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Volumn 153, Issue 3, 2009, Pages 173-180

Signaling activated by the death receptors of the TNFR family

Author keywords

Apoptosis; Caspases; Death domain; DISC; Necroptosis

Indexed keywords

PYRONIA TITHONUS;

EID: 70349985256     PISSN: 12138118     EISSN: 12138118     Source Type: Journal    
DOI: 10.5507/bp.2009.029     Document Type: Article
Times cited : (38)

References (98)
  • 1
    • 63149163677 scopus 로고    scopus 로고
    • The role of TNF superfamily members in T-cell function and diseases
    • Croft M. The role of TNF superfamily members in T-cell function and diseases. Nat Rev Immunol 2009; 9: 271-85
    • (2009) Nat Rev Immunol , vol.9 , pp. 271-285
    • Croft, M.1
  • 2
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley RM, Killeen N and Lenardo MJ. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 2001; 104: 487-501
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 3
    • 62849093368 scopus 로고    scopus 로고
    • Death receptor signal transducers: Nodes of coordination in immune signaling networks
    • Wilson NS, Dixit V and Ashkenazi A. Death receptor signal transducers: nodes of coordination in immune signaling networks. Nat Immunol 2009; 10: 348-55
    • (2009) Nat Immunol , vol.10 , pp. 348-355
    • Wilson, N.S.1    Dixit, V.2    Ashkenazi, A.3
  • 6
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumournecrosis factor-alpha from cells
    • Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slack JL, Wolfson MF, et al. A metalloproteinase disintegrin that releases tumournecrosis factor-alpha from cells. Nature 1997; 385: 729-33
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slack, J.L.5    Wolfson, M.F.6
  • 7
    • 0030055168 scopus 로고    scopus 로고
    • Human pro-tumor necrosis factor is a homotrimer
    • Tang P, Hung MC and Klostergaard J. Human pro-tumor necrosis factor is a homotrimer. Biochemistry 1996; 35: 8216-25
    • (1996) Biochemistry , vol.35 , pp. 8216-8225
    • Tang, P.1    Hung, M.C.2    Klostergaard, J.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, Siegel RM, Bui KL and Lenardo MJ. A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science 2000; 288: 2351-4
    • (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
  • 9
    • 34247899117 scopus 로고    scopus 로고
    • Three is better than one: Pre-ligand receptor assembly in the regulation of TNF receptor signaling
    • Chan FK. Three is better than one: pre-ligand receptor assembly in the regulation of TNF receptor signaling. Cytokine 2007; 37: 101-7
    • (2007) Cytokine , vol.37 , pp. 101-107
    • Chan, F.K.1
  • 10
    • 0037090252 scopus 로고    scopus 로고
    • Restricted localization of the TNF receptor CD120a to lipid rafts: A novel role for the death domain
    • Cottin V, Doan JE and Riches DW. Restricted localization of the TNF receptor CD120a to lipid rafts: a novel role for the death domain. J Immunol 2002; 168: 4095-102
    • (2002) J Immunol , vol.168 , pp. 4095-4102
    • Cottin, V.1    Doan, J.E.2    Riches, D.W.3
  • 11
    • 0038742813 scopus 로고    scopus 로고
    • Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation
    • Legler DF, Micheau O, Doucey MA, Tschopp J and Bron C. Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation. Immunity 2003; 18: 655-64
    • (2003) Immunity , vol.18 , pp. 655-664
    • Legler, D.F.1    Micheau, O.2    Doucey, M.A.3    Tschopp, J.4    Bron, C.5
  • 13
    • 44749093460 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of TNFR1 signaling
    • Wertz IE and Dixit VM. Ubiquitin-mediated regulation of TNFR1 signaling. Cytokine Growth Factor Rev 2008; 19: 313-24
    • (2008) Cytokine Growth Factor Rev , vol.19 , pp. 313-324
    • Wertz, I.E.1    Dixit, V.M.2
  • 14
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • Lee TH, Shank J, Cusson N and Kelliher MA. The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J Biol Chem 2004; 279: 33185-91
    • (2004) J Biol Chem , vol.279 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3    Kelliher, M.A.4
  • 16
    • 54049155149 scopus 로고    scopus 로고
    • c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation
    • Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN, Zobel K, Deshayes K, et al. c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation. J Biol Chem 2008; 283: 24295-9
    • (2008) J Biol Chem , vol.283 , pp. 24295-24299
    • Varfolomeev, E.1    Goncharov, T.2    Fedorova, A.V.3    Dynek, J.N.4    Zobel, K.5    Deshayes, K.6
  • 17
    • 0035965232 scopus 로고    scopus 로고
    • Critical roles of TRAF2 and TRAF5 in tumor necrosis factorinduced NF-kappa B activation and protection from cell death
    • Tada K, Okazaki T, Sakon S, Kobarai T, Kurosawa K, Yamaoka S, et al. Critical roles of TRAF2 and TRAF5 in tumor necrosis factorinduced NF-kappa B activation and protection from cell death. J Biol Chem 2001; 276: 36530-4
    • (2001) J Biol Chem , vol.276 , pp. 36530-36534
    • Tada, K.1    Okazaki, T.2    Sakon, S.3    Kobarai, T.4    Kurosawa, K.5    Yamaoka, S.6
  • 18
    • 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, Kraunus J, Billia F, Wakeham A, et al. Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity 1997; 7: 715-25
    • (1997) Immunity , vol.7 , pp. 715-725
    • Yeh, W.C.1    Shahinian, A.2    Speiser, D.3    Kraunus, J.4    Billia, F.5    Wakeham, A.6
  • 19
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP, Pineda G and Chen ZJ. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 2006; 22: 245-57
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 20
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • Wu CJ, Conze DB, Li T, Srinivasula SM and Ashwell JD. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat Cell Biol 2006; 8: 398-406
    • (2006) Nat Cell Biol , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 21
    • 30044449755 scopus 로고    scopus 로고
    • TAK1 is recruited to the tumor necrosis factor-alpha (TNF-alpha) receptor 1 complex in a receptor-interacting protein (RIP)-dependent manner and cooperates with MEKK3 leading to NF-kappaB activation
    • Blonska M, Shambharkar PB, Kobayashi M, Zhang D, Sakurai H, Su B, et al. TAK1 is recruited to the tumor necrosis factor-alpha (TNF-alpha) receptor 1 complex in a receptor-interacting protein (RIP)-dependent manner and cooperates with MEKK3 leading to NF-kappaB activation. J Biol Chem 2005; 280: 43056-63
    • (2005) J Biol Chem , vol.280 , pp. 43056-43063
    • Blonska, M.1    Shambharkar, P.B.2    Kobayashi, M.3    Zhang, D.4    Sakurai, H.5    Su, B.6
  • 22
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • Karin M and Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 2000; 18: 621-63
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 23
    • 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, Libby SL, Chien M, Lodolce JP, et al. Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. Science 2000; 289: 2350-4
    • (2000) Science , vol.289 , pp. 2350-2354
    • Lee, E.G.1    Boone, D.L.2    Chai, S.3    Libby, S.L.4    Chien, M.5    Lodolce, J.P.6
  • 24
    • 34548405689 scopus 로고    scopus 로고
    • Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and LPS- mediated NF-kappaB and JNK signaling
    • Shembade N, Harhaj NS, Liebl DJ and Harhaj EW. Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and LPS- mediated NF-kappaB and JNK signaling. Embo J 2007; 26: 3910-22
    • (2007) Embo J , vol.26 , pp. 3910-3922
    • Shembade, N.1    Harhaj, N.S.2    Liebl, D.J.3    Harhaj, E.W.4
  • 25
    • 39449083378 scopus 로고    scopus 로고
    • The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20
    • Shembade N, Harhaj NS, Parvatiyar K, Copeland NG, Jenkins NA, Matesic LE, et al. The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20. Nat Immunol 2008; 9: 254-62
    • (2008) Nat Immunol , vol.9 , pp. 254-262
    • Shembade, N.1    Harhaj, N.S.2    Parvatiyar, K.3    Copeland, N.G.4    Jenkins, N.A.5    Matesic, L.E.6
  • 26
    • 61949220270 scopus 로고    scopus 로고
    • The ubi- quitin-editing enzyme A20 requires RNF11 to downregulate NF- kappaB signalling
    • Shembade N, Parvatiyar K, Harhaj NS and Harhaj EW. The ubi- quitin-editing enzyme A20 requires RNF11 to downregulate NF- kappaB signalling. Embo J 2009; 28: 513-22
    • (2009) Embo J , vol.28 , pp. 513-522
    • Shembade, N.1    Parvatiyar, K.2    Harhaj, N.S.3    Harhaj, E.W.4
  • 28
    • 2942731503 scopus 로고    scopus 로고
    • Siah2 regulates stability of prolyl-hydroxylases, controls HIF1alpha abundance, and modulates physiological responses to hypoxia
    • Nakayama K, Frew IJ, Hagensen M, Skals M, Habelhah H, Bhoumik A, et al. Siah2 regulates stability of prolyl-hydroxylases, controls HIF1alpha abundance, and modulates physiological responses to hypoxia. Cell 2004; 117: 941-52
    • (2004) Cell , vol.117 , pp. 941-952
    • Nakayama, K.1    Frew, I.J.2    Hagensen, M.3    Skals, M.4    Habelhah, H.5    Bhoumik, A.6
  • 29
    • 1942533472 scopus 로고    scopus 로고
    • Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth
    • McDonald ER, 3rd and El-Deiry WS. Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth. Proc Natl Acad Sci U S A 2004; 101: 6170-5
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6170-6175
    • McDonald III, E.R.1    El-Deiry, W.S.2
  • 30
    • 43049174900 scopus 로고    scopus 로고
    • CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation
    • Liao W, Xiao Q, Tchikov V, Fujita K, Yang W, Wincovitch S, et al. CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation. Curr Biol 2008; 18: 641-9
    • (2008) Curr Biol , vol.18 , pp. 641-649
    • Liao, W.1    Xiao, Q.2    Tchikov, V.3    Fujita, K.4    Yang, W.5    Wincovitch, S.6
  • 31
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp TR, Nijman SM, Dirac AM and Bernards R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 2003; 424: 797-801
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 32
    • 4344561190 scopus 로고    scopus 로고
    • NF-kappaB is essential for induction of CYLD, the negative regulator of NF-kappaB: Evidence for a novel inducible autoregulatory feedback pathway
    • Jono H, Lim JH, Chen LF, Xu H, Trompouki E, Pan ZK, et al. NF-kappaB is essential for induction of CYLD, the negative regulator of NF-kappaB: evidence for a novel inducible autoregulatory feedback pathway. J Biol Chem 2004; 279: 36171-4
    • (2004) J Biol Chem , vol.279 , pp. 36171-36174
    • Jono, H.1    Lim, J.H.2    Chen, L.F.3    Xu, H.4    Trompouki, E.5    Pan, Z.K.6
  • 33
  • 34
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O and Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003; 114: 181-90
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 35
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang L, Du F and Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 2008; 133: 693-703
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 36
    • 47749089820 scopus 로고    scopus 로고
    • Regulation of TNFR1 and CD95 signalling by receptor compartmentalization
    • Schutze S, Tchikov V and Schneider-Brachert W. Regulation of TNFR1 and CD95 signalling by receptor compartmentalization. Nat Rev Mol Cell Biol 2008; 9: 655-62
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 655-662
    • Schutze, S.1    Tchikov, V.2    Schneider-Brachert, W.3
  • 38
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M, et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 2009; 137: 1112-23
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1    Challa, S.2    Moquin, D.3    Genga, R.4    Ray, T.D.5    Guildford, M.6
  • 40
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev A, Huang Z, Boyce M, Li Y, Jagtap P, Mizushima N, et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol 2005; 1: 112-9
    • (2005) Nat Chem Biol , vol.1 , pp. 112-119
    • Degterev, A.1    Huang, Z.2    Boyce, M.3    Li, Y.4    Jagtap, P.5    Mizushima, N.6
  • 41
    • 57649181391 scopus 로고    scopus 로고
    • Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway
    • Hitomi J, Christofferson DE, Ng A, Yao J, Degterev A, Xavier RJ, et al. Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell 2008; 135: 1311-23
    • (2008) Cell , vol.135 , pp. 1311-1323
    • Hitomi, J.1    Christofferson, D.E.2    Ng, A.3    Yao, J.4    Degterev, A.5    Xavier, R.J.6
  • 42
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • Feng S, Yang Y, Mei Y, Ma L, Zhu DE, Hoti N, et al. Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell Signal 2007; 19: 2056-67
    • (2007) Cell Signal , vol.19 , pp. 2056-2067
    • Feng, S.1    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.E.5    Hoti, N.6
  • 43
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L, et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 2009; 137: 1100-11
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6
  • 44
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang DW, Shao J, Lin J, Zhang N, Lu BJ, Lin SC, et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 2009; 325: 332-6
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1    Shao, J.2    Lin, J.3    Zhang, N.4    Lu, B.J.5    Lin, S.C.6
  • 45
    • 0025916387 scopus 로고
    • The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis
    • Itoh N, Yonehara S, Ishii A, Yonehara M, Mizushima S, Sameshima M, et al. The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis. Cell 1991; 66: 233-43
    • (1991) Cell , vol.66 , pp. 233-243
    • Itoh, N.1    Yonehara, S.2    Ishii, A.3    Yonehara, M.4    Mizushima, S.5    Sameshima, M.6
  • 48
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley SR, Schooley K, Smolak PJ, Din WS, Huang CP, Nicholl JK, et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 1995; 3: 673-82
    • (1995) Immunity , vol.3 , pp. 673-682
    • Wiley, S.R.1    Smolak, P.J.2    Din, W.S.3    Huang, C.P.4    Nicholl, J.K.5
  • 49
    • 17444424930 scopus 로고    scopus 로고
    • Genomic amplification of a decoy receptor for Fas ligand in lung and colon cancer
    • Pitti RM, Marsters SA, Lawrence DA, Roy M, Kischkel FC, Dowd P, et al. Genomic amplification of a decoy receptor for Fas ligand in lung and colon cancer. Nature 1998; 396: 699-703
    • (1998) Nature , vol.396 , pp. 699-703
    • Pitti, R.M.1    Marsters, S.A.2    Lawrence, D.A.3    Roy, M.4    Kischkel, F.C.5    Dowd, P.6
  • 51
    • 14644406398 scopus 로고    scopus 로고
    • The flip side of FLIP
    • Peter ME. The flip side of FLIP. Biochem J 2004; 382: e1-3
    • (2004) Biochem J , vol.382
    • Peter, M.E.1
  • 52
    • 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 ME. Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling. Embo J 2007; 26: 221-31
    • (2007) Embo J , vol.26 , pp. 221-231
    • Feig, C.1    Tchikov, V.2    Schutze, S.3    Peter, M.E.4
  • 53
    • 34250331231 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis is not required for tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis
    • Kohlhaas SL, Craxton A, Sun XM, Pinkoski MJ and Cohen GM. Receptor-mediated endocytosis is not required for tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis. J Biol Chem 2007; 282: 12831-41
    • (2007) J Biol Chem , vol.282 , pp. 12831-12841
    • Kohlhaas, S.L.1    Craxton, A.2    Sun, X.M.3    Pinkoski, M.J.4    Cohen, G.M.5
  • 55
    • 34948894931 scopus 로고    scopus 로고
    • Death-receptor O-glycosylation controls tumorcell sensitivity to the proapoptotic ligand Apo2L/TRAIL
    • Wagner KW, Punnoose EA, Januario T, Lawrence DA, Pitti RM, Lancaster K, et al. Death-receptor O-glycosylation controls tumorcell sensitivity to the proapoptotic ligand Apo2L/TRAIL. Nat Med 2007; 13: 1070-7
    • (2007) Nat Med , vol.13 , pp. 1070-1077
    • Wagner, K.W.1    Punnoose, E.A.2    Januario, T.3    Lawrence, D.A.4    Pitti, R.M.5    Lancaster, K.6
  • 57
    • 69249208481 scopus 로고    scopus 로고
    • XIAP discriminates between type I and type II FAS- induced apoptosis
    • Jost PJ, Grabow S, Gray D, McKenzie MD, Nachbur U, Huang DC, et al. XIAP discriminates between type I and type II FAS- induced apoptosis. Nature 2009; 460: 1035-9
    • (2009) Nature , vol.460 , pp. 1035-1039
    • Jost, P.J.1    Grabow, S.2    Gray, D.3    McKenzie, M.D.4    Nachbur, U.5    Huang, D.C.6
  • 58
    • 0036859738 scopus 로고    scopus 로고
    • Defining characteristics of Types I and II apoptotic cells in response to TRAIL
    • Ozoren N and El-Deiry WS. Defining characteristics of Types I and II apoptotic cells in response to TRAIL. Neoplasia 2002; 4: 551-7
    • (2002) Neoplasia , vol.4 , pp. 551-557
    • Ozoren, N.1    El-Deiry, W.S.2
  • 59
    • 0032832881 scopus 로고    scopus 로고
    • Differences between CD95 type I and II cells detected with the CD95 ligand
    • Schmitz I, Walczak H, Krammer PH and Peter ME. Differences between CD95 type I and II cells detected with the CD95 ligand. Cell Death Differ 1999; 6: 821-2
    • (1999) Cell Death Differ , vol.6 , pp. 821-822
    • Schmitz, I.1    Walczak, H.2    Krammer, P.H.3    Peter, M.E.4
  • 60
    • 0033944665 scopus 로고    scopus 로고
    • Bid, a critical mediator for apoptosis induced by the activation of Fas/TNF-R1 death receptors in hepatocytes
    • Yin XM. Bid, a critical mediator for apoptosis induced by the activation of Fas/TNF-R1 death receptors in hepatocytes. J Mol Med 2000; 78: 203-11
    • (2000) J Mol Med , vol.78 , pp. 203-211
    • Yin, X.M.1
  • 61
    • 0034534795 scopus 로고    scopus 로고
    • Post-translational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha J, Weiler S, Oh KJ, Wei MC and Korsmeyer SJ. Post-translational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 2000; 290: 1761-5
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 63
    • 67650741483 scopus 로고    scopus 로고
    • Mitochondrial targeting of tBid/Bax: A role for the TOM complex?
    • Ott M, Norberg E, Zhivotovsky B and Orrenius S. Mitochondrial targeting of tBid/Bax: a role for the TOM complex? Cell Death Differ 2009; 16: 1075-82
    • (2009) Cell Death Differ , vol.16 , pp. 1075-1082
    • Ott, M.1    Norberg, E.2    Zhivotovsky, B.3    Orrenius, S.4
  • 64
    • 0037115740 scopus 로고    scopus 로고
    • Bax oligomerization in mitochondrial membranes requires tBid (caspase- 8-cleaved Bid) and a mitochondrial protein
    • Roucou X, Montessuit S, Antonsson B and Martinou JC. Bax oligomerization in mitochondrial membranes requires tBid (caspase- 8-cleaved Bid) and a mitochondrial protein. Biochem J 2002; 368: 915-21
    • (2002) Biochem J , vol.368 , pp. 915-921
    • Roucou, X.1    Montessuit, S.2    Antonsson, B.3    Martinou, J.C.4
  • 65
    • 65349136027 scopus 로고    scopus 로고
    • Mitochondrial outer membrane proteins assist Bid in Bax- mediated lipidic pore formation
    • Schafer B, Quispe J, Choudhary V, Chipuk JE, Ajero TG, Du H, et al. Mitochondrial outer membrane proteins assist Bid in Bax- mediated lipidic pore formation. Mol Biol Cell 2009; 20: 2276-85
    • (2009) Mol Biol Cell , vol.20 , pp. 2276-2285
    • Schafer, B.1    Quispe, J.2    Choudhary, V.3    Chipuk, J.E.4    Ajero, T.G.5    Du, H.6
  • 66
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G, Galluzzi L and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007; 87: 99-163
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 68
    • 65449152836 scopus 로고    scopus 로고
    • Following TRAIL's path in the immune system
    • Falschlehner C, Schaefer U and Walczak H. Following TRAIL's path in the immune system. Immunology 2009; 127: 145-54
    • (2009) Immunology , vol.127 , pp. 145-154
    • Falschlehner, C.1    Schaefer, U.2    Walczak, H.3
  • 69
    • 60149085396 scopus 로고    scopus 로고
    • The many roles of FAS receptor signaling in the immune system
    • Strasser A, Jost PJ and Nagata S. The many roles of FAS receptor signaling in the immune system. Immunity 2009; 30: 180-92
    • (2009) Immunity , vol.30 , pp. 180-192
    • Strasser, A.1    Jost, P.J.2    Nagata, S.3
  • 70
    • 67649884532 scopus 로고    scopus 로고
    • CD95, BIM and T cell homeostasis
    • Bouillet P and O'Reilly LA. CD95, BIM and T cell homeostasis. Nat Rev Immunol 2009; 9: 514-9
    • (2009) Nat Rev Immunol , vol.9 , pp. 514-519
    • Bouillet, P.1    O'reilly, L.A.2
  • 72
    • 14544288632 scopus 로고    scopus 로고
    • CD4+ T-cell help controls CD8+ T-cell memory via TRAIL-mediated activation-induced cell death
    • Janssen EM, Droin NM, Lemmens EE, Pinkoski MJ, Bensinger SJ, Ehst BD, et al. CD4+ T-cell help controls CD8+ T-cell memory via TRAIL-mediated activation-induced cell death. Nature 2005; 434: 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
  • 73
    • 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, Thome M, Attinger A, Valitutti S, et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol 2000; 1: 489-95
    • (2000) Nat Immunol , vol.1 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3    Thome, M.4    Attinger, A.5    Valitutti, S.6
  • 74
    • 67449161828 scopus 로고    scopus 로고
    • CD95 co-stimulation blocks activation of naive T cells by inhibiting T cell receptor signaling
    • Strauss G, Lindquist JA, Arhel N, Felder E, Karl S, Haas TL, et al. CD95 co-stimulation blocks activation of naive T cells by inhibiting T cell receptor signaling. J Exp Med 2009; 206: 1379-93
    • (2009) J Exp Med , vol.206 , pp. 1379-1393
    • Strauss, G.1    Lindquist, J.A.2    Arhel, N.3    Felder, E.4    Karl, S.5    Haas, T.L.6
  • 75
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak H, Miller RE, Ariail K, Gliniak B, Griffith TS, Kubin M, et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med 1999; 5: 157-63
    • (1999) Nat Med , vol.5 , pp. 157-163
    • Walczak, H.1    Miller, R.E.2    Ariail, K.3    Gliniak, B.4    Griffith, T.S.5    Kubin, M.6
  • 76
    • 62449168519 scopus 로고    scopus 로고
    • TRAIL agonists on clinical trials for cancer therapy: The promises and the challenges
    • Bellail AC, Qi L, Mulligan P, Chhabra V and Hao C. TRAIL agonists on clinical trials for cancer therapy: the promises and the challenges. Rev Recent Clin Trials 2009; 4: 34-41
    • (2009) Rev Recent Clin Trials , vol.4 , pp. 34-41
    • Bellail, A.C.1    Qi, L.2    Mulligan, P.3    Chhabra, V.4    Hao, C.5
  • 77
    • 58149456883 scopus 로고    scopus 로고
    • Death receptors as targets for anti-cancer therapy
    • Papenfuss K, Cordier SM and Walczak H. Death receptors as targets for anti-cancer therapy. J Cell Mol Med 2008; 12: 2566-85
    • (2008) J Cell Mol Med , vol.12 , pp. 2566-2585
    • Papenfuss, K.1    Cordier, S.M.2    Walczak, H.3
  • 78
    • 0032775933 scopus 로고    scopus 로고
    • Involvement of a novel Tnf receptor homologue in hair follicle induction. Nat Genet 1999; 22: 370-4
    • Headon DJ and Overbeek PA. Involvement of a novel Tnf receptor homologue in hair follicle induction. Nat Genet 1999; 22: 370-4
    • Headon, D.J.1    Overbeek, P.A.2
  • 79
    • 0037573629 scopus 로고    scopus 로고
    • Permanent correction of an inherited ectodermal dysplasia with recombinant EDA
    • Gaide O and Schneider P. Permanent correction of an inherited ectodermal dysplasia with recombinant EDA. Nat Med 2003; 9: 614-8
    • (2003) Nat Med , vol.9 , pp. 614-618
    • Gaide, O.1    Schneider, P.2
  • 80
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A and Mosialos G. CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 2003; 424: 793-6
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 81
    • 0037022539 scopus 로고    scopus 로고
    • Identification of a novel death domain-containing adaptor molecule for ectodysplasin-A receptor that is mutated in crinkled mice
    • Yan M, Zhang Z, Brady JR, Schilbach S, Fairbrother WJ and Dixit VM. Identification of a novel death domain-containing adaptor molecule for ectodysplasin-A receptor that is mutated in crinkled mice. Curr Biol 2002; 12: 409-13
    • (2002) Curr Biol , vol.12 , pp. 409-413
    • Yan, M.1    Zhang, Z.2    Brady, J.R.3    Schilbach, S.4    Fairbrother, W.J.5    Dixit, V.M.6
  • 82
    • 66649136257 scopus 로고    scopus 로고
    • Multiple roles of the p75 neurotrophin receptor in the nervous system
    • Chen Y, Zeng J, Chen Y, Wang X, Yao G, Wang W, et al. Multiple roles of the p75 neurotrophin receptor in the nervous system. J Int Med Res 2009; 37: 281-8
    • (2009) J Int Med Res , vol.37 , pp. 281-288
    • Chen, Y.1    Zeng, J.2    Chen, Y.3    Wang, X.4    Yao, G.5    Wang, W.6
  • 83
    • 1642540257 scopus 로고    scopus 로고
    • Neurotrophins and their receptors: Signaling trios in complex biological systems
    • Teng KK and Hempstead BL. Neurotrophins and their receptors: signaling trios in complex biological systems. Cell Mol Life Sci 2004; 61: 35-48
    • (2004) Cell Mol Life Sci , vol.61 , pp. 35-48
    • Teng, K.K.1    Hempstead, B.L.2
  • 84
    • 0029805770 scopus 로고    scopus 로고
    • Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75
    • Casaccia-Bonnefil P, Carter BD, Dobrowsky RT and Chao MV. Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75. Nature 1996; 383: 716-9
    • (1996) Nature , vol.383 , pp. 716-719
    • Casaccia-Bonnefil, P.1    Carter, B.D.2    Dobrowsky, R.T.3    Chao, M.V.4
  • 85
    • 55749104402 scopus 로고    scopus 로고
    • Induction of proneurotrophins and activation of p75NTR-mediated apoptosis via neurotrophin receptor-interacting factor in hippocampal neurons after seizures
    • Volosin M, Trotter C, Cragnolini A, Kenchappa RS, Light M, Hempstead BL, et al. Induction of proneurotrophins and activation of p75NTR-mediated apoptosis via neurotrophin receptor-interacting factor in hippocampal neurons after seizures. J Neurosci 2008; 28: 9870-9
    • (2008) J Neurosci , vol.28 , pp. 9870-9879
    • Volosin, M.1    Trotter, C.2    Cragnolini, A.3    Kenchappa, R.S.4    Light, M.5    Hempstead, B.L.6
  • 86
    • 10544236916 scopus 로고    scopus 로고
    • Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95
    • Chinnaiyan AM, O'Rourke K, Yu GL, Lyons RH, Garg M, Duan DR, et al. Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95. Science 1996; 274: 990-2
    • (1996) Science , vol.274 , pp. 990-992
    • Chinnaiyan, A.M.1    O'rourke, K.2    Yu, G.L.3    Lyons, R.H.4    Garg, M.5    Duan, D.R.6
  • 87
    • 0032563275 scopus 로고    scopus 로고
    • Identification and functional characterization of DR6, a novel death domain-containing TNF receptor
    • Pan G, Bauer JH, Haridas V, Wang S, Liu D, Yu G, et al. Identification and functional characterization of DR6, a novel death domain-containing TNF receptor. FEBS Lett 1998; 431: 351-6
    • (1998) FEBS Lett , vol.431 , pp. 351-356
    • Pan, G.1    Bauer, J.H.2    Haridas, V.3    Wang, S.4    Liu, D.5    Yu, G.6
  • 88
    • 18344385475 scopus 로고    scopus 로고
    • TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell costimulator
    • Migone TS, Zhang J, Luo X, Zhuang L, Chen C, Hu B, et al. TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell costimulator. Immunity 2002; 16: 479-92
    • (2002) Immunity , vol.16 , pp. 479-492
    • Migone, T.S.1    Zhang, J.2    Luo, X.3    Zhuang, L.4    Chen, C.5    Hu, B.6
  • 89
    • 43549110073 scopus 로고    scopus 로고
    • Essential role of TNF receptor superfamily 25 (TNFRSF25) in the development of allergic lung inflammation
    • Fang L, Adkins B, Deyev V and Podack ER. Essential role of TNF receptor superfamily 25 (TNFRSF25) in the development of allergic lung inflammation. J Exp Med 2008; 205: 1037-48
    • (2008) J Exp Med , vol.205 , pp. 1037-1048
    • Fang, L.1    Adkins, B.2    Deyev, V.3    Podack, E.R.4
  • 90
    • 46749097474 scopus 로고    scopus 로고
    • The TNF-family receptor DR3 is essential for diverse T cell-mediated inflammatory diseases
    • Meylan F, Davidson TS, Kahle E, Kinder M, Acharya K, Jankovic D, et al. The TNF-family receptor DR3 is essential for diverse T cell-mediated inflammatory diseases. Immunity 2008; 29: 79-89
    • (2008) Immunity , vol.29 , pp. 79-89
    • Meylan, F.1    Davidson, T.S.2    Kahle, E.3    Kinder, M.4    Acharya, K.5    Jankovic, D.6
  • 92
    • 58149171978 scopus 로고    scopus 로고
    • The Death Receptor 3-TNF-like protein 1A pathway drives adverse bone pathology in inflammatory arthritis
    • Bull MJ, Williams AS, Mecklenburgh Z, Calder CJ, Twohig JP, Elford C, et al. The Death Receptor 3-TNF-like protein 1A pathway drives adverse bone pathology in inflammatory arthritis. J Exp Med 2008; 205: 2457-64
    • (2008) J Exp Med , vol.205 , pp. 2457-2464
    • Bull, M.J.1    Williams, A.S.2    Mecklenburgh, Z.3    Calder, C.J.4    Twohig, J.P.5    Elford, C.6
  • 93
    • 69949108378 scopus 로고    scopus 로고
    • Functional analysis of the posttranslational modifications of the Death Receptor 6
    • Klima M, Zajedova J, Doubravska L and Andera L. Functional analysis of the posttranslational modifications of the Death Receptor 6. Biochim Biophys Acta 2009;
    • (2009) Biochim Biophys Acta
    • Klima, M.1    Zajedova, J.2    Doubravska, L.3    Andera, L.4
  • 94
    • 0036784654 scopus 로고    scopus 로고
    • Accelerated onset and increased severity of acute graft-versus-host disease following adoptive transfer of DR6-deficient T cells
    • Liu J, Heuer JG, Na S, Galbreath E, Zhang T, Yang DD, et al. Accelerated onset and increased severity of acute graft-versus-host disease following adoptive transfer of DR6-deficient T cells. J Immunol 2002; 169: 3993-8
    • (2002) J Immunol , vol.169 , pp. 3993-3998
    • Liu, J.1    Heuer, J.G.2    Na, S.3    Galbreath, E.4    Zhang, T.5    Yang, D.D.6
  • 95
    • 0034903664 scopus 로고    scopus 로고
    • Enhanced CD4+ T cell proliferation and Th2 cytokine production in DR6-deficient mice
    • Liu J, Na S, Glasebrook A, Fox N, Solenberg PJ, Zhang Q, et al. Enhanced CD4+ T cell proliferation and Th2 cytokine production in DR6-deficient mice. Immunity 2001; 15: 23-34
    • (2001) Immunity , vol.15 , pp. 23-34
    • Liu, J.1    Na, S.2    Glasebrook, A.3    Fox, N.4    Solenberg, P.J.5    Zhang, Q.6
  • 96
    • 0037243911 scopus 로고    scopus 로고
    • Enhanced B cell expansion, survival, and humoral responses by targeting death receptor 6
    • Schmidt CS, Liu J, Zhang T, Song HY, Sandusky G, Mintze K, et al. Enhanced B cell expansion, survival, and humoral responses by targeting death receptor 6. J Exp Med 2003; 197: 51-62
    • (2003) J Exp Med , vol.197 , pp. 51-62
    • Schmidt, C.S.1    Liu, J.2    Zhang, T.3    Song, H.Y.4    Sandusky, G.5    Mintze, K.6
  • 97
    • 0035914945 scopus 로고    scopus 로고
    • Impaired c-Jun amino terminal kinase activity and T cell differentiation in death receptor 6-deficient mice
    • Zhao H, Yan M, Wang H, Erickson S, Grewal IS and Dixit VM. Impaired c-Jun amino terminal kinase activity and T cell differentiation in death receptor 6-deficient mice. J Exp Med 2001; 194: 1441-8
    • (2001) J Exp Med , vol.194 , pp. 1441-1448
    • Zhao, H.1    Yan, M.2    Wang, H.3    Erickson, S.4    Grewal, I.S.5    Dixit, V.M.6
  • 98
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD and Tessier-Lavigne M. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 2009; 457: 981-9
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'leary, D.D.3    Tessier-Lavigne, M.4


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