메뉴 건너뛰기




Volumn 15, Issue 6, 2015, Pages 362-374

Regulation of tumour necrosis factor signalling: Live or let die

Author keywords

[No Author keywords available]

Indexed keywords

CERTOLIZUMAB PEGOL; ETANERCEPT; GOLIMUMAB; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLIXIMAB; POLYUBIQUITIN; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 84929875491     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri3834     Document Type: Review
Times cited : (769)

References (179)
  • 1
    • 0021923645 scopus 로고
    • Human tumor necrosis factor. Production, purification, and characterization
    • Aggarwal, B. B. et al. Human tumor necrosis factor. Production, purification, and characterization. J. Biol. Chem. 260, 2345-2354 (1985).
    • (1985) J. Biol. Chem , vol.260 , pp. 2345-2354
    • Aggarwal, B.B.1
  • 2
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: A double-edged sword
    • Aggarwal, B. B. Signalling pathways of the TNF superfamily: a double-edged sword. Nature Rev. Immunol. 3, 745-756 (2003).
    • (2003) Nature Rev. Immunol , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 3
    • 84862962823 scopus 로고    scopus 로고
    • Historical perspectives on tumor necrosis factor and its superfamily: 25 years later, a golden journey
    • Aggarwal, B. B., Gupta, S. C. & Kim, J. H. Historical perspectives on tumor necrosis factor and its superfamily: 25 years later, a golden journey. Blood 119, 651-665 (2012).
    • (2012) Blood , vol.119 , pp. 651-665
    • Aggarwal, B.B.1    Gupta, S.C.2    Kim, J.H.3
  • 4
    • 0024281428 scopus 로고
    • A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: Ramifications for the complex physiology of TNF
    • Kriegler, M., Perez, C., DeFay, K., Albert, I. & Lu, S. D. A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell 53, 45-53 (1988).
    • (1988) Cell , vol.53 , pp. 45-53
    • Kriegler, M.1    Perez, C.2    Defay, K.3    Albert, I.4    Lu, S.D.5
  • 5
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-? from cells
    • Black, R. A. et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-? from cells. Nature 385, 729-733 (1997).
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1
  • 6
    • 0024357657 scopus 로고
    • The structure of tumor necrosis factor-? at 2.6 Å resolution. Implications for receptor binding
    • Eck, M. J. & Sprang, S. R. The structure of tumor necrosis factor-? at 2.6 Å resolution. Implications for receptor binding. J. Biol. Chem. 264, 17595-17605 (1989).
    • (1989) J. Biol. Chem , vol.264 , pp. 17595-17605
    • Eck, M.J.1    Sprang, S.R.2
  • 7
    • 0024539057 scopus 로고
    • Structure of tumour necrosis factor
    • Jones, E. Y., Stuart, D. I. & Walker, N. P. Structure of tumour necrosis factor. Nature 338, 225-228 (1989).
    • (1989) Nature , vol.338 , pp. 225-228
    • Jones, E.Y.1    Stuart, D.I.2    Walker, N.P.3
  • 8
    • 84855822415 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE
    • Adrain, C., Zettl, M., Christova, Y., Taylor, N. & Freeman, M. Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE. Science 335, 225-228 (2012).
    • (2012) Science , vol.335 , pp. 225-228
    • Adrain, C.1    Zettl, M.2    Christova, Y.3    Taylor, N.4    Freeman, M.5
  • 9
    • 84862909285 scopus 로고    scopus 로고
    • IRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS
    • McIlwain, D. R. et al. iRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS. Science 335, 229-232 (2012).
    • (2012) Science , vol.335 , pp. 229-232
    • McIlwain, D.R.1
  • 10
    • 77953136143 scopus 로고    scopus 로고
    • TNF receptor 2 pathway: Drug target for autoimmune diseases
    • Faustman, D. & Davis, M. TNF receptor 2 pathway: drug target for autoimmune diseases. Nature Rev. Drug Discov. 9, 482-493 (2010).
    • (2010) Nature Rev. Drug Discov , vol.9 , pp. 482-493
    • Faustman, D.1    Davis, M.2
  • 12
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia, L. A., Ayres, T. M., Wong, G. H. & Goeddel, D. V. A novel domain within the 55 kd TNF receptor signals cell death. Cell 74, 845-853 (1993).
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 13
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-?B activation
    • Hsu, H., Xiong, J. & Goeddel, D. V. The TNF receptor 1-associated protein TRADD signals cell death and NF-?B activation. Cell 81, 495-504 (1995).
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 14
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-?B by TNF receptor 2 and CD40
    • Rothe, M., Sarma, V., Dixit, V. M. & Goeddel, D. V. TRAF2-mediated activation of NF-?B by TNF receptor 2 and CD40. Science 269, 1424-1427 (1995).
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 15
    • 0026017971 scopus 로고
    • Interleukin-2 programs mouse T lymphocytes for apoptosis
    • Lenardo, M. J. Interleukin-2 programs mouse T lymphocytes for apoptosis. Nature 353, 858-861 (1991).
    • (1991) Nature , vol.353 , pp. 858-861
    • Lenardo, M.J.1
  • 16
    • 0033452005 scopus 로고    scopus 로고
    • Regulated commitment of TNF receptor signaling: A molecular switch for death or activation
    • Pimentel-Muinos, F. X. & Seed, B. Regulated commitment of TNF receptor signaling: a molecular switch for death or activation. Immunity 11, 783-793 (1999).
    • (1999) Immunity , vol.11 , pp. 783-793
    • Pimentel-Muinos, F.X.1    Seed, B.2
  • 17
    • 0038742813 scopus 로고    scopus 로고
    • Recruitment of TNF receptor 1 to lipid rafts is essential for TNF?-mediated NF-?B activation
    • Legler, D. F., Micheau, O., Doucey, M. A., Tschopp, J. & Bron, C. Recruitment of TNF receptor 1 to lipid rafts is essential for TNF?-mediated NF-?B activation. Immunity 18, 655-664 (2003).
    • (2003) Immunity , vol.18 , pp. 655-664
    • Legler, D.F.1    Micheau, O.2    Doucey, M.A.3    Tschopp, J.4    Bron, C.5
  • 18
    • 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, H. B., Baichwal, V. & Goeddel, D. V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4, 387-396 (1996).
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 19
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-?B but not Fas/APO-1-initiated apoptosis
    • Ting, A. T., Pimentel-Muinos, F. X. & Seed, B. RIP mediates tumor necrosis factor receptor 1 activation of NF-?B but not Fas/APO-1-initiated apoptosis. EMBO J. 15, 6189-6196 (1996).
    • (1996) EMBO J , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muinos, F.X.2    Seed, B.3
  • 20
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu, H., Shu, H. B., Pan, M. G. & Goeddel, D. V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84, 299-308 (1996).
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 21
    • 0034705271 scopus 로고    scopus 로고
    • A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction
    • Park, Y. C. et al. A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Cell 101, 777-787 (2000).
    • (2000) Cell , vol.101 , pp. 777-787
    • Park, Y.C.1
  • 22
    • 24744440776 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor 2 (TNFR2) signaling is negatively regulated by a novel, carboxyl-terminal TNFR-associated factor 2 (TRAF2)-binding site
    • Grech, A. P. et al. Tumor necrosis factor receptor 2 (TNFR2) signaling is negatively regulated by a novel, carboxyl-terminal TNFR-associated factor 2 (TRAF2)-binding site. J. Biol. Chem. 280, 31572-31581 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 31572-31581
    • Grech, A.P.1
  • 23
    • 0036629347 scopus 로고    scopus 로고
    • Apoptotic crosstalk of TNF receptors: TNF-R2-induces depletion of TRAF2 and IAP proteins and accelerates TNF-R1-dependent activation of caspase-8
    • Fotin-Mleczek, M. et al. Apoptotic crosstalk of TNF receptors: TNF-R2-induces depletion of TRAF2 and IAP proteins and accelerates TNF-R1-dependent activation of caspase-8. J. Cell Sci. 115, 2757-2770 (2002).
    • (2002) J. Cell Sci , vol.115 , pp. 2757-2770
    • Fotin-Mleczek, M.1
  • 24
    • 0031463025 scopus 로고    scopus 로고
    • Early lethality, functional NF-?B activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice
    • Yeh, W. C. et al. Early lethality, functional NF-?B activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity 7, 715-725 (1997).
    • (1997) Immunity , vol.7 , pp. 715-725
    • Yeh, W.C.1
  • 25
    • 50449088575 scopus 로고    scopus 로고
    • Beyond tumor necrosis factor receptor: TRADD signaling in toll-like receptors
    • Chen, N. J. et al. Beyond tumor necrosis factor receptor: TRADD signaling in toll-like receptors. Proc. Natl Acad. Sci. USA 105, 12429-12434 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12429-12434
    • Chen, N.J.1
  • 26
    • 50049125047 scopus 로고    scopus 로고
    • Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses
    • Ermolaeva, M. A. et al. Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses. Nature Immunol. 9, 1037-1046 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 1037-1046
    • Ermolaeva, M.A.1
  • 27
    • 50149089360 scopus 로고    scopus 로고
    • The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors
    • Pobezinskaya, Y. L. et al. The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors. Nature Immunol. 9, 1047-1054 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 1047-1054
    • Pobezinskaya, Y.L.1
  • 28
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin, A. et al. The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 12, 419-429 (2000).
    • (2000) Immunity , vol.12 , pp. 419-429
    • Devin, A.1
  • 29
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-?-induced I?B kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • Lee, T. H., Shank, J., Cusson, N. & Kelliher, M. A. The kinase activity of Rip1 is not required for tumor necrosis factor-?-induced I?B kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J. Biol. Chem. 279, 33185-33191 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3    Kelliher, M.A.4
  • 30
    • 50149121101 scopus 로고    scopus 로고
    • Both cIAP1 and cIAP2 regulate TNF?-mediated NF-?B activation
    • Mahoney, D. J. et al. Both cIAP1 and cIAP2 regulate TNF?-mediated NF-?B activation. Proc. Natl Acad. Sci. USA 105, 11778-11783 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 11778-11783
    • Mahoney, D.J.1
  • 33
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser, M. Origin and function of ubiquitin-like proteins. Nature 458, 422-429 (2009).
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 34
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNF? Requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea, C. K., Deng, L., Xia, Z. P., Pineda, G. & Chen, Z. J. Activation of IKK by TNF? requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell 22, 245-257 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 35
    • 33744951304 scopus 로고    scopus 로고
    • Ubiquitination of RIP is required for tumor necrosis factor ?-induced NF-?B activation
    • Li, H., Kobayashi, M., Blonska, M., You, Y. & Lin, X. Ubiquitination of RIP is required for tumor necrosis factor ?-induced NF-?B activation. J. Biol. Chem. 281, 13636-13643 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 13636-13643
    • Li, H.1    Kobayashi, M.2    Blonska, M.3    You, Y.4    Lin, X.5
  • 36
    • 44949240664 scopus 로고    scopus 로고
    • CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand, M. J. et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol. Cell 30, 689-700 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.1
  • 37
    • 77950352082 scopus 로고    scopus 로고
    • Crystal structures of the TRAF2: CIAP2 and the TRAF1: TRAF2: CIAP2 complexes: Affinity, specificity, and regulation
    • Zheng, C., Kabaleeswaran, V., Wang, Y., Cheng, G. & Wu, H. Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation. Mol. Cell 38, 101-113 (2010).
    • (2010) Mol. Cell , vol.38 , pp. 101-113
    • Zheng, C.1    Kabaleeswaran, V.2    Wang, Y.3    Cheng, G.4    Wu, H.5
  • 38
    • 70449424269 scopus 로고    scopus 로고
    • Structural basis for the lack of E2 interaction in the RING domain of TRAF2
    • Yin, Q., Lamothe, B., Darnay, B. G. & Wu, H. Structural basis for the lack of E2 interaction in the RING domain of TRAF2. Biochemistry 48, 10558-10567 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10558-10567
    • Yin, Q.1    Lamothe, B.2    Darnay, B.G.3    Wu, H.4
  • 39
    • 72149117664 scopus 로고    scopus 로고
    • TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-?b and to prevent TNF-induced apoptosis
    • Vince, J. E. et al. TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-?b and to prevent TNF-induced apoptosis. J. Biol. Chem. 284, 35906-35915 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 35906-35915
    • Vince, J.E.1
  • 40
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNF? and IL-1?
    • Xu, M., Skaug, B., Zeng, W. & Chen, Z. J. A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNF? and IL-1?. Mol. Cell 36, 302-314 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 41
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • Haas, T. L. et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol. Cell 36, 831-844 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 831-844
    • Haas, T.L.1
  • 42
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach, B. et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471, 591-596 (2011).
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1
  • 43
    • 78650300883 scopus 로고    scopus 로고
    • C-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling
    • Dynek, J. N. et al. c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling. EMBO J. 29, 4198-4209 (2010).
    • (2010) EMBO J , vol.29 , pp. 4198-4209
    • Dynek, J.N.1
  • 44
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-?B activation
    • Tokunaga, F. et al. Involvement of linear polyubiquitylation of NEMO in NF-?B activation. Nature Cell Biol. 11, 123-132 (2009).
    • (2009) Nature Cell Biol , vol.11 , pp. 123-132
    • Tokunaga, F.1
  • 45
    • 33750219981 scopus 로고    scopus 로고
    • A ubiquitin ligase complex assembles linear polyubiquitin chains
    • Kirisako, T. et al. A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J. 25, 4877-4887 (2006).
    • (2006) EMBO J , vol.25 , pp. 4877-4887
    • Kirisako, T.1
  • 46
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-?B activity and apoptosis
    • Ikeda, F. et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-?B activity and apoptosis. Nature 471, 637-641 (2011).
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1
  • 47
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-?B-activating linear ubiquitin chain assembly complex
    • Tokunaga, F. et al. SHARPIN is a component of the NF-?B-activating linear ubiquitin chain assembly complex. Nature 471, 633-636 (2011).
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1
  • 48
    • 77957252647 scopus 로고    scopus 로고
    • The IKK complex, a central regulator of NF-?B activation
    • Israel, A. The IKK complex, a central regulator of NF-?B activation. Cold Spring Harb. Perspect. Biol. 2, a000158 (2010).
    • (2010) Cold Spring Harb. Perspect. Biol , vol.2 , pp. a000158
    • Israel, A.1
  • 49
    • 33645312379 scopus 로고    scopus 로고
    • Circuitry of nuclear factor ?B signaling
    • Hoffmann, A. & Baltimore, D. Circuitry of nuclear factor ?B signaling. Immunol. Rev. 210, 171-186 (2006).
    • (2006) Immunol. Rev , vol.210 , pp. 171-186
    • Hoffmann, A.1    Baltimore, D.2
  • 50
    • 0037208074 scopus 로고    scopus 로고
    • Induction of the NF-?B cascade by recruitment of the scaffold molecule NEMO to the T cell receptor
    • Weil, R. et al. Induction of the NF-?B cascade by recruitment of the scaffold molecule NEMO to the T cell receptor. Immunity 18, 13-26 (2003).
    • (2003) Immunity , vol.18 , pp. 13-26
    • Weil, R.1
  • 51
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-?B activation [corrected]
    • Wu, C. J., Conze, D. B., Li, T., Srinivasula, S. M. & Ashwell, J. D. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-?B activation [corrected]. Nature Cell Biol. 8, 398-406 (2006).
    • (2006) Nature Cell Biol , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 52
    • 61649103747 scopus 로고    scopus 로고
    • Structural basis for recognition of diubiquitins by NEMO
    • Lo, Y. C. et al. Structural basis for recognition of diubiquitins by NEMO. Mol. Cell 33, 602-615 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 602-615
    • Lo, Y.C.1
  • 53
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-?B activation
    • Rahighi, S. et al. Specific recognition of linear ubiquitin chains by NEMO is important for NF-?B activation. Cell 136, 1098-1109 (2009).
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1
  • 54
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang, C. et al. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412, 346-351 (2001).
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1
  • 55
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TAB3 activate the NF-?B pathway through binding to polyubiquitin chains
    • Kanayama, A. et al. TAB2 and TAB3 activate the NF-?B pathway through binding to polyubiquitin chains. Mol. Cell 15, 535-548 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 535-548
    • Kanayama, A.1
  • 56
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim, J. H. et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev. 19, 2668-2681 (2005).
    • (2005) Genes Dev , vol.19 , pp. 2668-2681
    • Shim, J.H.1
  • 57
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • Komander, D. et al. Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep. 10, 466-473 (2009).
    • (2009) EMBO Rep , vol.10 , pp. 466-473
    • Komander, D.1
  • 58
    • 84884345970 scopus 로고    scopus 로고
    • Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains
    • Emmerich, C. H. et al. Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains. Proc. Natl Acad. Sci. USA 110, 15247-15252 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 15247-15252
    • Emmerich, C.H.1
  • 59
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau, O. & Tschopp, J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114, 181-190 (2003).
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 60
    • 70349176078 scopus 로고    scopus 로고
    • Procaspase 8 overexpression in non-small-cell lung cancer promotes apoptosis induced by FLIP silencing
    • Wilson, T. R. et al. Procaspase 8 overexpression in non-small-cell lung cancer promotes apoptosis induced by FLIP silencing. Cell Death Differ. 16, 1352-1361 (2009).
    • (2009) Cell Death Differ , vol.16 , pp. 1352-1361
    • Wilson, T.R.1
  • 61
    • 70549107710 scopus 로고    scopus 로고
    • Mitochondrial cell death effectors
    • Brenner, D. & Mak, T. W. Mitochondrial cell death effectors. Curr. Opin. Cell Biol. 21, 871-877 (2009).
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 871-877
    • Brenner, D.1    Mak, T.W.2
  • 62
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-?
    • He, S. et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-?. Cell 137, 1100-1111 (2009).
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 63
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho, Y. S. et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137, 1112-1123 (2009).
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1
  • 64
    • 43749122598 scopus 로고    scopus 로고
    • NF-?B suppression by the deubiquitinating enzyme Cezanne: A novel negative feedback loop in pro-inflammatory signaling
    • Enesa, K. et al. NF-?B suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling. J. Biol. Chem. 283, 7036-7045 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 7036-7045
    • Enesa, K.1
  • 65
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-?B signalling
    • Wertz, I. E. et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-?B signalling. Nature 430, 694-699 (2004).
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 66
    • 43049174900 scopus 로고    scopus 로고
    • CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-?B activation
    • Liao, W. et al. CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-?B activation. Curr. Biol. 18, 641-649 (2008).
    • (2008) Curr. Biol , vol.18 , pp. 641-649
    • Liao, W.1
  • 67
    • 84867062977 scopus 로고    scopus 로고
    • A20 inhibits LUBAC-mediated NF-?B activation by binding linear polyubiquitin chains via its zinc finger 7
    • Verhelst, K. et al. A20 inhibits LUBAC-mediated NF-?B activation by binding linear polyubiquitin chains via its zinc finger 7. EMBO J. 31, 3845-3855 (2012).
    • (2012) EMBO J , vol.31 , pp. 3845-3855
    • Verhelst, K.1
  • 68
    • 43049152912 scopus 로고    scopus 로고
    • TNF-? Induces two distinct caspase-8 activation pathways
    • Wang, L., Du, F. & Wang, X. TNF-? induces two distinct caspase-8 activation pathways. Cell 133, 693-703 (2008).
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 69
    • 57649181391 scopus 로고    scopus 로고
    • Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway
    • Hitomi, J. et al. Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell 135, 1311-1323 (2008).
    • (2008) Cell , vol.135 , pp. 1311-1323
    • Hitomi, J.1
  • 70
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-?B signalling by deubiquitination
    • Kovalenko, A. et al. The tumour suppressor CYLD negatively regulates NF-?B signalling by deubiquitination. Nature 424, 801-805 (2003).
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1
  • 71
    • 79960921946 scopus 로고    scopus 로고
    • The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • Tenev, T. et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol. Cell 43, 432-448 (2011).
    • (2011) Mol. Cell , vol.43 , pp. 432-448
    • Tenev, T.1
  • 72
    • 0034616945 scopus 로고    scopus 로고
    • Smac a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L. & Wang, X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42 (2000).
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 73
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • Wu, G. et al. Structural basis of IAP recognition by Smac/DIABLO. Nature 408, 1008-1012 (2000).
    • (2000) Nature , vol.408 , pp. 1008-1012
    • Wu, G.1
  • 74
    • 36148954336 scopus 로고    scopus 로고
    • IAP antagonists target cIAP1 to induce TNF?-dependent apoptosis
    • Vince, J. E. et al. IAP antagonists target cIAP1 to induce TNF?-dependent apoptosis. Cell 131, 682-693 (2007).
    • (2007) Cell , vol.131 , pp. 682-693
    • Vince, J.E.1
  • 75
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs NF-?B activation, and TNF?-dependent apoptosis
    • Varfolomeev, E. et al. IAP antagonists induce autoubiquitination of c-IAPs, NF-?B activation, and TNF?-dependent apoptosis. Cell 131, 669-681 (2007).
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1
  • 76
    • 2342445559 scopus 로고    scopus 로고
    • Smac/DIABLO selectively reduces the levels of c-IAP1 and c-IAP2 but not that of XIAP and livin in HeLa cells
    • Yang, Q. H. & Du, C. Smac/DIABLO selectively reduces the levels of c-IAP1 and c-IAP2 but not that of XIAP and livin in HeLa cells. J. Biol. Chem. 279, 16963-16970 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 16963-16970
    • Yang, Q.H.1    Du, C.2
  • 77
    • 56349164239 scopus 로고    scopus 로고
    • Noncanonical NF-?B activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK
    • Zarnegar, B. J. et al. Noncanonical NF-?B activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK. Nature Immunol. 9, 1371-1378 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 1371-1378
    • Zarnegar, B.J.1
  • 78
    • 35948994157 scopus 로고    scopus 로고
    • Autocrine TNF? Signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis
    • Petersen, S. L. et al. Autocrine TNF? signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis. Cancer Cell 12, 445-456 (2007).
    • (2007) Cancer Cell , vol.12 , pp. 445-456
    • Petersen, S.L.1
  • 80
    • 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. 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 85, 817-827 (1996).
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1
  • 81
    • 17644378775 scopus 로고    scopus 로고
    • C-FLIPR, a new regulator of death receptor-induced apoptosis
    • Golks, A., Brenner, D., Fritsch, C., Krammer, P. H. & Lavrik, I. N. c-FLIPR, a new regulator of death receptor-induced apoptosis. J. Biol. Chem. 280, 14507-14513 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 14507-14513
    • Golks, A.1    Brenner, D.2    Fritsch, C.3    Krammer, P.H.4    Lavrik, I.N.5
  • 83
    • 0036009115 scopus 로고    scopus 로고
    • NF-?B at the crossroads of life and death
    • Karin, M. & Lin, A. NF-?B at the crossroads of life and death. Nature Immunol. 3, 221-227 (2002).
    • (2002) Nature Immunol , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 84
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNF?-induced cell death by inducing c-FLIPL turnover
    • Chang, L. et al. The E3 ubiquitin ligase itch couples JNK activation to TNF?-induced cell death by inducing c-FLIPL turnover. Cell 124, 601-613 (2006).
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1
  • 85
    • 78751487532 scopus 로고    scopus 로고
    • FLIPL induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity
    • Pop, C. et al. FLIPL induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity. Biochem. J. 433, 447-457 (2011).
    • (2011) Biochem. J , vol.433 , pp. 447-457
    • Pop, C.1
  • 86
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIPL complex inhibits RIPK3-dependent necrosis
    • Oberst, A. et al. Catalytic activity of the caspase-8-FLIPL complex inhibits RIPK3-dependent necrosis. Nature 471, 363-367 (2011).
    • (2011) Nature , vol.471 , pp. 363-367
    • Oberst, A.1
  • 87
    • 84861712290 scopus 로고    scopus 로고
    • Survival function of the FADD-CASPASE-8-cFLIPL complex
    • Dillon, C. P. et al. Survival function of the FADD-CASPASE-8-cFLIPL complex. Cell Rep. 1, 401-407 (2012).
    • (2012) Cell Rep , vol.1 , pp. 401-407
    • Dillon, C.P.1
  • 88
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Irmler, M. et al. Inhibition of death receptor signals by cellular FLIP. Nature 388, 190-195 (1997).
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1
  • 89
    • 0030746740 scopus 로고    scopus 로고
    • Casper is a FADD-and caspase-related inducer of apoptosis
    • Shu, H. B., Halpin, D. R. & Goeddel, D. V. Casper is a FADD-and caspase-related inducer of apoptosis. Immunity 6, 751-763 (1997).
    • (1997) Immunity , vol.6 , pp. 751-763
    • Shu, H.B.1    Halpin, D.R.2    Goeddel, D.V.3
  • 90
    • 7344220967 scopus 로고    scopus 로고
    • Cell death attenuation by 'Usurpin' a mammalian DED-caspase homologue that precludes caspase-8 recruitment and activation by the CD-95 (Fas, APO-1) receptor complex
    • Rasper, D. M. et al. Cell death attenuation by 'Usurpin', a mammalian DED-caspase homologue that precludes caspase-8 recruitment and activation by the CD-95 (Fas, APO-1) receptor complex. Cell Death Differ. 5, 271-288 (1998).
    • (1998) Cell Death Differ , vol.5 , pp. 271-288
    • Rasper, D.M.1
  • 91
    • 79960922705 scopus 로고    scopus 로고
    • CIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • Feoktistova, M. et al. cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol. Cell 43, 449-463 (2011).
    • (2011) Mol. Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1
  • 92
    • 57649149333 scopus 로고    scopus 로고
    • Classification of cell death: Recommendations of the Nomenclature Committee on Cell Death 2009
    • Kroemer, G. et al. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ. 16, 3-11 (2009).
    • (2009) Cell Death Differ , vol.16 , pp. 3-11
    • Kroemer, G.1
  • 93
    • 84255210700 scopus 로고    scopus 로고
    • Molecular definitions of cell death subroutines: Recommendations of the Nomenclature Committee on Cell Death 2012
    • Galluzzi, L. et al. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ. 19, 107-120 (2012).
    • (2012) Cell Death Differ , vol.19 , pp. 107-120
    • Galluzzi, L.1
  • 94
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • Vercammen, D. et al. Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J. Exp. Med. 187, 1477-1485 (1998).
    • (1998) J. Exp. Med , vol.187 , pp. 1477-1485
    • Vercammen, D.1
  • 95
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler, N. et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nature Immunol. 1, 489-495 (2000).
    • (2000) Nature Immunol , vol.1 , pp. 489-495
    • Holler, N.1
  • 96
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang, D. W. et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 325, 332-336 (2009).
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1
  • 97
    • 33646234026 scopus 로고    scopus 로고
    • Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1
    • Zheng, L. et al. Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1. Mol. Cell. Biol. 26, 3505-3513 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 3505-3513
    • Zheng, L.1
  • 98
    • 79955761920 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein (cFLIP) isoforms block CD95-and TRAIL death receptor-induced gene induction irrespective of processing of caspase-8 or cFLIP in the death-inducing signaling complex
    • Kavuri, S. M. et al. Cellular FLICE-inhibitory protein (cFLIP) isoforms block CD95-and TRAIL death receptor-induced gene induction irrespective of processing of caspase-8 or cFLIP in the death-inducing signaling complex. J. Biol. Chem. 286, 16631-16646 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 16631-16646
    • Kavuri, S.M.1
  • 100
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: Crucial integrators of cellular stress
    • Meylan, E. & Tschopp, J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 30, 151-159 (2005).
    • (2005) Trends Biochem. Sci , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 101
    • 77957274045 scopus 로고    scopus 로고
    • Receptor-interacting protein (RIP) kinase family
    • Zhang, D., Lin, J. & Han, J. Receptor-interacting protein (RIP) kinase family. Cell. Mol. Immunol. 7, 243-249 (2010).
    • (2010) Cell. Mol. Immunol , vol.7 , pp. 243-249
    • Zhang, D.1    Lin, J.2    Han, J.3
  • 102
    • 0842304221 scopus 로고    scopus 로고
    • Kinase RIP3 is dispensable for normal NF-?Bs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4
    • Newton, K., Sun, X. & Dixit, V. M. Kinase RIP3 is dispensable for normal NF-?Bs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4. Mol. Cell. Biol. 24, 1464-1469 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 1464-1469
    • Newton, K.1    Sun, X.2    Dixit, V.M.3
  • 103
    • 84864240409 scopus 로고    scopus 로고
    • The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
    • Li, J. et al. The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150, 339-350 (2012).
    • (2012) Cell , vol.150 , pp. 339-350
    • Li, J.1
  • 104
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev, A. et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nature Chem. Biol. 1, 112-119 (2005).
    • (2005) Nature Chem. Biol , vol.1 , pp. 112-119
    • Degterev, A.1
  • 105
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • Feng, S. et al. Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell. Signal. 19, 2056-2067 (2007).
    • (2007) Cell. Signal , vol.19 , pp. 2056-2067
    • Feng, S.1
  • 106
    • 79952811804 scopus 로고    scopus 로고
    • RIP3 mediates the embryonic lethality of caspase-8-deficient mice
    • Kaiser, W. J. et al. RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature 471, 368-372 (2011).
    • (2011) Nature , vol.471 , pp. 368-372
    • Kaiser, W.J.1
  • 107
    • 79952780505 scopus 로고    scopus 로고
    • Functional complementation between FADD and RIP1 in embryos and lymphocytes
    • Zhang, H. et al. Functional complementation between FADD and RIP1 in embryos and lymphocytes. Nature 471, 373-376 (2011).
    • (2011) Nature , vol.471 , pp. 373-376
    • Zhang, H.1
  • 108
    • 84901649808 scopus 로고    scopus 로고
    • RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition
    • Kaiser, W. J. et al. RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition. Proc. Natl Acad. Sci. USA 111, 7753-7758 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7753-7758
    • Kaiser, W.J.1
  • 109
    • 83155192804 scopus 로고    scopus 로고
    • TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex i and II members
    • Vanlangenakker, N., Bertrand, M. J., Bogaert, P., Vandenabeele, P. & Vanden Berghe, T. TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members. Cell Death Dis. 2, e230 (2011).
    • (2011) Cell Death Dis , vol.2 , pp. e230
    • Vanlangenakker, N.1    Bertrand, M.J.2    Bogaert, P.3    Vandenabeele, P.4    Vanden Berghe, T.5
  • 110
    • 34547422758 scopus 로고    scopus 로고
    • Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis
    • Seymour, R. E. et al. Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis. Genes Immun. 8, 416-421 (2007).
    • (2007) Genes Immun , vol.8 , pp. 416-421
    • Seymour, R.E.1
  • 111
    • 84925358056 scopus 로고    scopus 로고
    • TNFR1-dependent cell death drives inflammation in Sharpin-deficient mice
    • Rickard, J. A. et al. TNFR1-dependent cell death drives inflammation in Sharpin-deficient mice. eLife 3, e03464 (2014).
    • (2014) ELife , vol.3 , pp. e03464
    • Rickard, J.A.1
  • 112
    • 84901678314 scopus 로고    scopus 로고
    • Cutting edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice
    • Berger, S. B. et al. Cutting edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice. J. Immunol. 192, 5476-5480 (2014).
    • (2014) J. Immunol , vol.192 , pp. 5476-5480
    • Berger, S.B.1
  • 113
    • 84907995994 scopus 로고    scopus 로고
    • HOIP deficiency causes embryonic lethality by aberrant TNFR1-mediated endothelial cell death
    • Peltzer, N. et al. HOIP deficiency causes embryonic lethality by aberrant TNFR1-mediated endothelial cell death. Cell Rep. 9, 153-165 (2014).
    • (2014) Cell Rep , vol.9 , pp. 153-165
    • Peltzer, N.1
  • 114
    • 84859467770 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
    • Zhao, J. et al. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc. Natl Acad. Sci. USA 109, 5322-5327 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 5322-5327
    • Zhao, J.1
  • 115
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • Sun, L. et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 148, 213-227 (2012).
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1
  • 116
    • 84884308522 scopus 로고    scopus 로고
    • The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism
    • Murphy, J. M. et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 39, 443-453 (2013).
    • (2013) Immunity , vol.39 , pp. 443-453
    • Murphy, J.M.1
  • 117
    • 84881184694 scopus 로고    scopus 로고
    • Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis
    • Wu, J. et al. Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis. Cell Res. 23, 994-1006 (2013).
    • (2013) Cell Res , vol.23 , pp. 994-1006
    • Wu, J.1
  • 118
    • 84885868361 scopus 로고    scopus 로고
    • Structural insights into RIP3-mediated necroptotic signaling
    • Xie, T. et al. Structural insights into RIP3-mediated necroptotic signaling. Cell Rep. 5, 70-78 (2013).
    • (2013) Cell Rep , vol.5 , pp. 70-78
    • Xie, T.1
  • 119
    • 84878755914 scopus 로고    scopus 로고
    • Diverse sequence determinants control human and mouse receptor interacting protein 3 (RIP3) and mixed lineage kinase domain-like (MLKL) interaction in necroptotic signaling
    • Chen, W. et al. Diverse sequence determinants control human and mouse receptor interacting protein 3 (RIP3) and mixed lineage kinase domain-like (MLKL) interaction in necroptotic signaling. J. Biol. Chem. 288, 16247-16261 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 16247-16261
    • Chen, W.1
  • 120
    • 84891343566 scopus 로고    scopus 로고
    • Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
    • Cai, Z. et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nature Cell Biol. 16, 55-65 (2014).
    • (2014) Nature Cell Biol , vol.16 , pp. 55-65
    • Cai, Z.1
  • 121
    • 84891739370 scopus 로고    scopus 로고
    • Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death
    • Chen, X. et al. Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death. Cell Res. 24, 105-121 (2014).
    • (2014) Cell Res , vol.24 , pp. 105-121
    • Chen, X.1
  • 122
    • 84898027331 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3
    • Wang, H. et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol. Cell 54, 133-146 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 133-146
    • Wang, H.1
  • 123
    • 38549102077 scopus 로고    scopus 로고
    • TNF-mediated inflammatory disease
    • Bradley, J. R. TNF-mediated inflammatory disease. J. Pathol. 214, 149-160 (2008).
    • (2008) J. Pathol , vol.214 , pp. 149-160
    • Bradley, J.R.1
  • 124
    • 84857687171 scopus 로고    scopus 로고
    • TNF superfamily in inflammatory disease: Translating basic insights
    • Croft, M. et al. TNF superfamily in inflammatory disease: translating basic insights. Trends Immunol. 33, 144-152 (2012).
    • (2012) Trends Immunol , vol.33 , pp. 144-152
    • Croft, M.1
  • 125
    • 84873411673 scopus 로고    scopus 로고
    • Clinical targeting of the TNF and TNFR superfamilies
    • Croft, M., Benedict, C. A. & Ware, C. F. Clinical targeting of the TNF and TNFR superfamilies. Nature Rev. Drug Discov. 12, 147-168 (2013).
    • (2013) Nature Rev. Drug Discov , vol.12 , pp. 147-168
    • Croft, M.1    Benedict, C.A.2    Ware, C.F.3
  • 126
    • 0022411888 scopus 로고
    • Passive immunization against cachectin/tumor necrosis factor protects mice from lethal effect of endotoxin
    • Beutler, B., Milsark, I. W. & Cerami, A. C. Passive immunization against cachectin/tumor necrosis factor protects mice from lethal effect of endotoxin. Science 229, 869-871 (1985).
    • (1985) Science , vol.229 , pp. 869-871
    • Beutler, B.1    Milsark, I.W.2    Cerami, A.C.3
  • 127
    • 23444446083 scopus 로고
    • Selected treatment strategies for septic shock based on proposed mechanisms of pathogenesis
    • Natanson, C., Hoffman, W. D., Suffredini, A. F., Eichacker, P. Q. & Danner, R. L. Selected treatment strategies for septic shock based on proposed mechanisms of pathogenesis. Ann. Intern. Med. 120, 771-783 (1994).
    • (1994) Ann. Intern. Med , vol.120 , pp. 771-783
    • Natanson, C.1    Hoffman, W.D.2    Suffredini, A.F.3    Eichacker, P.Q.4    Danner, R.L.5
  • 128
    • 0030917203 scopus 로고    scopus 로고
    • Monocyte deactivation in septic patients: Restoration by IFN-? Treatment
    • Docke, W. D. et al. Monocyte deactivation in septic patients: restoration by IFN-? treatment. Nature Med. 3, 678-681 (1997).
    • (1997) Nature Med , vol.3 , pp. 678-681
    • Docke, W.D.1
  • 129
    • 0034913364 scopus 로고    scopus 로고
    • Anti-tumor necrosis factor therapy in sepsis: Update on clinical trials and lessons learned
    • Reinhart, K. & Karzai, W. Anti-tumor necrosis factor therapy in sepsis: update on clinical trials and lessons learned. Crit. Care Med. 29, S121-125 (2001).
    • (2001) Crit. Care Med , vol.29 , pp. S121-125
    • Reinhart, K.1    Karzai, W.2
  • 130
    • 84897414193 scopus 로고    scopus 로고
    • Anti-TNF-? Therapy for patients with sepsis: A systematic meta-analysis
    • Lv, S. et al. Anti-TNF-? therapy for patients with sepsis: a systematic meta-analysis. Int. J. Clin. Pract. 68, 520-528 (2014).
    • (2014) Int. J. Clin. Pract , vol.68 , pp. 520-528
    • Lv, S.1
  • 131
    • 0026039673 scopus 로고
    • Transgenic mice expressing human tumour necrosis factor: A predictive genetic model of arthritis
    • Keffer, J. et al. Transgenic mice expressing human tumour necrosis factor: a predictive genetic model of arthritis. EMBO J. 10, 4025-4031 (1991).
    • (1991) EMBO J , vol.10 , pp. 4025-4031
    • Keffer, J.1
  • 132
    • 0024314554 scopus 로고
    • Inhibitory effect of TNF ? Antibodies on synovial cell interleukin-1 production in rheumatoid arthritis
    • Brennan, F. M., Chantry, D., Jackson, A., Maini, R. & Feldmann, M. Inhibitory effect of TNF ? antibodies on synovial cell interleukin-1 production in rheumatoid arthritis. Lancet 2, 244-247 (1989).
    • (1989) Lancet , vol.2 , pp. 244-247
    • Brennan, F.M.1    Chantry, D.2    Jackson, A.3    Maini, R.4    Feldmann, M.5
  • 133
    • 0013511183 scopus 로고    scopus 로고
    • Treatment of rheumatoid arthritis with a recombinant human tumor necrosis factor receptor (p75)-Fc fusion protein
    • Moreland, L. W. et al. Treatment of rheumatoid arthritis with a recombinant human tumor necrosis factor receptor (p75)-Fc fusion protein. N. Engl. J. Med. 337, 141-147 (1997).
    • (1997) N. Engl. J. Med , vol.337 , pp. 141-147
    • Moreland, L.W.1
  • 135
    • 84884225001 scopus 로고    scopus 로고
    • Genetics of psoriasis and pharmacogenetics of biological drugs
    • Prieto-Perez, R. et al. Genetics of psoriasis and pharmacogenetics of biological drugs. Autoimmune Dis. 2013, 613086 (2013).
    • (2013) Autoimmune Dis , vol.2013 , pp. 613086
    • Prieto-Perez, R.1
  • 136
    • 84890916350 scopus 로고    scopus 로고
    • New targets for mucosal healing and therapy in inflammatory bowel diseases
    • Neurath, M. F. New targets for mucosal healing and therapy in inflammatory bowel diseases. Mucosal Immunol. 7, 6-19 (2014).
    • (2014) Mucosal Immunol , vol.7 , pp. 6-19
    • Neurath, M.F.1
  • 137
    • 84860572793 scopus 로고    scopus 로고
    • Developments in therapies for spondyloarthritis
    • Sieper, J. Developments in therapies for spondyloarthritis. Nature Rev. Rheumatol. 8, 280-287 (2012).
    • (2012) Nature Rev. Rheumatol , vol.8 , pp. 280-287
    • Sieper, J.1
  • 138
    • 84883026168 scopus 로고    scopus 로고
    • Infliximab inhibits activation and effector functions of peripheral blood T cells in vitro from patients with clinically active ulcerative colitis
    • Dahlen, R. et al. Infliximab inhibits activation and effector functions of peripheral blood T cells in vitro from patients with clinically active ulcerative colitis. Scand. J. Immunol. 78, 275-284 (2013).
    • (2013) Scand. J. Immunol , vol.78 , pp. 275-284
    • Dahlen, R.1
  • 139
    • 67650079482 scopus 로고    scopus 로고
    • Etanercept treatment in children with new-onset type 1 diabetes: Pilot randomized, placebo-controlled, double-blind study
    • Mastrandrea, L. et al. Etanercept treatment in children with new-onset type 1 diabetes: pilot randomized, placebo-controlled, double-blind study. Diabetes Care 32, 1244-1249 (2009).
    • (2009) Diabetes Care , vol.32 , pp. 1244-1249
    • Mastrandrea, L.1
  • 140
    • 79960893564 scopus 로고    scopus 로고
    • Anti-TNF rescue CD4+Foxp3+ regulatory T cells in patients with type 1 diabetes from effects mediated by TNF
    • Ryba, M. et al. Anti-TNF rescue CD4+Foxp3+ regulatory T cells in patients with type 1 diabetes from effects mediated by TNF. Cytokine 55, 353-361 (2011).
    • (2011) Cytokine , vol.55 , pp. 353-361
    • Ryba, M.1
  • 141
    • 67349145254 scopus 로고    scopus 로고
    • Development of type 1 diabetes in a patient treated with anti-TNF-? Therapy for active rheumatoid arthritis
    • Tack, C. J., Kleijwegt, F. S., Van Riel, P. L. & Roep, B. O. Development of type 1 diabetes in a patient treated with anti-TNF-? therapy for active rheumatoid arthritis. Diabetologia 52, 1442-1444 (2009).
    • (2009) Diabetologia , vol.52 , pp. 1442-1444
    • Tack, C.J.1    Kleijwegt, F.S.2    Van Riel, P.L.3    Roep, B.O.4
  • 142
    • 0033763545 scopus 로고    scopus 로고
    • Development of diabetes mellitus during etanercept therapy in a child with systemic-onset juvenile rheumatoid arthritis
    • Bloom, B. J. Development of diabetes mellitus during etanercept therapy in a child with systemic-onset juvenile rheumatoid arthritis. Arthritis Rheum. 43, 2606-2608 (2000).
    • (2000) Arthritis Rheum , vol.43 , pp. 2606-2608
    • Bloom, B.J.1
  • 143
    • 0024366885 scopus 로고
    • Tumor necrosis factor identified in multiple sclerosis brain
    • Hofman, F. M., Hinton, D. R., Johnson, K. & Merrill, J. E. Tumor necrosis factor identified in multiple sclerosis brain. J. Exp. Med. 170, 607-612 (1989).
    • (1989) J. Exp. Med , vol.170 , pp. 607-612
    • Hofman, F.M.1    Hinton, D.R.2    Johnson, K.3    Merrill, J.E.4
  • 144
    • 55349135951 scopus 로고    scopus 로고
    • Novel therapeutic strategies for multiple sclerosis-A multifaceted adversary
    • Lopez-Diego, R. S. & Weiner, H. L. Novel therapeutic strategies for multiple sclerosis-a multifaceted adversary. Nature Rev. Drug Discov. 7, 909-925 (2008).
    • (2008) Nature Rev. Drug Discov , vol.7 , pp. 909-925
    • Lopez-Diego, R.S.1    Weiner, H.L.2
  • 145
    • 0035464263 scopus 로고    scopus 로고
    • Demyelinating and neurologic events reported in association with tumor necrosis factor ? Antagonism: By what mechanisms could tumor necrosis factor ? Antagonists improve rheumatoid arthritis but exacerbate multiple sclerosis
    • Robinson, W. H., Genovese, M. C. & Moreland, L. W. Demyelinating and neurologic events reported in association with tumor necrosis factor ? antagonism: by what mechanisms could tumor necrosis factor ? antagonists improve rheumatoid arthritis but exacerbate multiple sclerosis? Arthritis Rheum. 44, 1977-1983 (2001).
    • (2001) Arthritis Rheum , vol.44 , pp. 1977-1983
    • Robinson, W.H.1    Genovese, M.C.2    Moreland, L.W.3
  • 146
    • 79952573321 scopus 로고    scopus 로고
    • Monoclonal antibody therapy-associated neurological disorders
    • Bosch, X., Saiz, A. & Ramos-Casals, M. Monoclonal antibody therapy-associated neurological disorders. Nature Rev. Neurol. 7, 165-172 (2011).
    • (2011) Nature Rev. Neurol , vol.7 , pp. 165-172
    • Bosch, X.1    Saiz, A.2    Ramos-Casals, M.3
  • 147
    • 84865261493 scopus 로고    scopus 로고
    • TNF receptor 1 genetic risk mirrors outcome of anti-TNF therapy in multiple sclerosis
    • Gregory, A. P. et al. TNF receptor 1 genetic risk mirrors outcome of anti-TNF therapy in multiple sclerosis. Nature 488, 508-511 (2012).
    • (2012) Nature , vol.488 , pp. 508-511
    • Gregory, A.P.1
  • 148
    • 84891153241 scopus 로고    scopus 로고
    • Future prospects in biologic therapy for systemic lupus erythematosus
    • Stohl, W. Future prospects in biologic therapy for systemic lupus erythematosus. Nature Rev. Rheumatol. 9, 705-720 (2013).
    • (2013) Nature Rev. Rheumatol , vol.9 , pp. 705-720
    • Stohl, W.1
  • 149
    • 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. Selective death of autoreactive T cells in human diabetes by TNF or TNF receptor 2 agonism. Proc. Natl Acad. Sci. USA 105, 13644-13649 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 13644-13649
    • Ban, L.1
  • 150
    • 79959373435 scopus 로고    scopus 로고
    • Tumor necrosis factor induces GSK3 kinase-mediated cross-tolerance to endotoxin in macrophages
    • Park, S. H., Park-Min, K. H., Chen, J., Hu, X. & Ivashkiv, L. B. Tumor necrosis factor induces GSK3 kinase-mediated cross-tolerance to endotoxin in macrophages. Nature Immunol. 12, 607-615 (2011).
    • (2011) Nature Immunol , vol.12 , pp. 607-615
    • Park, S.H.1    Park-Min, K.H.2    Chen, J.3    Hu, X.4    Ivashkiv, L.B.5
  • 151
    • 84885801693 scopus 로고    scopus 로고
    • Clinical use of anti-TNF therapy and increased risk of infections
    • Ali, T. et al. Clinical use of anti-TNF therapy and increased risk of infections. Drug Healthc. Patient Saf. 5, 79-99 (2013).
    • (2013) Drug Healthc. Patient Saf , vol.5 , pp. 79-99
    • Ali, T.1
  • 152
    • 33646696885 scopus 로고    scopus 로고
    • Anti-TNF antibody therapy in rheumatoid arthritis and the risk of serious infections and malignancies: Systematic review and meta-analysis of rare harmful effects in randomized controlled trials
    • Bongartz, T. et al. Anti-TNF antibody therapy in rheumatoid arthritis and the risk of serious infections and malignancies: systematic review and meta-analysis of rare harmful effects in randomized controlled trials. JAMA 295, 2275-2285 (2006).
    • (2006) JAMA , vol.295 , pp. 2275-2285
    • Bongartz, T.1
  • 155
    • 84874656491 scopus 로고    scopus 로고
    • Immunogenicity of anti-TNF biologic therapies for rheumatoid arthritis
    • van Schouwenburg, P. A., Rispens, T. & Wolbink, G. J. Immunogenicity of anti-TNF biologic therapies for rheumatoid arthritis. Nature Rev. Rheumatol. 9, 164-172 (2013).
    • (2013) Nature Rev. Rheumatol , vol.9 , pp. 164-172
    • Van Schouwenburg, P.A.1    Rispens, T.2    Wolbink, G.J.3
  • 156
    • 84865732639 scopus 로고    scopus 로고
    • Paradoxical inflammation induced by anti-TNF agents in patients with IBD
    • Cleynen, I. & Vermeire, S. Paradoxical inflammation induced by anti-TNF agents in patients with IBD. Nature Rev. Gastroenterol. Hepatol. 9, 496-503 (2012).
    • (2012) Nature Rev. Gastroenterol. Hepatol , vol.9 , pp. 496-503
    • Cleynen, I.1    Vermeire, S.2
  • 157
    • 84889673425 scopus 로고    scopus 로고
    • Infectious and malignant complications of TNF inhibitor therapy in IBD
    • Targownik, L. E. & Bernstein, C. N. Infectious and malignant complications of TNF inhibitor therapy in IBD. Am. J. Gastroenterol. 108, 1835-1842 (2013).
    • (2013) Am. J. Gastroenterol , vol.108 , pp. 1835-1842
    • Targownik, L.E.1    Bernstein, C.N.2
  • 158
    • 84875720612 scopus 로고    scopus 로고
    • Challenges and approaches for the development of safer immunomodulatory biologics
    • Sathish, J. G. et al. Challenges and approaches for the development of safer immunomodulatory biologics. Nature Rev. Drug Discov. 12, 306-324 (2013).
    • (2013) Nature Rev. Drug Discov , vol.12 , pp. 306-324
    • Sathish, J.G.1
  • 159
    • 84921815675 scopus 로고    scopus 로고
    • Strategies to improve drug development for sepsis
    • Fink, M. P. & Warren, H. S. Strategies to improve drug development for sepsis. Nature Rev. Drug Discov. 13, 741-758 (2014).
    • (2014) Nature Rev. Drug Discov , vol.13 , pp. 741-758
    • Fink, M.P.1    Warren, H.S.2
  • 160
    • 84895153556 scopus 로고    scopus 로고
    • Emerging cell and cytokine targets in rheumatoid arthritis
    • Burmester, G. R., Feist, E. & Dorner, T. Emerging cell and cytokine targets in rheumatoid arthritis. Nature Rev. Rheumatol. 10, 77-88 (2014).
    • (2014) Nature Rev. Rheumatol , vol.10 , pp. 77-88
    • Burmester, G.R.1    Feist, E.2    Dorner, T.3
  • 162
    • 80051948193 scopus 로고    scopus 로고
    • New drugs beyond biologics in rheumatoid arthritis: The kinase inhibitors
    • Bonilla-Hernan, M. G., Miranda-Carus, M. E. & Martin-Mola, E. New drugs beyond biologics in rheumatoid arthritis: the kinase inhibitors. Rheumatol. 50, 1542-1550 (2011).
    • (2011) Rheumatol , vol.50 , pp. 1542-1550
    • Bonilla-Hernan, M.G.1    Miranda-Carus, M.E.2    Martin-Mola, E.3
  • 163
    • 84875689912 scopus 로고    scopus 로고
    • Phosphodiesterase 4-targeted treatments for autoimmune diseases
    • Kumar, N., Goldminz, A. M., Kim, N. & Gottlieb, A. B. Phosphodiesterase 4-targeted treatments for autoimmune diseases. BMC Med. 11, 96 (2013).
    • (2013) BMC Med , vol.11 , pp. 96
    • Kumar, N.1    Goldminz, A.M.2    Kim, N.3    Gottlieb, A.B.4
  • 164
    • 84897443197 scopus 로고    scopus 로고
    • Advances in targeting cyclic nucleotide phosphodiesterases
    • Maurice, D. H. et al. Advances in targeting cyclic nucleotide phosphodiesterases. Nature Rev. Drug Discov. 13, 290-314 (2014).
    • (2014) Nature Rev. Drug Discov , vol.13 , pp. 290-314
    • Maurice, D.H.1
  • 165
    • 84880269392 scopus 로고    scopus 로고
    • How cytokine networks fuel inflammation: Toward a cytokine-based disease taxonomy
    • Schett, G., Elewaut, D., McInnes, I. B., Dayer, J. M. & Neurath, M. F. How cytokine networks fuel inflammation: toward a cytokine-based disease taxonomy. Nature Med. 19, 822-824 (2013).
    • (2013) Nature Med , vol.19 , pp. 822-824
    • Schett, G.1    Elewaut, D.2    McInnes, I.B.3    Dayer, J.M.4    Neurath, M.F.5
  • 166
    • 27744586067 scopus 로고    scopus 로고
    • Small-molecule inhibition of TNF-?
    • He, M. M. et al. Small-molecule inhibition of TNF-?. Science 310, 1022-1025 (2005).
    • (2005) Science , vol.310 , pp. 1022-1025
    • He, M.M.1
  • 167
    • 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. The growth factor progranulin binds to TNF receptors and is therapeutic against inflammatory arthritis in mice. Science 332, 478-484 (2011).
    • (2011) Science , vol.332 , pp. 478-484
    • Tang, W.1
  • 168
    • 84873349403 scopus 로고    scopus 로고
    • IRHOM2 is a critical pathogenic mediator of inflammatory arthritis
    • Issuree, P. D. et al. iRHOM2 is a critical pathogenic mediator of inflammatory arthritis. J. Clin. Invest. 123, 928-932 (2013).
    • (2013) J. Clin. Invest , vol.123 , pp. 928-932
    • Issuree, P.D.1
  • 169
    • 44849120587 scopus 로고    scopus 로고
    • Drug insight: Tumor necrosis factor-converting enzyme as a pharmaceutical target for rheumatoid arthritis
    • Moss, M. L., Sklair-Tavron, L. & Nudelman, R. Drug insight: tumor necrosis factor-converting enzyme as a pharmaceutical target for rheumatoid arthritis. Nature Clin. Pract. Rheumatol. 4, 300-309 (2008).
    • (2008) Nature Clin. Pract. Rheumatol , vol.4 , pp. 300-309
    • Moss, M.L.1    Sklair-Tavron, L.2    Nudelman, R.3
  • 170
    • 84886095507 scopus 로고    scopus 로고
    • Antagonistic TNF receptor one-specific antibody (ATROSAB): Receptor binding and in vitro bioactivity
    • Richter, F. et al. Antagonistic TNF receptor one-specific antibody (ATROSAB): receptor binding and in vitro bioactivity. PLoS ONE 8, e72156 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e72156
    • Richter, F.1
  • 171
    • 0037331223 scopus 로고    scopus 로고
    • Listeria monocytogenes infection as a complication of treatment with tumor necrosis factor ?-neutralizing agents
    • Slifman, N. R., Gershon, S. K., Lee, J. H., Edwards, E. T. & Braun, M. M. Listeria monocytogenes infection as a complication of treatment with tumor necrosis factor ?-neutralizing agents. Arthritis Rheum. 48, 319-324 (2003).
    • (2003) Arthritis Rheum , vol.48 , pp. 319-324
    • Slifman, N.R.1    Gershon, S.K.2    Lee, J.H.3    Edwards, E.T.4    Braun, M.M.5
  • 172
    • 34447505845 scopus 로고    scopus 로고
    • Autoimmune diseases induced by TNF-targeted therapies: Analysis of 233 cases
    • Ramos-Casals, M. et al. Autoimmune diseases induced by TNF-targeted therapies: analysis of 233 cases. Medicine (Baltimore). 86, 242-251 (2007).
    • (2007) Medicine (Baltimore) , vol.86 , pp. 242-251
    • Ramos-Casals, M.1
  • 173
    • 37249063841 scopus 로고    scopus 로고
    • TNF?blockade in human diseases: An overview of efficacy and safety
    • Lin, J. et al. TNF? blockade in human diseases: an overview of efficacy and safety. Clin. Immunol. 126, 13-30 (2008).
    • (2008) Clin. Immunol , vol.126 , pp. 13-30
    • Lin, J.1
  • 174
    • 10744227300 scopus 로고    scopus 로고
    • Efficacy and safety of the fully human anti-tumour necrosis factor ? Monoclonal antibody adalimumab ( D2E7) in DMARD refractory patients with rheumatoid arthritis: A 12 week, Phase II study
    • van de Putte, L. B. et al. Efficacy and safety of the fully human anti-tumour necrosis factor ? monoclonal antibody adalimumab (D2E7) in DMARD refractory patients with rheumatoid arthritis: a 12 week, Phase II study. Ann. Rheum. Dis. 62, 1168-1177 (2003).
    • (2003) Ann. Rheum. Dis , vol.62 , pp. 1168-1177
    • Van De Putte, L.B.1
  • 175
    • 84859448342 scopus 로고    scopus 로고
    • Short-term risk of total malignancy and nonmelanoma skin cancers with certolizumab and golimumab in patients with rheumatoid arthritis: Metaanalysis of randomized controlled trials
    • le Blay, P., Mouterde, G., Barnetche, T., Morel, J. & Combe, B. Short-term risk of total malignancy and nonmelanoma skin cancers with certolizumab and golimumab in patients with rheumatoid arthritis: metaanalysis of randomized controlled trials. J. Rheumatol. 39, 712-715 (2012).
    • (2012) J. Rheumatol , vol.39 , pp. 712-715
    • Le Blay, P.1    Mouterde, G.2    Barnetche, T.3    Morel, J.4    Combe, B.5
  • 176
    • 78751680650 scopus 로고    scopus 로고
    • Certolizumab pegol in the treatment of rheumatoid arthritis: A comprehensive review of its clinical efficacy and safety
    • Mease, P. J. Certolizumab pegol in the treatment of rheumatoid arthritis: a comprehensive review of its clinical efficacy and safety. Rheumatol. 50, 261-270 (2011).
    • (2011) Rheumatol , vol.50 , pp. 261-270
    • Mease, P.J.1
  • 177
    • 78649344217 scopus 로고    scopus 로고
    • TNF-?antagonism in severe asthma? Recent Pat
    • Desai, D. & Brightling, C. TNF-? antagonism in severe asthma? Recent Pat. Inflamm. Allergy Drug Discov. 4, 193-200 (2010).
    • (2010) Inflamm. Allergy Drug Discov , vol.4 , pp. 193-200
    • Desai, D.1    Brightling, C.2
  • 178
    • 47149093236 scopus 로고    scopus 로고
    • Drug insight: Anti-tumor necrosis factor therapies for the vasculitic diseases
    • Langford, C. A. Drug insight: anti-tumor necrosis factor therapies for the vasculitic diseases. Nature Clin. Pract. Rheumatol. 4, 364-370 (2008).
    • (2008) Nature Clin. Pract. Rheumatol , vol.4 , pp. 364-370
    • Langford, C.A.1
  • 179
    • 78751662679 scopus 로고    scopus 로고
    • Type 1 diabetes: Etiology, immunology, and therapeutic strategies
    • van Belle, T. L., Coppieters, K. T. & von Herrath, M. G. Type 1 diabetes: etiology, immunology, and therapeutic strategies. Physiol. Rev. 91, 79-118 (2011).
    • (2011) Physiol. Rev , vol.91 , pp. 79-118
    • Van Belle, T.L.1    Coppieters, K.T.2    Von Herrath, M.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.