메뉴 건너뛰기




Volumn 54, Issue 1-3, 2012, Pages 214-226

NFκB and ubiquitination: Partners in disarming RIPK1-mediated cell death

Author keywords

Apoptosis; Caspase 8; Cell death; CYLD; Necroptosis; RIPK1; RIPK3; TNF; Ubiquitination

Indexed keywords

CASPASE; CASPASE 10; CASPASE 8; I KAPPA B ALPHA; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHOTRANSFERASE; PROTEIN RIPK1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUCCINATE DEHYDROGENASE (UBIQUINONE); TOLL LIKE RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED DEATH DOMAIN PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84867877809     PISSN: 0257277X     EISSN: 15590755     Source Type: Journal    
DOI: 10.1007/s12026-012-8321-7     Document Type: Review
Times cited : (27)

References (102)
  • 1
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • 10.1146/annurev.iy.12.040194.001041 8011280 1:CAS:528:DyaK2cXivFKjurY%3D
    • Baeuerle PA, Henkel T. Function and activation of NF-kappa B in the immune system. Annu Rev Immunol. 1994;12:141-79. doi: 10.1146/annurev.iy.12. 040194.001041.
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 2
    • 26944462054 scopus 로고    scopus 로고
    • The yins of T cell activation
    • 10.1126/stke.2652005re1 15632417
    • Liu JO. The yins of T cell activation. Sci STKE. 2005;2005(265):re1. doi: 10.1126/stke.2652005re1.
    • (2005) Sci STKE , vol.2005 , Issue.265 , pp. 1
    • Liu, J.O.1
  • 3
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-kappaB transcription factors in the immune system
    • 10.1146/annurev.immunol.021908.132641 19302050 1:CAS:528: DC%2BD1MXlsFSlt7o%3D
    • Vallabhapurapu S, Karin M. Regulation and function of NF-kappaB transcription factors in the immune system. Annu Rev Immunol. 2009;27:693-733. doi: 10.1146/annurev.immunol.021908.132641.
    • (2009) Annu Rev Immunol , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 4
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • 10.1146/annurev.immunol.18.1.621 10837071 1:CAS:528:DC%2BD3cXjs1Gmtro%3D
    • Karin M, Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol. 2000;18:621-63. doi: 10.1146/annurev.immunol.18.1.621.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 5
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases
    • 10.1126/stke.3572006re13 17047224
    • Hacker H, Karin M. Regulation and function of IKK and IKK-related kinases. Sci STKE. 2006;2006(357):re13. doi: 10.1126/stke.3572006re13.
    • (2006) Sci STKE , vol.2006 , Issue.357 , pp. 13
    • Hacker, H.1    Karin, M.2
  • 6
    • 83855162723 scopus 로고    scopus 로고
    • Principles of dimer-specific gene regulation revealed by a comprehensive characterization of NF-kappaB family DNA binding
    • 10.1038/ni.2151 22101729
    • Siggers T, Chang AB, Teixeira A, Wong D, Williams KJ, Ahmed B, et al. Principles of dimer-specific gene regulation revealed by a comprehensive characterization of NF-kappaB family DNA binding. Nat Immunol. 2011;13(1):95-102. doi: 10.1038/ni.2151.
    • (2011) Nat Immunol , vol.13 , Issue.1 , pp. 95-102
    • Siggers, T.1    Chang, A.B.2    Teixeira, A.3    Wong, D.4    Williams, K.J.5    Ahmed, B.6
  • 7
    • 80051988785 scopus 로고    scopus 로고
    • Hierarchies of NF-kappaB target-gene regulation
    • 10.1038/ni.2070 21772277 1:CAS:528:DC%2BC3MXptV2ju7w%3D
    • Smale ST. Hierarchies of NF-kappaB target-gene regulation. Nat Immunol. 2011;12(8):689-94. doi: 10.1038/ni.2070.
    • (2011) Nat Immunol , vol.12 , Issue.8 , pp. 689-694
    • Smale, S.T.1
  • 8
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • 10338206 1:CAS:528:DyaK1MXjt1Oru7w%3D
    • Laney JD, Hochstrasser M. Substrate targeting in the ubiquitin system. Cell. 1999;97(4):427-30.
    • (1999) Cell , vol.97 , Issue.4 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 9
    • 0034691673 scopus 로고    scopus 로고
    • SCF(beta-TRCP) and phosphorylation dependent ubiquitination of i kappa B alpha catalyzed by Ubc3 and Ubc4
    • 10.1038/sj.onc.1203647 10918611 1:CAS:528:DC%2BD3cXlslyhtrw%3D
    • Strack P, Caligiuri M, Pelletier M, Boisclair M, Theodoras A, Beer-Romero P, et al. SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I kappa B alpha catalyzed by Ubc3 and Ubc4. Oncogene. 2000;19(31):3529-36. doi: 10.1038/sj.onc.1203647.
    • (2000) Oncogene , vol.19 , Issue.31 , pp. 3529-3536
    • Strack, P.1    Caligiuri, M.2    Pelletier, M.3    Boisclair, M.4    Theodoras, A.5    Beer-Romero, P.6
  • 10
    • 17944401842 scopus 로고    scopus 로고
    • Identification of the receptor component of the IkappaBalpha-ubiquitin ligase
    • 10.1038/25159 9859996 1:CAS:528:DyaK1cXotVWnt78%3D
    • Yaron A, Hatzubai A, Davis M, Lavon I, Amit S, Manning AM, et al. Identification of the receptor component of the IkappaBalpha-ubiquitin ligase. Nature. 1998;396(6711):590-4. doi: 10.1038/25159.
    • (1998) Nature , vol.396 , Issue.6711 , pp. 590-594
    • Yaron, A.1    Hatzubai, A.2    Davis, M.3    Lavon, I.4    Amit, S.5    Manning, A.M.6
  • 11
  • 12
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-kappaB
    • 8864119 1:CAS:528:DyaK28XmsFOhu7Y%3D
    • Wang CY, Mayo MW, Baldwin AS Jr. TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kappaB. Science. 1996;274(5288):784-7.
    • (1996) Science , vol.274 , Issue.5288 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin Jr., A.S.3
  • 13
    • 79955620198 scopus 로고    scopus 로고
    • Constructing and decoding unconventional ubiquitin chains
    • 10.1038/nsmb.2066 21540891 1:CAS:528:DC%2BC3MXlsFKnur0%3D
    • Behrends C, Harper JW. Constructing and decoding unconventional ubiquitin chains. Nat Struct Mol Biol. 2011;18(5):520-8. doi: 10.1038/nsmb.2066.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.5 , pp. 520-528
    • Behrends, C.1    Harper, J.W.2
  • 14
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation
    • 10.1016/j.cell.2009.03.007 19303852 1:CAS:528:DC%2BD1MXltFSnt78%3D
    • Rahighi S, Ikeda F, Kawasaki M, Akutsu M, Suzuki N, Kato R, et al. Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. Cell. 2009;136(6):1098-109. doi: 10.1016/j.cell.2009.03. 007.
    • (2009) Cell , vol.136 , Issue.6 , pp. 1098-1109
    • Rahighi, S.1    Ikeda, F.2    Kawasaki, M.3    Akutsu, M.4    Suzuki, N.5    Kato, R.6
  • 15
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation
    • 10.1038/ncb1821 19136968 1:CAS:528:DC%2BD1MXht1Oqt7k%3D
    • Tokunaga F, Sakata S, Saeki Y, Satomi Y, Kirisako T, Kamei K, et al. Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation. Nat Cell Biol. 2009;11(2):123-32. doi: 10.1038/ncb1821.
    • (2009) Nat Cell Biol , vol.11 , Issue.2 , pp. 123-132
    • Tokunaga, F.1    Sakata, S.2    Saeki, Y.3    Satomi, Y.4    Kirisako, T.5    Kamei, K.6
  • 16
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • 12887920 1:CAS:528:DC%2BD3sXlvFCgu7Y%3D
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell. 2003;114(2):181-90.
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 17
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis
    • 8947041 1:CAS:528:DyaK28XnsFKrtLg%3D
    • Ting AT, Pimentel-Muinos FX, Seed B. RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis. EMBO J. 1996;15(22):6189-96.
    • (1996) EMBO J , vol.15 , Issue.22 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muinos, F.X.2    Seed, B.3
  • 18
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-kappaB signal
    • 9529147 1:CAS:528:DyaK1cXitFGgsLk%3D
    • Kelliher MA, Grimm S, Ishida Y, Kuo F, Stanger BZ, Leder P. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity. 1998;8(3):297-303.
    • (1998) Immunity , vol.8 , Issue.3 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3    Kuo, F.4    Stanger, B.Z.5    Leder, P.6
  • 19
    • 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
    • 10.1074/jbc.M404206200 15175328 1:CAS:528:DC%2BD2cXmtFOisb4%3D
    • Lee TH, Shank J, Cusson N, Kelliher MA. The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J Biol Chem. 2004;279(32):33185-91. doi: 10.1074/jbc.M404206200.
    • (2004) J Biol Chem , vol.279 , Issue.32 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3    Kelliher, M.A.4
  • 20
    • 0031463025 scopus 로고    scopus 로고
    • Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice
    • 9390694 1:CAS:528:DyaK2sXnvVWnu7s%3D
    • Yeh WC, Shahinian A, Speiser D, Kraunus J, Billia F, Wakeham A, et al. Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity. 1997;7(5):715-25.
    • (1997) Immunity , vol.7 , Issue.5 , pp. 715-725
    • Yeh, W.C.1    Shahinian, A.2    Speiser, D.3    Kraunus, J.4    Billia, F.5    Wakeham, A.6
  • 21
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • 10.1038/nature02794 15258597 1:CAS:528:DC%2BD2cXmt1Gisb8%3D
    • Wertz IE, O'Rourke KM, Zhou H, Eby M, Aravind L, Seshagiri S, et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature. 2004;430(7000):694-9. doi: 10.1038/nature02794.
    • (2004) Nature , vol.430 , Issue.7000 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3    Eby, M.4    Aravind, L.5    Seshagiri, S.6
  • 22
    • 0036337748 scopus 로고    scopus 로고
    • A20 inhibits tumor necrosis factor (TNF) alpha-induced apoptosis by disrupting recruitment of TRADD and RIP to the TNF receptor 1 complex in Jurkat T cells
    • 12167698 1:CAS:528:DC%2BD38Xmt1entrw%3D
    • He KL, Ting AT. A20 inhibits tumor necrosis factor (TNF) alpha-induced apoptosis by disrupting recruitment of TRADD and RIP to the TNF receptor 1 complex in Jurkat T cells. Mol Cell Biol. 2002;22(17):6034-45.
    • (2002) Mol Cell Biol , vol.22 , Issue.17 , pp. 6034-6045
    • He, K.L.1    Ting, A.T.2
  • 23
    • 33744951304 scopus 로고    scopus 로고
    • Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation
    • 10.1074/jbc.M600620200 16543241 1:CAS:528:DC%2BD28Xkt1ymtLc%3D
    • Li H, Kobayashi M, Blonska M, You Y, Lin X. Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation. J Biol Chem. 2006;281(19):13636-43. doi: 10.1074/jbc.M600620200.
    • (2006) J Biol Chem , vol.281 , Issue.19 , pp. 13636-13643
    • Li, H.1    Kobayashi, M.2    Blonska, M.3    You, Y.4    Lin, X.5
  • 24
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • 10.1016/j.molcel.2006.03.026 16603398 1:CAS:528:DC%2BD28Xkt1Gmtb8%3D
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell. 2006;22(2):245-57. doi: 10.1016/j.molcel.2006.03.026.
    • (2006) Mol Cell , vol.22 , Issue.2 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 25
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • 10.1038/ncb1384 16547522 1:CAS:528:DC%2BD28Xjt12qs7o%3D
    • Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat Cell Biol. 2006;8(4):398-406. doi: 10.1038/ncb1384.
    • (2006) Nat Cell Biol , vol.8 , Issue.4 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 26
    • 4344712350 scopus 로고    scopus 로고
    • TAB 2 and TAB 3 activate the NF-kappaB pathway through binding to polyubiquitin chains
    • 10.1016/j.molcel.2004.08.008 15327770 1:CAS:528:DC%2BD2cXns1ynurY%3D
    • Kanayama A, Seth RB, Sun L, Ea CK, Hong M, Shaito A, et al. TAB 2 and TAB 3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Mol Cell. 2004;15(4):535-48. doi: 10.1016/j.molcel.2004.08.008.
    • (2004) Mol Cell , vol.15 , Issue.4 , pp. 535-548
    • Kanayama, A.1    Seth, R.B.2    Sun, L.3    Ea, C.K.4    Hong, M.5    Shaito, A.6
  • 27
    • 49549117842 scopus 로고    scopus 로고
    • Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies
    • 10.1016/j.cell.2008.07.039 18724939 1:CAS:528:DC%2BD1cXhtVGqtrbK
    • Newton K, Matsumoto ML, Wertz IE, Kirkpatrick DS, Lill JR, Tan J, et al. Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies. Cell. 2008;134(4):668-78. doi: 10.1016/j.cell.2008.07.039.
    • (2008) Cell , vol.134 , Issue.4 , pp. 668-678
    • Newton, K.1    Matsumoto, M.L.2    Wertz, I.E.3    Kirkpatrick, D.S.4    Lill, J.R.5    Tan, J.6
  • 28
    • 40749139505 scopus 로고    scopus 로고
    • Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase
    • 10.1128/MCB.02380-06 18180283 1:CAS:528:DC%2BD1cXivVajtb8%3D
    • Windheim M, Stafford M, Peggie M, Cohen P. Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase. Mol Cell Biol. 2008;28(5):1783-91. doi: 10.1128/MCB.02380-06.
    • (2008) Mol Cell Biol , vol.28 , Issue.5 , pp. 1783-1791
    • Windheim, M.1    Stafford, M.2    Peggie, M.3    Cohen, P.4
  • 29
    • 36249008032 scopus 로고    scopus 로고
    • Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation
    • 10.1038/sj.emboj.7601897 17948050 1:CAS:528:DC%2BD2sXht12gtbbK
    • Oeckinghaus A, Wegener E, Welteke V, Ferch U, Arslan SC, Ruland J, et al. Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation. EMBO J. 2007;26(22):4634-45. doi: 10.1038/sj.emboj.7601897.
    • (2007) EMBO J , vol.26 , Issue.22 , pp. 4634-4645
    • Oeckinghaus, A.1    Wegener, E.2    Welteke, V.3    Ferch, U.4    Arslan, S.C.5    Ruland, J.6
  • 30
    • 42949098959 scopus 로고    scopus 로고
    • NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation
    • 10.1073/pnas.0712313105 18287044 1:CAS:528:DC%2BD1cXjtVSitrw%3D
    • Wu CJ, Ashwell JD. NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation. Proc Natl Acad Sci USA. 2008;105(8):3023-8. doi: 10.1073/pnas.0712313105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.8 , pp. 3023-3028
    • Wu, C.J.1    Ashwell, J.D.2
  • 31
    • 0041967294 scopus 로고    scopus 로고
    • Essential role for IKKgamma/NEMO in TCR-induced IL-2 expression in Jurkat T cells
    • 10.1002/eji.200323650 12884855 1:CAS:528:DC%2BD3sXlslWlsb8%3D
    • He KL, Ting AT. Essential role for IKKgamma/NEMO in TCR-induced IL-2 expression in Jurkat T cells. Eur J Immunol. 2003;33(7):1917-24. doi: 10.1002/eji.200323650.
    • (2003) Eur J Immunol , vol.33 , Issue.7 , pp. 1917-1924
    • He, K.L.1    Ting, A.T.2
  • 32
    • 77949332322 scopus 로고    scopus 로고
    • The RING domain of TRAF2 plays an essential role in the inhibition of TNFalpha-induced cell death but not in the activation of NF-kappaB
    • 10.1016/j.jmb.2010.01.008 20064526 1:CAS:528:DC%2BC3cXhs1ymu7Y%3D
    • Zhang L, Blackwell K, Shi Z, Habelhah H. The RING domain of TRAF2 plays an essential role in the inhibition of TNFalpha-induced cell death but not in the activation of NF-kappaB. J Mol Biol. 2010;396(3):528-39. doi: 10.1016/j.jmb.2010.01.008.
    • (2010) J Mol Biol , vol.396 , Issue.3 , pp. 528-539
    • Zhang, L.1    Blackwell, K.2    Shi, Z.3    Habelhah, H.4
  • 33
    • 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
    • 10.1016/j.molcel.2009.10.013 20005846 1:CAS:528:DC%2BC3cXht1Cjsr4%3D
    • Haas TL, Emmerich CH, Gerlach B, Schmukle AC, Cordier SM, 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. 2009;36(5):831-44. doi: 10.1016/j.molcel.2009.10.013.
    • (2009) Mol Cell , vol.36 , Issue.5 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6
  • 34
    • 44949240664 scopus 로고    scopus 로고
    • CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • 10.1016/j.molcel.2008.05.014 18570872 1:CAS:528:DC%2BD1cXnvFWnt74%3D
    • Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell. 2008;30(6):689-700. doi: 10.1016/j.molcel.2008.05.014.
    • (2008) Mol Cell , vol.30 , Issue.6 , pp. 689-700
    • Bertrand, M.J.1    Milutinovic, S.2    Dickson, K.M.3    Ho, W.C.4    Boudreault, A.5    Durkin, J.6
  • 35
    • 2442559290 scopus 로고    scopus 로고
    • Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro
    • 10.1016/j.febslet.2004.04.021 15147886 1:CAS:528:DC%2BD2cXktVOksrw%3D
    • Park SM, Yoon JB, Lee TH. Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro. FEBS Lett. 2004;566(1-3):151-6. doi: 10.1016/j.febslet.2004.04.021.
    • (2004) FEBS Lett , vol.566 , Issue.1-3 , pp. 151-156
    • Park, S.M.1    Yoon, J.B.2    Lee, T.H.3
  • 36
    • 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
    • 10.1074/jbc.M109.072256 19815541 1:CAS:528:DC%2BD1MXhsFCqu7%2FI
    • Vince JE, Pantaki D, Feltham R, Mace PD, Cordier SM, Schmukle AC, 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. 2009;284(51):35906-15. doi: 10.1074/jbc.M109.072256.
    • (2009) J Biol Chem , vol.284 , Issue.51 , 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
  • 37
    • 77953923379 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2
    • 10.1038/nature09128 20577214 1:CAS:528:DC%2BC3cXnvFSgs7s%3D
    • Alvarez SE, Harikumar KB, Hait NC, Allegood J, Strub GM, Kim EY, et al. Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2. Nature. 2010;465(7301):1084-8. doi: 10.1038/nature09128.
    • (2010) Nature , vol.465 , Issue.7301 , pp. 1084-1088
    • Alvarez, S.E.1    Harikumar, K.B.2    Hait, N.C.3    Allegood, J.4    Strub, G.M.5    Kim, E.Y.6
  • 38
    • 29444453188 scopus 로고    scopus 로고
    • The anti-death machinery in IKK/NF-kappaB signaling
    • 10.1007/s10875-005-8217-6 16380818 1:CAS:528:DC%2BD2MXhtlGhsb%2FL
    • Luo JL, Kamata H, Karin M. The anti-death machinery in IKK/NF-kappaB signaling. J Clin Immunol. 2005;25(6):541-50. doi: 10.1007/s10875-005-8217-6.
    • (2005) J Clin Immunol , vol.25 , Issue.6 , pp. 541-550
    • Luo, J.L.1    Kamata, H.2    Karin, M.3
  • 39
    • 0034743199 scopus 로고    scopus 로고
    • NF-kappaB signals induce the expression of c-FLIP
    • 10.1128/MCB.21.16.5299-5305.2001 11463813 1:CAS:528:DC%2BD3MXlslOjt7o%3D
    • Micheau O, Lens S, Gaide O, Alevizopoulos K, Tschopp J. NF-kappaB signals induce the expression of c-FLIP. Mol Cell Biol. 2001;21(16):5299-305. doi: 10.1128/MCB.21.16.5299-5305.2001.
    • (2001) Mol Cell Biol , vol.21 , Issue.16 , pp. 5299-5305
    • Micheau, O.1    Lens, S.2    Gaide, O.3    Alevizopoulos, K.4    Tschopp, J.5
  • 40
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • 7538908 1:CAS:528:DyaK2MXlvVGgtbc%3D
    • Stanger BZ, Leder P, Lee TH, Kim E, Seed B. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell. 1995;81(4):513-23.
    • (1995) Cell , vol.81 , Issue.4 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 41
    • 0036645407 scopus 로고    scopus 로고
    • The death domain kinase RIP protects thymocytes from tumor necrosis factor receptor type 2-induced cell death
    • 12093867 1:CAS:528:DC%2BD38Xlt1WhtL0%3D
    • Cusson N, Oikemus S, Kilpatrick ED, Cunningham L, Kelliher M. The death domain kinase RIP protects thymocytes from tumor necrosis factor receptor type 2-induced cell death. J Exp Med. 2002;196(1):15-26.
    • (2002) J Exp Med , vol.196 , Issue.1 , pp. 15-26
    • Cusson, N.1    Oikemus, S.2    Kilpatrick, E.D.3    Cunningham, L.4    Kelliher, M.5
  • 42
    • 0033965946 scopus 로고    scopus 로고
    • A crucial role for p80 TNF-R2 in amplifying p60 TNF-R1 apoptosis signals in T lymphocytes
    • 10.1002/1521-4141(200002)30:2<652: AID-IMMU652>3.0.CO;2-L 10671223 1:CAS:528:DC%2BD3cXhtF2qtrY%3D
    • Chan FK, Lenardo MJ. A crucial role for p80 TNF-R2 in amplifying p60 TNF-R1 apoptosis signals in T lymphocytes. Eur J Immunol. 2000;30(2):652-60. doi: 10.1002/1521-4141(200002)30:2<652::AID-IMMU652>3.0.CO;2-L.
    • (2000) Eur J Immunol , vol.30 , Issue.2 , pp. 652-660
    • Chan, F.K.1    Lenardo, M.J.2
  • 43
    • 0033452005 scopus 로고    scopus 로고
    • Regulated commitment of TNF receptor signaling: A molecular switch for death or activation
    • 10626900 1:CAS:528:DC%2BD3cXkt1Shtw%3D%3D
    • Pimentel-Muinos FX, Seed B. Regulated commitment of TNF receptor signaling: a molecular switch for death or activation. Immunity. 1999;11(6):783-93.
    • (1999) Immunity , vol.11 , Issue.6 , pp. 783-793
    • Pimentel-Muinos, F.X.1    Seed, B.2
  • 44
    • 0032553419 scopus 로고    scopus 로고
    • Nuclear factor kB-independent cytoprotective pathways originating at tumor necrosis factor receptor-associated factor 2
    • 9813034 1:CAS:528:DyaK1cXns1egu7g%3D
    • Natoli G, Costanzo A, Guido F, Moretti F, Bernardo A, Burgio VL, et al. Nuclear factor kB-independent cytoprotective pathways originating at tumor necrosis factor receptor-associated factor 2. J Biol Chem. 1998;273(47):31262- 72.
    • (1998) J Biol Chem , vol.273 , Issue.47 , pp. 31262-31272
    • Natoli, G.1    Costanzo, A.2    Guido, F.3    Moretti, F.4    Bernardo, A.5    Burgio, V.L.6
  • 45
    • 0005231498 scopus 로고    scopus 로고
    • Stimulus-dependent synergism of the antiapoptotic tumor necrosis factor receptor-associated factor 2 (TRAF2) and nuclear factor kappaB pathways
    • 9763618 1:CAS:528:DyaK1cXmsFals7o%3D
    • Lee SY, Kaufman DR, Mora AL, Santana A, Boothby M, Choi Y. Stimulus-dependent synergism of the antiapoptotic tumor necrosis factor receptor-associated factor 2 (TRAF2) and nuclear factor kappaB pathways. J Exp Med. 1998;188(7):1381-4.
    • (1998) J Exp Med , vol.188 , Issue.7 , pp. 1381-1384
    • Lee, S.Y.1    Kaufman, D.R.2    Mora, A.L.3    Santana, A.4    Boothby, M.5    Choi, Y.6
  • 46
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • 9733516 1:CAS:528:DyaK1cXmtVWhurk%3D
    • Wang CY, Mayo MW, Korneluk RG, Goeddel DV, Baldwin AS Jr. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science. 1998;281(5383):1680-3.
    • (1998) Science , vol.281 , Issue.5383 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin Jr., A.S.5
  • 47
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • 10894163 1:CAS:528:DC%2BD3cXkslagtbo%3D
    • Yeh WC, Itie A, Elia AJ, Ng M, Shu HB, Wakeham A, et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity. 2000;12(6):633-42.
    • (2000) Immunity , vol.12 , Issue.6 , pp. 633-642
    • Yeh, W.C.1    Itie, A.2    Elia, A.J.3    Ng, M.4    Shu, H.B.5    Wakeham, A.6
  • 48
    • 0026699666 scopus 로고
    • Transcriptional activation of the tumor necrosis factor alpha-inducible zinc finger protein, A20, is mediated by kappa B elements
    • 1381359 1:CAS:528:DyaK38XkvVCmurw%3D
    • Krikos A, Laherty CD, Dixit VM. Transcriptional activation of the tumor necrosis factor alpha-inducible zinc finger protein, A20, is mediated by kappa B elements. J Biol Chem. 1992;267(25):17971-6.
    • (1992) J Biol Chem , vol.267 , Issue.25 , pp. 17971-17976
    • Krikos, A.1    Laherty, C.D.2    Dixit, V.M.3
  • 49
    • 0034730713 scopus 로고    scopus 로고
    • Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice
    • 11009421 1:CAS:528:DC%2BD3cXmvF2qtbY%3D
    • Lee EG, Boone DL, Chai S, Libby SL, Chien M, Lodolce JP, et al. Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. Science. 2000;289(5488):2350-4.
    • (2000) Science , vol.289 , Issue.5488 , pp. 2350-2354
    • Lee, E.G.1    Boone, D.L.2    Chai, S.3    Libby, S.L.4    Chien, M.5    Lodolce, J.P.6
  • 50
    • 0027282044 scopus 로고
    • Bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
    • 8358789 1:CAS:528:DyaK3sXmsVans7g%3D
    • Boise LH, Gonzalez-Garcia M, Postema CE, Ding L, Lindsten T, Turka LA, et al. bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell. 1993;74(4):597-608.
    • (1993) Cell , vol.74 , Issue.4 , pp. 597-608
    • Boise, L.H.1    Gonzalez-Garcia, M.2    Postema, C.E.3    Ding, L.4    Lindsten, T.5    Turka, L.A.6
  • 51
    • 0033621956 scopus 로고    scopus 로고
    • The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L)
    • 10733571
    • Chen C, Edelstein LC, Gelinas C. The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L). Mol Cell Biol. 2000;20(8):2687-95.
    • (2000) Mol Cell Biol , vol.20 , Issue.8 , pp. 2687-2695
    • Chen, C.1    Edelstein, L.C.2    Gelinas, C.3
  • 52
    • 0028922885 scopus 로고
    • Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice
    • 7878471 1:CAS:528:DyaK2MXktlCltLk%3D
    • Motoyama N, Wang F, Roth KA, Sawa H, Nakayama K, Negishi I, et al. Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice. Science. 1995;267(5203):1506-10.
    • (1995) Science , vol.267 , Issue.5203 , pp. 1506-1510
    • Motoyama, N.1    Wang, F.2    Roth, K.A.3    Sawa, H.4    Nakayama, K.5    Negishi, I.6
  • 53
    • 0031693206 scopus 로고    scopus 로고
    • Apoptotic, non-apoptotic, and anti-apoptotic pathways of tumor necrosis factor signalling
    • 9776301 1:CAS:528:DyaK1cXmsVyrurc%3D
    • Natoli G, Costanzo A, Guido F, Moretti F, Levrero M. Apoptotic, non-apoptotic, and anti-apoptotic pathways of tumor necrosis factor signalling. Biochem Pharmacol. 1998;56(8):915-20.
    • (1998) Biochem Pharmacol , vol.56 , Issue.8 , pp. 915-920
    • Natoli, G.1    Costanzo, A.2    Guido, F.3    Moretti, F.4    Levrero, M.5
  • 54
    • 0037149542 scopus 로고    scopus 로고
    • TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2
    • 10.1038/416345a 11907583
    • Li X, Yang Y, Ashwell JD. TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. Nature. 2002;416(6878):345-7. doi: 10.1038/416345a.
    • (2002) Nature , vol.416 , Issue.6878 , pp. 345-347
    • Li, X.1    Yang, Y.2    Ashwell, J.D.3
  • 55
    • 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
    • 12077366 1:CAS:528:DC%2BD38XlsFCrtLc%3D
    • 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. 2002;115(Pt 13):2757-70.
    • (2002) J Cell Sci , vol.115 , Issue.PART 13 , pp. 2757-2770
    • Fotin-Mleczek, M.1    Henkler, F.2    Samel, D.3    Reichwein, M.4    Hausser, A.5    Parmryd, I.6
  • 56
    • 33847251527 scopus 로고    scopus 로고
    • Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling
    • 10.1016/j.cub.2007.01.027 17306544
    • O'Donnell MA, Legarda D, Skountzos P, Yeh WC, Ting AT. Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling. Curr Biol. 2007;17(5):418-24. doi: 10.1016/j.cub.2007.01.027.
    • (2007) Curr Biol , vol.17 , Issue.5 , pp. 418-424
    • O'Donnell, M.A.1    Legarda, D.2    Skountzos, P.3    Yeh, W.C.4    Ting, A.T.5
  • 57
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • 10.1016/j.cell.2008.03.036 18485876 1:CAS:528:DC%2BD1cXmsVOru78%3D
    • Wang L, Du F, Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell. 2008;133(4):693-703. doi: 10.1016/j.cell.2008.03.036.
    • (2008) Cell , vol.133 , Issue.4 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 58
    • 69049092633 scopus 로고    scopus 로고
    • NEMO/IKKgamma regulates an early NF-kappaB-independent cell-death checkpoint during TNF signaling
    • 10.1038/cdd.2009.41 19373245 1:CAS:528:DC%2BD1MXhtVamur%2FP
    • Legarda-Addison D, Hase H, O'Donnell MA, Ting AT. NEMO/IKKgamma regulates an early NF-kappaB-independent cell-death checkpoint during TNF signaling. Cell Death Differ. 2009;16(9):1279-88. doi: 10.1038/cdd.2009.41.
    • (2009) Cell Death Differ , vol.16 , Issue.9 , pp. 1279-1288
    • Legarda-Addison, D.1    Hase, H.2    O'Donnell, M.A.3    Ting, A.T.4
  • 59
    • 56249132503 scopus 로고    scopus 로고
    • Antigen-mediated T cell expansion regulated by parallel pathways of death
    • 10.1073/pnas.0808043105 18981423
    • Ch'en IL, Beisner DR, Degterev A, Lynch C, Yuan J, Hoffmann A, et al. Antigen-mediated T cell expansion regulated by parallel pathways of death. Proc Natl Acad Sci USA. 2008;105(45):17463-8. doi: 10.1073/pnas.0808043105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.45 , pp. 17463-17468
    • Ch'En, I.L.1    Beisner, D.R.2    Degterev, A.3    Lynch, C.4    Yuan, J.5    Hoffmann, A.6
  • 61
    • 80053087284 scopus 로고    scopus 로고
    • Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity
    • 10.1073/pnas.1102779108 21876153 1:CAS:528:DC%2BC3MXht1Gqt7zJ
    • Lu JV, Weist BM, van Raam BJ, Marro BS, Nguyen LV, Srinivas P, et al. Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity. Proc Natl Acad Sci USA. 2011;108(37):15312-7. doi: 10.1073/pnas.1102779108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.37 , pp. 15312-15317
    • Lu, J.V.1    Weist, B.M.2    Van Raam, B.J.3    Marro, B.S.4    Nguyen, L.V.5    Srinivas, P.6
  • 63
    • 3543097542 scopus 로고    scopus 로고
    • RIP links TLR4 to Akt and is essential for cell survival in response to LPS stimulation
    • 10.1084/jem.20040446 15280422 1:CAS:528:DC%2BD2cXmsVCkurk%3D
    • Vivarelli MS, McDonald D, Miller M, Cusson N, Kelliher M, Geha RS. RIP links TLR4 to Akt and is essential for cell survival in response to LPS stimulation. J Exp Med. 2004;200(3):399-404. doi: 10.1084/jem.20040446.
    • (2004) J Exp Med , vol.200 , Issue.3 , pp. 399-404
    • Vivarelli, M.S.1    McDonald, D.2    Miller, M.3    Cusson, N.4    Kelliher, M.5    Geha, R.S.6
  • 64
    • 29644433629 scopus 로고    scopus 로고
    • NF-kappaB protects macrophages from lipopolysaccharide-induced cell death: The role of caspase 8 and receptor-interacting protein
    • 10.1074/jbc.M510849200 16246838 1:CAS:528:DC%2BD2MXhtlajsrjM
    • Ma Y, Temkin V, Liu H, Pope RM. NF-kappaB protects macrophages from lipopolysaccharide-induced cell death: the role of caspase 8 and receptor-interacting protein. J Biol Chem. 2005;280(51):41827-34. doi: 10.1074/jbc.M510849200.
    • (2005) J Biol Chem , vol.280 , Issue.51 , pp. 41827-41834
    • Ma, Y.1    Temkin, V.2    Liu, H.3    Pope, R.M.4
  • 65
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • 10.1038/82732 11101870 1:CAS:528:DC%2BD3cXoslyru74%3D
    • Holler N, Zaru R, Micheau O, Thome M, Attinger A, Valitutti S, et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol. 2000;1(6):489-95. doi: 10.1038/82732.
    • (2000) Nat Immunol , vol.1 , Issue.6 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3    Thome, M.4    Attinger, A.5    Valitutti, S.6
  • 66
    • 0347065342 scopus 로고    scopus 로고
    • A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses
    • 10.1074/jbc.M305633200 14532286 1:CAS:528:DC%2BD3sXpslOgsrY%3D
    • Chan FK, Shisler J, Bixby JG, Felices M, Zheng L, Appel M, et al. A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses. J Biol Chem. 2003;278(51):51613-21. doi: 10.1074/jbc.M305633200.
    • (2003) J Biol Chem , vol.278 , Issue.51 , pp. 51613-51621
    • Chan, F.K.1    Shisler, J.2    Bixby, J.G.3    Felices, M.4    Zheng, L.5    Appel, M.6
  • 67
    • 77950366886 scopus 로고    scopus 로고
    • Decoding cell death signals in inflammation and immunity
    • 10.1016/j.cell.2010.02.015 20303871 1:CAS:528:DC%2BC3cXlsVSgurc%3D
    • Zitvogel L, Kepp O, Kroemer G. Decoding cell death signals in inflammation and immunity. Cell. 2010;140(6):798-804. doi: 10.1016/j.cell.2010. 02.015.
    • (2010) Cell , vol.140 , Issue.6 , pp. 798-804
    • Zitvogel, L.1    Kepp, O.2    Kroemer, G.3
  • 68
    • 67349124914 scopus 로고    scopus 로고
    • Immunogenic and tolerogenic cell death
    • 10.1038/nri2545 19365408 1:CAS:528:DC%2BD1MXksVyit7Y%3D
    • Green DR, Ferguson T, Zitvogel L, Kroemer G. Immunogenic and tolerogenic cell death. Nat Rev Immunol. 2009;9(5):353-63. doi: 10.1038/nri2545.
    • (2009) Nat Rev Immunol , vol.9 , Issue.5 , pp. 353-363
    • Green, D.R.1    Ferguson, T.2    Zitvogel, L.3    Kroemer, G.4
  • 69
    • 0033861807 scopus 로고    scopus 로고
    • Induction of necrotic-like cell death by tumor necrosis factor alpha and caspase inhibitors: Novel mechanism for killing virus-infected cells
    • 10906200 1:CAS:528:DC%2BD3cXlt1Grs7Y%3D
    • Li M, Beg AA. Induction of necrotic-like cell death by tumor necrosis factor alpha and caspase inhibitors: novel mechanism for killing virus-infected cells. J Virol. 2000;74(16):7470-7.
    • (2000) J Virol , vol.74 , Issue.16 , pp. 7470-7477
    • Li, M.1    Beg, A.A.2
  • 70
    • 33646234026 scopus 로고    scopus 로고
    • Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1
    • 10.1128/MCB.26.9.3505-3513.2006 16611992 1:CAS:528:DC%2BD28XksVKksLo%3D
    • Zheng L, Bidere N, Staudt D, Cubre A, Orenstein J, Chan FK, et al. Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1. Mol Cell Biol. 2006;26(9):3505-13. doi: 10.1128/MCB.26.9.3505-3513.2006.
    • (2006) Mol Cell Biol , vol.26 , Issue.9 , pp. 3505-3513
    • Zheng, L.1    Bidere, N.2    Staudt, D.3    Cubre, A.4    Orenstein, J.5    Chan, F.K.6
  • 71
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • 9565639 1:CAS:528:DyaK1cXivVGjur8%3D
    • Vercammen D, Beyaert R, Denecker G, Goossens V, Van Loo G, Declercq W, et al. Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J Exp Med. 1998;187(9):1477-85.
    • (1998) J Exp Med , vol.187 , Issue.9 , pp. 1477-1485
    • Vercammen, D.1    Beyaert, R.2    Denecker, G.3    Goossens, V.4    Van Loo, G.5    Declercq, W.6
  • 72
    • 0031052956 scopus 로고    scopus 로고
    • Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1beta-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1beta-induced fever
    • 9049422 1:CAS:528:DyaK2sXhsVaisr4%3D
    • Kettle S, Alcami A, Khanna A, Ehret R, Jassoy C, Smith GL. Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1beta-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1beta-induced fever. J Gen Virol. 1997;78(Pt 3):677-85.
    • (1997) J Gen Virol , vol.78 , Issue.PART 3 , pp. 677-685
    • Kettle, S.1    Alcami, A.2    Khanna, A.3    Ehret, R.4    Jassoy, C.5    Smith, G.L.6
  • 73
    • 0029813306 scopus 로고    scopus 로고
    • Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product
    • 8709286 1:CAS:528:DyaK28XkvFGgu74%3D
    • Dobbelstein M, Shenk T. Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product. J Virol. 1996;70(9):6479-85.
    • (1996) J Virol , vol.70 , Issue.9 , pp. 6479-6485
    • Dobbelstein, M.1    Shenk, T.2
  • 74
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • 10.1038/nature10558 22002608 1:CAS:528:DC%2BC3MXhtlWksr7E
    • Kayagaki N, Warming S, Lamkanfi M, Vande Walle L, Louie S, Dong J, et al. Non-canonical inflammasome activation targets caspase-11. Nature. 2011;479(7371):117-21. doi: 10.1038/nature10558.
    • (2011) Nature , vol.479 , Issue.7371 , pp. 117-121
    • Kayagaki, N.1    Warming, S.2    Lamkanfi, M.3    Vande Walle, L.4    Louie, S.5    Dong, J.6
  • 75
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme
    • 1339309 1:CAS:528:DyaK38Xks1yiu7Y%3D
    • Ray CA, Black RA, Kronheim SR, Greenstreet TA, Sleath PR, Salvesen GS, et al. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell. 1992;69(4):597-604.
    • (1992) Cell , vol.69 , Issue.4 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvesen, G.S.6
  • 76
    • 67249158956 scopus 로고    scopus 로고
    • Identification of a dendritic cell receptor that couples sensing of necrosis to immunity
    • 10.1038/nature07750 19219027 1:CAS:528:DC%2BD1MXhvFKjtLs%3D
    • Sancho D, Joffre OP, Keller AM, Rogers NC, Martinez D, Hernanz-Falcon P, et al. Identification of a dendritic cell receptor that couples sensing of necrosis to immunity. Nature. 2009;458(7240):899-903. doi: 10.1038/nature07750.
    • (2009) Nature , vol.458 , Issue.7240 , pp. 899-903
    • Sancho, D.1    Joffre, O.P.2    Keller, A.M.3    Rogers, N.C.4    Martinez, D.5    Hernanz-Falcon, P.6
  • 77
    • 52549125928 scopus 로고    scopus 로고
    • Mincle is an ITAM-coupled activating receptor that senses damaged cells
    • 10.1038/ni.1651 18776906 1:CAS:528:DC%2BD1cXhtFeit7jP
    • Yamasaki S, Ishikawa E, Sakuma M, Hara H, Ogata K, Saito T. Mincle is an ITAM-coupled activating receptor that senses damaged cells. Nat Immunol. 2008;9(10):1179-88. doi: 10.1038/ni.1651.
    • (2008) Nat Immunol , vol.9 , Issue.10 , pp. 1179-1188
    • Yamasaki, S.1    Ishikawa, E.2    Sakuma, M.3    Hara, H.4    Ogata, K.5    Saito, T.6
  • 78
    • 54049145131 scopus 로고    scopus 로고
    • The dendritic cell subtype-restricted C-type lectin Clec9A is a target for vaccine enhancement
    • 10.1182/blood-2008-05-155176 18669894 1:CAS:528:DC%2BD1cXht1OmurzP
    • Caminschi I, Proietto AI, Ahmet F, Kitsoulis S, Shin Teh J, Lo JC, et al. The dendritic cell subtype-restricted C-type lectin Clec9A is a target for vaccine enhancement. Blood. 2008;112(8):3264-73. doi: 10.1182/blood-2008-05- 155176.
    • (2008) Blood , vol.112 , Issue.8 , pp. 3264-3273
    • Caminschi, I.1    Proietto, A.I.2    Ahmet, F.3    Kitsoulis, S.4    Shin Teh, J.5    Lo, J.C.6
  • 79
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • 10.1016/j.cell.2009.05.021 19524512 1:CAS:528:DC%2BD1MXps1eiu70%3D
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L, et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell. 2009;137(6):1100-11. doi: 10.1016/j.cell.2009.05.021.
    • (2009) Cell , vol.137 , Issue.6 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6
  • 80
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • 10.1126/science.1172308 19498109 1:CAS:528:DC%2BD1MXos1Sqt7Y%3D
    • Zhang DW, Shao J, Lin J, Zhang N, Lu BJ, Lin SC, et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science. 2009;325(5938):332-6. doi: 10.1126/science.1172308.
    • (2009) Science , vol.325 , Issue.5938 , pp. 332-336
    • Zhang, D.W.1    Shao, J.2    Lin, J.3    Zhang, N.4    Lu, B.J.5    Lin, S.C.6
  • 81
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • 10.1016/j.cell.2009.05.037 19524513 1:CAS:528:DC%2BD1MXps1eiu7o%3D
    • Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M, et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell. 2009;137(6):1112-23. doi: 10.1016/j.cell.2009.05.037.
    • (2009) Cell , vol.137 , Issue.6 , pp. 1112-1123
    • Cho, Y.S.1    Challa, S.2    Moquin, D.3    Genga, R.4    Ray, T.D.5    Guildford, M.6
  • 82
    • 67650638892 scopus 로고    scopus 로고
    • RIP kinases at the crossroads of cell death and survival
    • 10.1016/j.cell.2009.07.006 19632174 1:CAS:528:DC%2BD1MXhtVSgtrzK
    • Declercq W, Vanden Berghe T, Vandenabeele P. RIP kinases at the crossroads of cell death and survival. Cell. 2009;138(2):229-32. doi: 10.1016/j.cell.2009.07.006.
    • (2009) Cell , vol.138 , Issue.2 , pp. 229-232
    • Declercq, W.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 83
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis
    • 10.1038/nature09852 21368763 1:CAS:528:DC%2BC3MXis1Crsrs%3D
    • Oberst A, Dillon CP, Weinlich R, McCormick LL, Fitzgerald P, Pop C, et al. Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature. 2011;471(7338):363-7. doi: 10.1038/nature09852.
    • (2011) Nature , vol.471 , Issue.7338 , pp. 363-367
    • Oberst, A.1    Dillon, C.P.2    Weinlich, R.3    McCormick, L.L.4    Fitzgerald, P.5    Pop, C.6
  • 84
    • 79952780505 scopus 로고    scopus 로고
    • Functional complementation between FADD and RIP1 in embryos and lymphocytes
    • 10.1038/nature09878 21368761 1:CAS:528:DC%2BC3MXis1Crsrg%3D
    • Zhang H, Zhou X, McQuade T, Li J, Chan FK, Zhang J. Functional complementation between FADD and RIP1 in embryos and lymphocytes. Nature. 2011;471(7338):373-6. doi: 10.1038/nature09878.
    • (2011) Nature , vol.471 , Issue.7338 , pp. 373-376
    • Zhang, H.1    Zhou, X.2    McQuade, T.3    Li, J.4    Chan, F.K.5    Zhang, J.6
  • 85
    • 80052845560 scopus 로고    scopus 로고
    • Caspase-8 regulates TNF-alpha-induced epithelial necroptosis and terminal ileitis
    • 10.1038/nature10400 21921917
    • Gunther C, Martini E, Wittkopf N, Amann K, Weigmann B, Neumann H, et al. Caspase-8 regulates TNF-alpha-induced epithelial necroptosis and terminal ileitis. Nature. 2011;477(7364):335-9. doi: 10.1038/nature10400.
    • (2011) Nature , vol.477 , Issue.7364 , pp. 335-339
    • Gunther, C.1    Martini, E.2    Wittkopf, N.3    Amann, K.4    Weigmann, B.5    Neumann, H.6
  • 86
    • 80052850704 scopus 로고    scopus 로고
    • FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation
    • 10.1038/nature10273 21804564 1:CAS:528:DC%2BC3MXhtFersLrF
    • Welz PS, Wullaert A, Vlantis K, Kondylis V, Fernandez-Majada V, Ermolaeva M, et al. FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation. Nature. 2011;477(7364):330-4. doi: 10.1038/nature10273.
    • (2011) Nature , vol.477 , Issue.7364 , pp. 330-334
    • Welz, P.S.1    Wullaert, A.2    Vlantis, K.3    Kondylis, V.4    Fernandez-Majada, V.5    Ermolaeva, M.6
  • 87
    • 80755132824 scopus 로고    scopus 로고
    • The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation
    • 10.1016/j.immuni.2011.08.014 22000287 1:CAS:528:DC%2BC3MXhtlyjs7zF
    • Bonnet MC, Preukschat D, Welz PS, van Loo G, Ermolaeva MA, Bloch W, et al. The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation. Immunity. 2011;35(4):572-82. doi: 10.1016/j.immuni.2011.08.014.
    • (2011) Immunity , vol.35 , Issue.4 , pp. 572-582
    • Bonnet, M.C.1    Preukschat, D.2    Welz, P.S.3    Van Loo, G.4    Ermolaeva, M.A.5    Bloch, W.6
  • 88
    • 57649181391 scopus 로고    scopus 로고
    • Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway
    • 10.1016/j.cell.2008.10.044 19109899 1:CAS:528:DC%2BD1MXisFyitg%3D%3D
    • Hitomi J, Christofferson DE, Ng A, Yao J, Degterev A, Xavier RJ, et al. Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell. 2008;135(7):1311-23. doi: 10.1016/j.cell.2008.10.044.
    • (2008) Cell , vol.135 , Issue.7 , pp. 1311-1323
    • Hitomi, J.1    Christofferson, D.E.2    Ng, A.3    Yao, J.4    Degterev, A.5    Xavier, R.J.6
  • 89
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • 10.1038/nri2337 18535581 1:CAS:528:DC%2BD1cXns1ehs7o%3D
    • Sun SC. Deubiquitylation and regulation of the immune response. Nat Rev Immunol. 2008;8(7):501-11. doi: 10.1038/nri2337.
    • (2008) Nat Rev Immunol , vol.8 , Issue.7 , pp. 501-511
    • Sun, S.C.1
  • 90
    • 77449150629 scopus 로고    scopus 로고
    • CYLD: A tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes
    • 10.1038/cdd.2009.43 1:CAS:528:DC%2BD1MXjslymsb0%3D
    • Sun SC. CYLD: a tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes. Cell Death Differ. 2009;17(1):25-34. doi: 10.1038/cdd.2009.43.
    • (2009) Cell Death Differ , vol.17 , Issue.1 , pp. 25-34
    • Sun, S.C.1
  • 91
    • 35548974703 scopus 로고    scopus 로고
    • Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD
    • 10.1016/j.devcel.2007.09.007 17981138 1:CAS:528:DC%2BD2sXhtlWitrfE
    • Wright A, Reiley WW, Chang M, Jin W, Lee AJ, Zhang M, et al. Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD. Dev Cell. 2007;13(5):705-16. doi: 10.1016/j.devcel.2007.09.007.
    • (2007) Dev Cell , vol.13 , Issue.5 , pp. 705-716
    • Wright, A.1    Reiley, W.W.2    Chang, M.3    Jin, W.4    Lee, A.J.5    Zhang, M.6
  • 92
    • 60649110012 scopus 로고    scopus 로고
    • TNFalpha-induced macrophage death via caspase-dependent and independent pathways
    • 10.1007/s10495-009-0311-4 19152111 1:CAS:528:DC%2BD1MXitVOrtb8%3D
    • Tran TM, Temkin V, Shi B, Pagliari L, Daniel S, Ferran C, et al. TNFalpha-induced macrophage death via caspase-dependent and independent pathways. Apoptosis. 2009;14(3):320-32. doi: 10.1007/s10495-009-0311-4.
    • (2009) Apoptosis , vol.14 , Issue.3 , pp. 320-332
    • Tran, T.M.1    Temkin, V.2    Shi, B.3    Pagliari, L.4    Daniel, S.5    Ferran, C.6
  • 93
    • 17144404884 scopus 로고    scopus 로고
    • Functional dichotomy of A20 in apoptotic and necrotic cell death
    • 10.1042/BJ20041443 15527421 1:CAS:528:DC%2BD2MXisFWgtr0%3D
    • Storz P, Doppler H, Ferran C, Grey ST, Toker A. Functional dichotomy of A20 in apoptotic and necrotic cell death. Biochem J. 2005;387(Pt 1):47-55. doi: 10.1042/BJ20041443.
    • (2005) Biochem J , vol.387 , Issue.PART 1 , pp. 47-55
    • Storz, P.1    Doppler, H.2    Ferran, C.3    Grey, S.T.4    Toker, A.5
  • 94
    • 5444223519 scopus 로고    scopus 로고
    • The ubiquitin-modifying enzyme A20 is required for termination of toll-like receptor responses
    • 10.1038/ni1110 15334086 1:CAS:528:DC%2BD2cXnvFCgsro%3D
    • Boone DL, Turer EE, Lee EG, Ahmad RC, Wheeler MT, Tsui C, et al. The ubiquitin-modifying enzyme A20 is required for termination of toll-like receptor responses. Nat Immunol. 2004;5(10):1052-60. doi: 10.1038/ni1110.
    • (2004) Nat Immunol , vol.5 , Issue.10 , pp. 1052-1060
    • Boone, D.L.1    Turer, E.E.2    Lee, E.G.3    Ahmad, R.C.4    Wheeler, M.T.5    Tsui, C.6
  • 96
    • 79955592698 scopus 로고    scopus 로고
    • T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1
    • 10.1038/emboj.2011.85 21448133 1:CAS:528:DC%2BC3MXjvFOnt78%3D
    • Staal J, Driege Y, Bekaert T, Demeyer A, Muyllaert D, Van Damme P, et al. T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1. EMBO J. 2011;30(9):1742-52. doi: 10.1038/emboj.2011.85.
    • (2011) EMBO J , vol.30 , Issue.9 , pp. 1742-1752
    • Staal, J.1    Driege, Y.2    Bekaert, T.3    Demeyer, A.4    Muyllaert, D.5    Van Damme, P.6
  • 97
    • 48349125069 scopus 로고    scopus 로고
    • The paracaspase MALT1 controls caspase-8 activation during lymphocyte proliferation
    • 10.1016/j.molcel.2008.06.008 18691973 1:CAS:528:DC%2BD1cXhtVSrsrnI
    • Kawadler H, Gantz MA, Riley JL, Yang X. The paracaspase MALT1 controls caspase-8 activation during lymphocyte proliferation. Mol Cell. 2008;31(3):415-21. doi: 10.1016/j.molcel.2008.06.008.
    • (2008) Mol Cell , vol.31 , Issue.3 , pp. 415-421
    • Kawadler, H.1    Gantz, M.A.2    Riley, J.L.3    Yang, X.4
  • 98
    • 77955109451 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response
    • 10.1038/ncb2006 20010814 1:CAS:528:DC%2BD1MXhsFynur3N
    • Ashida H, Kim M, Schmidt-Supprian M, Ma A, Ogawa M, Sasakawa C. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat Cell Biol. 2010;12(1):66-73. doi: 10.1038/ncb2006.
    • (2010) Nat Cell Biol , vol.12 , Issue.1 , pp. 66-73
    • Ashida, H.1    Kim, M.2    Schmidt-Supprian, M.3    Ma, A.4    Ogawa, M.5    Sasakawa, C.6
  • 99
    • 60649096938 scopus 로고    scopus 로고
    • Shigella targets the mitochondrial checkpoint of programmed necrosis
    • 10.1016/j.chom.2009.01.002 19218080 1:CAS:528:DC%2BD1MXivFehsr8%3D
    • Galluzzi L, Kroemer G. Shigella targets the mitochondrial checkpoint of programmed necrosis. Cell Host Microbe. 2009;5(2):107-9. doi: 10.1016/j.chom.2009.01.002.
    • (2009) Cell Host Microbe , vol.5 , Issue.2 , pp. 107-109
    • Galluzzi, L.1    Kroemer, G.2
  • 100
    • 84855764312 scopus 로고    scopus 로고
    • Cysteine methylation disrupts ubiquitin-chain sensing in NF-kappaB activation
    • 10.1038/nature10690 22158122
    • Zhang L, Ding X, Cui J, Xu H, Chen J, Gong YN, et al. Cysteine methylation disrupts ubiquitin-chain sensing in NF-kappaB activation. Nature. 2011;481(7380):204-8. doi: 10.1038/nature10690.
    • (2011) Nature , vol.481 , Issue.7380 , pp. 204-208
    • Zhang, L.1    Ding, X.2    Cui, J.3    Xu, H.4    Chen, J.5    Gong, Y.N.6
  • 101
    • 80053927315 scopus 로고    scopus 로고
    • The prevalence of TNFalpha-induced necrosis over apoptosis is determined by TAK1-RIP1 interplay
    • 10.1371/journal.pone.0026069
    • Arslan SC, Scheidereit C. The prevalence of TNFalpha-induced necrosis over apoptosis is determined by TAK1-RIP1 interplay. PLoS ONE. 2008;6(10):e26069. doi: 10.1371/journal.pone.0026069.
    • (2008) PLoS ONE , vol.6 , Issue.10 , pp. 26069
    • Arslan, S.C.1    Scheidereit, C.2
  • 102
    • 79952623655 scopus 로고    scopus 로고
    • CIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production
    • 10.1038/cdd.2010.138 21052097
    • Vanlangenakker N, Vanden Berge N, Berghe T, Bogaert P, Laukens B, Zoberl K, Deshayes K, et al. cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production. Cell Death Differ. 2010;18(4):656-65. doi: 10.1038/cdd.2010.138.
    • (2010) Cell Death Differ , vol.18 , Issue.4 , pp. 656-665
    • Vanlangenakker, N.1    Vanden Berge, N.2    Berghe, T.3    Bogaert, P.4    Laukens, B.5    Zoberl, K.6    Deshayes, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.