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Volumn 73, Issue 11-12, 2016, Pages 2165-2176

Poly-ubiquitination in TNFR1-mediated necroptosis

Author keywords

A20; c IAP1 2; CYLD; LUBAC; Necroptosis; RIPK1; TNFR1; Ubiquitination

Indexed keywords

I KAPPA B ALPHA; I KAPPA B KINASE BETA; MITOGEN ACTIVATED PROTEIN KINASE P38; MULTIPROTEIN COMPLEX; NECROSOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR RECEPTOR 1; UBIQUITIN; UNCLASSIFIED DRUG; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK1 PROTEIN, MOUSE; RIPK3 PROTEIN, MOUSE; TNFRSF1A PROTEIN, MOUSE; TUMOR NECROSIS FACTOR;

EID: 84962909249     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-016-2191-4     Document Type: Review
Times cited : (135)

References (104)
  • 1
    • 78751560494 scopus 로고    scopus 로고
    • Pathogen recognition by the innate immune system
    • COI: 1:CAS:528:DC%2BC3MXmtVCltw%3D%3D, PID: 21235323
    • Kumar H, Kawai T, Akira S (2011) Pathogen recognition by the innate immune system. Int Rev Immunol 30(1):16–34. doi:10.3109/08830185.2010.529976
    • (2011) Int Rev Immunol , vol.30 , Issue.1 , pp. 16-34
    • Kumar, H.1    Kawai, T.2    Akira, S.3
  • 2
    • 84886305117 scopus 로고    scopus 로고
    • Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death
    • COI: 1:CAS:528:DC%2BC3sXhs1WmsL%2FE, PID: 24129419
    • Ofengeim D, Yuan J (2013) Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death. Nat Rev Mol Cell Biol 14(11):727–736. doi:10.1038/nrm3683
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.11 , pp. 727-736
    • Ofengeim, D.1    Yuan, J.2
  • 3
    • 84894559172 scopus 로고    scopus 로고
    • Ubiquitin in the immune system
    • COI: 1:CAS:528:DC%2BC2cXhtVKjurzJ, PID: 24375678
    • Zinngrebe J, Montinaro A, Peltzer N, Walczak H (2014) Ubiquitin in the immune system. EMBO Rep 15(1):28–45. doi:10.1002/embr.201338025
    • (2014) EMBO Rep , vol.15 , Issue.1 , pp. 28-45
    • Zinngrebe, J.1    Montinaro, A.2    Peltzer, N.3    Walczak, H.4
  • 5
    • 84872820481 scopus 로고    scopus 로고
    • Linear ubiquitination: a newly discovered regulator of cell signalling
    • COI: 1:CAS:528:DC%2BC3sXht1Gmtbs%3D, PID: 23333406
    • Rieser E, Cordier SM, Walczak H (2013) Linear ubiquitination: a newly discovered regulator of cell signalling. Trends Biochem Sci 38(2):94–102. doi:10.1016/j.tibs.2012.11.007
    • (2013) Trends Biochem Sci , vol.38 , Issue.2 , pp. 94-102
    • Rieser, E.1    Cordier, S.M.2    Walczak, H.3
  • 6
    • 80054852212 scopus 로고    scopus 로고
    • TNF and ubiquitin at the crossroads of gene activation, cell death, inflammation, and cancer
    • COI: 1:CAS:528:DC%2BC3MXhsFagsL%2FI, PID: 22017428
    • Walczak H (2011) TNF and ubiquitin at the crossroads of gene activation, cell death, inflammation, and cancer. Immunol Rev 244(1):9–28. doi:10.1111/j.1600-065X.2011.01066.x
    • (2011) Immunol Rev , vol.244 , Issue.1 , pp. 9-28
    • Walczak, H.1
  • 7
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • COI: 1:CAS:528:DC%2BD1MXhtFGls7fM, PID: 19754430
    • Komander D (2009) The emerging complexity of protein ubiquitination. Biochem Soc Trans 37(Pt 5):937–953. doi:10.1042/BST0370937
    • (2009) Biochem Soc Trans , vol.37 , pp. 937-953
    • Komander, D.1
  • 8
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains—from structures to functions
    • COI: 1:CAS:528:DC%2BD1MXhtFGrsbrL, PID: 19773779
    • Dikic I, Wakatsuki S, Walters KJ (2009) Ubiquitin-binding domains—from structures to functions. Nat Rev Mol Cell Biol 10(10):659–671. doi:10.1038/nrm2767
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 9
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • COI: 1:CAS:528:DC%2BD1MXovFSru74%3D, PID: 19626045
    • Komander D, Clague MJ, Urbe S (2009) Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10(8):550–563. doi:10.1038/nrm2731
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.8 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 10
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1–RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • COI: 1:CAS:528:DC%2BD1MXps1eiu7o%3D, PID: 19524513
    • Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M, Chan FK (2009) Phosphorylation-driven assembly of the RIP1–RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137(6):1112–1123. 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    Chan, F.K.7
  • 11
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • COI: 1:CAS:528:DC%2BD1MXps1eiu70%3D, PID: 19524512
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L, Wang X (2009) Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 137(6):1100–1111. 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    Wang, X.7
  • 12
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • COI: 1:CAS:528:DC%2BC38XhtFKgsLY%3D, PID: 22265413
    • Sun L, Wang H, Wang Z, He S, Chen S, Liao D, Wang L, Yan J, Liu W, Lei X, Wang X (2012) Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 148(1–2):213–227. doi:10.1016/j.cell.2011.11.031
    • (2012) Cell , vol.148 , Issue.1-2 , pp. 213-227
    • Sun, L.1    Wang, H.2    Wang, Z.3    He, S.4    Chen, S.5    Liao, D.6    Wang, L.7    Yan, J.8    Liu, W.9    Lei, X.10    Wang, X.11
  • 13
    • 84859467770 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
    • COI: 1:CAS:528:DC%2BC38XlslOjs70%3D, PID: 22421439
    • Zhao J, Jitkaew S, Cai Z, Choksi S, Li Q, Luo J, Liu ZG (2012) Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc Natl Acad Sci USA 109(14):5322–5327. doi:10.1073/pnas.1200012109
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.14 , pp. 5322-5327
    • Zhao, J.1    Jitkaew, S.2    Cai, Z.3    Choksi, S.4    Li, Q.5    Luo, J.6    Liu, Z.G.7
  • 14
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • COI: 1:CAS:528:DC%2BD3sXlvFCgu7Y%3D, PID: 12887920
    • Micheau O, Tschopp J (2003) Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114(2):181–190
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 15
    • 0037815277 scopus 로고    scopus 로고
    • Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis
    • COI: 1:CAS:528:DC%2BD3sXlt1Cmuro%3D, PID: 12721308
    • Harper N, Hughes M, MacFarlane M, Cohen GM (2003) Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis. J Biol Chem 278(28):25534–25541. doi:10.1074/jbc.M303399200
    • (2003) J Biol Chem , vol.278 , Issue.28 , pp. 25534-25541
    • Harper, N.1    Hughes, M.2    MacFarlane, M.3    Cohen, G.M.4
  • 18
    • 2442559290 scopus 로고    scopus 로고
    • Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro
    • COI: 1:CAS:528:DC%2BD2cXktVOksrw%3D, PID: 15147886
    • Park SM, Yoon JB, Lee TH (2004) Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro. FEBS Lett 566(1–3):151–156. 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
  • 21
    • 54049155149 scopus 로고    scopus 로고
    • c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation
    • COI: 1:CAS:528:DC%2BD1cXhtVGktb7E, PID: 18621737
    • Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN, Zobel K, Deshayes K, Fairbrother WJ, Vucic D (2008) c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation. J Biol Chem 283(36):24295–24299. doi:10.1074/jbc.C800128200
    • (2008) J Biol Chem , vol.283 , Issue.36 , pp. 24295-24299
    • Varfolomeev, E.1    Goncharov, T.2    Fedorova, A.V.3    Dynek, J.N.4    Zobel, K.5    Deshayes, K.6    Fairbrother, W.J.7    Vucic, D.8
  • 25
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex
    • COI: 1:CAS:528:DC%2BC3MXktVGmurY%3D, PID: 21455180
    • Tokunaga F, Nakagawa T, Nakahara M, Saeki Y, Taniguchi M, Sakata S, Tanaka K, Nakano H, Iwai K (2011) SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex. Nature 471(7340):633–636. doi:10.1038/nature09815
    • (2011) Nature , vol.471 , Issue.7340 , pp. 633-636
    • Tokunaga, F.1    Nakagawa, T.2    Nakahara, M.3    Saeki, Y.4    Taniguchi, M.5    Sakata, S.6    Tanaka, K.7    Nakano, H.8    Iwai, K.9
  • 27
    • 84867096523 scopus 로고    scopus 로고
    • The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension
    • COI: 1:CAS:528:DC%2BC38XhtFCrtrzN, PID: 22863777
    • Smit JJ, Monteferrario D, Noordermeer SM, van Dijk WJ, van der Reijden BA, Sixma TK (2012) The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension. EMBO J 31(19):3833–3844. doi:10.1038/emboj.2012.217
    • (2012) EMBO J , vol.31 , Issue.19 , pp. 3833-3844
    • Smit, J.J.1    Monteferrario, D.2    Noordermeer, S.M.3    van Dijk, W.J.4    van der Reijden, B.A.5    Sixma, T.K.6
  • 29
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • COI: 1:CAS:528:DC%2BD3MXlsFGjsLs%3D, PID: 11460167
    • Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, Chen ZJ (2001) TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412(6844):346–351. doi:10.1038/35085597
    • (2001) Nature , vol.412 , Issue.6844 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.5    Chen, Z.J.6
  • 30
    • 4344712350 scopus 로고    scopus 로고
    • TAB 2 and TAB 3 activate the NF-kappaB pathway through binding to polyubiquitin chains
    • COI: 1:CAS:528:DC%2BD2cXns1ynurY%3D, PID: 15327770
    • Kanayama A, Seth RB, Sun L, Ea CK, Hong M, Shaito A, Chiu YH, Deng L, Chen ZJ (2004) TAB 2 and TAB 3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Mol Cell 15(4):535–548. 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    Chiu, Y.H.7    Deng, L.8    Chen, Z.J.9
  • 31
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • COI: 1:CAS:528:DC%2BD28Xkt1Gmtb8%3D, PID: 16603398
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ (2006) Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 22(2):245–257. 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
  • 32
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • COI: 1:CAS:528:DC%2BD28Xjt12qs7o%3D, PID: 16547522
    • Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD (2006) Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat Cell Biol 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
  • 33
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • COI: 1:CAS:528:DC%2BD1MXks1ShsbY%3D, PID: 19373254
    • Komander D, Reyes-Turcu F, Licchesi JD, Odenwaelder P, Wilkinson KD, Barford D (2009) Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep 10(5):466–473. doi:10.1038/embor.2009.55
    • (2009) EMBO Rep , vol.10 , Issue.5 , pp. 466-473
    • Komander, D.1    Reyes-Turcu, F.2    Licchesi, J.D.3    Odenwaelder, P.4    Wilkinson, K.D.5    Barford, D.6
  • 35
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta
    • COI: 1:CAS:528:DC%2BD1MXhsFWht7vJ, PID: 19854138
    • Xu M, Skaug B, Zeng W, Chen ZJ (2009) A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta. Mol Cell 36(2):302–314. doi:10.1016/j.molcel.2009.10.002
    • (2009) Mol Cell , vol.36 , Issue.2 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 36
    • 0028986075 scopus 로고
    • Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
    • COI: 1:CAS:528:DyaK2MXktlCltL8%3D, PID: 7878466
    • Brown K, Gerstberger S, Carlson L, Franzoso G, Siebenlist U (1995) Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 267(5203):1485–1488
    • (1995) Science , vol.267 , Issue.5203 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 37
    • 0028981050 scopus 로고
    • Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B
    • COI: 1:CAS:528:DyaK2MXjt12qt7Y%3D, PID: 7831327
    • Lin YC, Brown K, Siebenlist U (1995) Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B. Proc Natl Acad Sci USA 92(2):552–556
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.2 , pp. 552-556
    • Lin, Y.C.1    Brown, K.2    Siebenlist, U.3
  • 38
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP
    • COI: 1:CAS:528:DyaK1MXht1Kgt7s%3D, PID: 9990853
    • Spencer E, Jiang J, Chen ZJ (1999) Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP. Genes Dev 13(3):284–294
    • (1999) Genes Dev , vol.13 , Issue.3 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 39
    • 0033068154 scopus 로고    scopus 로고
    • The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
    • COI: 1:CAS:528:DyaK1MXht1Kgtrs%3D, PID: 9990852
    • Winston JT, Strack P, Beer-Romero P, Chu CY, Elledge SJ, Harper JW (1999) The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro. Genes Dev 13(3):270–283
    • (1999) Genes Dev , vol.13 , Issue.3 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 40
    • 43749122598 scopus 로고    scopus 로고
    • NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling
    • COI: 1:CAS:528:DC%2BD1cXivFyjtLY%3D, PID: 18178551
    • Enesa K, Zakkar M, Chaudhury H, le Luong A, Rawlinson L, Mason JC, Haskard DO, Dean JL, Evans PC (2008) NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling. J Biol Chem 283(11):7036–7045. doi:10.1074/jbc.M708690200
    • (2008) J Biol Chem , vol.283 , Issue.11 , pp. 7036-7045
    • Enesa, K.1    Zakkar, M.2    Chaudhury, H.3    le Luong, A.4    Rawlinson, L.5    Mason, J.C.6    Haskard, D.O.7    Dean, J.L.8    Evans, P.C.9
  • 44
    • 84903726513 scopus 로고    scopus 로고
    • The deubiquitinase activity of A20 is dispensable for NF-kappaB signaling
    • COI: 1:CAS:528:DC%2BC2cXht1ems7%2FF, PID: 24878851
    • De A, Dainichi T, Rathinam CV, Ghosh S (2014) The deubiquitinase activity of A20 is dispensable for NF-kappaB signaling. EMBO Rep 15(7):775–783. doi:10.15252/embr.201338305
    • (2014) EMBO Rep , vol.15 , Issue.7 , pp. 775-783
    • De, A.1    Dainichi, T.2    Rathinam, C.V.3    Ghosh, S.4
  • 46
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1
    • COI: 1:CAS:528:DC%2BC3cXkvFKl, PID: 19910467
    • Xu G, Tan X, Wang H, Sun W, Shi Y, Burlingame S, Gu X, Cao G, Zhang T, Qin J, Yang J (2010) Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1. J Biol Chem 285(2):969–978. doi:10.1074/jbc.M109.042689
    • (2010) J Biol Chem , vol.285 , Issue.2 , pp. 969-978
    • Xu, G.1    Tan, X.2    Wang, H.3    Sun, W.4    Shi, Y.5    Burlingame, S.6    Gu, X.7    Cao, G.8    Zhang, T.9    Qin, J.10    Yang, J.11
  • 47
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • COI: 1:CAS:528:DC%2BD3sXmt1antr4%3D, PID: 12917690
    • Brummelkamp TR, Nijman SM, Dirac AM, Bernards R (2003) Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 424(6950):797–801. doi:10.1038/nature01811
    • (2003) Nature , vol.424 , Issue.6950 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 48
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • COI: 1:CAS:528:DC%2BD3sXmt1ansbY%3D, PID: 12917691
    • Kovalenko A, Chable-Bessia C, Cantarella G, Israel A, Wallach D, Courtois G (2003) The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 424(6950):801–805. doi:10.1038/nature01802
    • (2003) Nature , vol.424 , Issue.6950 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 49
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • COI: 1:CAS:528:DC%2BD3sXmt1ansbc%3D, PID: 12917689
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A, Mosialos G (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424(6950):793–796. doi:10.1038/nature01803
    • (2003) Nature , vol.424 , Issue.6950 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 50
    • 35548974703 scopus 로고    scopus 로고
    • Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD
    • COI: 1:CAS:528:DC%2BD2sXhtlWitrfE, PID: 17981138
    • Wright A, Reiley WW, Chang M, Jin W, Lee AJ, Zhang M, Sun SC (2007) Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD. Dev Cell 13(5):705–716. 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    Sun, S.C.7
  • 51
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • COI: 1:CAS:528:DC%2BD2sXovFylsb4%3D, PID: 17644308
    • Feng S, Yang Y, Mei Y, Ma L, Zhu DE, Hoti N, Castanares M, Wu M (2007) Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell Signal 19(10):2056–2067. doi:10.1016/j.cellsig.2007.05.016
    • (2007) Cell Signal , vol.19 , Issue.10 , pp. 2056-2067
    • Feng, S.1    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.E.5    Hoti, N.6    Castanares, M.7    Wu, M.8
  • 52
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • COI: 1:CAS:528:DyaK1MXmvFOit78%3D, PID: 10521396
    • Lin Y, Devin A, Rodriguez Y, Liu ZG (1999) Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev 13(19):2514–2526
    • (1999) Genes Dev , vol.13 , Issue.19 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 55
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis
    • COI: 1:CAS:528:DC%2BC3MXis1Crsrs%3D, PID: 21368763
    • Oberst A, Dillon CP, Weinlich R, McCormick LL, Fitzgerald P, Pop C, Hakem R, Salvesen GS, Green DR (2011) Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature 471(7338):363–367. 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    Hakem, R.7    Salvesen, G.S.8    Green, D.R.9
  • 56
    • 0029992609 scopus 로고    scopus 로고
    • Suppression of TNF-alpha-induced apoptosis by NF-kappaB
    • PID: 8864120
    • Van Antwerp DJ, Martin SJ, Kafri T, Green DR, Verma IM (1996) Suppression of TNF-alpha-induced apoptosis by NF-kappaB. Science 274(5288):787–789
    • (1996) Science , vol.274 , Issue.5288 , pp. 787-789
    • Van Antwerp, D.J.1    Martin, S.J.2    Kafri, T.3    Green, D.R.4    Verma, I.M.5
  • 57
    • 0023691110 scopus 로고
    • Correlation between the anticellular and DNA fragmenting activities of tumor necrosis factor
    • COI: 1:CAS:528:DyaL1cXmt1ygsLk%3D, PID: 3167851
    • Rubin BY, Smith LJ, Hellermann GR, Lunn RM, Richardson NK, Anderson SL (1988) Correlation between the anticellular and DNA fragmenting activities of tumor necrosis factor. Cancer Res 48(21):6006–6010
    • (1988) Cancer Res , vol.48 , Issue.21 , pp. 6006-6010
    • Rubin, B.Y.1    Smith, L.J.2    Hellermann, G.R.3    Lunn, R.M.4    Richardson, N.K.5    Anderson, S.L.6
  • 58
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • COI: 1:CAS:528:DC%2BD1cXmsVOru78%3D, PID: 18485876
    • Wang L, Du F, Wang X (2008) TNF-alpha induces two distinct caspase-8 activation pathways. Cell 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
  • 59
    • 62849093368 scopus 로고    scopus 로고
    • Death receptor signal transducers: nodes of coordination in immune signaling networks
    • COI: 1:CAS:528:DC%2BD1MXjtlymsLw%3D, PID: 19295631
    • Wilson NS, Dixit V, Ashkenazi A (2009) Death receptor signal transducers: nodes of coordination in immune signaling networks. Nat Immunol 10(4):348–355. doi:10.1038/ni.1714
    • (2009) Nat Immunol , vol.10 , Issue.4 , pp. 348-355
    • Wilson, N.S.1    Dixit, V.2    Ashkenazi, A.3
  • 60
    • 84904047854 scopus 로고    scopus 로고
    • Functions of caspase 8: the identified and the mysterious
    • COI: 1:CAS:528:DC%2BC2cXoslCnurw%3D, PID: 24856110
    • Salvesen GS, Walsh CM (2014) Functions of caspase 8: the identified and the mysterious. Semin Immunol 26(3):246–252. doi:10.1016/j.smim.2014.03.005
    • (2014) Semin Immunol , vol.26 , Issue.3 , pp. 246-252
    • Salvesen, G.S.1    Walsh, C.M.2
  • 61
    • 84867877809 scopus 로고    scopus 로고
    • NFkappaB and ubiquitination: partners in disarming RIPK1-mediated cell death
    • PID: 22477525, COI: 1:CAS:528:DC%2BC38XhsFamt7fP
    • O’Donnell MA, Ting AT (2012) NFkappaB and ubiquitination: partners in disarming RIPK1-mediated cell death. Immunol Res 54(1–3):214–226. doi:10.1007/s12026-012-8321-7
    • (2012) Immunol Res , vol.54 , Issue.1-3 , pp. 214-226
    • O’Donnell, M.A.1    Ting, A.T.2
  • 62
    • 35948994157 scopus 로고    scopus 로고
    • Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis
    • COI: 1:CAS:528:DC%2BD2sXhtl2nurrN, PID: 17996648
    • Petersen SL, Wang L, Yalcin-Chin A, Li L, Peyton M, Minna J, Harran P, Wang X (2007) Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis. Cancer Cell 12(5):445–456. doi:10.1016/j.ccr.2007.08.029
    • (2007) Cancer Cell , vol.12 , Issue.5 , pp. 445-456
    • Petersen, S.L.1    Wang, L.2    Yalcin-Chin, A.3    Li, L.4    Peyton, M.5    Minna, J.6    Harran, P.7    Wang, X.8
  • 67
    • 84883770753 scopus 로고    scopus 로고
    • RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition
    • COI: 1:CAS:528:DC%2BC3sXhsVeis7nK, PID: 23892367
    • Dondelinger Y, Aguileta MA, Goossens V, Dubuisson C, Grootjans S, Dejardin E, Vandenabeele P, Bertrand MJ (2013) RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition. Cell Death Differ 20(10):1381–1392. doi:10.1038/cdd.2013.94
    • (2013) Cell Death Differ , vol.20 , Issue.10 , pp. 1381-1392
    • Dondelinger, Y.1    Aguileta, M.A.2    Goossens, V.3    Dubuisson, C.4    Grootjans, S.5    Dejardin, E.6    Vandenabeele, P.7    Bertrand, M.J.8
  • 69
    • 83155192804 scopus 로고    scopus 로고
    • TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members
    • COI: 1:CAS:528:DC%2BC38XmvVWn, PID: 22089168
    • Vanlangenakker N, Bertrand MJ, Bogaert P, Vandenabeele P, Vanden Berghe T (2011) TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members. Cell Death Dis 2:e230. doi:10.1038/cddis.2011.111
    • (2011) Cell Death Dis , vol.2 , pp. e230
    • Vanlangenakker, N.1    Bertrand, M.J.2    Bogaert, P.3    Vandenabeele, P.4    Vanden Berghe, T.5
  • 71
    • 33847251527 scopus 로고    scopus 로고
    • Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling
    • PID: 17306544, COI: 1:CAS:528:DC%2BD2sXisVChtLo%3D
    • O’Donnell MA, Legarda-Addison D, Skountzos P, Yeh WC, Ting AT (2007) Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling. Curr Biol 17(5):418–424. doi:10.1016/j.cub.2007.01.027
    • (2007) Curr Biol , vol.17 , Issue.5 , pp. 418-424
    • O’Donnell, M.A.1    Legarda-Addison, D.2    Skountzos, P.3    Yeh, W.C.4    Ting, A.T.5
  • 72
    • 79960922705 scopus 로고    scopus 로고
    • cIAPs block ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • COI: 1:CAS:528:DC%2BC3MXpvFSqtrY%3D, PID: 21737330
    • Feoktistova M, Geserick P, Kellert B, Dimitrova DP, Langlais C, Hupe M, Cain K, MacFarlane M, Hacker G, Leverkus M (2011) cIAPs block ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol Cell 43(3):449–463. doi:10.1016/j.molcel.2011.06.011
    • (2011) Mol Cell , vol.43 , Issue.3 , pp. 449-463
    • Feoktistova, M.1    Geserick, P.2    Kellert, B.3    Dimitrova, D.P.4    Langlais, C.5    Hupe, M.6    Cain, K.7    MacFarlane, M.8    Hacker, G.9    Leverkus, M.10
  • 74
    • 0027773019 scopus 로고
    • A spontaneous mutation characterized by chronic proliferative dermatitis in C57BL mice
    • COI: 1:STN:280:DyaK3szntVGktw%3D%3D, PID: 8362989
    • HogenEsch H, Gijbels MJ, Offerman E, van Hooft J, van Bekkum DW, Zurcher C (1993) A spontaneous mutation characterized by chronic proliferative dermatitis in C57BL mice. Am J Pathol 143(3):972–982
    • (1993) Am J Pathol , vol.143 , Issue.3 , pp. 972-982
    • HogenEsch, H.1    Gijbels, M.J.2    Offerman, E.3    van Hooft, J.4    van Bekkum, D.W.5    Zurcher, C.6
  • 75
    • 34547422758 scopus 로고    scopus 로고
    • Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis
    • COI: 1:CAS:528:DC%2BD2sXotVOhs74%3D, PID: 17538631
    • Seymour RE, Hasham MG, Cox GA, Shultz LD, Hogenesch H, Roopenian DC, Sundberg JP (2007) Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis. Genes Immun 8(5):416–421. doi:10.1038/sj.gene.6364403
    • (2007) Genes Immun , vol.8 , Issue.5 , pp. 416-421
    • Seymour, R.E.1    Hasham, M.G.2    Cox, G.A.3    Shultz, L.D.4    Hogenesch, H.5    Roopenian, D.C.6    Sundberg, J.P.7
  • 76
    • 0033120961 scopus 로고    scopus 로고
    • Absence of Peyer’s patches and abnormal lymphoid architecture in chronic proliferative dermatitis (cpdm/cpdm) mice
    • COI: 1:CAS:528:DyaK1MXitFGqt7k%3D, PID: 10201907
    • HogenEsch H, Janke S, Boggess D, Sundberg JP (1999) Absence of Peyer’s patches and abnormal lymphoid architecture in chronic proliferative dermatitis (cpdm/cpdm) mice. J Immunol 162(7):3890–3896
    • (1999) J Immunol , vol.162 , Issue.7 , pp. 3890-3896
    • HogenEsch, H.1    Janke, S.2    Boggess, D.3    Sundberg, J.P.4
  • 78
    • 16244377737 scopus 로고    scopus 로고
    • Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo
    • COI: 1:CAS:528:DC%2BD2MXjtlSjsL8%3D, PID: 15798218
    • Conze DB, Albert L, Ferrick DA, Goeddel DV, Yeh WC, Mak T, Ashwell JD (2005) Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo. Mol Cell Biol 25(8):3348–3356. doi:10.1128/MCB.25.8.3348-3356.2005
    • (2005) Mol Cell Biol , vol.25 , Issue.8 , pp. 3348-3356
    • Conze, D.B.1    Albert, L.2    Ferrick, D.A.3    Goeddel, D.V.4    Yeh, W.C.5    Mak, T.6    Ashwell, J.D.7
  • 79
    • 30744452261 scopus 로고    scopus 로고
    • Inhibitor of apoptosis protein cIAP2 is essential for lipopolysaccharide-induced macrophage survival
    • COI: 1:CAS:528:DC%2BD28XhtVOht7s%3D, PID: 16382159
    • Conte D, Holcik M, Lefebvre CA, Lacasse E, Picketts DJ, Wright KE, Korneluk RG (2006) Inhibitor of apoptosis protein cIAP2 is essential for lipopolysaccharide-induced macrophage survival. Mol Cell Biol 26(2):699–708. doi:10.1128/MCB.26.2.699-708.2006
    • (2006) Mol Cell Biol , vol.26 , Issue.2 , pp. 699-708
    • Conte, D.1    Holcik, M.2    Lefebvre, C.A.3    Lacasse, E.4    Picketts, D.J.5    Wright, K.E.6    Korneluk, R.G.7
  • 83
    • 0026691240 scopus 로고
    • The A20 zinc finger protein protects cells from tumor necrosis factor cytotoxicity
    • COI: 1:CAS:528:DyaK38Xks1yhsbc%3D, PID: 1618749
    • Opipari AW Jr, Hu HM, Yabkowitz R, Dixit VM (1992) The A20 zinc finger protein protects cells from tumor necrosis factor cytotoxicity. J Biol Chem 267(18):12424–12427
    • (1992) J Biol Chem , vol.267 , Issue.18 , pp. 12424-12427
    • Opipari, A.W.1    Hu, H.M.2    Yabkowitz, R.3    Dixit, V.M.4
  • 84
    • 77954391573 scopus 로고    scopus 로고
    • Enterocyte-specific A20 deficiency sensitizes to tumor necrosis factor-induced toxicity and experimental colitis
    • COI: 1:CAS:528:DC%2BC3cXovFaktb0%3D, PID: 20530205
    • Vereecke L, Sze M, Mc Guire C, Rogiers B, Chu Y, Schmidt-Supprian M, Pasparakis M, Beyaert R, van Loo G (2010) Enterocyte-specific A20 deficiency sensitizes to tumor necrosis factor-induced toxicity and experimental colitis. J Exp Med 207(7):1513–1523. doi:10.1084/jem.20092474
    • (2010) J Exp Med , vol.207 , Issue.7 , pp. 1513-1523
    • Vereecke, L.1    Sze, M.2    Mc Guire, C.3    Rogiers, B.4    Chu, Y.5    Schmidt-Supprian, M.6    Pasparakis, M.7    Beyaert, R.8    van Loo, G.9
  • 85
  • 86
    • 69049092633 scopus 로고    scopus 로고
    • NEMO/IKKgamma regulates an early NF-kappaB-independent cell-death checkpoint during TNF signaling
    • COI: 1:CAS:528:DC%2BD1MXhtVamur%2FP, PID: 19373245
    • Legarda-Addison D, Hase H, O’Donnell MA, Ting AT (2009) NEMO/IKKgamma regulates an early NF-kappaB-independent cell-death checkpoint during TNF signaling. Cell Death Differ 16(9):1279–1288. 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
  • 87
    • 84864389178 scopus 로고    scopus 로고
    • NEMO inhibits programmed necrosis in an NFkappaB-independent manner by restraining RIP1
    • PID: 22848449, COI: 1:CAS:528:DC%2BC38XhtFeisrrM
    • O’Donnell MA, Hase H, Legarda D, Ting AT (2012) NEMO inhibits programmed necrosis in an NFkappaB-independent manner by restraining RIP1. PLoS One 7(7):e41238. doi:10.1371/journal.pone.0041238
    • (2012) PLoS One , vol.7 , Issue.7 , pp. e41238
    • O’Donnell, M.A.1    Hase, H.2    Legarda, D.3    Ting, A.T.4
  • 88
    • 80053927315 scopus 로고    scopus 로고
    • The prevalence of TNFalpha-induced necrosis over apoptosis is determined by TAK1–RIP1 interplay
    • COI: 1:CAS:528:DC%2BC3MXhtl2mtb%2FO, PID: 22016814
    • Arslan SC, Scheidereit C (2011) The prevalence of TNFalpha-induced necrosis over apoptosis is determined by TAK1–RIP1 interplay. PLoS One 6(10):e26069. doi:10.1371/journal.pone.0026069
    • (2011) PLoS One , vol.6 , Issue.10 , pp. e26069
    • Arslan, S.C.1    Scheidereit, C.2
  • 89
    • 84894024528 scopus 로고    scopus 로고
    • TAK1 kinase switches cell fate from apoptosis to necrosis following TNF stimulation
    • COI: 1:CAS:528:DC%2BC2cXivFejsro%3D, PID: 24535827
    • Morioka S, Broglie P, Omori E, Ikeda Y, Takaesu G, Matsumoto K, Ninomiya-Tsuji J (2014) TAK1 kinase switches cell fate from apoptosis to necrosis following TNF stimulation. J Cell Biol 204(4):607–623. doi:10.1083/jcb.201305070
    • (2014) J Cell Biol , vol.204 , Issue.4 , pp. 607-623
    • Morioka, S.1    Broglie, P.2    Omori, E.3    Ikeda, Y.4    Takaesu, G.5    Matsumoto, K.6    Ninomiya-Tsuji, J.7
  • 90
    • 84884823502 scopus 로고    scopus 로고
    • CYLD deubiquitinates RIP1 in the TNFalpha-induced necrosome to facilitate kinase activation and programmed necrosis
    • COI: 1:CAS:528:DC%2BC3sXhsFyrurzK, PID: 24098568
    • Moquin DM, McQuade T, Chan FK (2013) CYLD deubiquitinates RIP1 in the TNFalpha-induced necrosome to facilitate kinase activation and programmed necrosis. PLoS One 8(10):e76841. doi:10.1371/journal.pone.0076841
    • (2013) PLoS One , vol.8 , Issue.10 , pp. e76841
    • Moquin, D.M.1    McQuade, T.2    Chan, F.K.3
  • 92
    • 79953282304 scopus 로고    scopus 로고
    • NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling
    • COI: 1:CAS:528:DC%2BC3MXktF2hurc%3D, PID: 21458669
    • Biton S, Ashkenazi A (2011) NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling. Cell 145(1):92–103. doi:10.1016/j.cell.2011.02.023
    • (2011) Cell , vol.145 , Issue.1 , pp. 92-103
    • Biton, S.1    Ashkenazi, A.2
  • 93
    • 84989885436 scopus 로고    scopus 로고
    • Cellular IAP proteins and LUBAC differentially regulate necrosome-associated RIP1 ubiquitination
    • PID: 26111062, COI: 1:CAS:528:DC%2BC2MXhtFOjt7rM
    • de Almagro MC, Goncharov T, Newton K, Vucic D (2015) Cellular IAP proteins and LUBAC differentially regulate necrosome-associated RIP1 ubiquitination. Cell Death Dis 6:e1800. doi:10.1038/cddis.2015.158
    • (2015) Cell Death Dis , vol.6 , pp. e1800
    • de Almagro, M.C.1    Goncharov, T.2    Newton, K.3    Vucic, D.4
  • 94
    • 80052638486 scopus 로고    scopus 로고
    • cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1–4)
    • COI: 1:CAS:528:DC%2BC3MXht1Glt7rI, PID: 21931591
    • Bertrand MJ, Lippens S, Staes A, Gilbert B, Roelandt R, De Medts J, Gevaert K, Declercq W, Vandenabeele P (2011) cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1–4). PLoS One 6(9):e22356. doi:10.1371/journal.pone.0022356
    • (2011) PLoS One , vol.6 , Issue.9 , pp. e22356
    • Bertrand, M.J.1    Lippens, S.2    Staes, A.3    Gilbert, B.4    Roelandt, R.5    De Medts, J.6    Gevaert, K.7    Declercq, W.8    Vandenabeele, P.9
  • 96
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • COI: 1:CAS:528:DC%2BC3MXhs12hurzM, PID: 22135298
    • Hornbeck PV, Kornhauser JM, Tkachev S, Zhang B, Skrzypek E, Murray B, Latham V, Sullivan M (2012) PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic acids research 40(database issue):D261–D270. doi:10.1093/nar/gkr1122
    • (2012) Nucleic acids research , vol.40 , Issue.database issue , pp. D261-D270
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 97
    • 84931068090 scopus 로고    scopus 로고
    • Targeting signaling factors for degradation, an emerging mechanism for TRAF functions
    • COI: 1:CAS:528:DC%2BC2MXhtVOntrzO, PID: 26085207
    • Yang XD, Sun SC (2015) Targeting signaling factors for degradation, an emerging mechanism for TRAF functions. Immunol Rev 266(1):56–71. doi:10.1111/imr.12311
    • (2015) Immunol Rev , vol.266 , Issue.1 , pp. 56-71
    • Yang, X.D.1    Sun, S.C.2
  • 99
    • 84870820660 scopus 로고    scopus 로고
    • Species-specific inhibition of RIG-I ubiquitination and IFN induction by the influenza A virus NS1 protein
    • COI: 1:CAS:528:DC%2BC38XhvVKjt7%2FJ, PID: 23209422
    • Rajsbaum R, Albrecht RA, Wang MK, Maharaj NP, Versteeg GA, Nistal-Villan E, Garcia-Sastre A, Gack MU (2012) Species-specific inhibition of RIG-I ubiquitination and IFN induction by the influenza A virus NS1 protein. PLoS Pathog 8(11):e1003059. doi:10.1371/journal.ppat.1003059
    • (2012) PLoS Pathog , vol.8 , Issue.11 , pp. e1003059
    • Rajsbaum, R.1    Albrecht, R.A.2    Wang, M.K.3    Maharaj, N.P.4    Versteeg, G.A.5    Nistal-Villan, E.6    Garcia-Sastre, A.7    Gack, M.U.8
  • 102
    • 77954593965 scopus 로고    scopus 로고
    • Virus inhibition of RIP3-dependent necrosis
    • COI: 1:CAS:528:DC%2BC3cXlsVWqsrY%3D, PID: 20413098
    • Upton JW, Kaiser WJ, Mocarski ES (2010) Virus inhibition of RIP3-dependent necrosis. Cell Host Microbe 7(4):302–313. doi:10.1016/j.chom.2010.03.006
    • (2010) Cell Host Microbe , vol.7 , Issue.4 , pp. 302-313
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 103
    • 84858420051 scopus 로고    scopus 로고
    • DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA
    • COI: 1:CAS:528:DC%2BC38XjvFOjs7o%3D, PID: 22423968
    • Upton JW, Kaiser WJ, Mocarski ES (2012) DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA. Cell Host Microbe 11(3):290–297. doi:10.1016/j.chom.2012.01.016
    • (2012) Cell Host Microbe , vol.11 , Issue.3 , pp. 290-297
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 104
    • 84055181328 scopus 로고    scopus 로고
    • Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3-mediated pathway
    • COI: 1:CAS:528:DC%2BC3MXhs12gtbbI, PID: 22123964
    • He S, Liang Y, Shao F, Wang X (2011) Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3-mediated pathway. Proc Natl Acad Sci USA 108(50):20054–20059. doi:10.1073/pnas.1116302108
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.50 , pp. 20054-20059
    • He, S.1    Liang, Y.2    Shao, F.3    Wang, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.