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Volumn 14, Issue 3-4, 2003, Pages 193-209

The signaling adaptors and pathways activated by TNF superfamily

Author keywords

Adaptor molecule; Apoptosis; Cell survival; Signal transduction

Indexed keywords

ADAPTOR PROTEIN; CASPASE 8; CASPASE 9; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; OSTEOPROTEGERIN; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND;

EID: 0038320263     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6101(03)00021-2     Document Type: Review
Times cited : (414)

References (171)
  • 1
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley RM, Killeen N, 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
  • 2
    • 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. Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity 2000;12:611-20.
    • (2000) Immunity , vol.12 , pp. 611-620
    • Kischkel, F.C.1    Lawrence, D.A.2    Chuntharapai, A.3
  • 3
    • 10544236916 scopus 로고    scopus 로고
    • Signal transduction by DR3, a death domain-containing receptor related to TNF-R1 and CD95
    • Chinnaiyan AM, O'Rourke K, Yu GL, et al. Signal transduction by DR3, a death domain-containing receptor related to TNF-R1 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
  • 4
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel FC, Hellbardt S, Behrmann I, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995;14:5579-88.
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3
  • 5
    • 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, Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death. Cell 1996;85:803-15.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 6
    • 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. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996;85:817-27.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 7
    • 0030925774 scopus 로고    scopus 로고
    • FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
    • Medema JP, Scaffidi C, Kischkel FC, et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J 1997;16:2794-804.
    • (1997) EMBO J , vol.16 , pp. 2794-2804
    • Medema, J.P.1    Scaffidi, C.2    Kischkel, F.C.3
  • 8
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation: The induced-proximity model
    • Salvesen GS, Dixit VM. Caspase activation: the induced-proximity model. Proc Natl Acad Sci USA 1999;96:10964-7.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 9
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang X, Chang HY, Baltimore D. Autoproteolytic activation of pro-caspases by oligomerization. Mol Cell 1998;1:319-25.
    • (1998) Mol Cell , vol.1 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 10
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2 BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng EH, Wei MC, Weiler S, et al. BCL-2 BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 2001;8:705-11.
    • (2001) Mol Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3
  • 11
    • 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, Yuan J. Cleavage of BID by caspase-8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998;94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 12
    • 0034663829 scopus 로고    scopus 로고
    • tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei MC, Lindsten T, Mootha VK, et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev 2000;14:2060-71.
    • (2000) Genes Dev , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3
  • 13
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997;90:405-13.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 14
    • 0037007101 scopus 로고    scopus 로고
    • Oligomerization and activation of caspase-9, induced by Apaf-1 CARD
    • Shiozaki EN, Chai J, Shi Y. Oligomerization and activation of caspase-9, induced by Apaf-1 CARD. Proc Natl Acad Sci USA 2002;99:4197-202.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4197-4202
    • Shiozaki, E.N.1    Chai, J.2    Shi, Y.3
  • 15
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger BZ, Leder P, Lee TH, Kim E, Seed B. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 1995;81:513-23.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 16
    • 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, Baichwal V, Goeddel DV. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 1996;4:387-96.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 17
    • 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. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity 1998;8:297-303.
    • (1998) Immunity , vol.8 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3
  • 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, 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
  • 19
    • 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, Goeddel DV, Karin M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell 1996;87:565-76.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 20
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a death domain-containing receptor for TRAIL
    • Pan G, Ni J, Wei YF, et al. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science 1997;277:815-8.
    • (1997) Science , vol.277 , pp. 815-818
    • Pan, G.1    Ni, J.2    Wei, Y.F.3
  • 21
    • 0037113868 scopus 로고    scopus 로고
    • Control of receptor-induced signaling complex (RISC) formation by the kinetics of ligand/receptor interaction
    • Krippner-Heidenreich A, Tubing F, Bryde S, et al. Control of receptor-induced signaling complex (RISC) formation by the kinetics of ligand/receptor interaction. J Biol Chem, 2002.
    • (2002) J Biol Chem
    • Krippner-Heidenreich, A.1    Tubing, F.2    Bryde, S.3
  • 22
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang Y, Woronicz JD, Liu W, Goeddel DV. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 1999;283:543-6.
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 23
    • 0036133127 scopus 로고    scopus 로고
    • Molecular ordering of the initial signaling events of CD95
    • Algeciras-Schimnich A, Shen L, Barnhart BC, et al. Molecular ordering of the initial signaling events of CD95. Mol Cell Biol 2002;22:207-20.
    • (2002) Mol Cell Biol , vol.22 , pp. 207-220
    • Algeciras-Schimnich, A.1    Shen, L.2    Barnhart, B.C.3
  • 24
    • 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, 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
  • 25
    • 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. 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;9:267-76.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3
  • 26
    • 0035824635 scopus 로고    scopus 로고
    • Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8
    • Kischkel FC, Lawrence DA, Tinel A, et al. Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J Biol Chem 2001;276:46639-46.
    • (2001) J Biol Chem , vol.276 , pp. 46639-46646
    • Kischkel, F.C.1    Lawrence, D.A.2    Tinel, A.3
  • 27
    • 18544383460 scopus 로고    scopus 로고
    • Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency
    • Chun HJ, Zheng L, Ahmad M, et al. Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 2002;419:395-9.
    • (2002) Nature , vol.419 , pp. 395-399
    • Chun, H.J.1    Zheng, L.2    Ahmad, M.3
  • 28
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Irmler M, Thome M, Hahne M, et al. Inhibition of death receptor signals by cellular FLIP. Nature 1997;388:190-5.
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1    Thome, M.2    Hahne, M.3
  • 29
    • 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. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev 1999;13:2514-26.
    • (1999) Genes Dev , vol.13 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 30
    • 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, Salvesen GS, Reed JC. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J 1997;16:6914-25.
    • (1997) EMBO J , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 31
    • 0029953942 scopus 로고    scopus 로고
    • Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors
    • Uren AG, Pakusch M, Hawkins CJ, Puls KL, Vaux DL. Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors. Proc Natl Acad Sci USA 1996;93:4974-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4974-4978
    • Uren, A.G.1    Pakusch, M.2    Hawkins, C.J.3    Puls, K.L.4    Vaux, D.L.5
  • 32
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • Suzuki Y, Nakabayashi Y, Takahashi R. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. Proc Natl Acad Sci USA 2001;98:8662-7.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 33
    • 0030854040 scopus 로고    scopus 로고
    • Localization of the major NF-kappaB-activating site and the sole TRAF3 binding site of LMP-1 defines two distinct signaling motifs
    • Brodeur SR, Cheng G, Baltimore D, Thorley-Lawson DA. Localization of the major NF-kappaB-activating site and the sole TRAF3 binding site of LMP-1 defines two distinct signaling motifs. J Biol Chem 1997;272:19777-84.
    • (1997) J Biol Chem , vol.272 , pp. 19777-19784
    • Brodeur, S.R.1    Cheng, G.2    Baltimore, D.3    Thorley-Lawson, D.A.4
  • 34
    • 0028936733 scopus 로고
    • Involvement of CRAF1, a Relative of TRAF, in CD40 signaling
    • Cheng G, Cleary AM, Ye Z, et al. Involvement of CRAF1, a Relative of TRAF, in CD40 signaling. Science 1995;267:1494-8.
    • (1995) Science , vol.267 , pp. 1494-1498
    • Cheng, G.1    Cleary, A.M.2    Ye, Z.3
  • 35
    • 0029956392 scopus 로고    scopus 로고
    • Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: Role in NF-kappaB activation
    • Devergne O, Hatzivassiliou E, Izumi KM, et al. Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation. Mol Cell Biol 1996;16:7098-108.
    • (1996) Mol Cell Biol , vol.16 , pp. 7098-7108
    • Devergne, O.1    Hatzivassiliou, E.2    Izumi, K.M.3
  • 36
    • 0032545465 scopus 로고    scopus 로고
    • The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-kappaB, a member of the TNFR superfamily
    • Galibert L, Tometsko ME, Anderson DM, Cosman D, Dougall WC. The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-kappaB, a member of the TNFR superfamily. J Biol Chem 1998;273:34120-7.
    • (1998) J Biol Chem , vol.273 , pp. 34120-34127
    • Galibert, L.1    Tometsko, M.E.2    Anderson, D.M.3    Cosman, D.4    Dougall, W.C.5
  • 37
    • 15844369897 scopus 로고    scopus 로고
    • CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins
    • Gedrich RW, Gilfillan MC, Duckett CS, Van Dongen JL, Thompson CB. CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins. J Biol Chem 199(5;271:12852-8.
    • (1996) J Biol Chem , vol.271 , pp. 12852-12858
    • Gedrich, R.W.1    Gilfillan, M.C.2    Duckett, C.S.3    Van Dongen, J.L.4    Thompson, C.B.5
  • 38
    • 0034254525 scopus 로고    scopus 로고
    • TNF receptor family member BCMA (B cell maturation) associates with TNF receptor-associated factor (TRAF)I, TRAF2, and TRAF3 and activates NF-kappaB, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase
    • Hatzoglou A, Roussel J, Bourgeade MF, et al. TNF receptor family member BCMA (B cell maturation) associates with TNF receptor-associated factor (TRAF)I, TRAF2, and TRAF3 and activates NF-kappaB, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase. J Immunol 2000;165:1322-30.
    • (2000) J Immunol , vol.165 , pp. 1322-1330
    • Hatzoglou, A.1    Roussel, J.2    Bourgeade, M.F.3
  • 39
    • 13044316551 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand
    • Hsu H, Lacey DL, Dunstan CR, et al. Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand. Proc Natl Acad Sci USA 1999;96:3540-5.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3540-3545
    • Hsu, H.1    Lacey, D.L.2    Dunstan, C.R.3
  • 40
    • 0027943499 scopus 로고
    • A novel RING finger protein interacts with the cytoplasmic domain of CD40
    • Hu HM, O'Rourke K, Boguski MS, Dixit VM. A novel RING finger protein interacts with the cytoplasmic domain of CD40. J Biol Chem 1994;269:30069-72.
    • (1994) J Biol Chem , vol.269 , pp. 30069-30072
    • Hu, H.M.1    O'Rourke, K.2    Boguski, M.S.3    Dixit, V.M.4
  • 41
    • 10544243364 scopus 로고    scopus 로고
    • Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region
    • Ishida T, Mizushima S, Azuma S, et al. Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region. J Biol Chem 1996;271:28745-8.
    • (1996) J Biol Chem , vol.271 , pp. 28745-28748
    • Ishida, T.1    Mizushima, S.2    Azuma, S.3
  • 42
    • 0029847814 scopus 로고    scopus 로고
    • TRAF5, a novel tumor necrosis factor receptor-associated factor family protein, mediates CD40 signaling
    • Ishida TK, Tojo T, Aoki T, et al. TRAF5, a novel tumor necrosis factor receptor-associated factor family protein, mediates CD40 signaling. Proc Natl Acad Sci USA 1996;93:9437-42.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9437-9442
    • Ishida, T.K.1    Tojo, T.2    Aoki, T.3
  • 43
    • 18244416073 scopus 로고    scopus 로고
    • TRAF4 expression in epithelial progenitor cells. Analysis in normal adult, fetal, and tumor tissues
    • Krajewska M, Krajewski S, Zapata JM, et al. TRAF4 expression in epithelial progenitor cells. Analysis in normal adult, fetal, and tumor tissues. Am J Pathol 1998;152:1549-61.
    • (1998) Am J Pathol , vol.152 , pp. 1549-1561
    • Krajewska, M.1    Krajewski, S.2    Zapata, J.M.3
  • 44
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos G, Birkenbach M, Yalamanchili R, et al. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell 1995;80:389-99.
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1    Birkenbach, M.2    Yalamanchili, R.3
  • 45
    • 0032563275 scopus 로고    scopus 로고
    • Identification and functional characterization of DR6, a novel death domain-containing TNF receptor
    • Pan G, Bauer JH, Haridas V, 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
  • 46
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-kappaB by TNF receptor 2 and CD40
    • Rothe M, Sarma V, Dixit VM, Goeddel DV. TRAF2-mediated activation of NF-kappaB by TNF receptor 2 and CD40. Science 1995;269:1424-7.
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 47
    • 0030925641 scopus 로고    scopus 로고
    • Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3
    • Sandberg M, Hammerschmidt W, Sugden B. Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3. J Virol 1997;71:4649-56.
    • (1997) J Virol , vol.71 , pp. 4649-4656
    • Sandberg, M.1    Hammerschmidt, W.2    Sugden, B.3
  • 48
    • 0028809176 scopus 로고
    • A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40
    • Sato T, Irie S, Reed JC. A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40. FEBS Lett 1995;358:113-8.
    • (1995) FEBS Lett , vol.358 , pp. 113-118
    • Sato, T.1    Irie, S.2    Reed, J.C.3
  • 49
    • 0035887040 scopus 로고    scopus 로고
    • TRAF6 is a critical mediator of signal transduction by the viral oncogene latent membrane protein 1
    • Schultheiss U, Puschner S, Kremmer E, et al. TRAF6 is a critical mediator of signal transduction by the viral oncogene latent membrane protein 1. EMBO J 2001;20:5678-91.
    • (2001) EMBO J , vol.20 , pp. 5678-5691
    • Schultheiss, U.1    Puschner, S.2    Kremmer, E.3
  • 50
    • 0035353181 scopus 로고    scopus 로고
    • RELT, a new member of the tumor necrosis factor receptor superfamily, is selectively expressed in hematopoietic tissues and activates transcription factor NF-kappaB
    • Sica GL, Zhu G, Tamada K, et al. RELT, a new member of the tumor necrosis factor receptor superfamily, is selectively expressed in hematopoietic tissues and activates transcription factor NF-kappaB. Blood 2001;97:2702-7.
    • (2001) Blood , vol.97 , pp. 2702-2707
    • Sica, G.L.1    Zhu, G.2    Tamada, K.3
  • 51
    • 0037160061 scopus 로고    scopus 로고
    • Role of TRAF3 and TRAF6 in the Activation of the NF-kappaB and JNK pathways by X-linked ectodermal dysplasia receptor
    • Sinha SK, Zachariah S, Quinones HI, Shindo M, Chaudhary PM. Role of TRAF3 and TRAF6 in the Activation of the NF-kappaB and JNK pathways by X-linked ectodermal dysplasia receptor. J Biol Chem 2002;277:44953-61.
    • (2002) J Biol Chem , vol.277 , pp. 44953-44961
    • Sinha, S.K.1    Zachariah, S.2    Quinones, H.I.3    Shindo, M.4    Chaudhary, P.M.5
  • 52
    • 0030911873 scopus 로고    scopus 로고
    • Lymphotoxin-beta receptor signaling complex: Role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor kappaB
    • VanArsdale TL, VanArsdale SL, Force WR, et al. Lymphotoxin-beta receptor signaling complex: role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor kappaB. Proc Natl Acad Sci USA 1997;94:2460-5.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2460-2465
    • VanArsdale, T.L.1    VanArsdale, S.L.2    Force, W.R.3
  • 53
    • 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. The TNF-receptor-associated factor family: scaffold molecules for cytokine receptors, kinases and their regulators. Cell Signal 2001;13:389-400.
    • (2001) Cell Signal , vol.13 , pp. 389-400
    • Wajant, H.1    Henkler, F.2    Scheurich, P.3
  • 54
    • 18244380611 scopus 로고    scopus 로고
    • A novel TNF receptor family member binds TWEAK and is implicated in angiogenesis
    • Wiley SR, Cassiano L, Lofton T, et al. A novel TNF receptor family member binds TWEAK and is implicated in angiogenesis. Immunity 2001;15:837-46.
    • (2001) Immunity , vol.15 , pp. 837-846
    • Wiley, S.R.1    Cassiano, L.2    Lofton, T.3
  • 55
    • 0033761628 scopus 로고    scopus 로고
    • Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors
    • Yan M, Wang LC, Hymowitz SG, et al. Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors. Science 2000;290:523-7.
    • (2000) Science , vol.290 , pp. 523-527
    • Yan, M.1    Wang, L.C.2    Hymowitz, S.G.3
  • 56
    • 0035087798 scopus 로고    scopus 로고
    • Complete structural characterisation of the mammalian and Drosophila TRAF genes: Implications for TRAF evolution and the role of RING finger splice variants
    • Grech A, Quinn R, Srinivasan D, Badoux X, Brink R. Complete structural characterisation of the mammalian and Drosophila TRAF genes: implications for TRAF evolution and the role of RING finger splice variants. Mol Immunol 2000;37:721-34.
    • (2000) Mol Immunol , vol.37 , pp. 721-734
    • Grech, A.1    Quinn, R.2    Srinivasan, D.3    Badoux, X.4    Brink, R.5
  • 57
    • 0028856787 scopus 로고
    • Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma
    • Regnier C, Tomasetto C, Moog-Lutz C, et al. Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma. J Biol Chem 1995;270:25715-21.
    • (1995) J Biol Chem , vol.270 , pp. 25715-25721
    • Regnier, C.1    Tomasetto, C.2    Moog-Lutz, C.3
  • 58
    • 0034697172 scopus 로고    scopus 로고
    • The Drosophila tumor necrosis factor receptor-associated factor-1 (DTRAF1) interacts with Pelle and regulates NF-kappaB activity
    • Zapata JM, Matsuzawa S, Godzik A, et al. The Drosophila tumor necrosis factor receptor-associated factor-1 (DTRAF1) interacts with Pelle and regulates NF-kappaB activity. J Biol Chem 2000;275:12102-7.
    • (2000) J Biol Chem , vol.275 , pp. 12102-12107
    • Zapata, J.M.1    Matsuzawa, S.2    Godzik, A.3
  • 59
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe M, Wong SC, Henzel WJ, Goeddel DV. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 1994;78:681-92.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 61
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park YC, Burkitt V, Villa AR, Tong L, Wu H. Structural basis for self-association and receptor recognition of human TRAF2. Nature 1999;398:533-8.
    • (1999) Nature , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3    Tong, L.4    Wu, H.5
  • 62
    • 0032566341 scopus 로고    scopus 로고
    • CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions: Regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization
    • Pullen SS, Miller HG, Everdeen DS, et al. CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions: regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization. Biochemistry 1998;37:11836-45.
    • (1998) Biochemistry , vol.37 , pp. 11836-11845
    • Pullen, S.S.1    Miller, H.G.2    Everdeen, D.S.3
  • 63
    • 0029917841 scopus 로고    scopus 로고
    • TANK, a co-inducer with TRAF2 of TNF and CD40L-mediated NF-κB activation
    • Cheng G, Baltimore D. TANK, a co-inducer with TRAF2 of TNF and CD40L-mediated NF-κB activation. Genes Dev 1996;10:963-73.
    • (1996) Genes Dev , vol.10 , pp. 963-973
    • Cheng, G.1    Baltimore, D.2
  • 64
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1
    • Malinin NL, Boldin MP, Kovalenko AV, Wallach D. MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1. Nature 1997;385:540-4.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 65
    • 12644272789 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated kinase cascades: Bifurcation of nuclear factor-κB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2
    • Song HY, Regnier CH, Kirschning CJ, Goeddel DV, Rothe M. Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-κB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. Proc Natl Acad Sci USA 1997;94:9792-6.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9792-9796
    • Song, H.Y.1    Regnier, C.H.2    Kirschning, C.J.3    Goeddel, D.V.4    Rothe, M.5
  • 66
    • 0029595282 scopus 로고
    • The TNF-R2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV. The TNF-R2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 1995;83:1243-52.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 68
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont PS. RING for destruction? Curr Biol 2000;10:R84-7.
    • (2000) Curr Biol , vol.10
    • Freemont, P.S.1
  • 69
    • 0037084504 scopus 로고    scopus 로고
    • All TRAFs are not created equal: Common and distinct molecular mechanisms of TRAF-mediated signal transduction
    • Chung JY, Park YC, Ye H, Wu H. All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction. J Cell Sci 2002;115:679-88.
    • (2002) J Cell Sci , vol.115 , pp. 679-688
    • Chung, J.Y.1    Park, Y.C.2    Ye, H.3    Wu, H.4
  • 70
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L, Wang C, Spencer E, et al. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000;103:351-61.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3
  • 71
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C, Deng L, Hong M, et al. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 2001;412:346-51.
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3
  • 72
    • 0029786304 scopus 로고    scopus 로고
    • Anatomy of TRAF2. Distinct domains for nuclear factor-κB activation and association with tumor necrosis factor signaling proteins
    • Takeuchi M, Rothe M, Goeddel D. Anatomy of TRAF2. Distinct domains for nuclear factor-κB activation and association with tumor necrosis factor signaling proteins. J Biol Chem 1996;271:19935-42.
    • (1996) J Biol Chem , vol.271 , pp. 19935-19942
    • Takeuchi, M.1    Rothe, M.2    Goeddel, D.3
  • 73
    • 0032512738 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor (TNFR)-associated factor 2A (TRAF2A), a TRAF2 splice variant with an extended RING finger domain that inhibits TNF-R2-mediated NF-κB activation
    • Brink R, Lodish H. Tumor necrosis factor receptor (TNFR)-associated factor 2A (TRAF2A), a TRAF2 splice variant with an extended RING finger domain that inhibits TNF-R2-mediated NF-κB activation. J Biol Chem 1998;273:4129-34.
    • (1998) J Biol Chem , vol.273 , pp. 4129-4134
    • Brink, R.1    Lodish, H.2
  • 74
    • 0032544710 scopus 로고    scopus 로고
    • An intact zinc ring finger is required for tumor necrosis factor receptor-associated factor-mediated nuclear factor-kappaB activation but is dispensable for c-Jun N-terminal kinase signaling
    • Dadgostar H, Cheng G. An intact zinc ring finger is required for tumor necrosis factor receptor-associated factor-mediated nuclear factor-kappaB activation but is dispensable for c-Jun N-terminal kinase signaling. J Biol Chem 1998;273:24775-80.
    • (1998) J Biol Chem , vol.273 , pp. 24775-24780
    • Dadgostar, H.1    Cheng, G.2
  • 75
    • 0033553392 scopus 로고    scopus 로고
    • CD40 signaling through tumor necrosis factor receptor-associated factors (TRAFs). Binding site specificity and activation of downstream pathways by distinct TRAFs
    • Pullen SS, Dang TT, Crute JJ, Kehry MR. CD40 signaling through tumor necrosis factor receptor-associated factors (TRAFs). Binding site specificity and activation of downstream pathways by distinct TRAFs. J Biol Chem 1999;274:14246-54.
    • (1999) J Biol Chem , vol.274 , pp. 14246-14254
    • Pullen, S.S.1    Dang, T.T.2    Crute, J.J.3    Kehry, M.R.4
  • 76
    • 0031962348 scopus 로고    scopus 로고
    • 4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth factor receptor subfamily that bind TNF receptor-associated factors and activate nuclear factor kappaB
    • Arch RH, Thompson CB. 4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth factor receptor subfamily that bind TNF receptor-associated factors and activate nuclear factor kappaB. Mol Cell Biol 1998;18:558-65.
    • (1998) Mol Cell Biol , vol.18 , pp. 558-565
    • Arch, R.H.1    Thompson, C.B.2
  • 77
    • 0033197872 scopus 로고    scopus 로고
    • The structural basis for the recognition of diverse receptor sequences by TRAF2
    • Ye H, Park YC, Kreishman M, Kieff E, Wu H. The structural basis for the recognition of diverse receptor sequences by TRAF2. Mol Cell 1999;4:321-30.
    • (1999) Mol Cell , vol.4 , pp. 321-330
    • Ye, H.1    Park, Y.C.2    Kreishman, M.3    Kieff, E.4    Wu, H.5
  • 78
    • 0030920913 scopus 로고    scopus 로고
    • Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1
    • Marsters SA, Ayres TM, Skubatch M, et al. Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1. J Biol Chem 1997;272:14029-32.
    • (1997) J Biol Chem , vol.272 , pp. 14029-14032
    • Marsters, S.A.1    Ayres, T.M.2    Skubatch, M.3
  • 79
    • 0033570096 scopus 로고    scopus 로고
    • TRAF family proteins interact with the common neurotrophin receptor and modulate apoptosis induction
    • Ye X, Mehlen P, Rabizadeh S, et al. TRAF family proteins interact with the common neurotrophin receptor and modulate apoptosis induction. J Biol Chem 1999;274:30202-8.
    • (1999) J Biol Chem , vol.274 , pp. 30202-30208
    • Ye, X.1    Mehlen, P.2    Rabizadeh, S.3
  • 80
    • 0033587691 scopus 로고    scopus 로고
    • Crystallographic analysis of CD40 recognition and signaling by human TRAF2
    • McWhirter SM, Pullen SS, Holton JM, et al. Crystallographic analysis of CD40 recognition and signaling by human TRAF2. Proc Natl Acad Sci USA 1999;96:8408-13.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8408-8413
    • McWhirter, S.M.1    Pullen, S.S.2    Holton, J.M.3
  • 81
    • 0034641743 scopus 로고    scopus 로고
    • Molecular basis for CD40 signaling mediated by TRAF3
    • Ni CZ, Welsh K, Leo E, et al. Molecular basis for CD40 signaling mediated by TRAF3. Proc Natl Acad Sci USA 2000;97:10395-9.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10395-10399
    • Ni, C.Z.1    Welsh, K.2    Leo, E.3
  • 82
    • 0036098501 scopus 로고    scopus 로고
    • The CD40-TRAF6 axis controls affinity maturation and the generation of long-lived plasma cells
    • Ahonen C, Manning E, Erickson LD, et al. The CD40-TRAF6 axis controls affinity maturation and the generation of long-lived plasma cells. Nat Immunol 2002;3:451-6.
    • (2002) Nat Immunol , vol.3 , pp. 451-456
    • Ahonen, C.1    Manning, E.2    Erickson, L.D.3
  • 83
    • 18644383624 scopus 로고    scopus 로고
    • The binding site for TRAF2 and TRAF3 but not for TRAF6 is essential for CD40-mediated immunoglobulin class switching
    • Jabara H, Laouini D, Tsitsikov E, et al. The binding site for TRAF2 and TRAF3 but not for TRAF6 is essential for CD40-mediated immunoglobulin class switching. Immunity 2002;17:265-76.
    • (2002) Immunity , vol.17 , pp. 265-276
    • Jabara, H.1    Laouini, D.2    Tsitsikov, E.3
  • 84
    • 0036195954 scopus 로고    scopus 로고
    • Dissection of B cell differentiation during primary immune responses in mice with altered CD40 signals
    • Yasui T, Muraoka M, Takaoka-Shichijo Y, et al. Dissection of B cell differentiation during primary immune responses in mice with altered CD40 signals. Int Immunol. 2002;14:319-29.
    • (2002) Int Immunol , vol.14 , pp. 319-329
    • Yasui, T.1    Muraoka, M.2    Takaoka-Shichijo, Y.3
  • 85
    • 0030292777 scopus 로고    scopus 로고
    • Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses
    • Xu Y, Cheng G, Baltimore D. Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses. Immunity 1996;5:407-15.
    • (1996) Immunity , vol.5 , pp. 407-415
    • Xu, Y.1    Cheng, G.2    Baltimore, D.3
  • 86
    • 0033561039 scopus 로고    scopus 로고
    • TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling
    • Lomaga MA, Yeh WC, Sarosi I, et al. TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling. Genes Dev 1999;13:1015-24.
    • (1999) Genes Dev , vol.13 , pp. 1015-1024
    • Lomaga, M.A.1    Yeh, W.C.2    Sarosi, I.3
  • 87
    • 6544270833 scopus 로고    scopus 로고
    • Severe osteopetrosis, defective interleukin-1 signalling and lymph node organogenesis in TRAF6-deficient mice
    • Naito A, Azuma S, Tanaka S, et al. Severe osteopetrosis, defective interleukin-1 signalling and lymph node organogenesis in TRAF6-deficient mice. Genes Cells 1999;4:353-62.
    • (1999) Genes Cells , vol.4 , pp. 353-362
    • Naito, A.1    Azuma, S.2    Tanaka, S.3
  • 88
    • 0033198702 scopus 로고    scopus 로고
    • TRAF2 deficiency results in hyperactivity of certain TNF-R1 signals and impairment of CD40-mediated responses
    • Nguyen LT, Duncan GS, Mirtsos C, et al. TRAF2 deficiency results in hyperactivity of certain TNF-R1 signals and impairment of CD40-mediated responses. Immunity 1999;11:379-89.
    • (1999) Immunity , vol.11 , pp. 379-389
    • Nguyen, L.T.1    Duncan, G.S.2    Mirtsos, C.3
  • 89
    • 0037114130 scopus 로고    scopus 로고
    • TNFR-associated factor-3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NF-κB activation and IL-10 production
    • Xu L, Shu H. TNFR-associated factor-3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NF-κB activation and IL-10 production. J Immunol 2002;169:6883-9.
    • (2002) J Immunol , vol.169 , pp. 6883-6889
    • Xu, L.1    Shu, H.2
  • 90
    • 0032101119 scopus 로고    scopus 로고
    • CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-1BB ligand
    • Saoulli K, Lee SY, Cannons JL, et al. CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-1BB ligand. J Exp Med 1998;187:1849-62.
    • (1998) J Exp Med , vol.187 , pp. 1849-1862
    • Saoulli, K.1    Lee, S.Y.2    Cannons, J.L.3
  • 91
    • 0037173095 scopus 로고    scopus 로고
    • TRAF6-deficient mice display hypohidrotic ectodermal dysplasia
    • Naito A, Yoshida H, Nishioka E, et al. TRAF6-deficient mice display hypohidrotic ectodermal dysplasia. Proc Natl Acad Sci USA 2002;99:8766-71.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8766-8771
    • Naito, A.1    Yoshida, H.2    Nishioka, E.3
  • 92
    • 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. Targeted disruption of Traf5 gene causes defects in CD40- and CD27-mediated lymphocyte activation. Proc Natl Acad Sci USA 1999;96:9803-8,
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9803-9808
    • Nakano, H.1    Sakon, S.2    Koseki, H.3
  • 93
    • 0030694108 scopus 로고    scopus 로고
    • IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling
    • Muzio M, Ni J, Feng P, Dixit VM. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science 1997;278:1612-5.
    • (1997) Science , vol.278 , pp. 1612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 94
    • 0033516561 scopus 로고    scopus 로고
    • IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family
    • Wesche H, Gao X, Li X, et al. IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family. J Biol Chem 1999;274:19403-10.
    • (1999) J Biol Chem , vol.274 , pp. 19403-19410
    • Wesche, H.1    Gao, X.2    Li, X.3
  • 95
    • 0037117543 scopus 로고    scopus 로고
    • IRAK-4: A novel member of the IRAK family with the properties of an IRAK-kinase
    • Li S, Strelow A, Fontana EJ, Wesche H. IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase. Proc Natl Acad Sci USA 2002;99:5567-72.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5567-5572
    • Li, S.1    Strelow, A.2    Fontana, E.J.3    Wesche, H.4
  • 96
    • 0034599961 scopus 로고    scopus 로고
    • Requirement of tumor necrosis factor receptor-associated factor (TRAF)6 in interleukin-17 signal transduction
    • Schwandner R, Yamaguchi K, Cao Z. Requirement of tumor necrosis factor receptor-associated factor (TRAF)6 in interleukin-17 signal transduction. J Exp Med 2000;191:1233-40.
    • (2000) J Exp Med , vol.191 , pp. 1233-1240
    • Schwandner, R.1    Yamaguchi, K.2    Cao, Z.3
  • 97
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F, Wang X, Bertolotti A, et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000;287:664-6.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3
  • 98
    • 0034255487 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interaction between TRAF2 and tumor necrosis factor receptor peptides by isothermal titration calorimetry
    • Ye H, Wu H. Thermodynamic characterization of the interaction between TRAF2 and tumor necrosis factor receptor peptides by isothermal titration calorimetry. Proc Natl Acad Sci USA 2000;97:8961-6.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8961-8966
    • Ye, H.1    Wu, H.2
  • 99
  • 100
    • 0034685914 scopus 로고    scopus 로고
    • Recruitment of CD40 and tumor necrosis factor receptor-associated factors 2 and 3 to membrane microdomains during CD40 signaling
    • Hostager BS, Catlett IM, Bishop GA. Recruitment of CD40 and tumor necrosis factor receptor-associated factors 2 and 3 to membrane microdomains during CD40 signaling. J Biol Chem 2000;275:15392-8.
    • (2000) J Biol Chem , vol.275 , pp. 15392-15398
    • Hostager, B.S.1    Catlett, I.M.2    Bishop, G.A.3
  • 101
    • 0034601071 scopus 로고    scopus 로고
    • CD40 signaling in human dendritic cells is initiated within membrane rafts
    • Vidalain PO, Azocar O, Servet-Delprat C, et al. CD40 signaling in human dendritic cells is initiated within membrane rafts. EMBO J 2000;19:3304-13.
    • (2000) EMBO J , vol.19 , pp. 3304-3313
    • Vidalain, P.O.1    Azocar, O.2    Servet-Delprat, C.3
  • 102
    • 0034723162 scopus 로고    scopus 로고
    • Membrane localization of TRAF3 enables JNK activation
    • Dadgostar H, Cheng G. Membrane localization of TRAF3 enables JNK activation. J Biol Chem 2000;275:2539-44.
    • (2000) J Biol Chem , vol.275 , pp. 2539-2544
    • Dadgostar, H.1    Cheng, G.2
  • 103
    • 0034674294 scopus 로고    scopus 로고
    • Translocation of TRAF proteins regulates apoptotic threshold of cells
    • Arch RH, Gedrich RW, Thompson CB. Translocation of TRAF proteins regulates apoptotic threshold of cells. Biochem Biophys Res Commun 2000;272:936-45.
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 936-945
    • Arch, R.H.1    Gedrich, R.W.2    Thompson, C.B.3
  • 104
    • 0035896650 scopus 로고    scopus 로고
    • Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors
    • Feng X, Gaeta ML, Madge LA, et al. Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors. J Biol Chem 2001;276:8341-9.
    • (2001) J Biol Chem , vol.276 , pp. 8341-8349
    • Feng, X.1    Gaeta, M.L.2    Madge, L.A.3
  • 105
    • 0026026410 scopus 로고
    • Cytokine-induced proliferation and immunoglobulin production of human B lymphocytes triggered through their CD40 antigen
    • Rousset F, Garcia E, Banchereau J. Cytokine-induced proliferation and immunoglobulin production of human B lymphocytes triggered through their CD40 antigen. J Exp Med 1991;173:705-10.
    • (1991) J Exp Med , vol.173 , pp. 705-710
    • Rousset, F.1    Garcia, E.2    Banchereau, J.3
  • 106
    • 0027223391 scopus 로고
    • Human B cell proliferation and Ig secretion induced by recombinant CD40 ligand are modulated by soluble cytokines
    • Armitage RJ, Macduff BM, Spriggs MK, Fanslow WC. Human B cell proliferation and Ig secretion induced by recombinant CD40 ligand are modulated by soluble cytokines. J Immunol 1993;150:3671-80.
    • (1993) J Immunol , vol.150 , pp. 3671-3680
    • Armitage, R.J.1    Macduff, B.M.2    Spriggs, M.K.3    Fanslow, W.C.4
  • 107
    • 0030851538 scopus 로고    scopus 로고
    • Assembly and regulation of the CD40 receptor complex in human B cells
    • Kuhne MR, Robbins M, Hambor JE, et al. Assembly and regulation of the CD40 receptor complex in human B cells. J Exp Med 1997;186:337-42.
    • (1997) J Exp Med , vol.186 , pp. 337-342
    • Kuhne, M.R.1    Robbins, M.2    Hambor, J.E.3
  • 108
    • 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. 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 1999;13:1297-308.
    • (1999) Genes Dev , vol.13 , pp. 1297-1308
    • Baud, V.1    Liu, Z.G.2    Bennett, B.3
  • 109
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001;70:503-33.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 110
    • 0034922161 scopus 로고    scopus 로고
    • The essential role of MEKK3 in TNF-induced NF-κB activation
    • Yang J, Lin Y, Guo Z, et al. The essential role of MEKK3 in TNF-induced NF-κB activation. Nat Immunol 2001;2:620-4.
    • (2001) Nat Immunol , vol.2 , pp. 620-624
    • Yang, J.1    Lin, Y.2    Guo, Z.3
  • 111
    • 0035896422 scopus 로고    scopus 로고
    • Defective lymphotoxin-β receptor-induced NF-κB transcriptional activity in NIK-deficient mice
    • Yin L, Wu L, Wesche H, et al. Defective lymphotoxin-β receptor-induced NF-κB transcriptional activity in NIK-deficient mice. Science 2001;291:2162-5.
    • (2001) Science , vol.291 , pp. 2162-2165
    • Yin, L.1    Wu, L.2    Wesche, H.3
  • 112
    • 0035809310 scopus 로고    scopus 로고
    • Essential role of nuclear factor (NF)-μB-inducing kinase and inhibitor of κB (IκB) kinase a in NF-κB activation through lymphotoxin P receptor, but not through tumor necrosis factor receptor I
    • Matsushima A, Kaisho T, Rennert PD, et al. Essential role of nuclear factor (NF)-μB-inducing kinase and inhibitor of κB (IκB) kinase a in NF-κB activation through lymphotoxin P receptor, but not through tumor necrosis factor receptor I. J Exp Med 2001;193:631-6.
    • (2001) J Exp Med , vol.193 , pp. 631-636
    • Matsushima, A.1    Kaisho, T.2    Rennert, P.D.3
  • 113
    • 17944378526 scopus 로고    scopus 로고
    • Activation by IKKα of a second, evolutionary conserved, NF-κB signaling pathway
    • Senftleben U, Cao Y, Xiao G, et al. Activation by IKKα of a second, evolutionary conserved, NF-κB signaling pathway. Science 2001;293:1495-9.
    • (2001) Science , vol.293 , pp. 1495-1499
    • Senftleben, U.1    Cao, Y.2    Xiao, G.3
  • 114
    • 0034745420 scopus 로고    scopus 로고
    • NF-κB-inducing kinase regulates the processing of NF-κB2 p100
    • Xiao G, Harhaj EW, Sun SC. NF-κB-inducing kinase regulates the processing of NF-κB2 p100. Mol Cell 2001;7:401-9.
    • (2001) Mol Cell , vol.7 , pp. 401-409
    • Xiao, G.1    Harhaj, E.W.2    Sun, S.C.3
  • 115
    • 0032583947 scopus 로고    scopus 로고
    • NF-κB-inducing kinase activates IKKα by phosphorylation of Ser-176
    • Ling L, Cao Z, Goeddel DV. NF-κB-inducing kinase activates IKKα by phosphorylation of Ser-176. Proc Natl Acad Sci USA 1998;95:3792-7.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3792-3797
    • Ling, L.1    Cao, Z.2    Goeddel, D.V.3
  • 116
    • 0032583949 scopus 로고    scopus 로고
    • Differential regulation of IκB kinases α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1
    • Nakano H, Shindo M, Sakon S, et al. Differential regulation of IκB kinases α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1. Proc Natl Acad Sci USA 1998;95:3537-42.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3537-3542
    • Nakano, H.1    Shindo, M.2    Sakon, S.3
  • 117
    • 0030611595 scopus 로고    scopus 로고
    • IκB kinase β: NF-κB activation and complex formation with IκB kinase α and NIK
    • Woronicz JD, Gao X, Cao Z, Rothe M, Goeddel DV. IκB kinase β: NF-κB activation and complex formation with IκB kinase α and NIK. Science 1997;278:866-9.
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 118
    • 0036794398 scopus 로고    scopus 로고
    • BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells
    • Claudio E, Brown K, Park S, Wang H, Siebenlist U. BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells. Nat Immunol 2002;3:958-65.
    • (2002) Nat Immunol , vol.3 , pp. 958-965
    • Claudio, E.1    Brown, K.2    Park, S.3    Wang, H.4    Siebenlist, U.5
  • 119
    • 0037107399 scopus 로고    scopus 로고
    • CD40 regulates the processing of NF-κB2 p100 to p52
    • Coope HJ, Atkinson PG, Huhse B, et al. CD40 regulates the processing of NF-κB2 p100 to p52. EMBO J 2002;21:5375-85.
    • (2002) EMBO J , vol.21 , pp. 5375-5385
    • Coope, H.J.1    Atkinson, P.G.2    Huhse, B.3
  • 120
    • 18644369740 scopus 로고    scopus 로고
    • BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-κB2
    • Kayagaki N, Yan M, Seshasayee D, et al. BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-κB2. Immunity 2002;17:515.
    • (2002) Immunity , vol.17 , pp. 515
    • Kayagaki, N.1    Yan, M.2    Seshasayee, D.3
  • 121
    • 0035860466 scopus 로고    scopus 로고
    • BAFF-R, a newly identified TNF receptor that specifically interacts with BAFF
    • Thompson JS, Bixler SA, Qian F, et al. BAFF-R, a newly identified TNF receptor that specifically interacts with BAFF. Science 2001;293:2108-11.
    • (2001) Science , vol.293 , pp. 2108-2111
    • Thompson, J.S.1    Bixler, S.A.2    Qian, F.3
  • 122
    • 0028486131 scopus 로고
    • Mice deficient for the CD40 ligand
    • Xu J, Foy TM, Laman JD, et al. Mice deficient for the CD40 ligand. Immunity 1994;1:423-31.
    • (1994) Immunity , vol.1 , pp. 423-431
    • Xu, J.1    Foy, T.M.2    Laman, J.D.3
  • 123
    • 0032127288 scopus 로고    scopus 로고
    • Lymph node genesis is induced by signaling through the lymphotoxin β receptor
    • Rennert PD, James D, Mackay F, Browning JL, Hochman PS. Lymph node genesis is induced by signaling through the lymphotoxin β receptor. Immunity 1998;9:71-9.
    • (1998) Immunity , vol.9 , pp. 71-79
    • Rennert, P.D.1    James, D.2    Mackay, F.3    Browning, J.L.4    Hochman, P.S.5
  • 124
    • 0028135424 scopus 로고
    • Humoral immune responses in CD40 ligand-deficient mice
    • Renshaw BR, Fanslow III WC, Armitage RJ, et al. Humoral immune responses in CD40 ligand-deficient mice. J Exp Med 1994;180:1889-900.
    • (1994) J Exp Med , vol.180 , pp. 1889-1900
    • Renshaw, B.R.1    Fanslow W.C. III2    Armitage, R.J.3
  • 125
    • 0030917003 scopus 로고    scopus 로고
    • Distinct roles in lymphoid organogenesis for lymphotoxins α and β revealed in lymphotoxin β-deficient mice
    • Koni PA, Sacca R, Lawton P, et al. Distinct roles in lymphoid organogenesis for lymphotoxins α and β revealed in lymphotoxin β-deficient mice. Immunity 1997;6:491-500.
    • (1997) Immunity , vol.6 , pp. 491-500
    • Koni, P.A.1    Sacca, R.2    Lawton, P.3
  • 126
    • 0029987925 scopus 로고    scopus 로고
    • The splenic marginal zone is absent in alymphoplastic aly mutant mice
    • Koike R, Nishimura T, Yasumizu R, et al. The splenic marginal zone is absent in alymphoplastic aly mutant mice. Eur J Immunol 1996;26:669-75.
    • (1996) Eur J Immunol , vol.26 , pp. 669-675
    • Koike, R.1    Nishimura, T.2    Yasumizu, R.3
  • 127
    • 0028447437 scopus 로고
    • The immune responses in CD40-deficient mice: Impaired immunoglobulin class switching and germinal center formation
    • Kawabe T, Naka T, Yoshida K, et al. The immune responses in CD40-deficient mice: impaired immunoglobulin class switching and germinal center formation. Immunity 1994;1:167-78.
    • (1994) Immunity , vol.1 , pp. 167-178
    • Kawabe, T.1    Naka, T.2    Yoshida, K.3
  • 128
    • 0032127301 scopus 로고    scopus 로고
    • The lymphotoxin β receptor controls organogenesis and affinity maturation in peripheral lymphoid tissues
    • Futterer A, Mink K, Luz A, Kosco-Vilbois MH, Pfeffer K. The lymphotoxin β receptor controls organogenesis and affinity maturation in peripheral lymphoid tissues. Immunity 1998;9:59-70.
    • (1998) Immunity , vol.9 , pp. 59-70
    • Futterer, A.1    Mink, K.2    Luz, A.3    Kosco-Vilbois, M.H.4    Pfeffer, K.5
  • 129
    • 0027493906 scopus 로고
    • In vivo CD40-gp39 interactions are essential for thymus-dependent humoral immunity. II. Prolonged suppression of the humoral immune response by an antibody to the ligand for CD40, gp39
    • Foy TM, Shepherd DM, Durie FH, et al. In vivo CD40-gp39 interactions are essential for thymus-dependent humoral immunity. II. Prolonged suppression of the humoral immune response by an antibody to the ligand for CD40, gp39. J Exp Med 1993;178:1567-75.
    • (1993) J Exp Med , vol.178 , pp. 1567-1575
    • Foy, T.M.1    Shepherd, D.M.2    Durie, F.H.3
  • 130
    • 0031964855 scopus 로고    scopus 로고
    • Mice deficient in nuclear factor (NF)-κB/p52 present with defects in humoral responses, germinal center reactions, and splenic microarchitecture
    • Franzoso G, Carlson L, Poljak L, et al. Mice deficient in nuclear factor (NF)-κB/p52 present with defects in humoral responses, germinal center reactions, and splenic microarchitecture. J Exp Med 1998;187:147-59.
    • (1998) J Exp Med , vol.187 , pp. 147-159
    • Franzoso, G.1    Carlson, L.2    Poljak, L.3
  • 131
    • 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. Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997;275:90-4.
    • (1997) Science , vol.275 , pp. 90-94
    • Ichijo, H.1    Nishida, E.2    Irie, K.3
  • 132
    • 0032158987 scopus 로고    scopus 로고
    • ASK1 is essential for JNK/SAPK activation by TRAF2
    • Nishitoh H, Saitoh M, Mochida Y, et al. ASK1 is essential for JNK/SAPK activation by TRAF2. Mol Cell 1998;2:389-95.
    • (1998) Mol Cell , vol.2 , pp. 389-395
    • Nishitoh, H.1    Saitoh, M.2    Mochida, Y.3
  • 133
    • 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, Mak TW, Woodgett JR. Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1). Oncogene 1999;18:5814-20.
    • (1999) Oncogene , vol.18 , pp. 5814-5820
    • Hoeflich, K.P.1    Yeh, W.C.2    Yao, Z.3    Mak, T.W.4    Woodgett, J.R.5
  • 134
    • 0035065836 scopus 로고    scopus 로고
    • ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
    • Tobiume K, Matsuzawa A, Takahashi T, et al. ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis. EMBO Rep 2001;2:222-8.
    • (2001) EMBO Rep , vol.2 , pp. 222-228
    • Tobiume, K.1    Matsuzawa, A.2    Takahashi, T.3
  • 135
    • 0031059833 scopus 로고    scopus 로고
    • A novel human SPS1/STE20 homologue, KHS, activates Jun N-terminal kinase
    • Tung RM, Blenis J. A novel human SPS1/STE20 homologue, KHS, activates Jun N-terminal kinase. Oncogene 1997;14:653-9.
    • (1997) Oncogene , vol.14 , pp. 653-659
    • Tung, R.M.1    Blenis, J.2
  • 136
    • 0031437885 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase/c-Jun N-terminal kinase, but not NF-κB, by the tumor necrosis factor (TNF) receptor 1 through a TNF receptor-associated factor 2- and germinal center kinase related-dependent pathway
    • Shi CS, Kehrl JH. Activation of stress-activated protein kinase/c-Jun N-terminal kinase, but not NF-κB, 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 1997;272:32102-7.
    • (1997) J Biol Chem , vol.272 , pp. 32102-32107
    • Shi, C.S.1    Kehrl, J.H.2
  • 137
    • 0028845253 scopus 로고
    • Activation of the SAPK pathway by the human STE20 homologue germinal centre kinase
    • Pombo CM, Kehrl JH, Sanchez I, et al. Activation of the SAPK pathway by the human STE20 homologue germinal centre kinase. Nature 1995;377:750-4.
    • (1995) Nature , vol.377 , pp. 750-754
    • Pombo, C.M.1    Kehrl, J.H.2    Sanchez, I.3
  • 138
    • 0028279796 scopus 로고
    • Differential expression of a novel protein kinase in human B lymphocytes. Preferential localization in the germinal center
    • Katz P, Whalen G, Kehrl JH. Differential expression of a novel protein kinase in human B lymphocytes. Preferential localization in the germinal center. J Biol Chem 1994;269:16802-9.
    • (1994) J Biol Chem , vol.269 , pp. 16802-16809
    • Katz, P.1    Whalen, G.2    Kehrl, J.H.3
  • 139
    • 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, et al. 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 1997;94:9687-92.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9687-9692
    • Diener, K.1    Wang, X.S.2    Chen, C.3
  • 140
    • 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, Kyriakis JM. 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 1998;273:22681-92.
    • (1998) J Biol Chem , vol.273 , pp. 22681-22692
    • Yuasa, T.1    Ohno, S.2    Kehrl, J.H.3    Kyriakis, J.M.4
  • 141
    • 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, Siebenlist U, Kehrl JH. TNF-mediated activation of the stress-activated protein kinase pathway: TNF receptor-associated factor 2 recruits and activates germinal center kinase related. J Immunol 1999;163:3279-85.
    • (1999) J Immunol , vol.163 , pp. 3279-3285
    • Shi, C.S.1    Leonardi, A.2    Kyriakis, J.3    Siebenlist, U.4    Kehrl, J.H.5
  • 142
    • 0032874034 scopus 로고    scopus 로고
    • TANK potentiates tumor necrosis factor receptor-associated factor-mediated c-Jun N-terminal kinase/stress-activated protein kinase activation through the germinal center kinase pathway
    • Chin AI, Shu J, Shan Shi C, et al. TANK potentiates tumor necrosis factor receptor-associated factor-mediated c-Jun N-terminal kinase/stress-activated protein kinase activation through the germinal center kinase pathway. Mol Cell Biol 1999;19:6665-72.
    • (1999) Mol Cell Biol , vol.19 , pp. 6665-6672
    • Chin, A.I.1    Shu, J.2    Shan Shi, C.3
  • 143
    • 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-κB activation
    • Yujiri T, Ware M, Widmann C, et al. MEK kinase 1 gene disruption alters cell migration and c-Jun NH2-terminal kinase regulation but does not cause a measurable defect in NF-κB activation. Proc Natl Acad Sci USA 2000;97:7272-7.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7272-7277
    • Yujiri, T.1    Ware, M.2    Widmann, C.3
  • 144
    • 0347667234 scopus 로고    scopus 로고
    • TRAF-interacting protein (TRIP): A novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-κB activation
    • Lee SY, Choi Y. TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-κB activation. J Exp Med 1997;185:1275-85.
    • (1997) J Exp Med , vol.185 , pp. 1275-1285
    • Lee, S.Y.1    Choi, Y.2
  • 145
    • 0034662854 scopus 로고    scopus 로고
    • T6BP, a TRAF6-interacting protein involved in IL-1 signaling
    • Ling L, Goeddel DV. T6BP, a TRAF6-interacting protein involved in IL-1 signaling. Proc Natl Acad Sci USA 2000;97:9567-72.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9567-9572
    • Ling, L.1    Goeddel, D.V.2
  • 146
    • 0037041013 scopus 로고    scopus 로고
    • A novel zinc finger protein that inhibits osteoclastogenesis and the function of tumor necrosis factor receptor-associated factor 6
    • Shin JN, Kim I, Lee JS, et al. A novel zinc finger protein that inhibits osteoclastogenesis and the function of tumor necrosis factor receptor-associated factor 6. J Biol Chem 2002;277:8346-53.
    • (2002) J Biol Chem , vol.277 , pp. 8346-8353
    • Shin, J.N.1    Kim, I.2    Lee, J.S.3
  • 147
    • 0031906851 scopus 로고    scopus 로고
    • Peg3/Pw1 is an imprinted gene involved in the TNF-NF-κB signal transduction pathway
    • Relaix F, Wei XJ, Wu X, Sassoon DA. Peg3/Pw1 is an imprinted gene involved in the TNF-NF-κB signal transduction pathway. Nat Genet 1998;18:287-91.
    • (1998) Nat Genet , vol.18 , pp. 287-291
    • Relaix, F.1    Wei, X.J.2    Wu, X.3    Sassoon, D.A.4
  • 148
    • 0037047064 scopus 로고    scopus 로고
    • Role of NF-κB activator Act1 in CD40-mediated signaling in epithelial cells
    • Qian Y, Zhao Z, Jiang Z, Li X. Role of NF-κB activator Act1 in CD40-mediated signaling in epithelial cells. Proc Natl Acad Sci USA 2002;99:9386-91.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9386-9391
    • Qian, Y.1    Zhao, Z.2    Jiang, Z.3    Li, X.4
  • 150
    • 0034066940 scopus 로고    scopus 로고
    • TRAF3 interacts with p62 nucleoporin, a component of the nuclear pore central plug that binds classical NLS-containing import complexes
    • Gamper C, van Eyndhoven WG, Schweiger E, et al. TRAF3 interacts with p62 nucleoporin, a component of the nuclear pore central plug that binds classical NLS-containing import complexes. Mol Immunol 2000;37:73-84.
    • (2000) Mol Immunol , vol.37 , pp. 73-84
    • Gamper, C.1    Van Eyndhoven, W.G.2    Schweiger, E.3
  • 151
    • 0034614656 scopus 로고    scopus 로고
    • Physical and functional interaction of filamin (actin-binding protein-280) and tumor necrosis factor receptor-associated factor 2
    • Leonardi A, Ellinger-Ziegelbauer H, Franzoso G, Brown K, Siebenlist U. Physical and functional interaction of filamin (actin-binding protein-280) and tumor necrosis factor receptor-associated factor 2. J Biol Chem 2000;275:271-8.
    • (2000) J Biol Chem , vol.275 , pp. 271-278
    • Leonardi, A.1    Ellinger-Ziegelbauer, H.2    Franzoso, G.3    Brown, K.4    Siebenlist, U.5
  • 152
    • 0034604714 scopus 로고    scopus 로고
    • MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network
    • Ling L, Goeddel DV. MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network. J Biol Chem 2000;275:23852-60.
    • (2000) J Biol Chem , vol.275 , pp. 23852-23860
    • Ling, L.1    Goeddel, D.V.2
  • 153
    • 0000564581 scopus 로고    scopus 로고
    • The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κB activation
    • Song HY, Rothe M, Goeddel DV. The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κB activation. Proc Natl Acad Sci USA 1996;93:6721-5.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6721-6725
    • Song, H.Y.1    Rothe, M.2    Goeddel, D.V.3
  • 154
    • 0029774552 scopus 로고    scopus 로고
    • I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction
    • Rothe M, Xiong J, Shu HB, et al. I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction. Proc Natl Acad Sci USA 1996;93:8241-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8241-8246
    • Rothe, M.1    Xiong, J.2    Shu, H.B.3
  • 155
    • 18344384218 scopus 로고    scopus 로고
    • Downstream regulator TANK binds to the CD40 recognition site on TRAF3
    • Li C, Ni CZ, Havert ML, et al. Downstream regulator TANK binds to the CD40 recognition site on TRAF3. Structure (Camb) 2002;10:403-11.
    • (2002) Structure (Camb) , vol.10 , pp. 403-411
    • Li, C.1    Ni, C.Z.2    Havert, M.L.3
  • 156
    • 0033485542 scopus 로고    scopus 로고
    • NF-κB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase
    • Pomerantz JL, Baltimore D. NF-κB activation by a signaling complex containing TRAF2, TANK and TBK1, a novel IKK-related kinase. EMBO J 1999;18:6694-704.
    • (1999) EMBO J , vol.18 , pp. 6694-6704
    • Pomerantz, J.L.1    Baltimore, D.2
  • 157
    • 0033624823 scopus 로고    scopus 로고
    • NF-kappaB activation through IKKi-dependent I-TRAF/TANK phosphorylation
    • Nomura F, Kawai T, Nakanishi K, Akira S. NF-kappaB activation through IKKi-dependent I-TRAF/TANK phosphorylation. Genes Cells 2000;5:191-202.
    • (2000) Genes Cells , vol.5 , pp. 191-202
    • Nomura, F.1    Kawai, T.2    Nakanishi, K.3    Akira, S.4
  • 158
    • 0037020147 scopus 로고    scopus 로고
    • Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases
    • Chariot A, Leonardi A, Muller J, et al. Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases. J Biol Chem 2002;277:37029-36.
    • (2002) J Biol Chem , vol.277 , pp. 37029-37036
    • Chariot, A.1    Leonardi, A.2    Muller, J.3
  • 160
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-kappaB
    • Wang CY, Mayo MW, Baldwin Jr AS. TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kappaB. Science 1996;274:784-7.
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin A.S., Jr.3
  • 161
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kappaB in preventing TNF-alpha-induced cell death
    • Beg AA, Baltimore D. An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 1996;274:782-4.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 162
    • 0036337748 scopus 로고    scopus 로고
    • A20 inhibits tumor necrosis factor (TNF) alpha-induced apoptosis by disrupting recruitment of TRADD and RIP to the TNF receptor 1 complex in Jurkat T cells
    • He KL, Ting AT. A20 inhibits tumor necrosis factor (TNF) alpha-induced apoptosis by disrupting recruitment of TRADD and RIP to the TNF receptor 1 complex in Jurkat T cells. Mol Cell Biol 2002;22:6034-45.
    • (2002) Mol Cell Biol , vol.22 , pp. 6034-6045
    • He, K.L.1    Ting, A.T.2
  • 163
    • 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, Goeddel DV, Baldwin Jr AS. NF-kappaB antiapoptosis: induction, of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 1998;281:1680-3.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin A.S., Jr.5
  • 164
    • 0035930326 scopus 로고    scopus 로고
    • Blocking caspase-3-mediated proteolysis of IKKbeta suppresses TNF-alpha-induced apoptosis
    • Tang G, Yang J, Minemoto Y, Lin A. Blocking caspase-3-mediated proteolysis of IKKbeta suppresses TNF-alpha-induced apoptosis. Mol Cell 2001;8:1005-16.
    • (2001) Mol Cell , vol.8 , pp. 1005-1016
    • Tang, G.1    Yang, J.2    Minemoto, Y.3    Lin, A.4
  • 165
    • 0035891320 scopus 로고    scopus 로고
    • Inhibition of JNK activation through NF-kappaB target genes
    • Tang G, Minemoto Y, Dibling B, et al. Inhibition of JNK activation through NF-kappaB target genes. Nature 2001;414:313-7.
    • (2001) Nature , vol.414 , pp. 313-317
    • Tang, G.1    Minemoto, Y.2    Dibling, B.3
  • 166
    • 0036882166 scopus 로고    scopus 로고
    • The absence of NF-kappaB-mediated inhibition of c-Jun N-terminal kinase activation contributes to tumor necrosis factor alpha-induced apoptosis
    • Tang F, Tang G, Xiang J, et al. The absence of NF-kappaB-mediated inhibition of c-Jun N-terminal kinase activation contributes to tumor necrosis factor alpha-induced apoptosis. Mol Cell Biol 2002;22:8571-9.
    • (2002) Mol Cell Biol , vol.22 , pp. 8571-8579
    • Tang, F.1    Tang, G.2    Xiang, J.3
  • 167
    • 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, Weissman AM, Ashwell JD. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 2000;288:874-7.
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 168
    • 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. TRAF1 is a negative regulator of TNF signaling. Enhanced TNF signaling in TRAF1-deficient mice. Immunity 2001;15:647-57.
    • (2001) Immunity , vol.15 , pp. 647-657
    • Tsitsikov, E.N.1    Laouini, D.2    Dunn, I.F.3
  • 169
    • 0016723594 scopus 로고
    • An endotoxin-induced serum factor that causes necrosis of tumors
    • Carswell EA, Old LJ, Kassel RL, et al. An endotoxin-induced serum factor that causes necrosis of tumors. Proc Natl Acad Sci USA 1975;72:3666-70.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3666-3670
    • Carswell, E.A.1    Old, L.J.2    Kassel, R.L.3
  • 170
    • 0032923705 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha antibody (infliximab) therapy profoundly down-regulates the inflammation in Crohn's ileocolitis
    • Baert FJ, D'Haens GR, Peeters M, et al. Tumor necrosis factor alpha antibody (infliximab) therapy profoundly down-regulates the inflammation in Crohn's ileocolitis. Gastroenterology 1999;116:22-8.
    • (1999) Gastroenterology , vol.116 , pp. 22-28
    • Baert, F.J.1    D'Haens, G.R.2    Peeters, M.3
  • 171
    • 0013511183 scopus 로고    scopus 로고
    • Treatment of rheumatoid arthritis with a recombinant human tumor necrosis factor receptor (p75)-Fc fusion protein
    • Moreland LW, Baumgartner SW, Schiff MH, et al. Treatment of rheumatoid arthritis with a recombinant human tumor necrosis factor receptor (p75)-Fc fusion protein. N Engl J Med 1997;337:141-7.
    • (1997) N Engl J Med , vol.337 , pp. 141-147
    • Moreland, L.W.1    Baumgartner, S.W.2    Schiff, M.H.3


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