메뉴 건너뛰기




Volumn 37, Issue 2, 2007, Pages 101-107

Three is better than one: Pre-ligand receptor assembly in the regulation of TNF receptor signaling

Author keywords

Apoptosis; PLAD; Pre ligand assembly domain; TNF; TRAIL

Indexed keywords

LIGAND; OLIGOMER; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 34247899117     PISSN: 10434666     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cyto.2007.03.005     Document Type: Review
Times cited : (148)

References (58)
  • 1
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signaling via EGF and FGF receptors
    • Schlessinger J. Common and distinct elements in cellular signaling via EGF and FGF receptors. Science 306 (2004) 1506-1507
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 3
    • 0035752146 scopus 로고    scopus 로고
    • Cytokines and immunodeficiency diseases
    • Leonard W.J. Cytokines and immunodeficiency diseases. Nat Rev Immunol 1 (2001) 200-208
    • (2001) Nat Rev Immunol , vol.1 , pp. 200-208
    • Leonard, W.J.1
  • 4
    • 0033725002 scopus 로고    scopus 로고
    • Signaling by the TNF receptor superfamily and T cell homeostasis
    • Chan F.K., Siegel M.R., and Lenardo J.M. Signaling by the TNF receptor superfamily and T cell homeostasis. Immunity 13 (2000) 419-422
    • (2000) Immunity , vol.13 , pp. 419-422
    • Chan, F.K.1    Siegel, M.R.2    Lenardo, J.M.3
  • 5
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: integrating mammalian biology
    • Locksley R.M., Killeen N., and Lenardo M.J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104 (2001) 487-501
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 6
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kDa TNF receptor-human TNF beta complex: implications for TNF receptor activation
    • Banner D.W., D'Arcy A., Janes W., Gentz R., Schoenfeld H.J., Broger C., et al. Crystal structure of the soluble human 55 kDa TNF receptor-human TNF beta complex: implications for TNF receptor activation. Cell 73 (1993) 431-445
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.J.5    Broger, C.6
  • 7
    • 0034613295 scopus 로고    scopus 로고
    • Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity
    • Cha S.S., Sung B.J., Kim Y.A., Song Y.L., Kim H.J., Kim S., et al. Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity. J Biol Chem 275 (2000) 31171-31177
    • (2000) J Biol Chem , vol.275 , pp. 31171-31177
    • Cha, S.S.1    Sung, B.J.2    Kim, Y.A.3    Song, Y.L.4    Kim, H.J.5    Kim, S.6
  • 8
    • 0033212968 scopus 로고    scopus 로고
    • Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5
    • Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., Kelley R.F., et al. Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5. Mol Cell 4 (1999) 563-571
    • (1999) Mol Cell , vol.4 , pp. 563-571
    • Hymowitz, S.G.1    Christinger, H.W.2    Fuh, G.3    Ultsch, M.4    O'Connell, M.5    Kelley, R.F.6
  • 9
    • 0032750511 scopus 로고    scopus 로고
    • Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation
    • Mongkolsapaya J., Grimes J.M., Chen N., Xu X.N., Stuart D.I., Jones E.Y., et al. Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation. Nat Struct Biol 6 (1999) 1048-1053
    • (1999) Nat Struct Biol , vol.6 , pp. 1048-1053
    • Mongkolsapaya, J.1    Grimes, J.M.2    Chen, N.3    Xu, X.N.4    Stuart, D.I.5    Jones, E.Y.6
  • 10
    • 0028985261 scopus 로고
    • Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects
    • Boldin M.P., Mett I.L., Varfolomeev E.E., Chumakov I., Shemer-Avni Y., Camonis J.H., 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 270 (1995) 387-391
    • (1995) J Biol Chem , vol.270 , pp. 387-391
    • Boldin, M.P.1    Mett, I.L.2    Varfolomeev, E.E.3    Chumakov, I.4    Shemer-Avni, Y.5    Camonis, J.H.6
  • 11
    • 0026751717 scopus 로고
    • The p70 tumor necrosis factor receptor mediates cytotoxicity
    • Heller R.A., Song K., Fan N., and Chang D.J. The p70 tumor necrosis factor receptor mediates cytotoxicity. Cell 70 (1992) 47-56
    • (1992) Cell , vol.70 , pp. 47-56
    • Heller, R.A.1    Song, K.2    Fan, N.3    Chang, D.J.4
  • 12
    • 0032055981 scopus 로고    scopus 로고
    • Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-kappa B activation, and c-Jun kinase activation
    • Haridas V., Darnay B.G., Natarajan K., Heller R., and Aggarwal B.B. Overexpression of the p80 TNF receptor leads to TNF-dependent apoptosis, nuclear factor-kappa B activation, and c-Jun kinase activation. J Immunol 160 (1998) 3152-3162
    • (1998) J Immunol , vol.160 , pp. 3152-3162
    • Haridas, V.1    Darnay, B.G.2    Natarajan, K.3    Heller, R.4    Aggarwal, B.B.5
  • 13
    • 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., Muhlenbeck F., Durkop H., Pfizenmaier K., et al. TNFR80-dependent enhancement of TNFR60-induced cell death is mediated by TNFR-associated factor 2 and is specific for TNFR60. J Immunol 161 (1998) 3136-3142
    • (1998) J Immunol , vol.161 , pp. 3136-3142
    • Weiss, T.1    Grell, M.2    Siemienski, K.3    Muhlenbeck, F.4    Durkop, H.5    Pfizenmaier, K.6
  • 14
    • 0031803058 scopus 로고    scopus 로고
    • Cooperation of both TNF receptors in inducing apoptosis: involvement of the TNF receptor-associated factor binding domain of the TNF receptor 75
    • Declercq W., Denecker G., Fiers W., and Vandenabeele P. Cooperation of both TNF receptors in inducing apoptosis: involvement of the TNF receptor-associated factor binding domain of the TNF receptor 75. J Immunol 161 (1998) 390-399
    • (1998) J Immunol , vol.161 , pp. 390-399
    • Declercq, W.1    Denecker, G.2    Fiers, W.3    Vandenabeele, P.4
  • 15
    • 0033965946 scopus 로고    scopus 로고
    • A crucial role for p80 TNF-R2 in amplifying p60 TNF-R1 apoptosis signals in T lymphocytes
    • Chan F.K., and Lenardo M.J. A crucial role for p80 TNF-R2 in amplifying p60 TNF-R1 apoptosis signals in T lymphocytes. Eur J Immunol 30 (2000) 652-660
    • (2000) Eur J Immunol , vol.30 , pp. 652-660
    • Chan, F.K.1    Lenardo, M.J.2
  • 16
    • 0347065342 scopus 로고    scopus 로고
    • A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses
    • Chan F.K., Shisler J., Bixby J.G., Felices M., Zheng L., Appel M., et al. A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses. J Biol Chem 278 (2003) 51613-51621
    • (2003) J Biol Chem , vol.278 , pp. 51613-51621
    • Chan, F.K.1    Shisler, J.2    Bixby, J.G.3    Felices, M.4    Zheng, L.5    Appel, M.6
  • 17
    • 33644821878 scopus 로고    scopus 로고
    • Causes and consequences of the autoimmune lymphoproliferative syndrome
    • Rao V.K., and Straus S.E. Causes and consequences of the autoimmune lymphoproliferative syndrome. Hematology 11 (2006) 15-23
    • (2006) Hematology , vol.11 , pp. 15-23
    • Rao, V.K.1    Straus, S.E.2
  • 18
    • 0034574306 scopus 로고    scopus 로고
    • The multifaceted role of Fas signaling in immune cell homeostasis and autoimmunity
    • Siegel R.M., Chan F.K., Chun H.J., and Lenardo M.J. The multifaceted role of Fas signaling in immune cell homeostasis and autoimmunity. Nat Immunol 1 (2000) 469-474
    • (2000) Nat Immunol , vol.1 , pp. 469-474
    • Siegel, R.M.1    Chan, F.K.2    Chun, H.J.3    Lenardo, M.J.4
  • 19
    • 0034733584 scopus 로고    scopus 로고
    • Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    • Siegel R.M., Frederiksen J.K., Zacharias D.A., Chan F.K., Johnson M., Lynch D., et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 288 (2000) 2354-2357
    • (2000) Science , vol.288 , pp. 2354-2357
    • Siegel, R.M.1    Frederiksen, J.K.2    Zacharias, D.A.3    Chan, F.K.4    Johnson, M.5    Lynch, D.6
  • 20
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    • Chan F.K., Chun H.J., Zheng L., Siegel R.M., Bui K.L., and Lenardo M.J. A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science 288 (2000) 2351-2354
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.1    Chun, H.J.2    Zheng, L.3    Siegel, R.M.4    Bui, K.L.5    Lenardo, M.J.6
  • 21
    • 0033621336 scopus 로고    scopus 로고
    • Identification and characterization of a ligand-independent oligomerization domain in the extracellular region of the CD95 death receptor
    • Papoff G., Hausler P., Eramo A., Pagano M.G., Di Leve G., Signore A., et al. Identification and characterization of a ligand-independent oligomerization domain in the extracellular region of the CD95 death receptor. J Biol Chem 274 (1999) 38241-38250
    • (1999) J Biol Chem , vol.274 , pp. 38241-38250
    • Papoff, G.1    Hausler, P.2    Eramo, A.3    Pagano, M.G.4    Di Leve, G.5    Signore, A.6
  • 23
    • 0029069758 scopus 로고
    • Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor
    • Naismith J.H., Devine T.Q., Brandhuber B.J., and Sprang S.R. Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor. J Biol Chem 270 (1995) 13303-13307
    • (1995) J Biol Chem , vol.270 , pp. 13303-13307
    • Naismith, J.H.1    Devine, T.Q.2    Brandhuber, B.J.3    Sprang, S.R.4
  • 24
    • 0030589099 scopus 로고    scopus 로고
    • Structures of the extracellular domain of the type I tumor necrosis factor receptor
    • Naismith J.H., Devine T.Q., Kohno T., and Sprang S.R. Structures of the extracellular domain of the type I tumor necrosis factor receptor. Structure 4 (1996) 1251-1262
    • (1996) Structure , vol.4 , pp. 1251-1262
    • Naismith, J.H.1    Devine, T.Q.2    Kohno, T.3    Sprang, S.R.4
  • 25
    • 0035421133 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein
    • Chan F.K., Siegel R.M., Zacharias D., Swofford R., Holmes K.L., Tsien R.Y., et al. Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein. Cytometry 44 (2001) 361-368
    • (2001) Cytometry , vol.44 , pp. 361-368
    • Chan, F.K.1    Siegel, R.M.2    Zacharias, D.3    Swofford, R.4    Holmes, K.L.5    Tsien, R.Y.6
  • 26
    • 29144496895 scopus 로고    scopus 로고
    • Preligand assembly domain-mediated ligand-independent association between TRAIL receptor 4 (TR4) and TR2 regulates TRAIL-induced apoptosis
    • Clancy L., Mruk K., Archer K., Woelfel M., Mongkolsapaya J., Screaton G., et al. Preligand assembly domain-mediated ligand-independent association between TRAIL receptor 4 (TR4) and TR2 regulates TRAIL-induced apoptosis. Proc Natl Acad Sci USA 102 (2005) 18099-18104
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18099-18104
    • Clancy, L.1    Mruk, K.2    Archer, K.3    Woelfel, M.4    Mongkolsapaya, J.5    Screaton, G.6
  • 27
    • 33748511011 scopus 로고    scopus 로고
    • Poxvirus tumor necrosis factor receptor (TNFR)-like T2 proteins contain a conserved preligand assembly domain that inhibits cellular TNFR1-induced cell death
    • Sedger L.M., Osvath S.R., Xu X.M., Li G., Chan F.K., Barrett J.W., et al. Poxvirus tumor necrosis factor receptor (TNFR)-like T2 proteins contain a conserved preligand assembly domain that inhibits cellular TNFR1-induced cell death. J Virol 80 (2006) 9300-9309
    • (2006) J Virol , vol.80 , pp. 9300-9309
    • Sedger, L.M.1    Osvath, S.R.2    Xu, X.M.3    Li, G.4    Chan, F.K.5    Barrett, J.W.6
  • 28
    • 0037846097 scopus 로고    scopus 로고
    • BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site
    • Gordon N.C., Pan B., Hymowitz S.G., Yin J., Kelley R.F., Cochran A.G., et al. BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site. Biochemistry 42 (2003) 5977-5983
    • (2003) Biochemistry , vol.42 , pp. 5977-5983
    • Gordon, N.C.1    Pan, B.2    Hymowitz, S.G.3    Yin, J.4    Kelley, R.F.5    Cochran, A.G.6
  • 29
    • 0030465072 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
    • Huang B., Eberstadt M., Olejniczak E.T., Meadows R.P., and Fesik S.W. NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain. Nature 384 (1996) 638-641
    • (1996) Nature , vol.384 , pp. 638-641
    • Huang, B.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Fesik, S.W.5
  • 30
    • 13044282468 scopus 로고    scopus 로고
    • Defective CD95/APO-1/Fas signal complex formation in the human autoimmune lymphoproliferative syndrome, type Ia
    • Martin D.A., Zheng L., Siegel R.M., Huang B., Fisher G.H., Wang J., et al. Defective CD95/APO-1/Fas signal complex formation in the human autoimmune lymphoproliferative syndrome, type Ia. Proc Natl Acad Sci USA 96 (1999) 4552-4557
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4552-4557
    • Martin, D.A.1    Zheng, L.2    Siegel, R.M.3    Huang, B.4    Fisher, G.H.5    Wang, J.6
  • 31
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park Y.C., Burkitt V., Villa A.R., Tong L., and Wu H. Structural basis for self-association and receptor recognition of human TRAF2. Nature 398 (1999) 533-538
    • (1999) Nature , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3    Tong, L.4    Wu, H.5
  • 32
    • 0033197872 scopus 로고    scopus 로고
    • The structural basis for the recognition of diverse receptor sequences by TRAF2
    • Ye H., Park Y.C., Kreishman M., Kieff E., and Wu H. The structural basis for the recognition of diverse receptor sequences by TRAF2. Mol Cell 4 (1999) 321-330
    • (1999) Mol Cell , vol.4 , pp. 321-330
    • Ye, H.1    Park, Y.C.2    Kreishman, M.3    Kieff, E.4    Wu, H.5
  • 34
    • 0034705271 scopus 로고    scopus 로고
    • A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction
    • Park Y.C., Ye H., Hsia C., Segal D., Rich R.L., Liou H.C., et al. A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Cell 101 (2000) 777-787
    • (2000) Cell , vol.101 , pp. 777-787
    • Park, Y.C.1    Ye, H.2    Hsia, C.3    Segal, D.4    Rich, R.L.5    Liou, H.C.6
  • 35
    • 9444268061 scopus 로고    scopus 로고
    • SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane
    • Siegel R.M., Muppidi J.R., Sarker M., Lobito A., Jen M., Martin D., et al. SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane. J Cell Biol 167 (2004) 735-744
    • (2004) J Cell Biol , vol.167 , pp. 735-744
    • Siegel, R.M.1    Muppidi, J.R.2    Sarker, M.3    Lobito, A.4    Jen, M.5    Martin, D.6
  • 36
    • 33846247103 scopus 로고    scopus 로고
    • Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling
    • Feig C., Tchikov V., Schutze S., and Peter M.E. Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling. EMBO J 26 (2007) 221-231
    • (2007) EMBO J , vol.26 , pp. 221-231
    • Feig, C.1    Tchikov, V.2    Schutze, S.3    Peter, M.E.4
  • 37
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang Y., Woronicz J.D., Liu W., and Goeddel D.V. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 283 (1999) 543-546
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 38
    • 33344476184 scopus 로고    scopus 로고
    • cFLIP regulation of lymphocyte activation and development
    • Budd R.C., Yeh W.C., and Tschopp J. cFLIP regulation of lymphocyte activation and development. Nat Rev Immunol 6 (2006) 196-204
    • (2006) Nat Rev Immunol , vol.6 , pp. 196-204
    • Budd, R.C.1    Yeh, W.C.2    Tschopp, J.3
  • 39
    • 0030949563 scopus 로고    scopus 로고
    • Resistance of cultured peripheral T cells towards activation-induced cell death involves a lack of recruitment of FLICE (MACH/caspase 8) to the CD95 death-inducing signaling complex
    • Peter M.E., Kischkel F.C., Scheuerpflug C.G., Medema J.P., Debatin K.M., and Krammer P.H. Resistance of cultured peripheral T cells towards activation-induced cell death involves a lack of recruitment of FLICE (MACH/caspase 8) to the CD95 death-inducing signaling complex. Eur J Immunol 27 (1997) 1207-1212
    • (1997) Eur J Immunol , vol.27 , pp. 1207-1212
    • Peter, M.E.1    Kischkel, F.C.2    Scheuerpflug, C.G.3    Medema, J.P.4    Debatin, K.M.5    Krammer, P.H.6
  • 41
    • 1142287412 scopus 로고    scopus 로고
    • Ligand-independent redistribution of Fas (CD95) into lipid rafts mediates clonotypic T cell death
    • Muppidi J.R., and Siegel R.M. Ligand-independent redistribution of Fas (CD95) into lipid rafts mediates clonotypic T cell death. Nat Immunol 5 (2004) 182-189
    • (2004) Nat Immunol , vol.5 , pp. 182-189
    • Muppidi, J.R.1    Siegel, R.M.2
  • 42
    • 0031572509 scopus 로고    scopus 로고
    • Maintenance of clonotype specificity in CD95/Apo-1/Fas-mediated apoptosis of mature T lymphocytes
    • Hornung F., Zheng L., and Lenardo M.J. Maintenance of clonotype specificity in CD95/Apo-1/Fas-mediated apoptosis of mature T lymphocytes. J Immunol 159 (1997) 3816-3822
    • (1997) J Immunol , vol.159 , pp. 3816-3822
    • Hornung, F.1    Zheng, L.2    Lenardo, M.J.3
  • 43
    • 19244387337 scopus 로고    scopus 로고
    • Differential TCR signaling regulates apoptosis and immunopathology during antigen responses in vivo
    • Combadiere B., Reis e Sousa C., Trageser C., Zheng L.X., Kim C.R., and Lenardo M.J. Differential TCR signaling regulates apoptosis and immunopathology during antigen responses in vivo. Immunity 9 (1998) 305-313
    • (1998) Immunity , vol.9 , pp. 305-313
    • Combadiere, B.1    Reis e Sousa, C.2    Trageser, C.3    Zheng, L.X.4    Kim, C.R.5    Lenardo, M.J.6
  • 44
    • 0033007321 scopus 로고    scopus 로고
    • Mature T lymphocyte apoptosis-immune regulation in a dynamic and unpredictable antigenic environment
    • Lenardo M., Chan K.M., Hornung F., McFarland H., Siegel R., Wang J., et al. Mature T lymphocyte apoptosis-immune regulation in a dynamic and unpredictable antigenic environment. Annu Rev Immunol 17 (1999) 221-253
    • (1999) Annu Rev Immunol , vol.17 , pp. 221-253
    • Lenardo, M.1    Chan, K.M.2    Hornung, F.3    McFarland, H.4    Siegel, R.5    Wang, J.6
  • 45
    • 0038320035 scopus 로고    scopus 로고
    • Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy
    • Almasan A., and Ashkenazi A. Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy. Cytokine Growth Factor Rev 14 (2003) 337-348
    • (2003) Cytokine Growth Factor Rev , vol.14 , pp. 337-348
    • Almasan, A.1    Ashkenazi, A.2
  • 46
    • 17044382532 scopus 로고    scopus 로고
    • Homomeric and heteromeric interactions of the extracellular domains of death receptors and death decoy receptors
    • Lee H.W., Lee S.H., Lee H.W., Ryu Y.W., Kwon M.H., and Kim Y.S. Homomeric and heteromeric interactions of the extracellular domains of death receptors and death decoy receptors. Biochem Biophys Res Commun 330 (2005) 1205-1212
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 1205-1212
    • Lee, H.W.1    Lee, S.H.2    Lee, H.W.3    Ryu, Y.W.4    Kwon, M.H.5    Kim, Y.S.6
  • 47
    • 33646016305 scopus 로고    scopus 로고
    • The generation of protective memory-like CD8(+) T cells during homeostatic proliferation requires CD4(+) T cells
    • Hamilton S.E., Wolkers M.C., Schoenberger S.P., and Jameson S.C. The generation of protective memory-like CD8(+) T cells during homeostatic proliferation requires CD4(+) T cells. Nat Immunol 7 (2006) 475-481
    • (2006) Nat Immunol , vol.7 , pp. 475-481
    • Hamilton, S.E.1    Wolkers, M.C.2    Schoenberger, S.P.3    Jameson, S.C.4
  • 48
    • 14544288632 scopus 로고    scopus 로고
    • CD4+ T-cell help controls CD8+ T-cell memory via TRAIL-mediated activation-induced cell death
    • Janssen E.M., Droin N.M., Lemmens E.E., Pinkoski M.J., Bensinger S.J., Ehst B.D., et al. CD4+ T-cell help controls CD8+ T-cell memory via TRAIL-mediated activation-induced cell death. Nature 434 (2005) 88-93
    • (2005) Nature , vol.434 , pp. 88-93
    • Janssen, E.M.1    Droin, N.M.2    Lemmens, E.E.3    Pinkoski, M.J.4    Bensinger, S.J.5    Ehst, B.D.6
  • 49
    • 0035863835 scopus 로고    scopus 로고
    • Roles of TNF-related apoptosis-inducing ligand in experimental autoimmune encephalomyelitis
    • Hilliard B., Wilmen A., Seidel C., Liu T.S., Goke R., and Chen Y. Roles of TNF-related apoptosis-inducing ligand in experimental autoimmune encephalomyelitis. J Immunol 166 (2001) 1314-1319
    • (2001) J Immunol , vol.166 , pp. 1314-1319
    • Hilliard, B.1    Wilmen, A.2    Seidel, C.3    Liu, T.S.4    Goke, R.5    Chen, Y.6
  • 50
    • 0041820127 scopus 로고    scopus 로고
    • Critical roles of tumor necrosis factor-related apoptosis-inducing ligand in type 1 diabetes
    • Lamhamedi-Cherradi S.E., Zheng S., Tisch R.M., and Chen Y.H. Critical roles of tumor necrosis factor-related apoptosis-inducing ligand in type 1 diabetes. Diabetes 52 (2003) 2274-2278
    • (2003) Diabetes , vol.52 , pp. 2274-2278
    • Lamhamedi-Cherradi, S.E.1    Zheng, S.2    Tisch, R.M.3    Chen, Y.H.4
  • 52
    • 0041765727 scopus 로고    scopus 로고
    • Blockade of tumor necrosis factor-related apoptosis-inducing ligand exacerbates type 1 diabetes in NOD mice
    • Mi Q.S., Ly D., Lamhamedi-Cherradi S.E., Salojin K.V., Zhou L., Grattan M., et al. Blockade of tumor necrosis factor-related apoptosis-inducing ligand exacerbates type 1 diabetes in NOD mice. Diabetes 52 (2003) 1967-1975
    • (2003) Diabetes , vol.52 , pp. 1967-1975
    • Mi, Q.S.1    Ly, D.2    Lamhamedi-Cherradi, S.E.3    Salojin, K.V.4    Zhou, L.5    Grattan, M.6
  • 53
    • 0034599757 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is an inhibitor of autoimmune inflammation and cell cycle progression
    • Song K., Chen Y., Goke R., Wilmen A., Seidel C., Goke A., et al. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is an inhibitor of autoimmune inflammation and cell cycle progression. J Exp Med 191 (2000) 1095-1104
    • (2000) J Exp Med , vol.191 , pp. 1095-1104
    • Song, K.1    Chen, Y.2    Goke, R.3    Wilmen, A.4    Seidel, C.5    Goke, A.6
  • 54
    • 29144522877 scopus 로고    scopus 로고
    • TNF-related apoptosis-inducing ligand (TRAIL)/Apo2L suppresses experimental autoimmune encephalomyelitis in mice
    • Cretney E., McQualter J.L., Kayagaki N., Yagita H., Bernard C.C., Grewal I.S., et al. TNF-related apoptosis-inducing ligand (TRAIL)/Apo2L suppresses experimental autoimmune encephalomyelitis in mice. Immunol Cell Biol 83 (2005) 511-519
    • (2005) Immunol Cell Biol , vol.83 , pp. 511-519
    • Cretney, E.1    McQualter, J.L.2    Kayagaki, N.3    Yagita, H.4    Bernard, C.C.5    Grewal, I.S.6
  • 55
    • 0036852215 scopus 로고    scopus 로고
    • To kill or be killed: viral evasion of apoptosis
    • Benedict C.A., Norris P.S., and Ware C.F. To kill or be killed: viral evasion of apoptosis. Nat Immunol 3 (2002) 1013-1018
    • (2002) Nat Immunol , vol.3 , pp. 1013-1018
    • Benedict, C.A.1    Norris, P.S.2    Ware, C.F.3
  • 56
    • 0029971614 scopus 로고    scopus 로고
    • Expression of the myxoma virus tumor necrosis factor receptor homologue and M11L genes is required to prevent virus-induced apoptosis in infected rabbit T lymphocytes
    • Macen J.L., Graham K.A., Lee S.F., Schreiber M., Boshkov L.K., and McFadden G. Expression of the myxoma virus tumor necrosis factor receptor homologue and M11L genes is required to prevent virus-induced apoptosis in infected rabbit T lymphocytes. Virology 218 (1996) 232-237
    • (1996) Virology , vol.218 , pp. 232-237
    • Macen, J.L.1    Graham, K.A.2    Lee, S.F.3    Schreiber, M.4    Boshkov, L.K.5    McFadden, G.6
  • 57
    • 0033758294 scopus 로고    scopus 로고
    • The pre-ligand binding assembly domain: a potential target of inhibition of tumour necrosis factor receptor function
    • Chan F.K. The pre-ligand binding assembly domain: a potential target of inhibition of tumour necrosis factor receptor function. Ann Rheum Dis 59 Suppl 1 (2000) i50-i53
    • (2000) Ann Rheum Dis , vol.59 , Issue.SUPPL. 1
    • Chan, F.K.1
  • 58
    • 27144479900 scopus 로고    scopus 로고
    • Amelioration of inflammatory arthritis by targeting the pre-ligand assembly domain of tumor necrosis factor receptors
    • Deng G.M., Zheng L., Chan F.K., and Lenardo M. Amelioration of inflammatory arthritis by targeting the pre-ligand assembly domain of tumor necrosis factor receptors. Nat Med 11 (2005) 1066-1072
    • (2005) Nat Med , vol.11 , pp. 1066-1072
    • Deng, G.M.1    Zheng, L.2    Chan, F.K.3    Lenardo, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.