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Volumn 116, Issue , 2016, Pages 1-10

TRAF2 multitasking in TNF receptor-induced signaling to NF-κB, MAP kinases and cell death

Author keywords

Apoptosis; Necroptosis; NF B; TNF; TRAF2

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; PSMD2 PROTEIN, HUMAN; TNF PROTEIN, HUMAN; TNFRSF1A PROTEIN, HUMAN; TNFRSF1B PROTEIN, HUMAN; TUMOR NECROSIS FACTOR;

EID: 84961837933     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2016.03.009     Document Type: Review
Times cited : (166)

References (88)
  • 1
    • 38549102077 scopus 로고    scopus 로고
    • TNF-mediated inflammatory disease
    • [1] Bradley, J.R., TNF-mediated inflammatory disease. J. Pathol. 214 (2008), 149–160.
    • (2008) J. Pathol. , vol.214 , pp. 149-160
    • Bradley, J.R.1
  • 2
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • [2] Baud, V., Karin, M., Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol. 11 (2001), 372–377.
    • (2001) Trends Cell Biol. , vol.11 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 3
    • 0036184885 scopus 로고    scopus 로고
    • TNF ligands and receptors–a matter of life and death
    • [3] MacEwan, D.J., TNF ligands and receptors–a matter of life and death. Br. J. Pharmacol. 135 (2002), 855–875.
    • (2002) Br. J. Pharmacol. , vol.135 , pp. 855-875
    • MacEwan, D.J.1
  • 4
    • 0031040432 scopus 로고    scopus 로고
    • Structural features and biochemical properties of TNF-alpha converting enzyme (TACE)
    • [4] Moss, M.L., Jin, S.L., Becherer, J.D., Bickett, D.M., Burkhart, W., Chen, W.J., et al. Structural features and biochemical properties of TNF-alpha converting enzyme (TACE). J. Neuroimmunol. 72 (1997), 127–129.
    • (1997) J. Neuroimmunol. , vol.72 , pp. 127-129
    • Moss, M.L.1    Jin, S.L.2    Becherer, J.D.3    Bickett, D.M.4    Burkhart, W.5    Chen, W.J.6
  • 5
    • 0028866022 scopus 로고
    • The transmembrane form of tumor-necrosis-factor is the prime activating ligand of the 80 kDa tumor-necrosis-factor receptor
    • [5] Grell, M., Douni, E., Wajant, H., Lohden, M., Clauss, M., Maxeiner, B., et al. The transmembrane form of tumor-necrosis-factor is the prime activating ligand of the 80 kDa tumor-necrosis-factor receptor. Cell 83 (1995), 793–802.
    • (1995) Cell , vol.83 , pp. 793-802
    • Grell, M.1    Douni, E.2    Wajant, H.3    Lohden, M.4    Clauss, M.5    Maxeiner, B.6
  • 6
    • 79952509253 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor cross-talk
    • [6] Naude, P.J., den Boer, J.A., Luiten, P.G., Eisel, U.L., Tumor necrosis factor receptor cross-talk. FEBS J. 278 (2011), 888–898.
    • (2011) FEBS J. , vol.278 , pp. 888-898
    • Naude, P.J.1    den Boer, J.A.2    Luiten, P.G.3    Eisel, U.L.4
  • 7
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • [7] Micheau, O., Tschopp, J., Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114 (2003), 181–190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 8
    • 84859072803 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor receptors
    • [8] Cabal-Hierro, L., Lazo, P.S., Signal transduction by tumor necrosis factor receptors. Cell. Signal., 24, 2012.
    • (2012) Cell. Signal. , vol.24
    • Cabal-Hierro, L.1    Lazo, P.S.2
  • 9
    • 84878816379 scopus 로고    scopus 로고
    • TRAF molecules in cell signaling and in human diseases
    • [9] Xie, P., TRAF molecules in cell signaling and in human diseases. J. Mol. Signaling, 8, 2013, 7.
    • (2013) J. Mol. Signaling , vol.8 , pp. 7
    • Xie, P.1
  • 10
    • 0037084504 scopus 로고    scopus 로고
    • All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction
    • [10] Chung, J.Y., Park, Y.C., Ye, H., Wu, H., All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction. J. Cell Sci. 115 (2002), 679–688.
    • (2002) J. Cell Sci. , vol.115 , pp. 679-688
    • Chung, J.Y.1    Park, Y.C.2    Ye, H.3    Wu, H.4
  • 12
    • 84931068090 scopus 로고    scopus 로고
    • Targeting signaling factors for degradation, an emerging mechanism for TRAF functions
    • [12] Yang, X.D., Sun, S.C., Targeting signaling factors for degradation, an emerging mechanism for TRAF functions. Immunol. Rev. 266 (2015), 56–71.
    • (2015) Immunol. Rev. , vol.266 , pp. 56-71
    • Yang, X.D.1    Sun, S.C.2
  • 13
    • 0030032106 scopus 로고    scopus 로고
    • TRADD–TRAF2 and TRADD–FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • [13] 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 (1996), 299–308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.-B.2    Pan, M.-G.3    Goeddel, D.V.4
  • 14
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell-death and NF-Kappa-B activation
    • [14] Hsu, H.L., Xiong, J., Goeddel, D.V., The TNF receptor 1-associated protein TRADD signals cell-death and NF-Kappa-B activation. Cell 81 (1995), 495–504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.L.1    Xiong, J.2    Goeddel, D.V.3
  • 15
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • [15] 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 (1996), 387–396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 16
    • 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
    • [16] Fotin-Mleczek, M., Henkler, F., Samel, D., Reichwein, M., Hausser, A., Parmryd, I., 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 (2002), 2757–2770.
    • (2002) J. Cell Sci. , vol.115 , pp. 2757-2770
    • Fotin-Mleczek, M.1    Henkler, F.2    Samel, D.3    Reichwein, M.4    Hausser, A.5    Parmryd, I.6
  • 17
    • 2442559290 scopus 로고    scopus 로고
    • Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro
    • [17] Park, S.M., Yoon, J.B., Lee, T.H., Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro. FEBS Lett. 566 (2004), 151–156.
    • (2004) FEBS Lett. , vol.566 , pp. 151-156
    • Park, S.M.1    Yoon, J.B.2    Lee, T.H.3
  • 18
    • 72149117664 scopus 로고    scopus 로고
    • TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (tnf) to efficiently activate nf-{kappa}b and to prevent tnf-induced apoptosis
    • [18] Vince, J.E., Pantaki, D., Feltham, R., Mace, P.D., Cordier, S.M., Schmukle, A.C., et al. TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (tnf) to efficiently activate nf-{kappa}b and to prevent tnf-induced apoptosis. J. Biol. Chem. 284 (2009), 35906–35915.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35906-35915
    • Vince, J.E.1    Pantaki, D.2    Feltham, R.3    Mace, P.D.4    Cordier, S.M.5    Schmukle, A.C.6
  • 19
    • 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
    • [19] Haas, T.L., Emmerich, C.H., Gerlach, B., Schmukle, A.C., Cordier, S.M., Rieser, E., 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, 2009.
    • (2009) Mol. Cell , vol.36
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6
  • 20
    • 54049155149 scopus 로고    scopus 로고
    • C-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation
    • [20] Varfolomeev, E., Goncharov, T., Fedorova, A.V., Dynek, J.N., Zobel, K., Deshayes, K., et al. C-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation. J. Biol. Chem. 283 (2008), 24295–24299.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24295-24299
    • Varfolomeev, E.1    Goncharov, T.2    Fedorova, A.V.3    Dynek, J.N.4    Zobel, K.5    Deshayes, K.6
  • 21
    • 84929875491 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor signalling: live or let die
    • [21] Brenner, D., Blaser, H., Mak, T.W., Regulation of tumour necrosis factor signalling: live or let die. Nat. Rev. Immunol. 15 (2015), 362–374.
    • (2015) Nat. Rev. Immunol. , vol.15 , pp. 362-374
    • Brenner, D.1    Blaser, H.2    Mak, T.W.3
  • 22
    • 44949240664 scopus 로고    scopus 로고
    • CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • [22] Bertrand, M.J., Milutinovic, S., Dickson, K.M., Ho, W.C., Boudreault, A., Durkin, J., et al. CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol. Cell 30 (2008), 689–700.
    • (2008) Mol. Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.1    Milutinovic, S.2    Dickson, K.M.3    Ho, W.C.4    Boudreault, A.5    Durkin, J.6
  • 23
    • 1542380581 scopus 로고    scopus 로고
    • Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB
    • [23] Habelhah, H., Takahashi, S., Cho, S.G., Kadoya, T., Watanabe, T., Ronai, Z., Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB. EMBO J. 23 (2004), 322–332.
    • (2004) EMBO J. , vol.23 , pp. 322-332
    • Habelhah, H.1    Takahashi, S.2    Cho, S.G.3    Kadoya, T.4    Watanabe, T.5    Ronai, Z.6
  • 24
    • 0038150358 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2)
    • [24] Shi, C.S., Kehrl, J.H., Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2). J. Biol. Chem. 278 (2003), 15429–15434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15429-15434
    • Shi, C.S.1    Kehrl, J.H.2
  • 25
    • 56349164232 scopus 로고    scopus 로고
    • Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling
    • [25] Vallabhapurapu, S., Matsuzawa, A., Zhang, W., Tseng, P.H., Keats, J.J., Wang, H., et al. Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling. Nat. Immunol. 9 (2008), 1364–1370.
    • (2008) Nat. Immunol. , vol.9 , pp. 1364-1370
    • Vallabhapurapu, S.1    Matsuzawa, A.2    Zhang, W.3    Tseng, P.H.4    Keats, J.J.5    Wang, H.6
  • 26
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • [26] Lee, T.H., Shank, J., Cusson, N., Kelliher, M.A., The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J. Biol. Chem. 279 (2004), 33185–33191.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3    Kelliher, M.A.4
  • 27
    • 0038742813 scopus 로고    scopus 로고
    • Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation
    • [27] Legler, D.F., Micheau, O., Doucey, M.A., Tschopp, J., Bron, C., Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation. Immunity 18 (2003), 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
  • 28
    • 77949332322 scopus 로고    scopus 로고
    • The RING domain of TRAF2 plays an essential role in the inhibition of TNFα-induced cell death but not in the activation of NF-κB
    • [28] Zhang, L., Blackwell, K., Shi, Z., Habelhah, H., The RING domain of TRAF2 plays an essential role in the inhibition of TNFα-induced cell death but not in the activation of NF-κB. J. Mol. Biol. 396 (2010), 528–539.
    • (2010) J. Mol. Biol. , vol.396 , pp. 528-539
    • Zhang, L.1    Blackwell, K.2    Shi, Z.3    Habelhah, H.4
  • 29
    • 0031463025 scopus 로고    scopus 로고
    • Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice
    • [29] Yeh, W.C., Shahinian, A., Speiser, D., Kraunus, J., Billia, F., Wakeham, A., et al. Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity 7 (1997), 715–725.
    • (1997) Immunity , vol.7 , pp. 715-725
    • Yeh, W.C.1    Shahinian, A.2    Speiser, D.3    Kraunus, J.4    Billia, F.5    Wakeham, A.6
  • 30
    • 0035965232 scopus 로고    scopus 로고
    • Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-κB activation and protection from cell death
    • [30] Tada, K., Okazaki, T., Sakon, S., Kobarai, T., Kurosawa, K., Yamaoka, S., et al. Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-κB activation and protection from cell death. J. Biol. Chem. 276 (2001), 36530–36534.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36530-36534
    • Tada, K.1    Okazaki, T.2    Sakon, S.3    Kobarai, T.4    Kurosawa, K.5    Yamaoka, S.6
  • 31
    • 65649150701 scopus 로고    scopus 로고
    • TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can activate IKK in TRAF2 and TRAF5 double knockout cells
    • [31] Zhang, L., Blackwell, K., Thomas, G.S., Sun, S., Yeh, W.C., Habelhah, H., TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can activate IKK in TRAF2 and TRAF5 double knockout cells. J. Mol. Biol. 389 (2009), 495–510.
    • (2009) J. Mol. Biol. , vol.389 , pp. 495-510
    • Zhang, L.1    Blackwell, K.2    Thomas, G.S.3    Sun, S.4    Yeh, W.C.5    Habelhah, H.6
  • 32
    • 56349164239 scopus 로고    scopus 로고
    • Noncanonical NF-kappaB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK
    • [32] Zarnegar, B.J., Wang, Y., Mahoney, D.J., Dempsey, P.W., Cheung, H.H., He, J., et al. Noncanonical NF-kappaB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK. Nat. Immunol. 9 (2008), 1371–1378.
    • (2008) Nat. Immunol. , vol.9 , pp. 1371-1378
    • Zarnegar, B.J.1    Wang, Y.2    Mahoney, D.J.3    Dempsey, P.W.4    Cheung, H.H.5    He, J.6
  • 33
    • 84912077303 scopus 로고    scopus 로고
    • Receptor proximal kinases in NF-kappaB signaling as potential therapeutic targets in cancer and inflammation
    • [33] Verstrepen, L., Beyaert, R., Receptor proximal kinases in NF-kappaB signaling as potential therapeutic targets in cancer and inflammation. Biochem. Pharmacol. 92 (2014), 519–529.
    • (2014) Biochem. Pharmacol. , vol.92 , pp. 519-529
    • Verstrepen, L.1    Beyaert, R.2
  • 35
    • 84893870874 scopus 로고    scopus 로고
    • A TRAF2 binding independent region of TNFR2 is responsible for TRAF2 depletion and enhancement of cytotoxicity driven by TNFR1
    • [35] Cabal-Hierro, L., Artime, N., Iglesias, J., Prado, M.A., Ugarte-Gil, L., Casado, P., et al. A TRAF2 binding independent region of TNFR2 is responsible for TRAF2 depletion and enhancement of cytotoxicity driven by TNFR1. Oncotarget 5 (2014), 224–236.
    • (2014) Oncotarget , vol.5 , pp. 224-236
    • Cabal-Hierro, L.1    Artime, N.2    Iglesias, J.3    Prado, M.A.4    Ugarte-Gil, L.5    Casado, P.6
  • 36
    • 84865497414 scopus 로고    scopus 로고
    • Both internalization and AIP1 association are required for tumor necrosis factor receptor 2-mediated JNK signaling
    • [36] Ji, W., Li, Y., Wan, T., Wang, J., Zhang, H., Chen, H., et al. Both internalization and AIP1 association are required for tumor necrosis factor receptor 2-mediated JNK signaling. Arterioscler. Thromb. Vasc. Biol. 32 (2012), 2271–2279.
    • (2012) Arterioscler. Thromb. Vasc. Biol. , vol.32 , pp. 2271-2279
    • Ji, W.1    Li, Y.2    Wan, T.3    Wang, J.4    Zhang, H.5    Chen, H.6
  • 38
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • [38] Rothe, M., Wong, S.C., Henzel, W.J., Goeddel, D.V., A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 78 (1994), 681–692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 39
    • 11244334124 scopus 로고    scopus 로고
    • TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation
    • [39] He, L., Grammer, A.C., Wu, X., Lipsky, P.E., TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation. J. Biol. Chem. 279 (2004), 55855–55865.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55855-55865
    • He, L.1    Grammer, A.C.2    Wu, X.3    Lipsky, P.E.4
  • 40
    • 77950352082 scopus 로고    scopus 로고
    • Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation
    • [40] 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 (2010), 101–113.
    • (2010) Mol. Cell , vol.38 , pp. 101-113
    • Zheng, C.1    Kabaleeswaran, V.2    Wang, Y.3    Cheng, G.4    Wu, H.5
  • 41
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • [41] Rothe, M., Pan, M.G., Henzel, W.J., Ayres, T.M., Goeddel, D.V., The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83 (1995), 1243–1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 42
    • 3543046113 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated neuroprotection against glutamate-induced excitotoxicity is enhanced by N-methyl-D-aspartate receptor activation essential role of a TNF receptor 2-mediated phosphatidylinositol 3-kinase-dependent NF-κB pathway
    • [42] Marchetti, L., Klein, M., Schlett, K., Pfizenmaier, K., Eisel, U.L.M., Tumor necrosis factor (TNF)-mediated neuroprotection against glutamate-induced excitotoxicity is enhanced by N-methyl-D-aspartate receptor activation essential role of a TNF receptor 2-mediated phosphatidylinositol 3-kinase-dependent NF-κB pathway. J. Biol. Chem. 279 (2004), 32869–32881.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32869-32881
    • Marchetti, L.1    Klein, M.2    Schlett, K.3    Pfizenmaier, K.4    Eisel, U.L.M.5
  • 43
    • 0345826140 scopus 로고    scopus 로고
    • Cell type-specific expression of the IkappaB kinases determines the significance of phosphatidylinositol 3-kinase/Akt signaling to NF-kappa B activation
    • [43] Gustin, J.A., Ozes, O.N., Akca, H., Pincheira, R., Mayo, L.D., Li, Q., et al. Cell type-specific expression of the IkappaB kinases determines the significance of phosphatidylinositol 3-kinase/Akt signaling to NF-kappa B activation. J. Biol. Chem. 279 (2004), 1615–1620.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1615-1620
    • Gustin, J.A.1    Ozes, O.N.2    Akca, H.3    Pincheira, R.4    Mayo, L.D.5    Li, Q.6
  • 44
    • 14644414800 scopus 로고    scopus 로고
    • Induction of apoptosis by TNF receptor 2 in a T-cell hybridoma is FADD dependent and blocked by caspase-8 inhibitors
    • [44] Depuydt, B., van Loo, G., Vandenabeele, P., Declercq, W., Induction of apoptosis by TNF receptor 2 in a T-cell hybridoma is FADD dependent and blocked by caspase-8 inhibitors. J. Cell Sci. 118 (2005), 497–504.
    • (2005) J. Cell Sci. , vol.118 , pp. 497-504
    • Depuydt, B.1    van Loo, G.2    Vandenabeele, P.3    Declercq, W.4
  • 45
    • 1642300863 scopus 로고    scopus 로고
    • The role of TNF and its family members in inflammation and cancer: lessons from gene deletion
    • [45] Aggarwal, B.B., Shishodia, S., Ashikawa, K., Bharti, A.C., The role of TNF and its family members in inflammation and cancer: lessons from gene deletion. Curr. Drug Targets Inflamm. Allergy 1 (2002), 327–341.
    • (2002) Curr. Drug Targets Inflamm. Allergy , vol.1 , pp. 327-341
    • Aggarwal, B.B.1    Shishodia, S.2    Ashikawa, K.3    Bharti, A.C.4
  • 46
    • 65049086930 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation
    • [46] Wicovsky, A., Henkler, F., Salzmann, S., Scheurich, P., Kneitz, C., Wajant, H., Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation. Oncogene 28 (2009), 1769–1781.
    • (2009) Oncogene , vol.28 , pp. 1769-1781
    • Wicovsky, A.1    Henkler, F.2    Salzmann, S.3    Scheurich, P.4    Kneitz, C.5    Wajant, H.6
  • 47
    • 84892449873 scopus 로고    scopus 로고
    • TNFR2 increases the sensitivity of ligand-induced activation of the p38 MAPK and NF-kappaB pathways and signals TRAF2 protein degradation in macrophages
    • [47] Ruspi, G., Schmidt, E.M., McCann, F., Feldmann, M., Williams, R.O., Stoop, A.A., et al. TNFR2 increases the sensitivity of ligand-induced activation of the p38 MAPK and NF-kappaB pathways and signals TRAF2 protein degradation in macrophages. Cell. Signal. 26 (2014), 683–690.
    • (2014) Cell. Signal. , vol.26 , pp. 683-690
    • Ruspi, G.1    Schmidt, E.M.2    McCann, F.3    Feldmann, M.4    Williams, R.O.5    Stoop, A.A.6
  • 48
    • 0037149542 scopus 로고    scopus 로고
    • TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2
    • [48] Li, X., Yang, Y., Ashwell, J.D., TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. Nature 416 (2002), 345–347.
    • (2002) Nature , vol.416 , pp. 345-347
    • Li, X.1    Yang, Y.2    Ashwell, J.D.3
  • 49
    • 77951234694 scopus 로고    scopus 로고
    • Membrane tumor necrosis factor (TNF) induces p100 processing via TNF receptor-2 (TNFR2)
    • [49] Rauert, H., Wicovsky, A., Muller, N., Siegmund, D., Spindler, V., Waschke, J., et al. Membrane tumor necrosis factor (TNF) induces p100 processing via TNF receptor-2 (TNFR2). J. Biol. Chem. 285 (2010), 7394–7404.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7394-7404
    • Rauert, H.1    Wicovsky, A.2    Muller, N.3    Siegmund, D.4    Spindler, V.5    Waschke, J.6
  • 50
    • 84858735072 scopus 로고    scopus 로고
    • The noncanonical NF-kappaB pathway
    • [50] Sun, S.C., The noncanonical NF-kappaB pathway. Immunol. Rev. 246 (2012), 125–140.
    • (2012) Immunol. Rev. , vol.246 , pp. 125-140
    • Sun, S.C.1
  • 51
    • 4444341939 scopus 로고    scopus 로고
    • Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles
    • [51] Schneider-Brachert, W., Tchikov, V., Neumeyer, J., Jakob, M., Winoto-Morbach, S., Held-Feindt, J., et al. Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles. Immunity 21 (2004), 415–428.
    • (2004) Immunity , vol.21 , pp. 415-428
    • Schneider-Brachert, W.1    Tchikov, V.2    Neumeyer, J.3    Jakob, M.4    Winoto-Morbach, S.5    Held-Feindt, J.6
  • 52
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • [52] Wang, L., Du, F., Wang, X., TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133 (2008), 693–703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 53
    • 79960921946 scopus 로고    scopus 로고
    • The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • [53] Tenev, T., Bianchi, K., Darding, M., Broemer, M., Langlais, C., Wallberg, F., et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol. Cell 43 (2011), 432–448.
    • (2011) Mol. Cell , vol.43 , pp. 432-448
    • Tenev, T.1    Bianchi, K.2    Darding, M.3    Broemer, M.4    Langlais, C.5    Wallberg, F.6
  • 54
    • 0033198702 scopus 로고    scopus 로고
    • TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses
    • [54] Nguyen, L.T., Duncan, G.S., Mirtsos, C., Ng, M., Speiser, D.E., Shahinian, A., et al. TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses. Immunity 11 (1999), 379–389.
    • (1999) Immunity , vol.11 , pp. 379-389
    • Nguyen, L.T.1    Duncan, G.S.2    Mirtsos, C.3    Ng, M.4    Speiser, D.E.5    Shahinian, A.6
  • 55
    • 79955951399 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factor (TRAF) 2 controls homeostasis of the colon to prevent spontaneous development of murine inflammatory bowel disease
    • [55] Piao, J.-H., Hasegawa, M., Heissig, B., Hattori, K., Takeda, K., Iwakura, Y., et al. Tumor necrosis factor receptor-associated factor (TRAF) 2 controls homeostasis of the colon to prevent spontaneous development of murine inflammatory bowel disease. J. Biol. Chem. 286 (2011), 17879–17888.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17879-17888
    • Piao, J.-H.1    Hasegawa, M.2    Heissig, B.3    Hattori, K.4    Takeda, K.5    Iwakura, Y.6
  • 56
    • 79953906762 scopus 로고    scopus 로고
    • In TNF-stimulated cells, RIPK1 promotes cell survival by stabilizing TRAF2 and cIAP1, which limits induction of non-canonical NF-kappaB and activation of caspase-8
    • [56] Gentle, I.E., Wong, W.W., Evans, J.M., Bankovacki, A., Cook, W.D., Khan, N.R., et al. In TNF-stimulated cells, RIPK1 promotes cell survival by stabilizing TRAF2 and cIAP1, which limits induction of non-canonical NF-kappaB and activation of caspase-8. J. Biol. Chem. 286 (2011), 13282–13291.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13282-13291
    • Gentle, I.E.1    Wong, W.W.2    Evans, J.M.3    Bankovacki, A.4    Cook, W.D.5    Khan, N.R.6
  • 57
    • 84871679702 scopus 로고    scopus 로고
    • TRAF2 sets a threshold for extrinsic apoptosis by tagging caspase-8 with a ubiquitin shutoff timer
    • [57] Gonzalvez, F., Lawrence, D., Yang, B., Yee, S., Pitti, R., Marsters, S., et al. TRAF2 sets a threshold for extrinsic apoptosis by tagging caspase-8 with a ubiquitin shutoff timer. Mol. Cell 48 (2012), 888–899.
    • (2012) Mol. Cell , vol.48 , pp. 888-899
    • Gonzalvez, F.1    Lawrence, D.2    Yang, B.3    Yee, S.4    Pitti, R.5    Marsters, S.6
  • 58
    • 84255210700 scopus 로고    scopus 로고
    • Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012
    • [58] Galluzzi, L., Vitale, I., Abrams, J.M., Alnemri, E.S., Baehrecke, E.H., Blagosklonny, M.V., et al. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ. 19 (2012), 107–120.
    • (2012) Cell Death Differ. , vol.19 , pp. 107-120
    • Galluzzi, L.1    Vitale, I.2    Abrams, J.M.3    Alnemri, E.S.4    Baehrecke, E.H.5    Blagosklonny, M.V.6
  • 59
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • [59] Holler, N., Zaru, R., Micheau, O., Thome, M., Attinger, A., Valitutti, S., et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1 (2000), 489–495.
    • (2000) Nat. Immunol. , vol.1 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3    Thome, M.4    Attinger, A.5    Valitutti, S.6
  • 60
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • [60] He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 137 (2009), 1100–1111.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6
  • 61
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • [61] Cho, Y.S., Challa, S., Moquin, D., Genga, R., Ray, T.D., Guildford, M., et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137 (2009), 1112–1123.
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1    Challa, S.2    Moquin, D.3    Genga, R.4    Ray, T.D.5    Guildford, M.6
  • 62
    • 84859467770 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
    • [62] Zhao, J., Jitkaew, S., Cai, Z., Choksi, S., Li, Q., Luo, 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. U.S.A. 109 (2012), 5322–5327.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 5322-5327
    • Zhao, J.1    Jitkaew, S.2    Cai, Z.3    Choksi, S.4    Li, Q.5    Luo, J.6
  • 63
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • [63] Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 148 (2012), 213–227.
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1    Wang, H.2    Wang, Z.3    He, S.4    Chen, S.5    Liao, D.6
  • 64
    • 84898027331 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3
    • [64] Wang, H., Sun, L., Su, L., Rizo, J., Liu, L., Wang, L.-F., et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol. Cell 54 (2014), 133–146.
    • (2014) Mol. Cell , vol.54 , pp. 133-146
    • Wang, H.1    Sun, L.2    Su, L.3    Rizo, J.4    Liu, L.5    Wang, L.-F.6
  • 66
    • 0032698901 scopus 로고    scopus 로고
    • TRAF1 is a TNF inducible regulator of NF-kappaB activation
    • [66] Carpentier, I., Beyaert, R., TRAF1 is a TNF inducible regulator of NF-kappaB activation. FEBS Lett. 460 (1999), 246–250.
    • (1999) FEBS Lett. , vol.460 , pp. 246-250
    • Carpentier, I.1    Beyaert, R.2
  • 67
    • 20044387665 scopus 로고    scopus 로고
    • TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination
    • [67] Wu, C.J., Conze, D.B., Li, X., Ying, S.X., Hanover, J.A., Ashwell, J.D., TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination. EMBO J. 24 (2005), 1886–1898.
    • (2005) EMBO J. , vol.24 , pp. 1886-1898
    • Wu, C.J.1    Conze, D.B.2    Li, X.3    Ying, S.X.4    Hanover, J.A.5    Ashwell, J.D.6
  • 68
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • [68] Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israel, A., Wallach, D., Courtois, G., The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 424 (2003), 801–805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 69
    • 58749100827 scopus 로고    scopus 로고
    • The zinc finger protein A20 targets TRAF2 to the lysosomes for degradation
    • [69] Li, L., Soetandyo, N., Wang, Q., Ye, Y., The zinc finger protein A20 targets TRAF2 to the lysosomes for degradation. Biochim. Biophys. Acta 1793 (2009), 346–353.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 346-353
    • Li, L.1    Soetandyo, N.2    Wang, Q.3    Ye, Y.4
  • 71
    • 84884224079 scopus 로고    scopus 로고
    • Involvement of A20 in the molecular switch that activates the non-canonical NF-small ka, CyrillicB pathway
    • [71] Yamaguchi, N., Oyama, M., Kozuka-Hata, H., Inoue, J., Involvement of A20 in the molecular switch that activates the non-canonical NF-small ka, CyrillicB pathway. Sci. Rep., 3, 2013, 2568.
    • (2013) Sci. Rep. , vol.3 , pp. 2568
    • Yamaguchi, N.1    Oyama, M.2    Kozuka-Hata, H.3    Inoue, J.4
  • 72
    • 58149301485 scopus 로고    scopus 로고
    • PKC phosphorylation of TRAF2 mediates IKKα/β recruitment and K63-linked polyubiquitination
    • [72] Li, S., Wang, L., Dorf, M.E., PKC phosphorylation of TRAF2 mediates IKKα/β recruitment and K63-linked polyubiquitination. Mol. Cell, 33, 2008.
    • (2008) Mol. Cell , vol.33
    • Li, S.1    Wang, L.2    Dorf, M.E.3
  • 73
    • 58249115041 scopus 로고    scopus 로고
    • TRAF2 phosphorylation modulates tumor necrosis factor alpha-induced gene expression and cell resistance to apoptosis
    • [73] Blackwell, K., Zhang, L., Thomas, G.S., Sun, S., Nakano, H., Habelhah, H., TRAF2 phosphorylation modulates tumor necrosis factor alpha-induced gene expression and cell resistance to apoptosis. Mol. Cell. Biol. 29 (2009), 303–314.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 303-314
    • Blackwell, K.1    Zhang, L.2    Thomas, G.S.3    Sun, S.4    Nakano, H.5    Habelhah, H.6
  • 74
    • 65949114424 scopus 로고    scopus 로고
    • Phosphorylation of TRAF2 within its RING domain inhibits stress-induced cell death by promoting IKK and suppressing JNK activation
    • [74] Thomas, G.S., Zhang, L., Blackwell, K., Habelhah, H., Phosphorylation of TRAF2 within its RING domain inhibits stress-induced cell death by promoting IKK and suppressing JNK activation. Cancer Res. 69 (2009), 3665–3672.
    • (2009) Cancer Res. , vol.69 , pp. 3665-3672
    • Thomas, G.S.1    Zhang, L.2    Blackwell, K.3    Habelhah, H.4
  • 75
    • 78651084030 scopus 로고    scopus 로고
    • TRAF2 phosphorylation promotes NF-kappaB-dependent gene expression and inhibits oxidative stress-induced cell death
    • [75] Zhang, L., Blackwell, K., Altaeva, A., Shi, Z., Habelhah, H., TRAF2 phosphorylation promotes NF-kappaB-dependent gene expression and inhibits oxidative stress-induced cell death. Mol. Biol. Cell 22 (2011), 128–140.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 128-140
    • Zhang, L.1    Blackwell, K.2    Altaeva, A.3    Shi, Z.4    Habelhah, H.5
  • 76
    • 84955203481 scopus 로고    scopus 로고
    • Safety of anti-TNF therapies in immune-mediated inflammatory diseases: focus on infections and malignancy
    • [76] Pereira, R., Lago, P., Faria, R., Torres, T., Safety of anti-TNF therapies in immune-mediated inflammatory diseases: focus on infections and malignancy. Drug Dev. Res. 76 (2015), 419–427.
    • (2015) Drug Dev. Res. , vol.76 , pp. 419-427
    • Pereira, R.1    Lago, P.2    Faria, R.3    Torres, T.4
  • 77
    • 79951501790 scopus 로고    scopus 로고
    • Cellular mechanisms of TNF function in models of inflammation and autoimmunity
    • [77] Apostolaki, M., Armaka, M., Victoratos, P., Kollias, G., Cellular mechanisms of TNF function in models of inflammation and autoimmunity. Curr. Dir. Autoimmun. 11 (2010), 1–26.
    • (2010) Curr. Dir. Autoimmun. , vol.11 , pp. 1-26
    • Apostolaki, M.1    Armaka, M.2    Victoratos, P.3    Kollias, G.4
  • 78
    • 77954391573 scopus 로고    scopus 로고
    • Enterocyte-specific A20 deficiency sensitizes to tumor necrosis factor-induced toxicity and experimental colitis
    • [78] Vereecke, L., Sze, M., Mc Guire, C., Rogiers, B., Chu, Y., Schmidt-Supprian, M., et al. Enterocyte-specific A20 deficiency sensitizes to tumor necrosis factor-induced toxicity and experimental colitis. J. Exp. Med. 207 (2010), 1513–1523.
    • (2010) J. Exp. Med. , vol.207 , pp. 1513-1523
    • Vereecke, L.1    Sze, M.2    Mc Guire, C.3    Rogiers, B.4    Chu, Y.5    Schmidt-Supprian, M.6
  • 80
    • 84900333477 scopus 로고    scopus 로고
    • Birinapant (TL32711), a bivalent SMAC mimetic, targets TRAF2-associated cIAPs, abrogates TNF-induced NF-κB activation, and is active in patient-derived xenograft models
    • [80] Benetatos, C.A., Mitsuuchi, Y., Burns, J.M., Neiman, E.M., Condon, S.M., Yu, G., et al. Birinapant (TL32711), a bivalent SMAC mimetic, targets TRAF2-associated cIAPs, abrogates TNF-induced NF-κB activation, and is active in patient-derived xenograft models. Mol. Cancer Ther. 13 (2014), 867–879.
    • (2014) Mol. Cancer Ther. , vol.13 , pp. 867-879
    • Benetatos, C.A.1    Mitsuuchi, Y.2    Burns, J.M.3    Neiman, E.M.4    Condon, S.M.5    Yu, G.6
  • 81
    • 84871862001 scopus 로고    scopus 로고
    • Downregulation of TRAF2 mediates NIK-induced pancreatic cancer cell proliferation and tumorigenicity
    • [81] Döppler, H., Liou, G.-Y., Storz, P., Downregulation of TRAF2 mediates NIK-induced pancreatic cancer cell proliferation and tumorigenicity. PLoS One, 8, 2013.
    • (2013) PLoS One , vol.8
    • Döppler, H.1    Liou, G.-Y.2    Storz, P.3
  • 82
    • 84954110027 scopus 로고    scopus 로고
    • Promises and challenges of Smac mimetics as cancer therapeutics
    • [82] Fulda, S., Promises and challenges of Smac mimetics as cancer therapeutics. Clin. Cancer Res. 21 (2015), 5030–5036.
    • (2015) Clin. Cancer Res. , vol.21 , pp. 5030-5036
    • Fulda, S.1
  • 83
    • 79951689476 scopus 로고    scopus 로고
    • SCF E3 ubiquitin ligases as anticancer targets
    • [83] Jia, L., Sun, Y., SCF E3 ubiquitin ligases as anticancer targets. Curr. Cancer Drug Targets 11 (2011), 347–356.
    • (2011) Curr. Cancer Drug Targets , vol.11 , pp. 347-356
    • Jia, L.1    Sun, Y.2
  • 84
    • 77951226295 scopus 로고    scopus 로고
    • Inhibiting TRAF2-mediated activation of NF-kappaB facilitates induction of AP-1
    • [84] Manna, S.K., Babajan, B., Raghavendra, P.B., Raviprakash, N., Sureshkumar, C., Inhibiting TRAF2-mediated activation of NF-kappaB facilitates induction of AP-1. J. Biol. Chem. 285 (2010), 11617–11627.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11617-11627
    • Manna, S.K.1    Babajan, B.2    Raghavendra, P.B.3    Raviprakash, N.4    Sureshkumar, C.5
  • 85
    • 84863115948 scopus 로고    scopus 로고
    • Studies on pharmacokinetics and tissue distribution of bifendate nanosuspensions for intravenous delivery
    • [85] Liu, Y., Zhang, D., Duan, C., Jia, L., Xie, P., Zheng, D., et al. Studies on pharmacokinetics and tissue distribution of bifendate nanosuspensions for intravenous delivery. J. Microencapsul. 29 (2012), 194–203.
    • (2012) J. Microencapsul. , vol.29 , pp. 194-203
    • Liu, Y.1    Zhang, D.2    Duan, C.3    Jia, L.4    Xie, P.5    Zheng, D.6
  • 86
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: a double-edged sword
    • [86] Aggarwal, B.B., Signalling pathways of the TNF superfamily: a double-edged sword. Nat. Rev. Immunol. 3 (2003), 745–756.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 87
    • 8444220390 scopus 로고    scopus 로고
    • TRAF2 differentially regulates the canonical and noncanonical pathways of NF-kappaB activation in mature B cells
    • [87] Grech, A.P., Amesbury, M., Chan, T., Gardam, S., Basten, A., Brink, R., TRAF2 differentially regulates the canonical and noncanonical pathways of NF-kappaB activation in mature B cells. Immunity 21 (2004), 629–642.
    • (2004) Immunity , vol.21 , pp. 629-642
    • Grech, A.P.1    Amesbury, M.2    Chan, T.3    Gardam, S.4    Basten, A.5    Brink, R.6
  • 88
    • 84961262986 scopus 로고    scopus 로고
    • TRAF2 regulates TNF and NF-kappaB signalling to suppress apoptosis and skin inflammation independently of Sphingosine kinase-1.eLife
    • [88] Etemadi, N., Chopin, M., Anderton, H., Tanzer, M.C., Rickard, J.A., Abeysekra, W., TRAF2 regulates TNF and NF-kappaB signalling to suppress apoptosis and skin inflammation independently of Sphingosine kinase-1.eLife., 4, 2015.
    • (2015) , vol.4
    • Etemadi, N.1    Chopin, M.2    Anderton, H.3    Tanzer, M.C.4    Rickard, J.A.5    Abeysekra, W.6


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