (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
  • 135
    • 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 ZG, Hsu H, Goeddell DV, 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: 565-576
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddell, D.V.3    Karin, M.4
  • 136
    • 12644272789 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated kinase cascades: Bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2
    • Song HY, Regnier CH, Kirschning CJ at al. (1997) Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. Proc. Natl. Acad. Sci. USA 94: 9792-9796
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9792-9796
    • Song, H.Y.1    Regnier, C.H.2    Kirschning, C.J.3
  • 137
    • 0008206988 scopus 로고    scopus 로고
    • TRAF2 is essential for JNK but not NF-kappaB activation and regulates lymphocyte proliferation and survival
    • Lee SY, Reichlin A, Santana A at al. (1997) TRAF2 is essential for JNK but not NF-kappaB activation and regulates lymphocyte proliferation and survival. Immunity 7: 703-713
    • (1997) Immunity , vol.7 , pp. 703-713
    • Lee, S.Y.1    Reichlin, A.2    Santana, A.3
  • 138
    • 0031463025 scopus 로고    scopus 로고
    • Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice
    • Yeh WC, Shahinian A, Speiser D at al. (1997) Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity 7: 715-725
    • (1997) Immunity , vol.7 , pp. 715-725
    • Yeh, W.C.1    Shahinian, A.2    Speiser, D.3
  • 139
    • 0034992168 scopus 로고    scopus 로고
    • MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines
    • Tournier C, Dong C, Turner TK et al. (2001) MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines. Genes Dev. 15: 1419-1426
    • (2001) Genes Dev. , vol.15 , pp. 1419-1426
    • Tournier, C.1    Dong, C.2    Turner, T.K.3
  • 140
    • 0032585615 scopus 로고    scopus 로고
    • Synergistic activation of SAPK1/JNK1 by two MAP kinase kinases in vitro
    • Lawler S, Fleming Y, Goedert M and Cohen P (1998) Synergistic activation of SAPK1/JNK1 by two MAP kinase kinases in vitro. Curr. Biol. 8: 1387-1390
    • (1998) Curr. Biol. , vol.8 , pp. 1387-1390
    • Lawler, S.1    Fleming, Y.2    Goedert, M.3    Cohen, P.4
  • 141
    • 0030702895 scopus 로고    scopus 로고
    • A novel SAPK/JNK kinase, MKK7, stimulated by TNFalpha and cellular stresses
    • Moriguchi T, Toyoshima F, Masuyama N at al. (1997) A novel SAPK/JNK kinase, MKK7, stimulated by TNFalpha and cellular stresses. EMBO J. 16: 7045-7053
    • (1997) EMBO J. , vol.16 , pp. 7045-7053
    • Moriguchi, T.1    Toyoshima, F.2    Masuyama, N.3
  • 142
    • 0032158987 scopus 로고    scopus 로고
    • ASK1 is essential for JNK/SAPK activation by TRAF2
    • Nishitoh H, Saitoh M, Mochida Y et al. (1998) ASK1 is essential for JNK/SAPK activation by TRAF2. Mol. Cell 2: 389-395
    • (1998) Mol. Cell , vol.2 , pp. 389-395
    • Nishitoh, H.1    Saitoh, M.2    Mochida, Y.3
  • 143
    • 0033554554 scopus 로고    scopus 로고
    • Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)
    • Hoeflich KP, Yeh WC, Yao Z at al. (1999) Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1). Oncogene 18: 5814-5820
    • (1999) Oncogene , vol.18 , pp. 5814-5820
    • Hoeflich, K.P.1    Yeh, W.C.2    Yao, Z.3
  • 144
    • 0035065836 scopus 로고    scopus 로고
    • ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
    • Tobiume K, Matsuzawa A, Takahashi T at al. (2001). ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis. EMBO Rep. 2: 222-228
    • (2001) EMBO Rep. , vol.2 , pp. 222-228
    • Tobiume, K.1    Matsuzawa, A.2    Takahashi, T.3
  • 145
    • 0033605292 scopus 로고    scopus 로고
    • Signaling by the germinal center kinase family of protein kinases
    • Kyriakis JM (1999) Signaling by the germinal center kinase family of protein kinases. J. Biol. Chem. 274: 5259-5262
    • (1999) J. Biol. Chem. , vol.274 , pp. 5259-5262
    • Kyriakis, J.M.1
  • 146
    • 0032575591 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38. Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/ERK kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38
    • Yuasa T, Ohno S, Kehrl JH and Kyriakis JM (1998) Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38. Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/ERK kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38. J. Biol. Chem. 273: 22681-22692
    • (1998) J. Biol. Chem. , vol.273 , pp. 22681-22692
    • Yuasa, T.1    Ohno, S.2    Kehrl, J.H.3    Kyriakis, J.M.4
  • 147
    • 12644257580 scopus 로고    scopus 로고
    • Activation of the c-Jun N-terminal kinase pathway by a novel protein kinase related to human germinal center kinase
    • Diener K, Wang XS, Chen C at al. (1997) Activation of the c-Jun N-terminal kinase pathway by a novel protein kinase related to human germinal center kinase. Proc. Natl. Acad. Sci. USA 94: 9687-9692
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9687-9692
    • Diener, K.1    Wang, X.S.2    Chen, C.3
  • 148
    • 0031437885 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase/c-Jun N-terminal kinase, but not NF-kappaB, by the tumor necrosis factor (TNF) receptor 1 through a TNF receptor-associated factor 2- and germinal center kinase related-dependent pathway
    • Shi CS and Kehrl JH (1997) Activation of stress-activated protein kinase/c-Jun N-terminal kinase, but not NF-kappaB, by the tumor necrosis factor (TNF) receptor 1 through a TNF receptor-associated factor 2- and germinal center kinase related-dependent pathway. J. Biol. Chem. 272: 32102-32107
    • (1997) J. Biol. Chem. , vol.272 , pp. 32102-32107
    • Shi, C.S.1    Kehrl, J.H.2
  • 149
    • 0033593470 scopus 로고    scopus 로고
    • A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway
    • Yao Z, Zhou G, Wang XS et al. (1999) A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway. J. Biol. Chem. 274: 2118-2125
    • (1999) J. Biol. Chem. , vol.274 , pp. 2118-2125
    • Yao, Z.1    Zhou, G.2    Wang, X.S.3
  • 150
    • 0034617070 scopus 로고    scopus 로고
    • NESK, a member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and is expressed during the late stages of embryogenesis
    • Nakano K, Yamauchi J, Nakagawa K et al. (2000) NESK, a member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and is expressed during the late stages of embryogenesis. J. Biol. Chem. 275: 20553-20559
    • (2000) J. Biol. Chem. , vol.275 , pp. 20553-20559
    • Nakano, K.1    Yamauchi, J.2    Nakagawa, K.3
  • 151
    • 0032697488 scopus 로고    scopus 로고
    • TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton
    • Fu CA, Shen M, Huang BC et al. (1999) TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton. J. Biol. Chem. 274: 30729-30737
    • (1999) J. Biol. Chem. , vol.274 , pp. 30729-30737
    • Fu, C.A.1    Shen, M.2    Huang, B.C.3
  • 152
    • 0033568595 scopus 로고    scopus 로고
    • TNF-mediated activation of the stress-activated protein kinase pathway: TNF receptor-associated factor 2 recruits and activates germinal center kinase related
    • Shi CS, Leonardi A, Kyriakis J et al. (1999) TNF-mediated activation of the stress-activated protein kinase pathway: TNF receptor-associated factor 2 recruits and activates germinal center kinase related. J. Immunol. 163: 3279-3285
    • (1999) J. Immunol. , vol.163 , pp. 3279-3285
    • Shi, C.S.1    Leonardi, A.2    Kyriakis, J.3
  • 153
    • 0036143713 scopus 로고    scopus 로고
    • Direct activation of mitogen-activated protein kinase kinase kinase MEKK1 by the Ste20p homologue GCK and the adapter protein TRAF2
    • Chadee DN, Yuasa T and Kyriakis JM (2002) Direct activation of mitogen-activated protein kinase kinase kinase MEKK1 by the Ste20p homologue GCK and the adapter protein TRAF2. Mol. Cell Biol. 22: 737-749
    • (2002) Mol. Cell Biol. , vol.22 , pp. 737-749
    • Chadee, D.N.1    Yuasa, T.2    Kyriakis, J.M.3
  • 154
    • 14444281569 scopus 로고    scopus 로고
    • Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways
    • Ichijo H, Nishida E, Irie K et al. (1997) Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 275: 90-94
    • (1997) Science , vol.275 , pp. 90-94
    • Ichijo, H.1    Nishida, E.2    Irie, K.3
  • 155
    • 0035900676 scopus 로고    scopus 로고
    • Reactive oxygen species are downstream products of TRAF-mediated signal transduction
    • Chandel NS, Schumacker PT and Arch RH (2001) Reactive oxygen species are downstream products of TRAF-mediated signal transduction. J. Biol. Chem. 276: 42728-42736
    • (2001) J. Biol. Chem. , vol.276 , pp. 42728-42736
    • Chandel, N.S.1    Schumacker, P.T.2    Arch, R.H.3
  • 156
    • 0032504189 scopus 로고    scopus 로고
    • Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction
    • Gotoh Y and Cooper JA (1998) Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction. J. Biol. Chem. 273: 17477-17482
    • (1998) J. Biol. Chem. , vol.273 , pp. 17477-17482
    • Gotoh, Y.1    Cooper, J.A.2
  • 157
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M, Nishitoh H, Fujii M et al. (1998) Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 17: 2596-2606
    • (1998) EMBO J. , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3
  • 158
    • 0025887488 scopus 로고
    • Protective activity of adult T cell leukemia-derived factor (ADF) against tumor necrosis factor-dependent cytotoxicity on U937 cells
    • Matsuda M, Masutani H, Nakamura H et al. (1991) Protective activity of adult T cell leukemia-derived factor (ADF) against tumor necrosis factor-dependent cytotoxicity on U937 cells. J. Immunol. 147: 3837-3841
    • (1991) J. Immunol. , vol.147 , pp. 3837-3841
    • Matsuda, M.1    Masutani, H.2    Nakamura, H.3
  • 159
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H, Nishitoh H, Ichijo H and Kyriakis JM (2000) Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol. Cell Biol. 20: 2198-2208
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 160
    • 0032571569 scopus 로고    scopus 로고
    • TRAF2 plays a dual role in NF-kappaB-dependent gene activation by mediating the TNF-induced activation of p38 MAPK and IkappaB kinase pathways
    • Carpentier I, Declercq W, Malinin NL et al. (1998) TRAF2 plays a dual role in NF-kappaB-dependent gene activation by mediating the TNF-induced activation of p38 MAPK and IkappaB kinase pathways. FEBS Lett. 425: 195-198
    • (1998) FEBS Lett. , vol.425 , pp. 195-198
    • Carpentier, I.1    Declercq, W.2    Malinin, N.L.3
  • 161
    • 0028845253 scopus 로고
    • Activation of the SAPK pathway by the human STE20 homologue germinal centre kinase
    • Pombo CM, Kehrl JH, Sanchez I et al. (1995) Activation of the SAPK pathway by the human STE20 homologue germinal centre kinase. Nature 377: 750-754
    • (1995) Nature , vol.377 , pp. 750-754
    • Pombo, C.M.1    Kehrl, J.H.2    Sanchez, I.3
  • 162
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-kappaB signal
    • Kelliher MA, Grimm S, Ishida Y et al. (1998) The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity 8: 297-303
    • (1998) Immunity , vol.8 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3
  • 163
    • 0033616588 scopus 로고    scopus 로고
    • Requirement of mitogen-activated protein kinase kinase 3 (MKK3) for tumor necrosis factor-induced cytokine expression
    • Wysk M, Yang DD, Lu HT et al. (1999) Requirement of mitogen-activated protein kinase kinase 3 (MKK3) for tumor necrosis factor-induced cytokine expression. Proc. Natl. Acad. Sci. USA 96: 3763-3768
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3763-3768
    • Wysk, M.1    Yang, D.D.2    Lu, H.T.3
  • 164
    • 0342758711 scopus 로고    scopus 로고
    • p38 MAPK signalling cascades: Ancient roles and new functions
    • Martin-Blanco E (2000) p38 MAPK signalling cascades: ancient roles and new functions. Bioessays 22: 637-645
    • (2000) Bioessays , vol.22 , pp. 637-645
    • Martin-Blanco, E.1
  • 165
    • 0033568608 scopus 로고    scopus 로고
    • The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism
    • Winzen R, Kracht M, Ritter B et al. (1999) The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism. EMBO J. 18: 4969-4980
    • (1999) EMBO J. , vol.18 , pp. 4969-4980
    • Winzen, R.1    Kracht, M.2    Ritter, B.3
  • 166
    • 0032544234 scopus 로고    scopus 로고
    • Regulation of interleukin 1beta-induced interleukin-6 gene expression in human fibroblast-like synoviocytes by p38 mitogen-activated protein kinase
    • Miyazawa K, Mori A, Miyata H et al. (1998) Regulation of interleukin 1beta-induced interleukin-6 gene expression in human fibroblast-like synoviocytes by p38 mitogen-activated protein kinase. J. Biol. Chem. 273: 24832-24838
    • (1998) J. Biol. Chem. , vol.273 , pp. 24832-24838
    • Miyazawa, K.1    Mori, A.2    Miyata, H.3
  • 167
    • 0032488837 scopus 로고    scopus 로고
    • p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-kappaB p65 transactivation mediated by tumor necrosis factor
    • Vanden Berghe W, Plaisance S, Boone E et al. (1998) p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-kappaB p65 transactivation mediated by tumor necrosis factor. J. Biol. Chem. 273: 3285-3290
    • (1998) J. Biol. Chem. , vol.273 , pp. 3285-3290
    • Vanden Berghe, W.1    Plaisance, S.2    Boone, E.3
  • 168
    • 0029983730 scopus 로고    scopus 로고
    • The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor
    • Beyaert R, Cuenda A, Vanden Berghe W et al. (1996) The p38/RK mitogen-activated protein kinase pathway regulates interleukin-6 synthesis response to tumor necrosis factor. EMBO J. 15: 1914-1923
    • (1996) EMBO J. , vol.15 , pp. 1914-1923
    • Beyaert, R.1    Cuenda, A.2    Vanden Berghe, W.3
  • 169
    • 0030595340 scopus 로고    scopus 로고
    • FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase
    • Adam-Klages S, Adam D, Wiegmann K et al. (1996) FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase. Cell 86: 937-947
    • (1996) Cell , vol.86 , pp. 937-947
    • Adam-Klages, S.1    Adam, D.2    Wiegmann, K.3
  • 170
    • 0033522399 scopus 로고    scopus 로고
    • Impaired neutral sphingomyelinase activation and cutaneous barrier repair in FAN-deficient mice
    • Kreder D, Krut O, Adam-Klages S et al. (1999) Impaired neutral sphingomyelinase activation and cutaneous barrier repair in FAN-deficient mice. EMBO J. 18: 2472-2479
    • (1999) EMBO J. , vol.18 , pp. 2472-2479
    • Kreder, D.1    Krut, O.2    Adam-Klages, S.3
  • 171
    • 0032553310 scopus 로고    scopus 로고
    • Tumor necrosis factor induces ceramide oscillations and negatively controls sphingolipid synthases by caspases in apoptotic Kym-1 cells
    • Bourteele S, Hausser A, Doppler H et al. (1998) Tumor necrosis factor induces ceramide oscillations and negatively controls sphingolipid synthases by caspases in apoptotic Kym-1 cells. J. Biol. Chem. 273: 31245-31251
    • (1998) J. Biol. Chem. , vol.273 , pp. 31245-31251
    • Bourteele, S.1    Hausser, A.2    Doppler, H.3
  • 172
  • 173
    • 0034596278 scopus 로고    scopus 로고
    • Activation of ERK1/2 and cPLA(2) by the p55 TNF receptor occurs independently of FAN
    • Luschen S, Adam D, Ussat S et al. (2000) Activation of ERK1/2 and cPLA(2) by the p55 TNF receptor occurs independently of FAN. Biochem. Biophys. Res. Commun. 274: 506-512
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 506-512
    • Luschen, S.1    Adam, D.2    Ussat, S.3
  • 174
    • 0029038912 scopus 로고
    • A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'
    • Boldin MP, Mett IL, Wallach D (1995) A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'. FEBS Lett. 367: 39-44
    • (1995) FEBS Lett. , vol.367 , pp. 39-44
    • Boldin, M.P.1    Mett, I.L.2    Wallach, D.3
  • 175
    • 8944258100 scopus 로고    scopus 로고
    • cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11
    • Tsurumi C, Shimizu Y, Seeki M et al. (1996) cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11. Eur. J. Biochem. 239: 912-921
    • (1996) Eur. J. Biochem. , vol.239 , pp. 912-921
    • Tsurumi, C.1    Shimizu, Y.2    Seeki, M.3
  • 176
    • 0031135534 scopus 로고    scopus 로고
    • Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: Identity with subunit 2 of the 26S protease
    • Dunbar JD, Song HY, Guo D et al. (1997) Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: identity with subunit 2 of the 26S protease. J. Immunol. 158: 4252-4259
    • (1997) J. Immunol. , vol.158 , pp. 4252-4259
    • Dunbar, J.D.1    Song, H.Y.2    Guo, D.3
  • 177
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song HY, Dunbar JD, Zhang YX et al. (1995) Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 270: 3574-3581
    • (1995) J. Biol. Chem. , vol.270 , pp. 3574-3581
    • Song, H.Y.1    Dunbar, J.D.2    Zhang, Y.X.3
  • 178
    • 0034603178 scopus 로고    scopus 로고
    • The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties
    • Felts SJ, Owen BA, Nguyen P et al. (2000) The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 275: 3305-3312
    • (2000) J. Biol. Chem. , vol.275 , pp. 3305-3312
    • Felts, S.J.1    Owen, B.A.2    Nguyen, P.3
  • 179
    • 0027076644 scopus 로고
    • Tumor necrosis factor stimulates multiple serine/threonine protein kinases in Swiss 3T3 and L929 cells. Implication of casein kinase-2 and extracellular signal-regulated kinases in the tumor necrosis factor signal transduction pathway
    • Van Lint J, Agostinis P, Vandevoorde V et al. (1992) Tumor necrosis factor stimulates multiple serine/threonine protein kinases in Swiss 3T3 and L929 cells. Implication of casein kinase-2 and extracellular signal-regulated kinases in the tumor necrosis factor signal transduction pathway. J. Biol. Chem. 267: 25916-25921
    • (1992) J. Biol. Chem. , vol.267 , pp. 25916-25921
    • Van Lint, J.1    Agostinis, P.2    Vandevoorde, V.3
  • 180
    • 0027209271 scopus 로고
    • Tumor necrosis factor-induced activation and increased tyrosine phosphorylation of mitogen-activated protein (MAP) kinase in human fibroblasts
    • Vietor I, Schwenger P, Li W et al. (1993) Tumor necrosis factor-induced activation and increased tyrosine phosphorylation of mitogen-activated protein (MAP) kinase in human fibroblasts. J. Biol. Chem. 268: 18994-18999
    • (1993) J. Biol. Chem. , vol.268 , pp. 18994-18999
    • Vietor, I.1    Schwenger, P.2    Li, W.3
  • 181
    • 0040885889 scopus 로고    scopus 로고
    • Regulation of Raf-1 kinase by TNF via its second messenger ceramide and cross-talk with mitogenic signalling
    • Muller G, Storz P, Bourteele S et al. (1998) Regulation of Raf-1 kinase by TNF via its second messenger ceramide and cross-talk with mitogenic signalling. EMBO J. 17: 732-742
    • (1998) EMBO J. , vol.17 , pp. 732-742
    • Muller, G.1    Storz, P.2    Bourteele, S.3
  • 182
    • 0035504199 scopus 로고    scopus 로고
    • Type II tumour necrosis factor-alpha receptor (TNFR2) activates c-Jun N- terminal kinase (JNK) but not mitogen-activated protein kinase (MAPK) or p38 MAPK pathways
    • Jupp OJ, McFarlane SM, Anderson HM et al. (2001) Type II tumour necrosis factor-alpha receptor (TNFR2) activates c-Jun N- terminal kinase (JNK) but not mitogen-activated protein kinase (MAPK) or p38 MAPK pathways. Biochem. J. 359: 525-535
    • (2001) Biochem. J. , vol.359 , pp. 525-535
    • Jupp, O.J.1    McFarlane, S.M.2    Anderson, H.M.3
  • 183
    • 0030910313 scopus 로고    scopus 로고
    • MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase
    • Schievella AR, Chen JH, Graham JR and Lin LL (1997) MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase. J. Biol. Chem. 272: 12069-12075
    • (1997) J. Biol. Chem. , vol.272 , pp. 12069-12075
    • Schievella, A.R.1    Chen, J.H.2    Graham, J.R.3    Lin, L.L.4
  • 184
    • 0032510222 scopus 로고    scopus 로고
    • MADD is highly homologous to a Rab3 guanine-nucleotide exchange protein (Rab3-GEP)
    • Brown TL and Howe PH (1998) MADD is highly homologous to a Rab3 guanine-nucleotide exchange protein (Rab3-GEP). Curr. Biol. 8: R191
    • (1998) Curr. Biol. , vol.8
    • Brown, T.L.1    Howe, P.H.2
  • 185
    • 0030498642 scopus 로고    scopus 로고
    • DENN, a novel human gene differentially expressed in normal and neoplastic cells
    • Chow VT and Lee SS (1996) DENN, a novel human gene differentially expressed in normal and neoplastic cells. DNA Seq. 6: 263-273
    • (1996) DNA Seq. , vol.6 , pp. 263-273
    • Chow, V.T.1    Lee, S.S.2
  • 186
    • 0033532626 scopus 로고    scopus 로고
    • Identification of Grb2 as a novel binding partner of tumor necrosis factor (TNF) receptor I
    • Hildt E and Oess S (1999) Identification of Grb2 as a novel binding partner of tumor necrosis factor (TNF) receptor I. J. Exp. Med., 189: 1707-1714
    • (1999) J. Exp. Med. , vol.189 , pp. 1707-1714
    • Hildt, E.1    Oess, S.2
  • 187
    • 0028838235 scopus 로고
    • Phosphorylation of Raf by ceramide-activated protein kinase
    • Yao B, Zhang Y, Delikat S et al. (1995) Phosphorylation of Raf by ceramide-activated protein kinase. Nature 378: 307-310
    • (1995) Nature , vol.378 , pp. 307-310
    • Yao, B.1    Zhang, Y.2    Delikat, S.3
  • 188
    • 0035965998 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha supports the survival of osteoclasts through the activation of Akt and ERK
    • Lee SE, Chung WJ, Kwak HB et al. (2001) Tumor necrosis factor-alpha supports the survival of osteoclasts through the activation of Akt and ERK. J. Biol. Chem. 276: 49343-49349
    • (2001) J. Biol. Chem. , vol.276 , pp. 49343-49349
    • Lee, S.E.1    Chung, W.J.2    Kwak, H.B.3
  • 189
    • 0035940129 scopus 로고    scopus 로고
    • The pathogenesis of vasodilatory shock
    • Landry DW and Oliver JA (2001) The pathogenesis of vasodilatory shock. N. Engl. J. Med. 345: 588-595
    • (2001) N. Engl. J. Med. , vol.345 , pp. 588-595
    • Landry, D.W.1    Oliver, J.A.2
  • 190
    • 0034637585 scopus 로고    scopus 로고
    • Inhibition of death receptor-mediated gene induction by a cycloheximide- sensitive factor occurs at the level of or upstream of Fas-associated death domain protein (FADD)
    • Wajant H, Haas E, Schwenzer R et al. (2000) Inhibition of death receptor-mediated gene induction by a cycloheximide- sensitive factor occurs at the level of or upstream of Fas-associated death domain protein (FADD). J. Biol. Chem. 275: 24357-24366
    • (2000) J. Biol. Chem. , vol.275 , pp. 24357-24366
    • Wajant, H.1    Haas, E.2    Schwenzer, R.3
  • 191
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally
    • Varfolomeev EE, Schuchmann M, Luria V et al. (1998) Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 9: 267-276
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3
  • 192
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I, Xu CJ, Juo P et al. (1999) Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22: 623-633
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3
  • 193
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • Zhang J, Cado D, Chen A et al. (1998) Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 392: 296-300
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3
  • 194
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Yeh WC, Pompa JL, McCurrach ME et al. (1998) FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science 279: 1954-1958
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    Pompa, J.L.2    McCurrach, M.E.3
  • 195
    • 0033662433 scopus 로고    scopus 로고
    • Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5
    • Kischkel FC, Lawrence DA, Chuntharapai A et al. (2000) Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity 12: 611-620
    • (2000) Immunity , vol.12 , pp. 611-620
    • Kischkel, F.C.1    Lawrence, D.A.2    Chuntharapai, A.3
  • 196
    • 0033667778 scopus 로고    scopus 로고
    • FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2 1669
    • Sprick MR, Weigand MA, Rieser E et al. (2000) FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2 1669. Immunity 12: 599-609
    • (2000) Immunity , vol.12 , pp. 599-609
    • Sprick, M.R.1    Weigand, M.A.2    Rieser, E.3
  • 197
    • 0033790715 scopus 로고    scopus 로고
    • TRAIL receptor-2 signals apoptosis through FADD and caspase-8
    • Bodmer JL, Holler N, Reynard S et al. (2000) TRAIL receptor-2 signals apoptosis through FADD and caspase-8. Nat. Cell Biol. 2: 241-243
    • (2000) Nat. Cell Biol. , vol.2 , pp. 241-243
    • Bodmer, J.L.1    Holler, N.2    Reynard, S.3
  • 198
    • 0033428024 scopus 로고    scopus 로고
    • FADD is required for multiple signaling events downstream of the receptor Fas
    • Juo P, Woo MS, Kuo CJ et al. (1999) FADD is required for multiple signaling events downstream of the receptor Fas. Cell Growth Differ. 10: 797-804
    • (1999) Cell Growth Differ. , vol.10 , pp. 797-804
    • Juo, P.1    Woo, M.S.2    Kuo, C.J.3
  • 199
    • 0032505127 scopus 로고    scopus 로고
    • Essential requirement for caspase-8/FLICE in the initiation of the Fas- induced apoptotic cascade
    • Juo P, Kuo CJ, Yuan J and Blenis J (1998) Essential requirement for caspase-8/FLICE in the initiation of the Fas- induced apoptotic cascade. Curr. Biol. 8: 1001-1008
    • (1998) Curr. Biol. , vol.8 , pp. 1001-1008
    • Juo, P.1    Kuo, C.J.2    Yuan, J.3    Blenis, J.4
  • 200
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke K, Tewari M, and Dixit VM (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
  • 201
    • 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 MP, Goncharov TM, Goltsev YV 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
  • 202
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M, Chinnaiyan AM, Kischkel FC et al. (1996) FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85: 817-827
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 203
    • 0036133127 scopus 로고    scopus 로고
    • Molecular ordering of the initial signaling events of CD95
    • Algeciras-Schimnich A, Shen L, Barnhart BC et al. (2002) Molecular ordering of the initial signaling events of CD95. Mol. Cell Biol. 22: 207-220
    • (2002) Mol. Cell Biol. , vol.22 , pp. 207-220
    • Algeciras-Schimnich, A.1    Shen, L.2    Barnhart, B.C.3
  • 204
    • 0031092638 scopus 로고    scopus 로고
    • Enhancement of TNF receptor p60-mediated cytotoxicity by TNF receptor p80: Requirement of the TNF receptor-associated factor-2 binding site
    • Weiss T, Grell M, Hessabi B et al. (1997) Enhancement of TNF receptor p60-mediated cytotoxicity by TNF receptor p80: requirement of the TNF receptor-associated factor-2 binding site. J. Immunol. 158: 2398-2404
    • (1997) J. Immunol. , vol.158 , pp. 2398-2404
    • Weiss, T.1    Grell, M.2    Hessabi, B.3
  • 205
    • 0032530378 scopus 로고    scopus 로고
    • TNFR80-dependent enhancement of TNFR60-induced cell death is mediated by TNFR-associated factor 2 and is specific for TNFR60
    • Weiss T, Grell M, Siemienski K et al. (1998) TNFR80-dependent enhancement of TNFR60-induced cell death is mediated by TNFR-associated factor 2 and is specific for TNFR60. J. Immunol. 161: 3136-3142
    • (1998) J. Immunol. , vol.161 , pp. 3136-3142
    • Weiss, T.1    Grell, M.2    Siemienski, K.3
  • 206
    • 0030828690 scopus 로고    scopus 로고
    • CD30-dependent degradation of TRAF2: Implications for negative regulation of TRAF signaling and the control of cell survival
    • Duckett CS and Thompson CB (1997) CD30-dependent degradation of TRAF2: implications for negative regulation of TRAF signaling and the control of cell survival. Genes Dev. 11: 2810-2821
    • (1997) Genes Dev. , vol.11 , pp. 2810-2821
    • Duckett, C.S.1    Thompson, C.B.2
  • 207
    • 0037149542 scopus 로고    scopus 로고
    • TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2
    • Li X, Yang Y and Ashwell JD (2002) TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. Nature 416: 345-347
    • (2002) Nature , vol.416 , pp. 345-347
    • Li, X.1    Yang, Y.2    Ashwell, J.D.3
  • 208
    • 0033965946 scopus 로고    scopus 로고
    • A crucial role for p80 TNF-R2 in amplifying p60 TNF-R1 apoptosis signals in T lymphocytes
    • Chan FK and Lenardo MJ (2000) A crucial role for p80 TNF-R2 in amplifying p60 TNF-R1 apoptosis signals in T lymphocytes. Eur. J. Immunol. 30: 652-660
    • (2000) Eur. J. Immunol. , vol.30 , pp. 652-660
    • Chan, F.K.1    Lenardo, M.J.2
  • 209
    • 0037205442 scopus 로고    scopus 로고
    • Regulation of TRAF2 signaling by self-induced degradation
    • Brown KD, Hostager BS and Bishop GA (2002) Regulation of TRAF2 signaling by self-induced degradation. J. Biol. Chem. 277: 19433-19438
    • (2002) J. Biol. Chem. , vol.277 , pp. 19433-19438
    • Brown, K.D.1    Hostager, B.S.2    Bishop, G.A.3
  • 210
    • 0036629347 scopus 로고    scopus 로고
    • Apoptotic crosstalk of TNF receptors: TNF-R2-induces depletion of TRAF2 and IAP proteins and accelerates TNF-R1-dependent activation of caspase-8
    • Fotin-Mleczek M, Henkler F, Samel D et al. (2002) Apoptotic crosstalk of TNF receptors: TNF-R2-induces depletion of TRAF2 and IAP proteins and accelerates TNF-R1-dependent activation of caspase-8. J. Cell Sci. 115: 2757-2770
    • (2002) J. Cell Sci. , vol.115 , pp. 2757-2770
    • Fotin-Mleczek, M.1    Henkler, F.2    Samel, D.3
  • 211
    • 0030447483 scopus 로고    scopus 로고
    • The tumor necrosis factor receptor 2 signal transducers TRAF2 and c- IAP1 are components of the tumor necrosis factor receptor 1 signaling complex
    • Shu HB, Takeuchi M and Goeddel DV (1996) The tumor necrosis factor receptor 2 signal transducers TRAF2 and c- IAP1 are components of the tumor necrosis factor receptor 1 signaling complex. Proc. Natl. Acad. Sci. USA 93: 13973-13978
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13973-13978
    • Shu, H.B.1    Takeuchi, M.2    Goeddel, D.V.3
  • 212
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan MG, Henzel WJ et al. (1995) The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral 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
  • 213
    • 0035092810 scopus 로고    scopus 로고
    • Baculoviruses and apoptosis: The good, the bad, and the ugly
    • Clem RJ (2001) Baculoviruses and apoptosis: the good, the bad, and the ugly. Cell Death Differ. 8: 137-143
    • (2001) Cell Death Differ. , vol.8 , pp. 137-143
    • Clem, R.J.1
  • 214
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N, Deveraux QL, Takahashi R et al. (1997) The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 16: 6914-6925
    • (1997) EMBO J. , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3
  • 215
    • 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 et al. (1998) NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 281: 1680-1683
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3
  • 216
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang Y, Fang S, Jensen JP et al. (2000) Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288: 874-877
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3
  • 217
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro ubiquitination of caspases-3 and -7
    • Huang H, Joazeiro CA, Bonfoco E et al. (2000) The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro ubiquitination of caspases-3 and -7. J. Biol. Chem. 275: 26661-26664
    • (2000) J. Biol. Chem. , vol.275 , pp. 26661-26664
    • Huang, H.1    Joazeiro, C.A.2    Bonfoco, E.3
  • 218
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H et al. (1998) Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94: 481-490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3
  • 219
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ and Yuan J (1998) Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94: 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 220
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai J, Du C, Wu JW et al. (2000) Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 406: 855-862
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3
  • 221
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M et al. (2000) Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102: 43-53
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3
  • 222
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH et al. (2001) Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292: 727-730
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 223
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X (2001) The expanding role of mitochondria in apoptosis. Genes Dev. 15: 2922-2933
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 224
    • 0034737736 scopus 로고    scopus 로고
    • Caspase-8 activation and bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis
    • Tang D, Lahti JM and Kidd VJ (2000) Caspase-8 activation and bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis. J. Biol. Chem. 275: 9303-9307
    • (2000) J. Biol. Chem. , vol.275 , pp. 9303-9307
    • Tang, D.1    Lahti, J.M.2    Kidd, V.J.3
  • 225
    • 0034699353 scopus 로고    scopus 로고
    • Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis
    • Engels IH, Stepczynska A, Stroh C et al. (2000) Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis. Oncogene 19: 4563-4573
    • (2000) Oncogene , vol.19 , pp. 4563-4573
    • Engels, I.H.1    Stepczynska, A.2    Stroh, C.3
  • 226
    • 0035283079 scopus 로고    scopus 로고
    • Activation of caspase-8 in drug-induced apoptosis of B-lymphoid cells is independent of CD95/Fas receptor-ligand interaction and occurs downstream of caspase-3
    • Wieder T, Essmann F, Prokop A et al. (2001) Activation of caspase-8 in drug-induced apoptosis of B-lymphoid cells is independent of CD95/Fas receptor-ligand interaction and occurs downstream of caspase-3. Blood 97: 1378-1387
    • (2001) Blood , vol.97 , pp. 1378-1387
    • Wieder, T.1    Essmann, F.2    Prokop, A.3
  • 227
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (APO-1/Fas) signaling pathways
    • Scaffidi C, Fulda S, Srinivasan A et al. (1998) Two CD95 (APO-1/Fas) signaling pathways. EMBO J. 17: 1675-1687
    • (1998) EMBO J. , vol.17 , pp. 1675-1687
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3
  • 228
    • 0033516570 scopus 로고    scopus 로고
    • The human tumor necrosis factor (TNF) receptor-associated factor 1 gene (TRAF1) is upregulated by cytokines of the TNF ligand family and modulates TNF-induced activation of NF-kappaB and c-Jun N-terminal kinase
    • Schwenzer R, Siemienski K, Liptay S et al. (1999) The human tumor necrosis factor (TNF) receptor-associated factor 1 gene (TRAF1) is upregulated by cytokines of the TNF ligand family and modulates TNF-induced activation of NF-kappaB and c-Jun N-terminal kinase. J. Biol. Chem. 274: 19368-19374
    • (1999) J. Biol. Chem. , vol.274 , pp. 19368-19374
    • Schwenzer, R.1    Siemienski, K.2    Liptay, S.3
  • 229
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control
    • Chu ZL, McKinsey TA, Liu L et al. (1997) Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control. Proc. Natl. Acad. Sci. USA 94: 10057-10062
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10057-10062
    • Chu, Z.L.1    McKinsey, T.A.2    Liu, L.3
  • 230
    • 0034744033 scopus 로고    scopus 로고
    • NF-kappaB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling
    • Kreuz S, Siegmund D, Scheurich P and Wajant H (2001) NF-kappaB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling. Mol. Cell Biol. 21: 3964-3973
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3964-3973
    • Kreuz, S.1    Siegmund, D.2    Scheurich, P.3    Wajant, H.4
  • 231
    • 0034743199 scopus 로고    scopus 로고
    • NF-kappaB signals induce the expression of c-FLIP
    • Micheau O, Lens S, Gaide O et al. (2001) NF-kappaB signals induce the expression of c-FLIP. Mol. Cell Biol. 21: 5299-5305
    • (2001) Mol. Cell Biol. , vol.21 , pp. 5299-5305
    • Micheau, O.1    Lens, S.2    Gaide, O.3
  • 232
    • 0032516651 scopus 로고    scopus 로고
    • IEX-1L, an apoptosis inhibitor involved in NF-kappaB-mediated cell survival
    • Wu MX, Ao Z, Prasad KV et al. (1998) IEX-1L, an apoptosis inhibitor involved in NF-kappaB-mediated cell survival. Science 281: 998-1001
    • (1998) Science , vol.281 , pp. 998-1001
    • Wu, M.X.1    Ao, Z.2    Prasad, K.V.3
  • 233
    • 0032588317 scopus 로고    scopus 로고
    • NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis
    • Wang CY, Guttridge DC, Mayo MW and Baldwin Jr AS (1999) NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis. Mol. Cell Biol. 19: 5923-5929
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5923-5929
    • Wang, C.Y.1    Guttridge, D.C.2    Mayo, M.W.3    Baldwin A.S., Jr.4
  • 234
    • 0033529416 scopus 로고    scopus 로고
    • NF-kappaB-mediated upregulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signaling in B lymphocytes
    • Lee HH, Dadgostar H, Cheng Q et al. (1999) NF-kappaB-mediated upregulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signaling in B lymphocytes. Proc. Natl. Acad. Sci. USA 96: 9136-9141
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9136-9141
    • Lee, H.H.1    Dadgostar, H.2    Cheng, Q.3
  • 235
    • 0033558215 scopus 로고    scopus 로고
    • The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis
    • Zong WX, Edelstein LC, Chen C et al. (1999) The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis. Genes Dev. 13: 382-387
    • (1999) Genes Dev. , vol.13 , pp. 382-387
    • Zong, W.X.1    Edelstein, L.C.2    Chen, C.3
  • 236
    • 0032490670 scopus 로고    scopus 로고
    • Nuclear factor (NF)-kappaB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor alpha- induced apoptosis
    • Stehlik C, de Martin R, Kumabashiri I et al. (1998) Nuclear factor (NF)-kappaB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor alpha- induced apoptosis. J. Exp. Med. 188: 211-216
    • (1998) J. Exp. Med. , vol.188 , pp. 211-216
    • Stehlik, C.1    de Martin, R.2    Kumabashiri, I.3
  • 237
    • 0345561544 scopus 로고    scopus 로고
    • Tumor necrosis factor induces Bcl-2 and Bcl-x expression through NFkappaB activation in primary hippocampal neurons
    • Tamatani M, Che YH, Matsuzaki H et al. (1999) Tumor necrosis factor induces Bcl-2 and Bcl-x expression through NFkappaB activation in primary hippocampal neurons. J. Biol. Chem. 274: 8531-8538
    • (1999) J. Biol. Chem. , vol.274 , pp. 8531-8538
    • Tamatani, M.1    Che, Y.H.2    Matsuzaki, H.3
  • 238
    • 0033621956 scopus 로고    scopus 로고
    • The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L)
    • Chen C, Edelstein LC and Gelinas C (2000) The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L). Mol. Cell Biol. 20: 2687-2695
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2687-2695
    • Chen, C.1    Edelstein, L.C.2    Gelinas, C.3
  • 239
    • 0035920230 scopus 로고    scopus 로고
    • Rel/NF-kappa B transcription factors protect against tumor necrosis factor (TNF)- related apoptosis-inducing ligand (TRAIL)-induced apoptosis by up-regulating the TRAIL decoy receptor DcR1
    • Bernard D, Quatannens B, Vandenbunder B and Abbadie C (2001) Rel/NF-kappa B transcription factors protect against tumor necrosis factor (TNF)- related apoptosis-inducing ligand (TRAIL)-induced apoptosis by up-regulating the TRAIL decoy receptor DcR1. J. Biol. Chem. 276: 27322-27328
    • (2001) J. Biol. Chem. , vol.276 , pp. 27322-27328
    • Bernard, D.1    Quatannens, B.2    Vandenbunder, B.3    Abbadie, C.4
  • 240
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • Brunet A, Bonni A, Zigmond MJ et al. (1999) Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96: 857-868
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1    Bonni, A.2    Zigmond, M.J.3
  • 241
    • 0032515027 scopus 로고    scopus 로고
    • Regulation of cell death protease caspase-9 by phosphorylation
    • Cardone MH, Roy N, Stennicke HR et al. (1998) Regulation of cell death protease caspase-9 by phosphorylation. Science 282: 1318-1321
    • (1998) Science , vol.282 , pp. 1318-1321
    • Cardone, M.H.1    Roy, N.2    Stennicke, H.R.3
  • 242
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L, Gonzalez-Garcia M, Page C et al. (1997) Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278: 687-689
    • (1997) Science , vol.278 , pp. 687-689
    • del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3
  • 243
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin Y, Devin A, Rodriguez Y, Liu ZG (1999) Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev. 13: 2514-2526
    • (1999) Genes Dev. , vol.13 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 244
    • 0033955634 scopus 로고    scopus 로고
    • Activation of a pro-apoptotic amplification loop through inhibition of NF-kappaB-dependent survival signals by caspase-mediated inactivation of RIP
    • Martinon F, Holler N, Richard C and Tschopp J (2000) Activation of a pro-apoptotic amplification loop through inhibition of NF-kappaB-dependent survival signals by caspase-mediated inactivation of RIP. FEBS Lett. 468: 134-136
    • (2000) FEBS Lett. , vol.468 , pp. 134-136
    • Martinon, F.1    Holler, N.2    Richard, C.3    Tschopp, J.4
  • 245
    • 0033966264 scopus 로고    scopus 로고
    • Caspase-induced inactivation of the anti-apoptotic TRAF1 during Fas ligand-mediated apoptosis
    • Irmler M, Steiner V, Ruegg C et al. (2000) Caspase-induced inactivation of the anti-apoptotic TRAF1 during Fas ligand-mediated apoptosis. FEBS Lett. 468: 129-133
    • (2000) FEBS Lett. , vol.468 , pp. 129-133
    • Irmler, M.1    Steiner, V.2    Ruegg, C.3
  • 246
    • 0030613770 scopus 로고    scopus 로고
    • Phosphorylation of IkappaB-alpha inhibits its cleavage by caspase CPP32 in vitro
    • Barkett M, Xue D, Horvitz HR and Gilmore TD (1997) Phosphorylation of IkappaB-alpha inhibits its cleavage by caspase CPP32 in vitro. J. Biol. Chem. 272: 29419-29422
    • (1997) J. Biol. Chem. , vol.272 , pp. 29419-29422
    • Barkett, M.1    Xue, D.2    Horvitz, H.R.3    Gilmore, T.D.4
  • 247
    • 0035930326 scopus 로고    scopus 로고
    • Blocking caspase-3-mediated proteolysis of IKKbeta suppresses TNF-alpha-induced apoptosis
    • Tang G, Yang J, Minemoto Y and Lin A (2001) Blocking caspase-3-mediated proteolysis of IKKbeta suppresses TNF-alpha-induced apoptosis. Mol. Cell 8: 1005-1016
    • (2001) Mol. Cell , vol.8 , pp. 1005-1016
    • Tang, G.1    Yang, J.2    Minemoto, Y.3    Lin, A.4
  • 248
    • 0035805496 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of hematopoietic progenitor kinase 1 (HPK1) converts an activator of NFkappaB into an inhibitor of NFkappaB
    • Arnold R, Liou J, Drexler HC et al. (2001) Caspase-mediated cleavage of hematopoietic progenitor kinase 1 (HPK1) converts an activator of NFkappaB into an inhibitor of NFkappaB. J. Biol. Chem. 276: 14675-14684
    • (2001) J. Biol. Chem. , vol.276 , pp. 14675-14684
    • Arnold, R.1    Liou, J.2    Drexler, H.C.3
  • 249
    • 0034646478 scopus 로고    scopus 로고
    • Activation of NF-kappaB by FADD, Casper, and Caspase-8
    • Hu WH, Johnson H and Shu HB (2000) Activation of NF-kappaB by FADD, Casper, and Caspase-8. J. Biol. Chem. 275: 10838-10844
    • (2000) J. Biol. Chem. , vol.275 , pp. 10838-10844
    • Hu, W.H.1    Johnson, H.2    Shu, H.B.3
  • 250
    • 0032032627 scopus 로고    scopus 로고
    • CD95 (Fas)-induced caspase-mediated proteolysis of NF-kappaB
    • Ravi R, Bedi A, Fuchs EJ and Bedi A (1998) CD95 (Fas)-induced caspase-mediated proteolysis of NF-kappaB. Cancer Res. 58: 882-886
    • (1998) Cancer Res. , vol.58 , pp. 882-886
    • Ravi, R.1    Bedi, A.2    Fuchs, E.J.3    Bedi, A.4
  • 251
    • 0033174072 scopus 로고    scopus 로고
    • Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-kappa B loop
    • Levkau B, Scatena M, Giachelli CM et al. (1999) Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-kappa B loop. Nat. Cell Biol. 1: 227-233
    • (1999) Nat. Cell Biol. , vol.1 , pp. 227-233
    • Levkau, B.1    Scatena, M.2    Giachelli, C.M.3
  • 252
    • 0033615961 scopus 로고    scopus 로고
    • p53 inhibits alpha 6 beta 4 integrin survival signaling by promoting the caspase 3-dependent cleavage of AKT/PKB
    • Bachelder RE, Ribick MJ, Marchetti A et al. (1999) p53 inhibits alpha 6 beta 4 integrin survival signaling by promoting the caspase 3-dependent cleavage of AKT/PKB. J. Cell Biol. 147: 1063-1072
    • (1999) J. Cell Biol. , vol.147 , pp. 1063-1072
    • Bachelder, R.E.1    Ribick, M.J.2    Marchetti, A.3
  • 253
    • 0030780804 scopus 로고    scopus 로고
    • Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
    • Yang DD, Kuan CY, Whitmarsh AJ et al. (1997) Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature 389: 865-870
    • (1997) Nature , vol.389 , pp. 865-870
    • Yang, D.D.1    Kuan, C.Y.2    Whitmarsh, A.J.3
  • 254
    • 0032979438 scopus 로고    scopus 로고
    • Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation
    • Behrens A, Sibilia M and Wagner EF (1999) Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nat. Genet. 21: 326-329
    • (1999) Nat. Genet. , vol.21 , pp. 326-329
    • Behrens, A.1    Sibilia, M.2    Wagner, E.F.3
  • 255
    • 0034607702 scopus 로고    scopus 로고
    • Requirement of JNK for stress-induced activation of the cytochrome c- mediated death pathway
    • Tournier C, Hess P, Yang DD et al. (2000) Requirement of JNK for stress-induced activation of the cytochrome c- mediated death pathway. Science 288: 870-874
    • (2000) Science , vol.288 , pp. 870-874
    • Tournier, C.1    Hess, P.2    Yang, D.D.3
  • 256
    • 15644381250 scopus 로고    scopus 로고
    • Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress- activated protein kinases in the presence of the constitutively active GTP-binding protein Rac1
    • Maundrell K, Antonsson B, Magnenat E et al. (1997) Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress- activated protein kinases in the presence of the constitutively active GTP-binding protein Rac1. J. Biol. Chem. 272: 25238-25242
    • (1997) J. Biol. Chem. , vol.272 , pp. 25238-25242
    • Maundrell, K.1    Antonsson, B.2    Magnenat, E.3
  • 257
    • 0033499801 scopus 로고    scopus 로고
    • BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M
    • Yamamoto K, Ichijo H and Korsmeyer SJ (1999) BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol. Cell Biol. 19: 8469-8478
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 258
    • 0033616709 scopus 로고    scopus 로고
    • Deletion of the loop region of Bcl-2 completely blocks paclitaxel-induced apoptosis
    • Srivastava RK, Mi QS, Hardwick JM and Longo DL (1999) Deletion of the loop region of Bcl-2 completely blocks paclitaxel-induced apoptosis. Proc. Natl. Acad. Sci. USA 96: 3775-3780
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3775-3780
    • Srivastava, R.K.1    Mi, Q.S.2    Hardwick, J.M.3    Longo, D.L.4
  • 259
    • 0033118607 scopus 로고    scopus 로고
    • The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development
    • Kuan CY, Yang DD, Samanta Roy DR et al. (1999) The Jnk1 and Jnk2 protein kinases are required for regional specific apoptosis during early brain development. Neuron 22: 667-676
    • (1999) Neuron , vol.22 , pp. 667-676
    • Kuan, C.Y.1    Yang, D.D.2    Samanta Roy, D.R.3
  • 260
    • 0031029214 scopus 로고    scopus 로고
    • Stress-signalling kinase Sek1 protects thymocytes from apoptosis mediated by CD95 and CD3
    • Nishina H, Fischer KD, Radvanyi L et al. (1997) Stress-signalling kinase Sek1 protects thymocytes from apoptosis mediated by CD95 and CD3. Nature 385: 350-353
    • (1997) Nature , vol.385 , pp. 350-353
    • Nishina, H.1    Fischer, K.D.2    Radvanyi, L.3
  • 261
    • 85047700485 scopus 로고    scopus 로고
    • Differential effects of JNK1 and JNK2 on signal specific induction of apoptosis
    • Hochedlinger K, Wagner EF and Sabapathy K (2002) Differential effects of JNK1 and JNK2 on signal specific induction of apoptosis. Oncogene 21: 2441-2445
    • (2002) Oncogene , vol.21 , pp. 2441-2445
    • Hochedlinger, K.1    Wagner, E.F.2    Sabapathy, K.3
  • 262
    • 0036086898 scopus 로고    scopus 로고
    • Increased cytochrome P-450 2E1 expression sensitizes hepatocytes to c-Jun-mediated cell death from TNF-alpha
    • Liu H, Jones BE, Bradham C and Czaja MJ (2002) Increased cytochrome P-450 2E1 expression sensitizes hepatocytes to c-Jun-mediated cell death from TNF-alpha. Am. J. Physiol. Gastrointest. Liver Physiol. 282: G257-G266
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.282
    • Liu, H.1    Jones, B.E.2    Bradham, C.3    Czaja, M.J.4
  • 263
    • 0036009411 scopus 로고    scopus 로고
    • NF-kappaB inhibition sensitizes hepatocytes to TNF-induced apoptosis through a sustained activation of JNK and c-Jun
    • Liu H, Lo CR and Czaja MJ (2002) NF-kappaB inhibition sensitizes hepatocytes to TNF-induced apoptosis through a sustained activation of JNK and c-Jun. Hepatology 35: 772-778
    • (2002) Hepatology , vol.35 , pp. 772-778
    • Liu, H.1    Lo, C.R.2    Czaja, M.J.3
  • 264
    • 0032512847 scopus 로고    scopus 로고
    • Correlation between sustained c-Jun N-terminal protein kinase activation and apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells
    • Guo YL, Baysal K, Kang B et al. (1998) Correlation between sustained c-Jun N-terminal protein kinase activation and apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells. J. Biol. Chem. 273: 4027-4034
    • (1998) J. Biol. Chem. , vol.273 , pp. 4027-4034
    • Guo, Y.L.1    Baysal, K.2    Kang, B.3
  • 265
    • 0032562781 scopus 로고    scopus 로고
    • Inhibition of the expression of mitogen-activated protein phosphatase-1 potentiates apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells
    • Guo YL, Kang B and Williamson JR (1998) Inhibition of the expression of mitogen-activated protein phosphatase-1 potentiates apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells. J. Biol. Chem. 273: 10362-10366
    • (1998) J. Biol. Chem. , vol.273 , pp. 10362-10366
    • Guo, Y.L.1    Kang, B.2    Williamson, J.R.3
  • 266
    • 0036234472 scopus 로고    scopus 로고
    • Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid- dependent pathway in tumor necrosis factor-induced apoptosis
    • Gabai VL, Mabuchi K, Mosser DD and Sherman MY (2002) Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid- dependent pathway in tumor necrosis factor-induced apoptosis. Mol. Cell Biol. 22: 3415-3424
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3415-3424
    • Gabai, V.L.1    Mabuchi, K.2    Mosser, D.D.3    Sherman, M.Y.4
  • 267
    • 0035891320 scopus 로고    scopus 로고
    • Inhibition of JNK activation through NF-kappaB target genes
    • Tang G, Minemoto Y, Dibling B et al. (2001) Inhibition of JNK activation through NF-kappaB target genes. Nature 414: 313-317
    • (2001) Nature , vol.414 , pp. 313-317
    • Tang, G.1    Minemoto, Y.2    Dibling, B.3
  • 268
    • 0035913158 scopus 로고    scopus 로고
    • NF-kappa B activation results in rapid inactivation of JNK in TNF alpha-treated Ewing sarcoma cells: A mechanism for the anti-apoptotic effect of NF-kappa B
    • Javelaud D and Besancon F (2001) NF-kappa B activation results in rapid inactivation of JNK in TNF alpha-treated Ewing sarcoma cells: a mechanism for the anti-apoptotic effect of NF-kappa B. Oncogene 20: 4365-4372
    • (2001) Oncogene , vol.20 , pp. 4365-4372
    • Javelaud, D.1    Besancon, F.2
  • 269
    • 0032484009 scopus 로고    scopus 로고
    • TRAIL/Apo2L activates c-Jun NH2-terminal kinase (JNK) via caspase- dependent and caspase-independent pathways
    • Muhlenbeck F, Haas E, Schwenzer R et al. (1998) TRAIL/Apo2L activates c-Jun NH2-terminal kinase (JNK) via caspase- dependent and caspase-independent pathways. J. Biol. Chem. 273: 33091-33098
    • (1998) J. Biol. Chem. , vol.273 , pp. 33091-33098
    • Muhlenbeck, F.1    Haas, E.2    Schwenzer, R.3
  • 270
    • 0032562704 scopus 로고    scopus 로고
    • Early activation of c-Jun N-terminal kinase and p38 kinase regulate cell survival in response to tumor necrosis factor alpha
    • Roulston A, Reinhard C, Amiri P and Williams LT (1998) Early activation of c-Jun N-terminal kinase and p38 kinase regulate cell survival in response to tumor necrosis factor alpha. J. Biol. Chem. 273: 10232-10239
    • (1998) J. Biol. Chem. , vol.273 , pp. 10232-10239
    • Roulston, A.1    Reinhard, C.2    Amiri, P.3    Williams, L.T.4
  • 271
    • 0031016440 scopus 로고    scopus 로고
    • Lack of a role for Jun kinase and AP-1 in Fas-induced apoptosis
    • Lenczowski JM, Dominguez L, Eder AM et al. (1997) Lack of a role for Jun kinase and AP-1 in Fas-induced apoptosis. Mol. Cell Biol. 17: 170-181
    • (1997) Mol. Cell Biol. , vol.17 , pp. 170-181
    • Lenczowski, J.M.1    Dominguez, L.2    Eder, A.M.3
  • 272
    • 0033040818 scopus 로고    scopus 로고
    • JNK/SAPK activity contributes to TRAIL-induced apoptosis
    • Herr I, Wilhelm D, Meyer E et al. (1999) JNK/SAPK activity contributes to TRAIL-induced apoptosis. Cell Death Differ. 6: 130-135
    • (1999) Cell Death Differ. , vol.6 , pp. 130-135
    • Herr, I.1    Wilhelm, D.2    Meyer, E.3
  • 273
    • 0035848864 scopus 로고    scopus 로고
    • HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell
    • Geleziunas R, Xu W, Takeda K et al. (2001) HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell. Nature 410: 834-838
    • (2001) Nature , vol.410 , pp. 834-838
    • Geleziunas, R.1    Xu, W.2    Takeda, K.3
  • 274
    • 0034714355 scopus 로고    scopus 로고
    • Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation
    • Hatai T, Matsuzawa A, Inoshita S et al. (2000) Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation. J. Biol. Chem. 275: 26576-26581
    • (2000) J. Biol. Chem. , vol.275 , pp. 26576-26581
    • Hatai, T.1    Matsuzawa, A.2    Inoshita, S.3
  • 275
    • 0035965345 scopus 로고    scopus 로고
    • A kinase-independent function of Ask1 in caspase-independent cell death
    • Charette SJ, Lambert H, Landry J (2001) A kinase-independent function of Ask1 in caspase-independent cell death. J. Biol. Chem. 276: 36071-36074
    • (2001) J. Biol. Chem. , vol.276 , pp. 36071-36074
    • Charette, S.J.1    Lambert, H.2    Landry, J.3
  • 276
    • 0035889252 scopus 로고    scopus 로고
    • Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling
    • De Smaele E, Zazzeroni F, Papa S et al. (2001) Induction of gadd45beta by NF-kappaB downregulates pro-apoptotic JNK signalling. Nature 414: 308-313
    • (2001) Nature , vol.414 , pp. 308-313
    • De Smaele, E.1    Zazzeroni, F.2    Papa, S.3
  • 277
    • 0029912652 scopus 로고    scopus 로고
    • rac1 regulates a cytokine-stimulated, redox-dependent pathway necessary for NF-kappaB activation
    • Sulciner DJ, Irani K, Yu ZX et al. (1996) rac1 regulates a cytokine-stimulated, redox-dependent pathway necessary for NF-kappaB activation. Mol. Cell Biol. 16: 7115-7121
    • (1996) Mol. Cell Biol. , vol.16 , pp. 7115-7121
    • Sulciner, D.J.1    Irani, K.2    Yu, Z.X.3
  • 278
    • 0027328056 scopus 로고
    • Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF
    • Schulze-Osthoff K, Beyaert R, Vandevoorde V et al. (1993) Depletion of the mitochondrial electron transport abrogates the cytotoxic and gene-inductive effects of TNF. EMBO J. 12: 3095-3104
    • (1993) EMBO J. , vol.12 , pp. 3095-3104
    • Schulze-Osthoff, K.1    Beyaert, R.2    Vandevoorde, V.3
  • 279
    • 0034725109 scopus 로고    scopus 로고
    • Selective involvement of superoxide anion, but not downstream compounds hydrogen peroxide and peroxynitrite, in tumor necrosis factor-alpha-induced apoptosis of rat mesangial cells
    • Moreno-Manzano V, Ishikawa Y, Lucio-Cazana J and Kitamura M (2000) Selective involvement of superoxide anion, but not downstream compounds hydrogen peroxide and peroxynitrite, in tumor necrosis factor-alpha-induced apoptosis of rat mesangial cells. J. Biol. Chem. 275: 12684-12691
    • (2000) J. Biol. Chem. , vol.275 , pp. 12684-12691
    • Moreno-Manzano, V.1    Ishikawa, Y.2    Lucio-Cazana, J.3    Kitamura, M.4
  • 280
    • 0033389017 scopus 로고    scopus 로고
    • Induction of inducible nitric oxide synthase is an essential part of tumor necrosis factor-alpha-induced apoptosis in MCF-7 and other epithelial tumor cells
    • Binder C, Schulz M, Hiddemann W and Oellerich M (1999) Induction of inducible nitric oxide synthase is an essential part of tumor necrosis factor-alpha-induced apoptosis in MCF-7 and other epithelial tumor cells. Lab. Invest. 79: 1703-1712
    • (1999) Lab. Invest. , vol.79 , pp. 1703-1712
    • Binder, C.1    Schulz, M.2    Hiddemann, W.3    Oellerich, M.4
  • 281
    • 0032191654 scopus 로고    scopus 로고
    • TNF-alpha activates at least two apoptotic signaling cascades
    • Sidoti-de Fraisse C, Rincheval V, Risler Y et al. (1998) TNF-alpha activates at least two apoptotic signaling cascades. Oncogene 17: 1639-1651
    • (1998) Oncogene , vol.17 , pp. 1639-1651
    • Sidoti-de Fraisse, C.1    Rincheval, V.2    Risler, Y.3
  • 282
    • 0024428198 scopus 로고
    • Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor
    • Wong GH, Elwell JH, Oberley LW and Goeddel DV (1989) Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor. Cell 58: 923-931
    • (1989) Cell , vol.58 , pp. 923-931
    • Wong, G.H.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 283
    • 0024202127 scopus 로고
    • Induction of manganous superoxide dismutase by tumor necrosis factor: Possible protective mechanism
    • Wong GH and Goeddel DV (1988) Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism. Science 242: 941-944
    • (1988) Science , vol.242 , pp. 941-944
    • Wong, G.H.1    Goeddel, D.V.2
  • 284
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M and Jaattela M (2001) Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. Mol. Cell Biol. 2: 589-598
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 285
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler N, Zaru R, Micheau O et al. (2000) Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1: 489-495
    • (2000) Nat. Immunol. , vol.1 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3
  • 286
    • 0034637510 scopus 로고    scopus 로고
    • Sensitization to death receptor cytotoxicity by inhibition of fas- associated death domain protein (FADD)/caspase signaling. Requirement of cell cycle progression
    • Luschen S, Ussat S, Scherer G et al. (2000) Sensitization to death receptor cytotoxicity by inhibition of fas- associated death domain protein (FADD)/caspase signaling. Requirement of cell cycle progression. J. Biol. Chem. 275: 24670-24678
    • (2000) J. Biol. Chem. , vol.275 , pp. 24670-24678
    • Luschen, S.1    Ussat, S.2    Scherer, G.3
  • 287
    • 0033579422 scopus 로고    scopus 로고
    • Resistance to the cytotoxic effects of tumor necrosis factor alpha can be overcome by inhibition of a FADD/caspase-dependent signaling pathway
    • Khwaja A and Tatton L (1999) Resistance to the cytotoxic effects of tumor necrosis factor alpha can be overcome by inhibition of a FADD/caspase-dependent signaling pathway. J. Biol. Chem. 274: 36817-36823
    • (1999) J. Biol. Chem. , vol.274 , pp. 36817-36823
    • Khwaja, A.1    Tatton, L.2
  • 288
    • 0032494143 scopus 로고    scopus 로고
    • Dual signaling of the Fas receptor: Initiation of both apoptotic and necrotic cell death pathways
    • Vercammen D, Brouckaert G, Denecker G et al. (1998) Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways. J. Exp. Med. 188: 919-930
    • (1998) J. Exp. Med. , vol.188 , pp. 919-930
    • Vercammen, D.1    Brouckaert, G.2    Denecker, G.3
  • 289
    • 0033861807 scopus 로고    scopus 로고
    • Induction of necrotic-like cell death by tumor necrosis factor alpha and caspase inhibitors: Novel mechanism for killing virus-infected cells
    • Li M and Beg AA (2000) Induction of necrotic-like cell death by tumor necrosis factor alpha and caspase inhibitors: novel mechanism for killing virus-infected cells. J. Virol. 74: 7470-7477
    • (2000) J. Virol. , vol.74 , pp. 7470-7477
    • Li, M.1    Beg, A.A.2
  • 290
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • Vercammen D, Beyaert R, Denecker G et al. (1998) Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J. Exp. Med. 187: 1477-1485
    • (1998) J. Exp. Med. , vol.187 , pp. 1477-1485
    • Vercammen, D.1    Beyaert, R.2    Denecker, G.3
  • 291
    • 0032583164 scopus 로고    scopus 로고
    • Caspase-independent cell killing by Fas-associated protein with death domain
    • Kawahara A, Ohsawa Y, Matsumura H et al. (1998) Caspase-independent cell killing by Fas-associated protein with death domain. J. Cell Biol. 143: 1353-1360
    • (1998) J. Cell Biol. , vol.143 , pp. 1353-1360
    • Kawahara, A.1    Ohsawa, Y.2    Matsumura, H.3
  • 292
    • 0027513548 scopus 로고
    • Expression of BCL-2 protein enhances the survival of mouse fibrosarcoid cells in tumor necrosis factor-mediated cytotoxicity
    • Hennet T, Bertoni G, Richter C and Peterhans E (1993) Expression of BCL-2 protein enhances the survival of mouse fibrosarcoid cells in tumor necrosis factor-mediated cytotoxicity. Cancer Res. 53: 1456-1460
    • (1993) Cancer Res. , vol.53 , pp. 1456-1460
    • Hennet, T.1    Bertoni, G.2    Richter, C.3    Peterhans, E.4
  • 293
    • 0027473778 scopus 로고
    • Tumour necrosis factor-alpha induces superoxide anion generation in mitochondria of L929 cells
    • Hennet T, Richter C and Peterhans E (1993) Tumour necrosis factor-alpha induces superoxide anion generation in mitochondria of L929 cells. Biochem. J. 289: 587-592
    • (1993) Biochem. J. , vol.289 , pp. 587-592
    • Hennet, T.1    Richter, C.2    Peterhans, E.3
  • 294
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation
    • Schulze-Osthoff K, Bakker AC, Vanhaesebroeck B et al. (1992) Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J. Biol. Chem. 267: 5317-5323
    • (1992) J. Biol. Chem. , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3
  • 295
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist M, Single B, Castoldi AF et al. (1997) Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J. Exp. Med. 185: 1481-1486
    • (1997) J. Exp. Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3
  • 296
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y, Shimizu S and Tsujimoto Y (1997) Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res. 57: 1835-1840
    • (1997) Cancer Res. , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 297
    • 0032494108 scopus 로고    scopus 로고
    • Differential regulation and ATP requirement for caspase-8 and caspase-3 activation during
    • Ferrari D, Stepczynska A, Los M et al. (1998) Differential regulation and ATP requirement for caspase-8 and caspase-3 activation during. J. Exp. Med. 188: 979-984
    • (1998) J. Exp. Med. , vol.188 , pp. 979-984
    • Ferrari, D.1    Stepczynska, A.2    Los, M.3
  • 298
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha HC and Snyder SH (1999) Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc. Natl. Acad. Sci. USA 96: 13978-13982
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13978-13982
    • Ha, H.C.1    Snyder, S.H.2
  • 299
    • 0034760530 scopus 로고    scopus 로고
    • Gain-of-function of poly(ADP-ribose) polymerase-1 upon cleavage by apoptotic proteases: Implications for apoptosis
    • D'Amours D, Sallmann FR, Dixit VM and Poirier GG (2001) Gain-of-function of poly(ADP-ribose) polymerase-1 upon cleavage by apoptotic proteases: implications for apoptosis. J. Cell Sci. 114: 3771-3778
    • (2001) J. Cell Sci. , vol.114 , pp. 3771-3778
    • D'Amours, D.1    Sallmann, F.R.2    Dixit, V.M.3    Poirier, G.G.4
  • 300
    • 0036196425 scopus 로고    scopus 로고
    • Activation and Caspase-mediated inhibition of PARP: A molecular switch between fibroblast necrosis and apoptosis in death receptor signaling
    • Los M, Mozoluk M, Ferrari D et al. (2002) Activation and Caspase-mediated inhibition of PARP: A molecular switch between fibroblast necrosis and apoptosis in death receptor signaling. Mol. Biol. Cell 13: 978-988
    • (2002) Mol. Biol. Cell , vol.13 , pp. 978-988
    • Los, M.1    Mozoluk, M.2    Ferrari, D.3
  • 301
    • 0028001530 scopus 로고
    • Divergent signalling via APO-1/Fas and the TNF receptor, two homologous molecules involved in physiological cell death
    • Schulze-Osthoff K, Krammer PH and Droge W (1994) Divergent signalling via APO-1/Fas and the TNF receptor, two homologous molecules involved in physiological cell death. EMBO J. 13: 4587-4596
    • (1994) EMBO J. , vol.13 , pp. 4587-4596
    • Schulze-Osthoff, K.1    Krammer, P.H.2    Droge, W.3
  • 303
    • 0028108015 scopus 로고
    • Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling
    • Wiegmann K, Schutze S, Machleidt T et al. (1994) Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling. Cell 78: 1005-1015
    • (1994) Cell , vol.78 , pp. 1005-1015
    • Wiegmann, K.1    Schutze, S.2    Machleidt, T.3
  • 304
    • 0026560014 scopus 로고
    • Tumor necrosis factor-alpha activates the sphingomyelin signal transduction pathway in a cell-free system
    • Dressler KA, Mathias S and Kolesnick RN (1992) Tumor necrosis factor-alpha activates the sphingomyelin signal transduction pathway in a cell-free system. Science 255: 1715-1718
    • (1992) Science , vol.255 , pp. 1715-1718
    • Dressler, K.A.1    Mathias, S.2    Kolesnick, R.N.3
  • 305
    • 0032869856 scopus 로고    scopus 로고
    • Functional analysis of acid and neutral sphingomyelinases in vitro and in vivo
    • Stoffel W (1999) Functional analysis of acid and neutral sphingomyelinases in vitro and in vivo. Chem. Phys. Lipids 102: 107-121
    • (1999) Chem. Phys. Lipids , vol.102 , pp. 107-121
    • Stoffel, W.1
  • 306
    • 0035808364 scopus 로고    scopus 로고
    • Cell autonomous apoptosis defects in acid sphingomyelinase knockout fibroblasts
    • Lozano J, Menendez S, Morales A et al. (2001) Cell autonomous apoptosis defects in acid sphingomyelinase knockout fibroblasts. J. Biol. Chem. 276: 442-448
    • (2001) J. Biol. Chem. , vol.276 , pp. 442-448
    • Lozano, J.1    Menendez, S.2    Morales, A.3
  • 307
    • 0034605034 scopus 로고    scopus 로고
    • Overexpression of acid ceramidase protects from tumor necrosis factor-induced cell death
    • Strelow A, Bernardo K, Adam-Klages S et al. (2000) Overexpression of acid ceramidase protects from tumor necrosis factor-induced cell death. J. Exp. Med. 192: 601-612
    • (2000) J. Exp. Med. , vol.192 , pp. 601-612
    • Strelow, A.1    Bernardo, K.2    Adam-Klages, S.3
  • 308
    • 0033605293 scopus 로고    scopus 로고
    • Requirement of FADD for tumor necrosis factor-induced activation of acid sphingomyelinase
    • Wiegmann K, Schwandner R, Krut O et al. (1999) Requirement of FADD for tumor necrosis factor-induced activation of acid sphingomyelinase. J. Biol. Chem. 274: 5267-5270
    • (1999) J. Biol. Chem. , vol.274 , pp. 5267-5270
    • Wiegmann, K.1    Schwandner, R.2    Krut, O.3
  • 309
    • 0032489554 scopus 로고    scopus 로고
    • TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase
    • Schwandner R, Wiegmann K, Bernardo K et al. (1998) TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase. J. Biol. Chem. 273: 5916-5922
    • (1998) J. Biol. Chem. , vol.273 , pp. 5916-5922
    • Schwandner, R.1    Wiegmann, K.2    Bernardo, K.3
  • 310
    • 0033214095 scopus 로고    scopus 로고
    • Cathepsin D targeted by acid sphingomyelinase-derived ceramide
    • Heinrich M, Wickel M, Schneider-Brachert W et al. (1999) Cathepsin D targeted by acid sphingomyelinase-derived ceramide. EMBO J. 18: 5252-5263
    • (1999) EMBO J. , vol.18 , pp. 5252-5263
    • Heinrich, M.1    Wickel, M.2    Schneider-Brachert, W.3
  • 311
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death
    • Bursch W (2001) The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ. 8: 569-581
    • (2001) Cell Death Differ. , vol.8 , pp. 569-581
    • Bursch, W.1
  • 312
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route
    • Stoka V, Turk B, Schendel SL et al. (2001) Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J. Biol. Chem. 276: 3149-3157
    • (2001) J. Biol. Chem. , vol.276 , pp. 3149-3157
    • Stoka, V.1    Turk, B.2    Schendel, S.L.3
  • 313
    • 0035947776 scopus 로고    scopus 로고
    • Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor
    • Foghsgaard L, Wissing D, Mauch D et al. (2001) Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor. J. Cell Biol. 153: 999-1010
    • (2001) J. Cell Biol. , vol.153 , pp. 999-1010
    • Foghsgaard, L.1    Wissing, D.2    Mauch, D.3
  • 314
    • 0033756474 scopus 로고    scopus 로고
    • Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
    • Guicciardi ME, Deussing J, Miyoshi H et al. (2000) Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J. Clin. Invest. 106: 1127-1137
    • (2000) J. Clin. Invest. , vol.106 , pp. 1127-1137
    • Guicciardi, M.E.1    Deussing, J.2    Miyoshi, H.3
  • 315
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha
    • Deiss LP, Galinka H, Berissi H et al. (1996) Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBO J. 15: 3861-3870
    • (1996) EMBO J. , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3
  • 316
    • 0035180207 scopus 로고    scopus 로고
    • Cathepsin B knockout mice are resistant to tumor necrosis factor-alpha-mediated hepatocyte apoptosis and liver injury: Implications for therapeutic applications
    • Guicciardi ME, Miyoshi H, Bronk SF and Gores GJ (2001) Cathepsin B knockout mice are resistant to tumor necrosis factor-alpha-mediated hepatocyte apoptosis and liver injury: implications for therapeutic applications. Am. J. Pathol. 159: 2045-2054
    • (2001) Am. J. Pathol. , vol.159 , pp. 2045-2054
    • Guicciardi, M.E.1    Miyoshi, H.2    Bronk, S.F.3    Gores, G.J.4
  • 317
    • 0026751717 scopus 로고
    • The p70 tumor necrosis factor receptor mediates cytotoxicity
    • Heller RA, Song K, Fan N and Chang DJ (1992) The p70 tumor necrosis factor receptor mediates cytotoxicity. Cell 70: 47-56
    • (1992) Cell , vol.70 , pp. 47-56
    • Heller, R.A.1    Song, K.2    Fan, N.3    Chang, D.J.4
  • 318
    • 0027308663 scopus 로고
    • Tumor necrosis factor's cytotoxic activity is signaled by the p55 TNF receptor
    • Tartaglia LA, Rothe M, Hu YF and Goeddel DV (1993) Tumor necrosis factor's cytotoxic activity is signaled by the p55 TNF receptor. Cell 73: 213-216
    • (1993) Cell , vol.73 , pp. 213-216
    • Tartaglia, L.A.1    Rothe, M.2    Hu, Y.F.3    Goeddel, D.V.4
  • 319
    • 0028930776 scopus 로고
    • Both TNF receptors are required for TNF-mediated induction of apoptosis in PC60 cells
    • Vandenabeele P, Declercq W, Vanhaesebroeck B et al. (1995) Both TNF receptors are required for TNF-mediated induction of apoptosis in PC60 cells. J. Immunol. 154: 2904-2913
    • (1995) J. Immunol. , vol.154 , pp. 2904-2913
    • Vandenabeele, P.1    Declercq, W.2    Vanhaesebroeck, B.3
  • 320
    • 0028337454 scopus 로고
    • Dual role of the p75 tumor necrosis factor (TNF) receptor in TNF cytotoxicity
    • Bigda J, Beletsky I, Brakebusch C et al. (1994) Dual role of the p75 tumor necrosis factor (TNF) receptor in TNF cytotoxicity. J. Exp. Med. 180: 445-460
    • (1994) J. Exp. Med. , vol.180 , pp. 445-460
    • Bigda, J.1    Beletsky, I.2    Brakebusch, C.3
  • 321
    • 0027315251 scopus 로고
    • TR60 and TR80 tumor necrosis factor (TNF)-receptors can independently mediate cytolysis
    • Grell M, Scheurich P, Meager A and Pfizenmaier K (1993) TR60 and TR80 tumor necrosis factor (TNF)-receptors can independently mediate cytolysis. Lymphokine Cytokine Res. 12: 143-148
    • (1993) Lymphokine Cytokine Res. , vol.12 , pp. 143-148
    • Grell, M.1    Scheurich, P.2    Meager, A.3    Pfizenmaier, K.4
  • 322
    • 0027959655 scopus 로고
    • Involvement of the tumor necrosis factor receptor p75 in mediating cytotoxicity and gene regulating activities
    • Medvedev AE, Sundan A and Espevik T (1994) Involvement of the tumor necrosis factor receptor p75 in mediating cytotoxicity and gene regulating activities. Eur. J. Immunol. 24: 2842-2849
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2842-2849
    • Medvedev, A.E.1    Sundan, A.2    Espevik, T.3
  • 323
    • 0033152828 scopus 로고    scopus 로고
    • Induction of cell death by tumour necrosis factor (TNF) receptor 2, CD40 and CD30: A role for TNF-R1 activation by endogenous membrane-anchored TNF
    • Grell M, Zimmermann G, Gottfried E et al. (1999) Induction of cell death by tumour necrosis factor (TNF) receptor 2, CD40 and CD30: a role for TNF-R1 activation by endogenous membrane-anchored TNF. EMBO J 18: 3034-3043
    • (1999) EMBO J , vol.18 , pp. 3034-3043
    • Grell, M.1    Zimmermann, G.2    Gottfried, E.3
  • 324
    • 0029025252 scopus 로고
    • Cytotoxicity in L929 murine fibrosarcoma cells after triggering of transfected human p75 tumour necrosis factor (TNF) receptor is mediated by endogenous murine TNF
    • Vercammen D,Vandenabeele P, Declercq W et al. (1995) Cytotoxicity in L929 murine fibrosarcoma cells after triggering of transfected human p75 tumour necrosis factor (TNF) receptor is mediated by endogenous murine TNF. Cytokine 7: 463-470
    • (1995) Cytokine , vol.7 , pp. 463-470
    • Vercammen, D.1    Vandenabeele, P.2    Declercq, W.3
  • 325
    • 0032993566 scopus 로고    scopus 로고
    • TWEAK can induce cell death via endogenous TNF and TNF receptor 1
    • Schneider P, Schwenzer R, Haas E et al. (1999) TWEAK can induce cell death via endogenous TNF and TNF receptor 1. Eur. J. Immunol. 29: 1785-1792
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1785-1792
    • Schneider, P.1    Schwenzer, R.2    Haas, E.3
  • 326
    • 0033912082 scopus 로고    scopus 로고
    • CD40 induces apoptosis in carcinoma cells through activation of cytotoxic ligands of the tumor necrosis factor superfamily
    • Eliopoulos AG, Davies C, Knox PG et al. (2000) CD40 induces apoptosis in carcinoma cells through activation of cytotoxic ligands of the tumor necrosis factor superfamily. Mol. Cell Biol 20: 5503-5515
    • (2000) Mol. Cell Biol , vol.20 , pp. 5503-5515
    • Eliopoulos, A.G.1    Davies, C.2    Knox, P.G.3
  • 327
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • Yeh WC, Itie A, Elia AJ et al. (2000) Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity 12: 633-642
    • (2000) Immunity , vol.12 , pp. 633-642
    • Yeh, W.C.1    Itie, A.2    Elia, A.J.3
  • 328
    • 0033634878 scopus 로고    scopus 로고
    • JunD protects cells from p53-dependent senescence and apoptosis
    • Weitzman JB, Fiette L, Matsuo K and Yaniv M (2000) JunD protects cells from p53-dependent senescence and apoptosis. Mol. Cell 6: 1109-1119
    • (2000) Mol. Cell , vol.6 , pp. 1109-1119
    • Weitzman, J.B.1    Fiette, L.2    Matsuo, K.3    Yaniv, M.4
  • 329
    • 0033532386 scopus 로고    scopus 로고
    • The IKKbeta subunit of IkappaB kinase (IKK) is essential for nuclear factor kappaB activation and prevention of apoptosis
    • Li ZW, Chu W, Hu Y et al. (1999) The IKKbeta subunit of IkappaB kinase (IKK) is essential for nuclear factor kappaB activation and prevention of apoptosis. J. Exp. Med 189: 1839-1845
    • (1999) J. Exp. Med , vol.189 , pp. 1839-1845
    • Li, Z.W.1    Chu, W.2    Hu, Y.3
  • 330
    • 0034745021 scopus 로고    scopus 로고
    • IKKbeta is essential for protecting T cells from TNFalpha-induced apoptosis
    • Senftleben U, Li ZW, Baud V and Karin M (2001) IKKbeta is essential for protecting T cells from TNFalpha-induced apoptosis. Immunity 14: 217-230
    • (2001) Immunity , vol.14 , pp. 217-230
    • Senftleben, U.1    Li, Z.W.2    Baud, V.3    Karin, M.4
  • 331
    • 0035896422 scopus 로고    scopus 로고
    • Defective lymphotoxin-beta receptor-induced NF-kappaB transcriptional activity in NIK-deficient mice
    • Yin L, Wu L, Wesche H et al. (2001) Defective lymphotoxin-beta receptor-induced NF-kappaB transcriptional activity in NIK-deficient mice. Science 291: 2162-2165
    • (2001) Science , vol.291 , pp. 2162-2165
    • Yin, L.1    Wu, L.2    Wesche, H.3
  • 332
    • 0030984490 scopus 로고    scopus 로고
    • PARP is important for genomic stability but dispensable in apoptosis
    • Wang ZQ, Stingl L, Morrison C et al. (1997) PARP is important for genomic stability but dispensable in apoptosis. Genes Dev. 11: 2347-2358
    • (1997) Genes Dev. , vol.11 , pp. 2347-2358
    • Wang, Z.Q.1    Stingl, L.2    Morrison, C.3
  • 333
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B
    • Beg AA, Sha WC, Bronson RT et al. (1995) Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-kappa B. Nature 376: 167-170
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3
  • 334
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kappaB in preventing TNF-alpha-induced cell death
    • Beg AA and Baltimore D (1996) An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 274: 782-784
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 335
    • 0034752285 scopus 로고    scopus 로고
    • TRAF1 is a negative regulator of TNF signaling. Enhanced TNF signaling in TRAF1-deficient mice
    • Tsitsikov EN, Laouini D, Dunn IF et al. (2001) TRAF1 is a negative regulator of TNF signaling. Enhanced TNF signaling in TRAF1-deficient mice. Immunity 15: 647-657
    • (2001) Immunity , vol.15 , pp. 647-657
    • Tsitsikov, E.N.1    Laouini, D.2    Dunn, I.F.3
  • 336
    • 0033578329 scopus 로고    scopus 로고
    • Targeted disruption of TRAF5 gene causes defects in CD40- and CD27-mediated lymphocyte activation
    • Nakano H, Sakon S, Koseki H et al. (1999) Targeted disruption of TRAF5 gene causes defects in CD40- and CD27-mediated lymphocyte activation. Proc. Natl. Acad. Sci. USA 96: 9803-9808
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9803-9808
    • Nakano, H.1    Sakon, S.2    Koseki, H.3
  • 337
    • 0035965232 scopus 로고    scopus 로고
    • Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF- kappa B activation and protection from cell death
    • Tada K, Okazaki T, Sakon S et al. (2001) Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF- kappa B activation and protection from cell death. J. Biol. Chem. 276: 36530-36534
    • (2001) J. Biol. Chem. , vol.276 , pp. 36530-36534
    • Tada, K.1    Okazaki, T.2    Sakon, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.