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Volumn 32, Issue 13, 2012, Pages 2515-2529

The Tumor Necrosis Factor Receptor Stalk Regions Define Responsiveness to Soluble versus Membrane-Bound Ligand

Author keywords

[No Author keywords available]

Indexed keywords

TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2;

EID: 84864018997     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.06458-11     Document Type: Article
Times cited : (48)

References (80)
  • 1
    • 33750269857 scopus 로고    scopus 로고
    • Transmembrane TNF protects mutant mice against intracellular bacterial infections, chronic inflammation and autoimmunity
    • Alexopoulou L, et al. 2006. Transmembrane TNF protects mutant mice against intracellular bacterial infections, chronic inflammation and autoimmunity. Eur. J. Immunol. 36:2768 -2780.
    • (2006) Eur. J. Immunol. , vol.36 , pp. 2768-2780
    • Alexopoulou, L.1
  • 2
    • 43649105672 scopus 로고    scopus 로고
    • An essential role for transmembrane TNF in the resolution of the inflammatory lesion induced by Leishmania major infection
    • Allenbach C, Launois P, Mueller C, Tacchini-Cottier F. 2008. An essential role for transmembrane TNF in the resolution of the inflammatory lesion induced by Leishmania major infection. Eur. J. Immunol. 38:720- 731.
    • (2008) Eur. J. Immunol. , vol.38 , pp. 720-731
    • Allenbach, C.1    Launois, P.2    Mueller, C.3    Tacchini-Cottier, F.4
  • 3
    • 79951501790 scopus 로고    scopus 로고
    • Cellular mechanisms of TNF function in models of inflammation and autoimmunity
    • Apostolaki M, Armaka M, Victoratos P, Kollias G. 2010. Cellular mechanisms of TNF function in models of inflammation and autoimmunity. Curr. Dir. Autoimmun. 11:1-26.
    • (2010) Curr. Dir. Autoimmun. , vol.11 , pp. 1-26
    • Apostolaki, M.1    Armaka, M.2    Victoratos, P.3    Kollias, G.4
  • 4
    • 51649084550 scopus 로고    scopus 로고
    • Selective death of autoreactive T cells in human diabetes by TNF or TNF receptor 2 agonism
    • Ban L, et al. 2008. Selective death of autoreactive T cells in human diabetes by TNF or TNF receptor 2 agonism. Proc. Natl. Acad. Sci. U. S. A. 105:13644 -13649.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13644-13649
    • Ban, L.1
  • 5
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation
    • Banner DW, et al. 1993. Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation. Cell 73:431- 445.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1
  • 6
    • 77952924538 scopus 로고    scopus 로고
    • Antiinflammatory effects of tumor necrosis factor on hematopoietic cells in a murine model of erosive arthritis
    • Bluml S, et al. 2010. Antiinflammatory effects of tumor necrosis factor on hematopoietic cells in a murine model of erosive arthritis. Arthritis Rheum. 62:1608 -1619.
    • (2010) Arthritis Rheum , vol.62 , pp. 1608-1619
    • Bluml, S.1
  • 7
    • 77952290633 scopus 로고    scopus 로고
    • Single chain TNF derivatives with individually mutated receptor binding sites reveal differential stoichiometry of ligand receptor complex formation for TNFR1 and TNFR2
    • Boschert V, et al. 2010. Single chain TNF derivatives with individually mutated receptor binding sites reveal differential stoichiometry of ligand receptor complex formation for TNFR1 and TNFR2. Cell Signal 22:1088- 1096.
    • (2010) Cell Signal , vol.22 , pp. 1088-1096
    • Boschert, V.1
  • 8
    • 38949206321 scopus 로고    scopus 로고
    • TACI, unlike BAFF-R, is solely activated by oligomeric BAFF and APRIL to support survival of activated B cells and plasmablasts
    • Bossen C, et al. 2008. TACI, unlike BAFF-R, is solely activated by oligomeric BAFF and APRIL to support survival of activated B cells and plasmablasts. Blood 111:1004 -1012.
    • (2008) Blood , vol.111 , pp. 1004-1012
    • Bossen, C.1
  • 9
    • 71349086770 scopus 로고    scopus 로고
    • Dual function of cysteine rich domain (CRD) 1 of TNF receptor type 1: conformational stabilization of CRD2 and control of receptor responsiveness
    • Branschadel M, et al. 2010. Dual function of cysteine rich domain (CRD) 1 of TNF receptor type 1: conformational stabilization of CRD2 and control of receptor responsiveness. Cell Signal 22:404-414.
    • (2010) Cell Signal , vol.22 , pp. 404-414
    • Branschadel, M.1
  • 10
    • 27944432140 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-functionalized nanostructured particles for the stimulation of membrane TNF-specific cell responses
    • Bryde S, et al. 2005. Tumor necrosis factor (TNF)-functionalized nanostructured particles for the stimulation of membrane TNF-specific cell responses. Bioconjug. Chem. 16:1459 -1467.
    • (2005) Bioconjug. Chem. , vol.16 , pp. 1459-1467
    • Bryde, S.1
  • 11
    • 36448978124 scopus 로고    scopus 로고
    • TNF-alpha is critical for antitumor but not antiviral T cell immunity in mice
    • Calzascia T, et al. 2007. TNF-alpha is critical for antitumor but not antiviral T cell immunity in mice. J. Clin. Invest. 117:3833-3845.
    • (2007) J. Clin. Invest. , vol.117 , pp. 3833-3845
    • Calzascia, T.1
  • 12
    • 34247899117 scopus 로고    scopus 로고
    • Three is better than one: pre-ligand receptor assembly in the regulation of TNF receptor signaling
    • Chan FK. 2007. Three is better than one: pre-ligand receptor assembly in the regulation of TNF receptor signaling. Cytokine 37:101-107.
    • (2007) Cytokine , vol.37 , pp. 101-107
    • Chan, F.K.1
  • 13
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligandindependent receptor assembly and signaling
    • Chan FK, et al. 2000. A domain in TNF receptors that mediates ligandindependent receptor assembly and signaling. Science 288:2351-2354.
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.1
  • 14
    • 80052680230 scopus 로고    scopus 로고
    • Contrasting effects of TNF and anti-TNF on the activation of effector T cells and regulatory T cells in autoimmunity
    • Chen X, Oppenheim JJ. 2011. Contrasting effects of TNF and anti-TNF on the activation of effector T cells and regulatory T cells in autoimmunity. FEBS Lett. 585:3611-3618.
    • (2011) FEBS Lett , vol.585 , pp. 3611-3618
    • Chen, X.1    Oppenheim, J.J.2
  • 15
    • 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. 2002. Restricted localization of the TNF receptor CD120a to lipid rafts: a novel role for the death domain. J. Immunol. 168:4095- 4102.
    • (2002) J. Immunol. , vol.168 , pp. 4095-4102
    • Cottin, V.1    Doan, J.E.2    Riches, D.W.3
  • 16
    • 77954932140 scopus 로고    scopus 로고
    • Targeting of tumor necrosis factor receptor 1 to low density plasma membrane domains in human endothelial cells
    • D'Alessio A, et al. 2010. Targeting of tumor necrosis factor receptor 1 to low density plasma membrane domains in human endothelial cells. J. Biol. Chem. 285:23868 -23879.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23868-23879
    • D'Alessio, A.1
  • 17
    • 71849095544 scopus 로고    scopus 로고
    • Equilibrium mechanisms of receptor clustering
    • Duke T, Graham I. 2009. Equilibrium mechanisms of receptor clustering. Prog. Biophys. Mol. Biol. 100:18 -24.
    • (2009) Prog. Biophys. Mol. Biol. , vol.100 , pp. 18-24
    • Duke, T.1    Graham, I.2
  • 18
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains: an overview
    • Epand RM, Thomas A, Brasseur R, Epand RF. 2010. Cholesterol interaction with proteins that partition into membrane domains: an overview. Subcell. Biochem. 51:253-278.
    • (2010) Subcell. Biochem. , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 19
    • 77957794023 scopus 로고    scopus 로고
    • Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95C terminus
    • Esposito D, et al. 2010. Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95C terminus. Structure 18:1378 -1390.
    • (2010) Structure , vol.18 , pp. 1378-1390
    • Esposito, D.1
  • 20
    • 77953136143 scopus 로고    scopus 로고
    • TNF receptor 2 pathway: drug target for autoimmune diseases
    • Faustman D, Davis M. 2010. TNF receptor 2 pathway: drug target for autoimmune diseases. Nat. Rev. Drug Discov. 9:482- 493.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 482-493
    • Faustman, D.1    Davis, M.2
  • 21
    • 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, Peter ME. 2007. Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling. EMBO J. 26:221-231.
    • (2007) EMBO J , vol.26 , pp. 221-231
    • Feig, C.1    Tchikov, V.2    Schutze, S.3    Peter, M.E.4
  • 22
    • 0036548875 scopus 로고    scopus 로고
    • Neurodegenerative and neuroprotective effects of tumor necrosis factor (TNF) in retinal ischemia: opposite roles of TNF receptor 1 and TNF receptor 2
    • Fontaine V, et al. 2002. Neurodegenerative and neuroprotective effects of tumor necrosis factor (TNF) in retinal ischemia: opposite roles of TNF receptor 1 and TNF receptor 2. J. Neurosci. 22:RC216.
    • (2002) J. Neurosci. , vol.22
    • Fontaine, V.1
  • 23
    • 77952549882 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy reveals topological segregation of the two tumor necrosis factor membrane receptors
    • Gerken M, et al. 2010. Fluorescence correlation spectroscopy reveals topological segregation of the two tumor necrosis factor membrane receptors. Biochim. Biophys. Acta 1798:1081-1089.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1081-1089
    • Gerken, M.1
  • 24
    • 0028866022 scopus 로고
    • The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor
    • Grell M, et al. 1995. The transmembrane form of tumor necrosis factor is the prime activating ligand of the 80 kDa tumor necrosis factor receptor. Cell 83:793- 802.
    • (1995) Cell , vol.83 , pp. 793-802
    • Grell, M.1
  • 25
    • 0031882913 scopus 로고    scopus 로고
    • The type 1 receptor (CD120a) is the high-affinity receptor for soluble tumor necrosis factor
    • Grell M, Wajant H, Zimmermann G, Scheurich P. 1998. The type 1 receptor (CD120a) is the high-affinity receptor for soluble tumor necrosis factor. Proc. Natl. Acad. Sci. U. S. A. 95:570 -575.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 570-575
    • Grell, M.1    Wajant, H.2    Zimmermann, G.3    Scheurich, P.4
  • 26
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding AS, Hancock JF. 2008. Using plasma membrane nanoclusters to build better signaling circuits. Trends Cell Biol. 18:364 -371.
    • (2008) Trends Cell Biol , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 27
    • 16844381848 scopus 로고    scopus 로고
    • The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability
    • Henkler F, et al. 2005. The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability. J. Cell Biol. 168:1087-1098.
    • (2005) J. Cell Biol. , vol.168 , pp. 1087-1098
    • Henkler, F.1
  • 28
    • 0037315457 scopus 로고    scopus 로고
    • Two adjacent trimeric Fas ligands are required for Fas signaling and formation of a death-inducing signaling complex
    • Holler N, et al. 2003. Two adjacent trimeric Fas ligands are required for Fas signaling and formation of a death-inducing signaling complex. Mol. Cell. Biol. 23:1428 -1440.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1428-1440
    • Holler, N.1
  • 29
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H, Shu HB, Pan MG, Goeddel DV. 1996. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84:299 -308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 30
    • 33845921822 scopus 로고    scopus 로고
    • Spatial compartmentalization of tumor necrosis factor (TNF) receptor 1-dependent signaling pathways in human airway smooth muscle cells. Lipid rafts are essential for TNF-alphamediated activation of RhoA but dispensable for the activation of the NF-kappaB and MAPK pathways
    • Hunter I, Nixon GF. 2006. Spatial compartmentalization of tumor necrosis factor (TNF) receptor 1-dependent signaling pathways in human airway smooth muscle cells. Lipid rafts are essential for TNF-alphamediated activation of RhoA but dispensable for the activation of the NF-kappaB and MAPK pathways. J. Biol. Chem. 281:34705-34715.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34705-34715
    • Hunter, I.1    Nixon, G.F.2
  • 31
    • 30744461133 scopus 로고    scopus 로고
    • TNF receptor type 2 (p75) functions as a costimulator for antigen-driven T cell responses in vivo
    • Kim EY, Priatel JJ, Teh SJ, Teh HS. 2006. TNF receptor type 2 (p75) functions as a costimulator for antigen-driven T cell responses in vivo. J. Immunol. 176:1026 -1035.
    • (2006) J. Immunol. , vol.176 , pp. 1026-1035
    • Kim, E.Y.1    Priatel, J.J.2    Teh, S.J.3    Teh, H.S.4
  • 32
    • 4644296132 scopus 로고    scopus 로고
    • Critical role of TNF receptor type-2 (p75) as a costimulator for IL-2 induction and T cell survival: a functional link to CD28
    • Kim EY, Teh HS. 2004. Critical role of TNF receptor type-2 (p75) as a costimulator for IL-2 induction and T cell survival: a functional link to CD28. J. Immunol. 173:4500-4509.
    • (2004) J. Immunol. , vol.173 , pp. 4500-4509
    • Kim, E.Y.1    Teh, H.S.2
  • 33
    • 0035892888 scopus 로고    scopus 로고
    • TNF type 2 receptor (p75) lowers the threshold of T cell activation
    • Kim EY, Teh HS. 2001. TNF type 2 receptor (p75) lowers the threshold of T cell activation. J. Immunol. 167:6812- 6820.
    • (2001) J. Immunol. , vol.167 , pp. 6812-6820
    • Kim, E.Y.1    Teh, H.S.2
  • 34
    • 77956395771 scopus 로고    scopus 로고
    • Critical role for TNF in the induction of human antigen-specific regulatory T cells by tolerogenic dendritic cells
    • Kleijwegt FS, et al. 2010. Critical role for TNF in the induction of human antigen-specific regulatory T cells by tolerogenic dendritic cells. J. Immunol. 185:1412-1418.
    • (2010) J. Immunol. , vol.185 , pp. 1412-1418
    • Kleijwegt, F.S.1
  • 35
    • 69949108378 scopus 로고    scopus 로고
    • Functional analysis of the posttranslational modifications of the death receptor 6
    • Klima M, Zajedova J, Doubravska L, Andera L. 2009. Functional analysis of the posttranslational modifications of the death receptor 6. Biochim. Biophys. Acta 1793:1579 -1587.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1579-1587
    • Klima, M.1    Zajedova, J.2    Doubravska, L.3    Andera, L.4
  • 36
    • 0036694562 scopus 로고    scopus 로고
    • Role of TNF/TNFR in autoimmunity: specific TNF receptor blockade may be advantageous to anti-TNF treatments
    • Kollias G, Kontoyiannis D. 2002. Role of TNF/TNFR in autoimmunity: specific TNF receptor blockade may be advantageous to anti-TNF treatments. Cytokine Growth Factor Rev. 13:315-321.
    • (2002) Cytokine Growth Factor Rev , vol.13 , pp. 315-321
    • Kollias, G.1    Kontoyiannis, D.2
  • 37
    • 41149115774 scopus 로고    scopus 로고
    • A humanized tumor necrosis factor receptor 1 (TNFR1)-specific antagonistic antibody for selective inhibition of tumor necrosis factor (TNF) action
    • Kontermann RE, et al. 2008. A humanized tumor necrosis factor receptor 1 (TNFR1)-specific antagonistic antibody for selective inhibition of tumor necrosis factor (TNF) action. J. Immunother. 31:225-234.
    • (2008) J. Immunother. , vol.31 , pp. 225-234
    • Kontermann, R.E.1
  • 38
    • 0037113868 scopus 로고    scopus 로고
    • Control of receptor-induced signaling complex formation by the kinetics of ligand/receptor interaction
    • Krippner-Heidenreich A, et al. 2002. Control of receptor-induced signaling complex formation by the kinetics of ligand/receptor interaction. J. Biol. Chem. 277:44155- 44163.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44155-44163
    • Krippner-Heidenreich, A.1
  • 39
    • 0030851538 scopus 로고    scopus 로고
    • Assembly and regulation of the CD40 receptor complex in human B cells
    • Kuhne MR, et al. 1997. Assembly and regulation of the CD40 receptor complex in human B cells. J. Exp. Med. 186:337-342.
    • (1997) J. Exp. Med. , vol.186 , pp. 337-342
    • Kuhne, M.R.1
  • 40
    • 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, Bron C. 2003. Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation. Immunity 18:655- 664.
    • (2003) Immunity , vol.18 , pp. 655-664
    • Legler, D.F.1    Micheau, O.2    Doucey, M.A.3    Tschopp, J.4    Bron, C.5
  • 41
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: integrating mammalian biology
    • Locksley RM, Killeen N, Lenardo MJ. 2001. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104:487-501.
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 43
    • 63849224157 scopus 로고    scopus 로고
    • Anti-inflammatory effects of tumour necrosis factor (TNF)-alpha are mediated via TNF-R2 (p75) in tolerogenic transforming growth factor-beta-treated antigen-presenting cells
    • Masli S, Turpie B. 2009. Anti-inflammatory effects of tumour necrosis factor (TNF)-alpha are mediated via TNF-R2 (p75) in tolerogenic transforming growth factor-beta-treated antigen-presenting cells. Immunology 127:62-72.
    • (2009) Immunology , vol.127 , pp. 62-72
    • Masli, S.1    Turpie, B.2
  • 44
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. 2003. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114:181-190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 45
    • 78449233994 scopus 로고    scopus 로고
    • Solution of the structure of the TNF-TNFR2 complex
    • doi:10.1126/scisignal.2000954
    • Mukai Y, et al. 2010. Solution of the structure of the TNF-TNFR2 complex. Sci. Signal 3:ra83. doi:10.1126/scisignal.2000954.
    • (2010) Sci. Signal. , vol.3
    • Mukai, Y.1
  • 46
    • 42449106534 scopus 로고    scopus 로고
    • Activity of soluble OX40 ligand is enhanced by oligomerization and cell surface immobilization
    • Muller N, Wyzgol A, Munkel S, Pfizenmaier K, Wajant H. 2008. Activity of soluble OX40 ligand is enhanced by oligomerization and cell surface immobilization. FEBS J. 275:2296 -2304.
    • (2008) FEBS J , vol.275 , pp. 2296-2304
    • Muller, N.1    Wyzgol, A.2    Munkel, S.3    Pfizenmaier, K.4    Wajant, H.5
  • 47
    • 1142287412 scopus 로고    scopus 로고
    • Ligand-independent redistribution of Fas (CD95) into lipid rafts mediates clonotypic T cell death
    • Muppidi JR, Siegel RM. 2004. Ligand-independent redistribution of Fas (CD95) into lipid rafts mediates clonotypic T cell death. Nat. Immunol. 5:182-189.
    • (2004) Nat. Immunol. , vol.5 , pp. 182-189
    • Muppidi, J.R.1    Siegel, R.M.2
  • 48
    • 5644222552 scopus 로고    scopus 로고
    • Life and death decisions: secondary complexes and lipid rafts in TNF receptor family signal transduction
    • Muppidi JR, Tschopp J, Siegel RM. 2004. Life and death decisions: secondary complexes and lipid rafts in TNF receptor family signal transduction. Immunity 21:461- 465.
    • (2004) Immunity , vol.21 , pp. 461-465
    • Muppidi, J.R.1    Tschopp, J.2    Siegel, R.M.3
  • 49
    • 0029069758 scopus 로고
    • Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor
    • Naismith JH, Devine TQ, Brandhuber BJ, Sprang SR. 1995. Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor. J. Biol. Chem. 270:13303-13307.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13303-13307
    • Naismith, J.H.1    Devine, T.Q.2    Brandhuber, B.J.3    Sprang, S.R.4
  • 51
  • 52
    • 0034597013 scopus 로고    scopus 로고
    • CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway
    • Parlato S, et al. 2000. CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway. EMBO J. 19:5123-5134.
    • (2000) EMBO J , vol.19 , pp. 5123-5134
    • Parlato, S.1
  • 53
    • 0027456514 scopus 로고
    • Biochemical characterization of the extracellular domain of the 75-kilodalton tumor necrosis factor receptor
    • Pennica D, et al. 1993. Biochemical characterization of the extracellular domain of the 75-kilodalton tumor necrosis factor receptor. Biochemistry 32:3131-3138.
    • (1993) Biochemistry , vol.32 , pp. 3131-3138
    • Pennica, D.1
  • 54
    • 0031985413 scopus 로고    scopus 로고
    • TNF receptor-deficient mice reveal divergent roles for p55 and p75 in several models of inflammation
    • Peschon JJ, et al. 1998. TNF receptor-deficient mice reveal divergent roles for p55 and p75 in several models of inflammation. J. Immunol. 160:943- 952.
    • (1998) J. Immunol. , vol.160 , pp. 943-952
    • Peschon, J.J.1
  • 55
    • 0023245022 scopus 로고
    • Tumor necrosis factor (TNF) alpha: control of TNF-sensitivity and molecular mechanisms of TNF-mediated growth inhibition
    • Pfizenmaier K, Kronke M, Scheurich P, Nagel GA. 1987. Tumor necrosis factor (TNF) alpha: control of TNF-sensitivity and molecular mechanisms of TNF-mediated growth inhibition. Blut 55:1-10.
    • (1987) Blut , vol.55 , pp. 1-10
    • Pfizenmaier, K.1    Kronke, M.2    Scheurich, P.3    Nagel, G.A.4
  • 56
    • 79961138056 scopus 로고    scopus 로고
    • Tumor necrosis factor restricts hematopoietic stem cell activity in mice: involvement of two distinct receptors
    • Pronk CJ, Veiby OP, Bryder D, Jacobsen SE. 2011. Tumor necrosis factor restricts hematopoietic stem cell activity in mice: involvement of two distinct receptors. J. Exp. Med. 208:1563-1570.
    • (2011) J. Exp. Med. , vol.208 , pp. 1563-1570
    • Pronk, C.J.1    Veiby, O.P.2    Bryder, D.3    Jacobsen, S.E.4
  • 57
    • 67349258025 scopus 로고    scopus 로고
    • Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation
    • Rabinovich GA, Toscano MA. 2009. Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat. Rev. Immunol. 9:338 -352.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 59
    • 38449115712 scopus 로고    scopus 로고
    • Cutting edge: Rac GTPases sensitize activated T cells to die via Fas
    • Ramaswamy M, et al. 2007. Cutting edge: Rac GTPases sensitize activated T cells to die via Fas. J. Immunol. 179:6384-6388.
    • (2007) J. Immunol. , vol.179 , pp. 6384-6388
    • Ramaswamy, M.1
  • 60
    • 71949099511 scopus 로고    scopus 로고
    • Nanoscale arrangement of apoptotic ligands reveals a demand for a minimal lateral distance for efficient death receptor activation
    • Ranzinger J, et al. 2009. Nanoscale arrangement of apoptotic ligands reveals a demand for a minimal lateral distance for efficient death receptor activation. Nano Lett. 9:4240-4245.
    • (2009) Nano Lett , vol.9 , pp. 4240-4245
    • Ranzinger, J.1
  • 61
    • 77951234694 scopus 로고    scopus 로고
    • Membrane tumor necrosis factor (TNF) induces p100 processing via TNF receptor-2 (TNFR2)
    • Rauert H, et al. 2010. Membrane tumor necrosis factor (TNF) induces p100 processing via TNF receptor-2 (TNFR2). J. Biol. Chem. 285:7394- 7404.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7394-7404
    • Rauert, H.1
  • 62
    • 40449113243 scopus 로고    scopus 로고
    • TNF-alpha is critical to facilitate hemopoietic stem cell engraftment and function
    • Rezzoug F, et al. 2008. TNF-alpha is critical to facilitate hemopoietic stem cell engraftment and function. J. Immunol. 180:49 -57.
    • (2008) J. Immunol. , vol.180 , pp. 49-57
    • Rezzoug, F.1
  • 63
    • 50249118029 scopus 로고    scopus 로고
    • A novel juxtamembrane domain in tumor necrosis factor receptor superfamily molecules activates Rac1 and controls neurite growth
    • Ruan W, Lee CT, Desbarats J. 2008. A novel juxtamembrane domain in tumor necrosis factor receptor superfamily molecules activates Rac1 and controls neurite growth. Mol. Biol. Cell 19:3192-3202.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3192-3202
    • Ruan, W.1    Lee, C.T.2    Desbarats, J.3
  • 64
    • 17944381638 scopus 로고    scopus 로고
    • Membrane-bound TNF supports secondary lymphoid organ structure but is subservient to secreted TNF in driving autoimmune inflammation
    • Ruuls SR, et al. 2001. Membrane-bound TNF supports secondary lymphoid organ structure but is subservient to secreted TNF in driving autoimmune inflammation. Immunity 15:533-543.
    • (2001) Immunity , vol.15 , pp. 533-543
    • Ruuls, S.R.1
  • 65
    • 3543037051 scopus 로고    scopus 로고
    • T cell-derived tumour necrosis factor is essential, but not sufficient, for protection against Mycobacterium tuberculosis infection
    • Saunders BM, Briscoe H, Britton WJ. 2004. T cell-derived tumour necrosis factor is essential, but not sufficient, for protection against Mycobacterium tuberculosis infection. Clin. Exp. Immunol. 137:279 -287.
    • (2004) Clin. Exp. Immunol. , vol.137 , pp. 279-287
    • Saunders, B.M.1    Briscoe, H.2    Britton, W.J.3
  • 66
    • 33947172058 scopus 로고    scopus 로고
    • Life and death in the granuloma: immunopathology of tuberculosis
    • Saunders BM, Britton WJ. 2007. Life and death in the granuloma: immunopathology of tuberculosis. Immunol. Cell Biol. 85:103-111.
    • (2007) Immunol. Cell Biol. , vol.85 , pp. 103-111
    • Saunders, B.M.1    Britton, W.J.2
  • 67
    • 4444341939 scopus 로고    scopus 로고
    • Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles
    • Schneider-Brachert W, et al. 2004. Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles. Immunity 21:415- 428.
    • (2004) Immunity , vol.21 , pp. 415-428
    • Schneider-Brachert, W.1
  • 68
    • 0034733584 scopus 로고    scopus 로고
    • Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    • Siegel RM, et al. 2000. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 288:2354- 2357.
    • (2000) Science , vol.288 , pp. 2354-2357
    • Siegel, R.M.1
  • 69
    • 9444268061 scopus 로고    scopus 로고
    • SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane
    • Siegel RM, et al. 2004. SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane. J. Cell Biol. 167:735-744.
    • (2004) J. Cell Biol. , vol.167 , pp. 735-744
    • Siegel, R.M.1
  • 70
    • 33845882484 scopus 로고    scopus 로고
    • Biologic therapies in rheumatology: lessons learned, future directions
    • Strand V, Kimberly R, Isaacs JD. 2007. Biologic therapies in rheumatology: lessons learned, future directions. Nat. Rev. Drug Discov. 6:75-92.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 75-92
    • Strand, V.1    Kimberly, R.2    Isaacs, J.D.3
  • 71
    • 70350446680 scopus 로고    scopus 로고
    • Biological activity of ectodysplasin A is conditioned by its collagen and heparan sulfate proteoglycan-binding domains
    • Swee LK, et al. 2009. Biological activity of ectodysplasin A is conditioned by its collagen and heparan sulfate proteoglycan-binding domains. J. Biol. Chem. 284:27567-27576.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27567-27576
    • Swee, L.K.1
  • 72
    • 50549094089 scopus 로고    scopus 로고
    • Interpreting crosstalk between TNF-alpha and NGF: potential implications for disease
    • Takei Y, Laskey R. 2008. Interpreting crosstalk between TNF-alpha and NGF: potential implications for disease. Trends Mol. Med. 14: 381-388.
    • (2008) Trends Mol. Med. , vol.14 , pp. 381-388
    • Takei, Y.1    Laskey, R.2
  • 73
    • 79955477738 scopus 로고    scopus 로고
    • The growth factor progranulin binds to TNF receptors and is therapeutic against inflammatory arthritis in mice
    • Tang W, et al. 2011. The growth factor progranulin binds to TNF receptors and is therapeutic against inflammatory arthritis in mice. Science 332:478-484.
    • (2011) Science , vol.332 , pp. 478-484
    • Tang, W.1
  • 74
    • 77956615515 scopus 로고    scopus 로고
    • Activation of TNF receptor 2 in microglia promotes induction of anti-inflammatory pathways
    • Veroni C, et al. 2010. Activation of TNF receptor 2 in microglia promotes induction of anti-inflammatory pathways. Mol. Cell Neurosci. 45:234- 244.
    • (2010) Mol. Cell Neurosci. , vol.45 , pp. 234-244
    • Veroni, C.1
  • 75
    • 34948894931 scopus 로고    scopus 로고
    • Death-receptor O-glycosylation controls tumor-cell sensitivity to the proapoptotic ligand Apo2L/TRAIL
    • Wagner KW, et al. 2007. Death-receptor O-glycosylation controls tumor-cell sensitivity to the proapoptotic ligand Apo2L/TRAIL. Nat. Med. 13:1070 -1077.
    • (2007) Nat. Med. , vol.13 , pp. 1070-1077
    • Wagner, K.W.1
  • 76
    • 0035811587 scopus 로고    scopus 로고
    • Differential activation of TRAIL-R1 and -2 by soluble and membrane TRAIL allows selective surface antigen-directed activation of TRAIL-R2 by a soluble TRAIL derivative
    • Wajant H, et al. 2001. Differential activation of TRAIL-R1 and -2 by soluble and membrane TRAIL allows selective surface antigen-directed activation of TRAIL-R2 by a soluble TRAIL derivative. Oncogene 20: 4101-4106.
    • (2001) Oncogene , vol.20 , pp. 4101-4106
    • Wajant, H.1
  • 78
    • 33750485302 scopus 로고    scopus 로고
    • Risk and prevention of tuberculosis and other serious opportunistic infections associated with the inhibition of tumor necrosis factor
    • Winthrop KL. 2006. Risk and prevention of tuberculosis and other serious opportunistic infections associated with the inhibition of tumor necrosis factor. Nat. Clin. Pract Rheumatol. 2:602- 610.
    • (2006) Nat. Clin. Pract Rheumatol. , vol.2 , pp. 602-610
    • Winthrop, K.L.1
  • 79
    • 68149156979 scopus 로고    scopus 로고
    • Trimer stabilization, oligomerization, and antibody-mediated cell surface immobilization improve the activity of soluble trimers of CD27L, CD40L, 41BBL, and glucocorticoid-induced TNF receptor ligand
    • Wyzgol A, et al. 2009. Trimer stabilization, oligomerization, and antibody-mediated cell surface immobilization improve the activity of soluble trimers of CD27L, CD40L, 41BBL, and glucocorticoid-induced TNF receptor ligand. J. Immunol. 183:1851-1861.
    • (2009) J. Immunol. , vol.183 , pp. 1851-1861
    • Wyzgol, A.1
  • 80
    • 0036346992 scopus 로고    scopus 로고
    • Negative regulation of CD45 by differential homodimerization of the alternatively spliced isoforms
    • Xu Z, Weiss A. 2002. Negative regulation of CD45 by differential homodimerization of the alternatively spliced isoforms. Nat. Immunol. 3:764 -771.
    • (2002) Nat. Immunol. , vol.3 , pp. 764-771
    • Xu, Z.1    Weiss, A.2


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