메뉴 건너뛰기




Volumn 63, Issue 3, 2013, Pages 225-229

The TNF cytokine family: One track in a road paved by many

Author keywords

Apoptosis; Caspase 8; NF kappa B; Signaling; TNF

Indexed keywords

ETANERCEPT; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LYMPHOTOXIN; ONERCEPT; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 84881612886     PISSN: 10434666     EISSN: 10960023     Source Type: Journal    
DOI: 10.1016/j.cyto.2013.05.027     Document Type: Article
Times cited : (18)

References (34)
  • 1
    • 0022369998 scopus 로고
    • Tumor necrosis factor (TNF)
    • Old L.J. Tumor necrosis factor (TNF). Science 1985, 230:630-632.
    • (1985) Science , vol.230 , pp. 630-632
    • Old, L.J.1
  • 3
    • 0014311519 scopus 로고
    • Lymphocyte in vitro cytotoxicity: mechanisms of immune and non-immune small lymphocyte mediated target L cell destruction
    • Granger G.A., Kolb W.P. Lymphocyte in vitro cytotoxicity: mechanisms of immune and non-immune small lymphocyte mediated target L cell destruction. J Immunol 1968, 101:111-120.
    • (1968) J Immunol , vol.101 , pp. 111-120
    • Granger, G.A.1    Kolb, W.P.2
  • 4
    • 0014400299 scopus 로고
    • Cytotoxicity mediated by soluble antigen and lymphocytes in delayed hypersensitivity. III. Analysis of mechanism
    • Ruddle N.H., Waksman B.H. Cytotoxicity mediated by soluble antigen and lymphocytes in delayed hypersensitivity. III. Analysis of mechanism. J Exp Med 1968, 128:1267-1279.
    • (1968) J Exp Med , vol.128 , pp. 1267-1279
    • Ruddle, N.H.1    Waksman, B.H.2
  • 5
    • 0022371461 scopus 로고
    • Identity of tumour necrosis factor and the macrophage-secreted factor cachectin
    • Beutler B., Greenwald D., Hulmes J.D., Chang M., Pan Y.C., Mathison J., et al. Identity of tumour necrosis factor and the macrophage-secreted factor cachectin. Nature 1985, 316:552-554.
    • (1985) Nature , vol.316 , pp. 552-554
    • Beutler, B.1    Greenwald, D.2    Hulmes, J.D.3    Chang, M.4    Pan, Y.C.5    Mathison, J.6
  • 6
    • 0020286403 scopus 로고
    • Regulation of susceptibility to natural killer cells' cytotoxicity and regulation of HLA synthesis: differing efficacies of alpha, beta, and gamma interferons
    • Wallach D. Regulation of susceptibility to natural killer cells' cytotoxicity and regulation of HLA synthesis: differing efficacies of alpha, beta, and gamma interferons. J Interferon Res 1982, 2:329-338.
    • (1982) J Interferon Res , vol.2 , pp. 329-338
    • Wallach, D.1
  • 7
    • 0020583547 scopus 로고
    • Interferon-induced resistance to the killing by NK cells: a preferential effect of IFN-gamma
    • Wallach D. Interferon-induced resistance to the killing by NK cells: a preferential effect of IFN-gamma. Cell Immunol 1983, 75:390-395.
    • (1983) Cell Immunol , vol.75 , pp. 390-395
    • Wallach, D.1
  • 8
    • 0019929408 scopus 로고
    • Preferential effect of gamma interferon on the synthesis of HLA antigens and their mRNAs in human cells
    • Wallach D., Fellous M., Revel M. Preferential effect of gamma interferon on the synthesis of HLA antigens and their mRNAs in human cells. Nature 1982, 299:833-836.
    • (1982) Nature , vol.299 , pp. 833-836
    • Wallach, D.1    Fellous, M.2    Revel, M.3
  • 9
    • 0020581129 scopus 로고
    • Enhanced release of lymphotoxins by interferon-treated cells
    • Wallach D., Hahn T. Enhanced release of lymphotoxins by interferon-treated cells. Cell Immunol 1983, 76:390-396.
    • (1983) Cell Immunol , vol.76 , pp. 390-396
    • Wallach, D.1    Hahn, T.2
  • 10
    • 0021321027 scopus 로고
    • Preparations of lymphotoxin induce resistance to their own cytotoxic effect
    • Wallach D. Preparations of lymphotoxin induce resistance to their own cytotoxic effect. J Immunol 1984, 132:2464-2469.
    • (1984) J Immunol , vol.132 , pp. 2464-2469
    • Wallach, D.1
  • 11
    • 0023221456 scopus 로고
    • Down regulation of the receptors for tumor necrosis factor by interleukin 1 and 4 beta-phorbol-12-myristate-13-acetate
    • Holtmann H., Wallach D. Down regulation of the receptors for tumor necrosis factor by interleukin 1 and 4 beta-phorbol-12-myristate-13-acetate. J Immunol 1987, 139:1161-1167.
    • (1987) J Immunol , vol.139 , pp. 1161-1167
    • Holtmann, H.1    Wallach, D.2
  • 12
    • 0023950524 scopus 로고
    • Interrelated effects of tumor necrosis factor and interleukin 1 on cell viability
    • Holtmann H., Hahn T., Wallach D. Interrelated effects of tumor necrosis factor and interleukin 1 on cell viability. Immunobiology 1988, 177:7-22.
    • (1988) Immunobiology , vol.177 , pp. 7-22
    • Holtmann, H.1    Hahn, T.2    Wallach, D.3
  • 13
    • 0342388877 scopus 로고
    • Use of monoclonal antibodies to a human cytotoxin for its isolation and for examining the self-induction of resistance to this protein
    • Hahn T., Toker L., Budilovsky S., Aderka D., Eshhar Z., Wallach D. Use of monoclonal antibodies to a human cytotoxin for its isolation and for examining the self-induction of resistance to this protein. Proc Natl Acad Sci USA 1985, 82:3814-3818.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3814-3818
    • Hahn, T.1    Toker, L.2    Budilovsky, S.3    Aderka, D.4    Eshhar, Z.5    Wallach, D.6
  • 14
    • 0025082527 scopus 로고
    • Antibodies to a soluble form of a tumor necrosis factor (TNF) receptor have TNF-like activity
    • Engelmann H., Holtmann H., Brakebusch C., Avni Y.S., Sarov I., Nophar Y., et al. Antibodies to a soluble form of a tumor necrosis factor (TNF) receptor have TNF-like activity. J Biol Chem. 1990, 265:14497-14504.
    • (1990) J Biol Chem. , vol.265 , pp. 14497-14504
    • Engelmann, H.1    Holtmann, H.2    Brakebusch, C.3    Avni, Y.S.4    Sarov, I.5    Nophar, Y.6
  • 15
    • 0022614133 scopus 로고
    • Binding of human TNF-alpha to high-affinity cell surface receptors: effect of IFN
    • Israel S., Hahn T., Holtmann H., Wallach D. Binding of human TNF-alpha to high-affinity cell surface receptors: effect of IFN. Immunol Lett 1986, 12:217-224.
    • (1986) Immunol Lett , vol.12 , pp. 217-224
    • Israel, S.1    Hahn, T.2    Holtmann, H.3    Wallach, D.4
  • 16
    • 0024307648 scopus 로고
    • A tumor necrosis factor-binding protein purified to homogeneity from human urine protects cells from tumor necrosis factor toxicity
    • Engelmann H., Aderka D., Rubinstein M., Rotman D., Wallach D. A tumor necrosis factor-binding protein purified to homogeneity from human urine protects cells from tumor necrosis factor toxicity. J Biol Chem 1989, 264:11974-11980.
    • (1989) J Biol Chem , vol.264 , pp. 11974-11980
    • Engelmann, H.1    Aderka, D.2    Rubinstein, M.3    Rotman, D.4    Wallach, D.5
  • 17
    • 0025165135 scopus 로고
    • Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors
    • Engelmann H., Novick D., Wallach D. Two tumor necrosis factor-binding proteins purified from human urine. Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors. J Biol Chem 1990, 265:1531-1536.
    • (1990) J Biol Chem , vol.265 , pp. 1531-1536
    • Engelmann, H.1    Novick, D.2    Wallach, D.3
  • 18
    • 0025113598 scopus 로고
    • Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R cloned using amino acid data of its soluble form, encodes for both the cell surface and a soluble form of the receptor
    • Nophar Y., Kemper O., Brakebusch C., Engelmann H., Zwang R., Aderka D., et al. Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R cloned using amino acid data of its soluble form, encodes for both the cell surface and a soluble form of the receptor. EMBO J 1990, 9:3269-3278.
    • (1990) EMBO J , vol.9 , pp. 3269-3278
    • Nophar, Y.1    Kemper, O.2    Brakebusch, C.3    Engelmann, H.4    Zwang, R.5    Aderka, D.6
  • 19
    • 0026563754 scopus 로고
    • Cytoplasmic truncation of the p55 tumour necrosis factor (TNF) receptor abolishes signalling, but not induced shedding of the receptor
    • Brakebusch C., Nophar Y., Kemper O., Engelmann H., Wallach D. Cytoplasmic truncation of the p55 tumour necrosis factor (TNF) receptor abolishes signalling, but not induced shedding of the receptor. EMBO J. 1992, 11:943-950.
    • (1992) EMBO J. , vol.11 , pp. 943-950
    • Brakebusch, C.1    Nophar, Y.2    Kemper, O.3    Engelmann, H.4    Wallach, D.5
  • 20
    • 0028588080 scopus 로고
    • Structural requirements for inducible shedding of the p55 tumor necrosis factor receptor
    • Brakebusch C., Varfolomeev E.E., Batkin M., Wallach D. Structural requirements for inducible shedding of the p55 tumor necrosis factor receptor. J Biol Chem 1994, 269:32488-32496.
    • (1994) J Biol Chem , vol.269 , pp. 32488-32496
    • Brakebusch, C.1    Varfolomeev, E.E.2    Batkin, M.3    Wallach, D.4
  • 21
    • 0028985261 scopus 로고
    • Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects
    • Boldin M.P., Mett I.L., Varfolomeev E.E., Chumakov I., Shemer A.Y., Camonis J.H., et al. Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects. J Biol Chem 1995, 270:387-391.
    • (1995) J Biol Chem , vol.270 , pp. 387-391
    • Boldin, M.P.1    Mett, I.L.2    Varfolomeev, E.E.3    Chumakov, I.4    Shemer, A.Y.5    Camonis, J.H.6
  • 22
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin M.P., Varfolomeev E.E., Pancer Z., Mett I.L., Camonis J.H., Wallach D. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J Biol Chem 1995, 270:7795-7798.
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 23
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 1996, 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
  • 24
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1
    • Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D. MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1. Nature 1997, 385:540-544.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 25
    • 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 S.Q., Kovalenko A., Cantarella G., Wallach D. Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation. Immunity 2000, 12:301-311.
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 26
    • 5644302162 scopus 로고    scopus 로고
    • Receptor-specific signaling for both the alternative and the canonical NF-kappaB activation pathways by NF-kappaB-inducing kinase
    • Ramakrishnan P., Wang W., Wallach D. Receptor-specific signaling for both the alternative and the canonical NF-kappaB activation pathways by NF-kappaB-inducing kinase. Immunity 2004, 21:477-489.
    • (2004) Immunity , vol.21 , pp. 477-489
    • Ramakrishnan, P.1    Wang, W.2    Wallach, D.3
  • 27
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko A., Chable-Bessia C., Cantarella G., Israel A., Wallach D., Courtois G. The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 2003, 424:801-805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 29
    • 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 E.E., Schuchmann M., Luria V., Chiannilkulchai N., Beckmann J.S., Mett I.L., et al. 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 1998, 9:267-276.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3    Chiannilkulchai, N.4    Beckmann, J.S.5    Mett, I.L.6
  • 31
    • 52149095957 scopus 로고    scopus 로고
    • Mutation of a self-processing site in caspase-8 compromises its apoptotic but not its nonapoptotic functions in bacterial artificial chromosome-transgenic mice
    • Kang T.B., Oh G.-S., Scandella E., Bolinger B., Ludewig B., Kovalenko A., et al. Mutation of a self-processing site in caspase-8 compromises its apoptotic but not its nonapoptotic functions in bacterial artificial chromosome-transgenic mice. J Immunol 2008, 181:2522-2532.
    • (2008) J Immunol , vol.181 , pp. 2522-2532
    • Kang, T.B.1    Oh, G.-S.2    Scandella, E.3    Bolinger, B.4    Ludewig, B.5    Kovalenko, A.6
  • 32
    • 70350484946 scopus 로고    scopus 로고
    • Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease
    • Kovalenko A., Kim J.C., Kang T.B., Rajput A., Bogdanov K., Dittrich-Breiholz O., et al. Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease. J Exp Med 2009, 206:2161-2177.
    • (2009) J Exp Med , vol.206 , pp. 2161-2177
    • Kovalenko, A.1    Kim, J.C.2    Kang, T.B.3    Rajput, A.4    Bogdanov, K.5    Dittrich-Breiholz, O.6
  • 33
    • 79952770123 scopus 로고    scopus 로고
    • RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein
    • Rajput A., Kovalenko A., Bogdanov K., Yang S.H., Kang T.B., Kim J.C., et al. RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein. Immunity 2011, 34:340-351.
    • (2011) Immunity , vol.34 , pp. 340-351
    • Rajput, A.1    Kovalenko, A.2    Bogdanov, K.3    Yang, S.H.4    Kang, T.B.5    Kim, J.C.6
  • 34
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • Kang T.B., Yang S.H., Toth B., Kovalenko A., Wallach D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 2013, 38:27-40.
    • (2013) Immunity , vol.38 , pp. 27-40
    • Kang, T.B.1    Yang, S.H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.