메뉴 건너뛰기




Volumn 403, Issue , 2017, Pages 95-117

IAPs and cell death

Author keywords

[No Author keywords available]

Indexed keywords

INHIBITOR OF APOPTOSIS PROTEIN; TUMOR NECROSIS FACTOR; X LINKED INHIBITOR OF APOPTOSIS;

EID: 85017541015     PISSN: 0070217X     EISSN: 21969965     Source Type: Book Series    
DOI: 10.1007/82_2016_507     Document Type: Chapter
Times cited : (40)

References (161)
  • 1
    • 84908110109 scopus 로고    scopus 로고
    • BID-dependent release of mitochondrial SMAC dampens XIAP-mediated immunity against Shigella
    • Andree M, Seeger JM, Schüll S, Coutelle O et al (2014) BID-dependent release of mitochondrial SMAC dampens XIAP-mediated immunity against Shigella. EMBO J 33:2171-2187
    • (2014) EMBO J , vol.33 , pp. 2171-2187
    • Andree, M.1    Seeger, J.M.2    Schüll, S.3    Coutelle, O.4
  • 2
    • 0032582662 scopus 로고    scopus 로고
    • The Drosophila Gene Hid is a direct molecular target of ras-dependent survival signaling
    • Bergmann A, Agapite J, McCall K, Steller H (1998) The Drosophila Gene Hid is a direct molecular target of ras-dependent survival signaling. Cell 95:331-341
    • (1998) Cell , vol.95 , pp. 331-341
    • Bergmann, A.1    Agapite, J.2    McCall, K.3    Steller, H.4
  • 3
    • 44949240664 scopus 로고    scopus 로고
    • CI AP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand MJ, Milutinovic S, Dickson KM, Ho WC et al (2008) cI AP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell 30:689-700
    • (2008) Mol Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.1    Milutinovic, S.2    Dickson, K.M.3    Ho, W.C.4
  • 4
    • 66949138341 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2
    • Bertrand MJ, Doiron K, Labbé K, Korneluk RG et al (2009) Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2. Immunity 30(6):789-801
    • (2009) Immunity , vol.30 , Issue.6 , pp. 789-801
    • Bertrand, M.J.1    Doiron, K.2    Labbé, K.3    Korneluk, R.G.4
  • 5
    • 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)
    • Bertrand MJ, Lippens S, Staes A, Gilbert B et al (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:e22356
    • (2011) Plos ONE , vol.6
    • Bertrand, M.J.1    Lippens, S.2    Staes, A.3    Gilbert, B.4
  • 6
    • 78651184265 scopus 로고
    • On the development of insect polyhedrosis and granulosis virus particles
    • Bird FT (1964) On the development of insect polyhedrosis and granulosis virus particles. Can J Microbiol 10:49-52
    • (1964) Can J Microbiol , vol.10 , pp. 49-52
    • Bird, F.T.1
  • 7
    • 0028274132 scopus 로고
    • An apoptosis inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with cys/his sequence motif
    • Birnbaum MJ, Clem RJ, Miller LK (1994) An apoptosis inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with cys/his sequence motif. J Virol 68:2521-2528
    • (1994) J Virol , vol.68 , pp. 2521-2528
    • Birnbaum, M.J.1    Clem, R.J.2    Miller, L.K.3
  • 8
    • 84878376898 scopus 로고    scopus 로고
    • Two coordinated mechanisms underlie tumor necrosis factor alpha-induced immediate and delayed IjB kinase activation
    • Blackwell K, Zhang L, Workman LM, Ting AT et al (2013) Two coordinated mechanisms underlie tumor necrosis factor alpha-induced immediate and delayed IjB kinase activation. Mol Cell Biol 33:1901-1915
    • (2013) Mol Cell Biol , vol.33 , pp. 1901-1915
    • Blackwell, K.1    Zhang, L.2    Workman, L.M.3    Ting, A.T.4
  • 9
    • 58249086500 scopus 로고    scopus 로고
    • Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2
    • Blankenship JW, Varfolomeev E, Goncharov T, Fedorova AV et al (2009) Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2. Biochem J 417:149-160
    • (2009) Biochem J , vol.417 , pp. 149-160
    • Blankenship, J.W.1    Varfolomeev, E.2    Goncharov, T.3    Fedorova, A.V.4
  • 11
    • 78649980427 scopus 로고    scopus 로고
    • Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases
    • Broemer M, Tenev T, Rigbolt KT, Hempel S et al (2010) Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases. Mol Cell 40:810-822
    • (2010) Mol Cell , vol.40 , pp. 810-822
    • Broemer, M.1    Tenev, T.2    Rigbolt, K.T.3    Hempel, S.4
  • 12
    • 84969595271 scopus 로고    scopus 로고
    • The caspase-8 inhibitor emricasan combines with the SMAC mimetic birinapant to induce necroptosis and treat acute myeloid leukemia
    • Brumatti G, Ma C, Lalaoui N, Nguyen NY et al (2016) The caspase-8 inhibitor emricasan combines with the SMAC mimetic birinapant to induce necroptosis and treat acute myeloid leukemia. Sci Transl Med 8:339ra69
    • (2016) Sci Transl Med , vol.8
    • Brumatti, G.1    Ma, C.2    Lalaoui, N.3    Nguyen, N.Y.4
  • 13
    • 84954358726 scopus 로고    scopus 로고
    • The evolution of BIR domain and its containing proteins
    • Cao L, Wang Z, Yang X, Xie L, Yu L (2008) The evolution of BIR domain and its containing proteins. FEBS Lett 582:3817-3822
    • (2008) FEBS Lett , vol.582 , pp. 3817-3822
    • Cao, L.1    Wang, Z.2    Yang, X.3    Xie, L.4    Yu, L.5
  • 14
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai J, Du C, Wu JW, Kyin S et al (2000) Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 406:855-862
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3    Kyin, S.4
  • 15
    • 0035831021 scopus 로고    scopus 로고
    • Structural basis of caspase-7 inhibition by XIAP
    • Chai J, Shiozaki E, Srinivasula SM, Wu Q et al (2001) Structural basis of caspase-7 inhibition by XIAP. Cell 104:769-780
    • (2001) Cell , vol.104 , pp. 769-780
    • Chai, J.1    Shiozaki, E.2    Srinivasula, S.M.3    Wu, Q.4
  • 16
    • 0029742260 scopus 로고    scopus 로고
    • Grim, a novel cell death gene in Drosophila
    • Chen P, Nordstrom W, Gish B, Abrams JM (1996) Grim, a novel cell death gene in Drosophila. Genes Dev 10:1773-1782
    • (1996) Genes Dev , vol.10 , pp. 1773-1782
    • Chen, P.1    Nordstrom, W.2    Gish, B.3    Abrams, J.M.4
  • 17
    • 50449088575 scopus 로고    scopus 로고
    • Beyond tumor necrosis factor receptor: TRADD signaling in toll-like receptors
    • Chen NJ, Chio II, Lin WJ, Duncan G et al (2008) Beyond tumor necrosis factor receptor: TRADD signaling in toll-like receptors. Proc Natl Acad Sci USA 105:12429-12434
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12429-12434
    • Chen, N.J.1    Chio, I.I.2    Lin, W.J.3    Duncan, G.4
  • 18
    • 84984822442 scopus 로고    scopus 로고
    • Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis
    • Chen X, He WT, Hu L, Li J et al (2016) Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis. Cell Res 26: 1007-1020
    • (2016) Cell Res , vol.26 , pp. 1007-1020
    • Chen, X.1    He, W.T.2    Hu, L.3    Li, J.4
  • 19
    • 84990061907 scopus 로고    scopus 로고
    • XIAP deficiency and MEFV variants resulting in an autoinflammatory lymphoproliferative syndrome
    • Christiansen M, Ammann S, Speckmann C, Mogensen TH (2016) XIAP deficiency and MEFV variants resulting in an autoinflammatory lymphoproliferative syndrome. BMJ Case Rep
    • (2016) BMJ Case Rep
    • Christiansen, M.1    Ammann, S.2    Speckmann, C.3    Mogensen, T.H.4
  • 20
    • 84928206139 scopus 로고    scopus 로고
    • Viral IAPs, then and now
    • Clem RJ (2015) Viral IAPs, then and now. Semin Cell Dev Biol 39:72-79
    • (2015) Semin Cell Dev Biol , vol.39 , pp. 72-79
    • Clem, R.J.1
  • 21
    • 84978476553 scopus 로고    scopus 로고
    • Cell death is not essential for caspase-1-mediated interleukin-1b activation and secretion
    • Conos SA, Lawlor KE, Vaux DL, Vince JE, Lindqvist LM (2016) Cell death is not essential for caspase-1-mediated interleukin-1b activation and secretion. Cell Death Differ 23:1827-1838
    • (2016) Cell Death Differ , vol.23 , pp. 1827-1838
    • Conos, S.A.1    Lawlor, K.E.2    Vaux, D.L.3    Vince, J.E.4    Lindqvist, L.M.5
  • 22
    • 0027537461 scopus 로고
    • An apoptosis inhibiting baculovirus gene with a zinc finger like motif
    • Crook NE, Clem RJ, Miller LK (1993) An apoptosis inhibiting baculovirus gene with a zinc finger like motif. J Virol 67:2168-2174
    • (1993) J Virol , vol.67 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 23
    • 84863000898 scopus 로고    scopus 로고
    • The Ubiquitin Ligase XIAP Recruits LUBAC for NOD2 signaling in inflammation and innate immunity
    • Damgaard RB, Nachbur U, Yabal M, Wong WW et al (2012) The Ubiquitin Ligase XIAP Recruits LUBAC for NOD2 signaling in inflammation and innate immunity. Mol Cell 46:746-758
    • (2012) Mol Cell , vol.46 , pp. 746-758
    • Damgaard, R.B.1    Nachbur, U.2    Yabal, M.3    Wong, W.W.4
  • 24
    • 84907210946 scopus 로고    scopus 로고
    • RIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis
    • Dannappel M, Vlantis K, Kumari S, Polykratis A et al (2014) RIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis. Nature 513:90-94
    • (2014) Nature , vol.513 , pp. 90-94
    • Dannappel, M.1    Vlantis, K.2    Kumari, S.3    Polykratis, A.4
  • 25
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux QL, Takahashi R, Salvesen GS, Reed JC (1997) X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388:300-304
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 26
    • 0032522738 scopus 로고    scopus 로고
    • IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases
    • Deveraux QL, Roy N, Stennicke HR, Van Arsdale T et al (1998) IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. EMBO J 17:2215-2223
    • (1998) EMBO J , vol.17 , pp. 2215-2223
    • Deveraux, Q.L.1    Roy, N.2    Stennicke, H.R.3    van Arsdale, T.4
  • 27
    • 0033215040 scopus 로고    scopus 로고
    • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    • Deveraux QL, Leo E, Stennicke HR, Welsh K et al (1999) Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J 18:5242-5251
    • (1999) EMBO J , vol.18 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicke, H.R.3    Welsh, K.4
  • 28
    • 84864318803 scopus 로고    scopus 로고
    • A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death
    • Dickens LS, Boyd RS, Jukes-Jones R, Hughes MA et al (2012) A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death. Mol Cell 47:291-305
    • (2012) Mol Cell , vol.47 , pp. 291-305
    • Dickens, L.S.1    Boyd, R.S.2    Jukes-Jones, R.3    Hughes, M.A.4
  • 29
    • 84978419608 scopus 로고    scopus 로고
    • Pore-forming activity and structural autoinhibition of the gasdermin family
    • Ding J, Wang K, Liu W, She Y et al (2016) Pore-forming activity and structural autoinhibition of the gasdermin family. Nature 535:111-116
    • (2016) Nature , vol.535 , pp. 111-116
    • Ding, J.1    Wang, K.2    Liu, W.3    She, Y.4
  • 30
    • 0036809813 scopus 로고    scopus 로고
    • IAP degradation: Decisive blow or altruistic sacrifice?
    • Ditzel M, Meier P (2002) IAP degradation: decisive blow or altruistic sacrifice? Trends Cell Biol 12:449-452
    • (2002) Trends Cell Biol , vol.12 , pp. 449-452
    • Ditzel, M.1    Meier, P.2
  • 31
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X (2000) Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102:33-42
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 32
    • 15844425961 scopus 로고    scopus 로고
    • A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors
    • Duckett CS, Nava VE, Gedrich RW, Clem RJ et al (1996) A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors. EMBO J 15:2685-2694
    • (1996) EMBO J , vol.15 , pp. 2685-2694
    • Duckett, C.S.1    Nava, V.E.2    Gedrich, R.W.3    Clem, R.J.4
  • 33
    • 78650300883 scopus 로고    scopus 로고
    • C-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling
    • Dynek JN, Goncharov T, Dueber EC, Fedorova AV et al (2010) c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling. EMBO J 29:4198-4209
    • (2010) EMBO J , vol.29 , pp. 4198-4209
    • Dynek, J.N.1    Goncharov, T.2    Dueber, E.C.3    Fedorova, A.V.4
  • 34
    • 33645640920 scopus 로고    scopus 로고
    • The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases
    • Eckelman BP, Salvesen GS (2006) The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases. J Biol Chem 281:3254-3260
    • (2006) J Biol Chem , vol.281 , pp. 3254-3260
    • Eckelman, B.P.1    Salvesen, G.S.2
  • 35
    • 50049125047 scopus 로고    scopus 로고
    • Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses
    • Ermolaeva MA, Michallet MC, Papadopoulou N, Utermöhlen O et al (2008) Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses. Nat Immunol 9:1037-1046
    • (2008) Nat Immunol , vol.9 , pp. 1037-1046
    • Ermolaeva, M.A.1    Michallet, M.C.2    Papadopoulou, N.3    Utermöhlen, O.4
  • 36
    • 84961262986 scopus 로고    scopus 로고
    • TRAF2 regulates TNF and NF-jB signalling to suppress apoptosis and skin inflammation independently of Sphingosine kinase-1
    • Etemadi N, Chopin M, Anderton H, Tanzer MC et al (2015) TRAF2 regulates TNF and NF-jB signalling to suppress apoptosis and skin inflammation independently of Sphingosine kinase-1. Elife 4:e10592
    • (2015) Elife , pp. 4
    • Etemadi, N.1    Chopin, M.2    Erton, H.3    Tanzer, M.C.4
  • 37
    • 77952912228 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding
    • Feltham R, Moulin M, Vince JE, Mace PD et al (2010) Tumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding. J Biol Chem 285:17525-17536
    • (2010) J Biol Chem , vol.285 , pp. 17525-17536
    • Feltham, R.1    Moulin, M.2    Vince, J.E.3    Mace, P.D.4
  • 38
    • 79955759159 scopus 로고    scopus 로고
    • Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization
    • Feltham R, Bettjeman B, Budhidarmo R, Mace PD et al (2011) Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization. J Biol Chem 286:17015-17028
    • (2011) J Biol Chem , vol.286 , pp. 17015-17028
    • Feltham, R.1    Bettjeman, B.2    Budhidarmo, R.3    Mace, P.D.4
  • 39
    • 79960922705 scopus 로고    scopus 로고
    • CIAPs block ripoptosome formation, a RIP1/Caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • Feoktistova M, Geserick P, Kellert B, Dimitrova DP et al (2011) cIAPs block ripoptosome formation, a RIP1/Caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol Cell 43:449-463
    • (2011) Mol Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1    Geserick, P.2    Kellert, B.3    Dimitrova, D.P.4
  • 40
    • 0345654358 scopus 로고    scopus 로고
    • Crystal structure of baculovirus P35: Role of a novel reactive site loop in apoptotic caspase inhibition
    • Fisher AJ, Cruz W, Zoog SJ, Schneider CL, Friesen PD (1999) Crystal structure of baculovirus P35: role of a novel reactive site loop in apoptotic caspase inhibition. EMBO J 18:2031-2039
    • (1999) EMBO J , vol.18 , pp. 2031-2039
    • Fisher, A.J.1    Cruz, W.2    Zoog, S.J.3    Schneider, C.L.4    Friesen, P.D.5
  • 41
    • 76149118435 scopus 로고    scopus 로고
    • Small-molecule pan-IAP antagonists: A patent review
    • Flygare JA, Fairbrother WJ (2010) Small-molecule pan-IAP antagonists: a patent review. Expert Opin Ther Pat 20:251-267
    • (2010) Expert Opin Ther Pat , vol.20 , pp. 251-267
    • Flygare, J.A.1    Fairbrother, W.J.2
  • 42
    • 0036341291 scopus 로고    scopus 로고
    • Smac agonists sensitize for Apo2L/TRAIL-or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo
    • Fulda S, Wick W, Weller M, Debatin KM (2002) Smac agonists sensitize for Apo2L/TRAIL-or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo. Nat Med 8:808-815
    • (2002) Nat Med , vol.8 , pp. 808-815
    • Fulda, S.1    Wick, W.2    Weller, M.3    Debatin, K.M.4
  • 43
    • 84962219519 scopus 로고    scopus 로고
    • Human monocytes engage an alternative inflammasome pathway
    • Gaidt MM, Ebert TS, Chauhan D, Schmidt T et al (2016) Human monocytes engage an alternative inflammasome pathway. Immunity 44:833-846
    • (2016) Immunity , vol.44 , pp. 833-846
    • Gaidt, M.M.1    Ebert, T.S.2    Chauhan, D.3    Schmidt, T.4
  • 44
    • 37549000486 scopus 로고    scopus 로고
    • A Smac mimetic rescue screen reveals roles for inhibitor of apoptosis proteins in tumor necrosis factor-alpha signaling
    • Gaither A, Porter D, Yao Y, Borawski J et al (2007) A Smac mimetic rescue screen reveals roles for inhibitor of apoptosis proteins in tumor necrosis factor-alpha signaling. Cancer Res 67:11493-11498
    • (2007) Cancer Res , vol.67 , pp. 11493-11498
    • Gaither, A.1    Porter, D.2    Yao, Y.3    Borawski, J.4
  • 45
    • 79954450542 scopus 로고    scopus 로고
    • New perspectives in TNF-R1-induced NF-jB signaling
    • Gentle IE, Silke J (2011) New perspectives in TNF-R1-induced NF-jB signaling. Adv Exp Med Biol, pp. 79-88
    • (2011) Adv Exp Med Biol , pp. 79-88
    • Gentle, I.E.1    Silke, J.2
  • 46
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • United States Gerlach B, Cordier SM, Schmukle AC, Emmerich CH et al (2011) Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471:591-596
    • (2011) Nature , vol.471 , pp. 591-596
    • United States Gerlach, B.1    Cordier, S.M.2    Schmukle, A.C.3    Emmerich, C.H.4
  • 47
    • 76149104286 scopus 로고    scopus 로고
    • Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment
    • Geserick P, Hupe M, Moulin M, Wong WW et al (2009) Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment. J Cell Biol 187:1037-1054
    • (2009) J Cell Biol , vol.187 , pp. 1037-1054
    • Geserick, P.1    Hupe, M.2    Moulin, M.3    Wong, W.W.4
  • 48
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • Haas TL, Emmerich CH, Gerlach B, Schmukle AC et al (2009) Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol Cell 36:831-844
    • (2009) Mol Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4
  • 49
    • 84883790050 scopus 로고    scopus 로고
    • Cytoplasmic LPS activates caspase-11: Implications in TLR4-independent endotoxic shock
    • Hagar JA, Powell DA, Aachoui Y, Ernst RK, Miao EA (2013) Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science 341:1250-1253
    • (2013) Science , vol.341 , pp. 1250-1253
    • Hagar, J.A.1    Powell, D.A.2    Aachoui, Y.3    Ernst, R.K.4    Miao, E.A.5
  • 51
    • 0029583176 scopus 로고
    • Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death
    • Hay BA, Wassarman DA, Rubin GM (1995) Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death. Cell 83:1253-1262
    • (1995) Cell , vol.83 , pp. 1253-1262
    • Hay, B.A.1    Wassarman, D.A.2    Rubin, G.M.3
  • 52
    • 84949091051 scopus 로고    scopus 로고
    • Gasdermin D is an executor of pyroptosis and required for interleukin-1b secretion
    • He WT, Wan H, Hu L, Chen P et al (2015) Gasdermin D is an executor of pyroptosis and required for interleukin-1b secretion. Cell Res 25:1285-1298
    • (2015) Cell Res , vol.25 , pp. 1285-1298
    • He, W.T.1    Wan, H.2    Hu, L.3    Chen, P.4
  • 53
    • 84942778286 scopus 로고    scopus 로고
    • CIAP2 supports viability of mice lacking cIAP1 and XIAP
    • Heard KN, Bertrand MJ, Barker PA (2015) cIAP2 supports viability of mice lacking cIAP1 and XIAP. EMBO J 34:2393-2395
    • (2015) EMBO J , vol.34 , pp. 2393-2395
    • Heard, K.N.1    Bertrand, M.J.2    Barker, P.A.3
  • 54
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
    • Hegde R, Srinivasula SM, Zhang Z, Wassell R et al (2002) Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction. J Biol Chem 277:432-438
    • (2002) J Biol Chem , vol.277 , pp. 432-438
    • Hegde, R.1    Srinivasula, S.M.2    Zhang, Z.3    Wassell, R.4
  • 55
    • 0141643236 scopus 로고    scopus 로고
    • The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein
    • Hegde R, Srinivasula SM, Datta P, Madesh M et al (2003) The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein. J Biol Chem 278:38699-38706
    • (2003) J Biol Chem , vol.278 , pp. 38699-38706
    • Hegde, R.1    Srinivasula, S.M.2    Datta, P.3    Madesh, M.4
  • 56
    • 84961225981 scopus 로고    scopus 로고
    • CYLD limits Lys63-and Met1-linked ubiquitin at receptor complexes to regulate innate immune signaling
    • Hrdinka M, Fiil BK, Zucca M, Leske D et al (2016) CYLD limits Lys63-and Met1-linked ubiquitin at receptor complexes to regulate innate immune signaling. Cell Rep 14:2846-2858
    • (2016) Cell Rep , vol.14 , pp. 2846-2858
    • Hrdinka, M.1    Fiil, B.K.2    Zucca, M.3    Leske, D.4
  • 57
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP. Differential roles of the linker versus the BIR domain
    • Huang Y, Park YC, Rich RL, Segal D et al (2001) Structural basis of caspase inhibition by XIAP. Differential roles of the linker versus the BIR domain. Cell 104:781-790
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4
  • 58
    • 84962604276 scopus 로고    scopus 로고
    • Co-operative and hierarchical binding of c-FLIP and Caspase-8: A unified model defines how c-FLIP isoforms differentially control cell fate
    • Hughes MA, Powley IR, Jukes-Jones R, Horn S et al (2016) Co-operative and hierarchical binding of c-FLIP and Caspase-8: a unified model defines how c-FLIP isoforms differentially control cell fate. Mol Cell 61:834-849
    • (2016) Mol Cell , vol.61 , pp. 834-849
    • Hughes, M.A.1    Powley, I.R.2    Jukes-Jones, R.3    Horn, S.4
  • 59
    • 33748747696 scopus 로고    scopus 로고
    • Genetically modified baculoviruses: A historical overview and future outlook
    • Inceoglu AB, Kamita SG, Hammock BD (2006) Genetically modified baculoviruses: a historical overview and future outlook. Adv Virus Res 68:323-360
    • (2006) Adv Virus Res , vol.68 , pp. 323-360
    • Inceoglu, A.B.1    Kamita, S.G.2    Hammock, B.D.3
  • 60
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro CA, Wing SS, Huang H, Leverson JD et al (1999) The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science 286:309-312
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4
  • 61
    • 79952811804 scopus 로고    scopus 로고
    • RIP3 mediates the embryonic lethality of caspase-8-deficient mice
    • Kaiser WJ, Upton JW, Long AB, Livingston-Rosanoff D et al (2011) RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature 471:368-372
    • (2011) Nature , vol.471 , pp. 368-372
    • Kaiser, W.J.1    Upton, J.W.2    Long, A.B.3    Livingston-Rosanoff, D.4
  • 62
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • Kang TB, Yang SH, Toth B, Kovalenko A, Wallach D (2013) Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 38:27-40
    • (2013) Immunity , vol.38 , pp. 27-40
    • Kang, T.B.1    Yang, S.H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5
  • 63
    • 84932601454 scopus 로고    scopus 로고
    • Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3
    • Kang S, Fernandes-Alnemri T, Rogers C, Mayes L et al (2015) Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3. Nat Commun 6:7515
    • (2015) Nat Commun , vol.6 , pp. 7515
    • Kang, S.1    Fernandes-Alnemri, T.2    Rogers, C.3    Mayes, L.4
  • 64
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • Kayagaki N, Warming S, Lamkanfi M, Vande Walle L et al (2011) Non-canonical inflammasome activation targets caspase-11. Nature 479:117-121
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1    Warming, S.2    Lamkanfi, M.3    Vande Walle, L.4
  • 65
    • 84883775365 scopus 로고    scopus 로고
    • Noncanonical inflammasome activation by intracellular LPS independent of TLR4
    • Kayagaki N, Wong MT, Stowe IB, Ramani SR et al (2013) Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 341:1246-1249
    • (2013) Science , vol.341 , pp. 1246-1249
    • Kayagaki, N.1    Wong, M.T.2    Stowe, I.B.3    Ramani, S.R.4
  • 66
    • 84942856523 scopus 로고    scopus 로고
    • Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
    • Kayagaki N, Stowe IB, Lee BL, O’Rourke K et al (2015) Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature 526:666-671
    • (2015) Nature , vol.526 , pp. 666-671
    • Kayagaki, N.1    Stowe, I.B.2    Lee, B.L.3    O’Rourke, K.4
  • 67
    • 84859464225 scopus 로고    scopus 로고
    • An inactivating caspase 11 passenger mutation originating from the 129 murine strain in mice targeted for c-IAP1
    • Kenneth NS, Younger JM, Hughes ED, Marcotte D, et al. (2012) An inactivating caspase 11 passenger mutation originating from the 129 murine strain in mice targeted for c-IAP1. Biochem J 443:355-359
    • (2012) Biochem J , vol.443 , pp. 355-359
    • Kenneth, N.S.1    Younger, J.M.2    Hughes, E.D.3    Marcotte, D.4
  • 70
    • 84990241371 scopus 로고    scopus 로고
    • Formation and removal of poly-ubiquitin chains in the regulation of tumor necrosis factor-induced gene activation and cell death
    • Kupka S, Reichert M, Draber P, Walczak H (2016a) Formation and removal of poly-ubiquitin chains in the regulation of tumor necrosis factor-induced gene activation and cell death. FEBS J 283:2626-2639
    • (2016) FEBS J , vol.283 , pp. 2626-2639
    • Kupka, S.1    Reichert, M.2    Draber, P.3    Walczak, H.4
  • 71
    • 84990210741 scopus 로고    scopus 로고
    • SPATA2-mediated binding of CYLD to HOIP enables CYLD recruitment to signaling complexes
    • Kupka S, De Miguel D, Draber P, Martino L et al (2016b) SPATA2-mediated binding of CYLD to HOIP enables CYLD recruitment to signaling complexes. Cell Rep 16:2271-2280
    • (2016) Cell Rep , vol.16 , pp. 2271-2280
    • Kupka, S.1    de Miguel, D.2    Draber, P.3    Martino, L.4
  • 72
    • 84928208327 scopus 로고    scopus 로고
    • XIAP deficiency syndrome in humans
    • Latour S, Aguilar C (2015) XIAP deficiency syndrome in humans. Semin Cell Dev Biol 39:115-123
    • (2015) Semin Cell Dev Biol , vol.39 , pp. 115-123
    • Latour, S.1    Aguilar, C.2
  • 73
    • 84923674191 scopus 로고    scopus 로고
    • RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL
    • Lawlor KE, Khan N, Mildenhall A, Gerlic M et al (2015) RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL. Nat Commun 6:6282
    • (2015) Nat Commun , vol.6 , pp. 6282
    • Lawlor, K.E.1    Khan, N.2    Mildenhall, A.3    Gerlic, M.4
  • 74
    • 0008206988 scopus 로고    scopus 로고
    • Traf2 is essential for jnk but not nf-kappa-b activation and regulates lymphocyte proliferation and survival
    • Lee SY, Reichlin A, Santana A, Sokol KA et al (1997) Traf2 is essential for jnk but not nf-kappa-b activation and regulates lymphocyte proliferation and survival. Immunity 7:703-713
    • (1997) Immunity , vol.7 , pp. 703-713
    • Lee, S.Y.1    Reichlin, A.2    Santana, A.3    Sokol, K.A.4
  • 75
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM et al (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4
  • 76
    • 4444243683 scopus 로고    scopus 로고
    • A small molecule Smac mimic potentiates TRAIL-and TNFa-mediated cell death
    • Li L, Thomas RM, Suzuki H, De Brabander JK et al (2004) A small molecule Smac mimic potentiates TRAIL-and TNFa-mediated cell death. Science 305:1471-1474
    • (2004) Science , vol.305 , pp. 1471-1474
    • Li, L.1    Thomas, R.M.2    Suzuki, H.3    de Brabander, J.K.4
  • 77
    • 13344278692 scopus 로고    scopus 로고
    • Suppression of apoptosis in mammalian cells by naip and a related family of iap genes
    • Liston P, Roy N, Tamai K, Lefebvre C et al (1996) Suppression of apoptosis in mammalian cells by naip and a related family of iap genes. Nature 379:349-353
    • (1996) Nature , vol.379 , pp. 349-353
    • Liston, P.1    Roy, N.2    Tamai, K.3    Lefebvre, C.4
  • 80
    • 0037016707 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a Reaper-like motif
    • Martins LM, Iaccarino I, Tenev T, Gschmeissner S et al (2002) The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a Reaper-like motif. J Biol Chem 277:439-444
    • (2002) J Biol Chem , vol.277 , pp. 439-444
    • Martins, L.M.1    Iaccarino, I.2    Tenev, T.3    Gschmeissner, S.4
  • 81
    • 84870950668 scopus 로고    scopus 로고
    • NLRP1 inflammasome activation induces pyroptosis of hematopoietic progenitor cells
    • Masters SL, Gerlic M, Metcalf D, Preston S et al (2012) NLRP1 inflammasome activation induces pyroptosis of hematopoietic progenitor cells. Immunity 37:1009-1023
    • (2012) Immunity , vol.37 , pp. 1009-1023
    • Masters, S.L.1    Gerlic, M.2    Metcalf, D.3    Preston, S.4
  • 82
    • 84969626016 scopus 로고    scopus 로고
    • Activation of concurrent apoptosis and necroptosis by SMAC mimetics for the treatment of refractory and relapsed ALL
    • McComb S, Aguadé-Gorgorió J, Harder L, Marovca B et al (2016) Activation of concurrent apoptosis and necroptosis by SMAC mimetics for the treatment of refractory and relapsed ALL. Sci Transl Med 8:339ra70
    • (2016) Sci Transl Med , vol.8
    • McComb, S.1    Aguadé-Gorgorió, J.2    Harder, L.3    Marovca, B.4
  • 83
    • 80052626087 scopus 로고    scopus 로고
    • The NLRP3 inflammasome in health and disease: The good, the bad and the ugly
    • Menu P, Vince JE (2011) The NLRP3 inflammasome in health and disease: the good, the bad and the ugly. Clin Exp Immunol 166:1-15
    • (2011) Clin Exp Immunol , vol.166 , pp. 1-15
    • Menu, P.1    Vince, J.E.2
  • 84
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • Miao EA, Leaf IA, Treuting PM, Mao DP et al (2010) Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol 11:1136-1142
    • (2010) Nat Immunol , vol.11 , pp. 1136-1142
    • Miao, E.A.1    Leaf, I.A.2    Treuting, P.M.3    Mao, D.P.4
  • 86
    • 79959870486 scopus 로고    scopus 로고
    • Apoptotic and non-apoptotic caspase functions in neural development
    • Miura M (2011) Apoptotic and non-apoptotic caspase functions in neural development. Neurochem Res 36:1253-1260
    • (2011) Neurochem Res , vol.36 , pp. 1253-1260
    • Miura, M.1
  • 87
    • 84859424337 scopus 로고    scopus 로고
    • IAPs limit activation of RIP kinases by TNF receptor 1 during development
    • Moulin M, Anderton H, Voss AK, Thomas T et al (2012) IAPs limit activation of RIP kinases by TNF receptor 1 during development. EMBO J 31:1679-1691
    • (2012) EMBO J , vol.31 , pp. 1679-1691
    • Moulin, M.1    Erton, H.2    Voss, A.K.3    Thomas, T.4
  • 89
    • 84879596906 scopus 로고    scopus 로고
    • K+ efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • Muñoz-Planillo R, Kuffa P, Martínez-Colón G, Smith BL et al (2013) K+ efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity 38:1142-1153
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Muñoz-Planillo, R.1    Kuffa, P.2    Martínez-Colón, G.3    Smith, B.L.4
  • 90
    • 84890824095 scopus 로고    scopus 로고
    • Local apoptosis modulates early mammalian brain development through the elimination of morphogen-producing cells
    • Nonomura K, Yamaguchi Y, Hamachi M, Koike M et al (2013) Local apoptosis modulates early mammalian brain development through the elimination of morphogen-producing cells. Dev Cell 27:621-634
    • (2013) Dev Cell , vol.27 , pp. 621-634
    • Nonomura, K.1    Yamaguchi, Y.2    Hamachi, M.3    Koike, M.4
  • 91
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis
    • Oberst A, Dillon CP, Weinlich R, McCormick LL et al (2011) Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature 471:363-367
    • (2011) Nature , vol.471 , pp. 363-367
    • Oberst, A.1    Dillon, C.P.2    Weinlich, R.3    McCormick, L.L.4
  • 92
    • 11844275937 scopus 로고    scopus 로고
    • XIAP-deficiency leads to delayed lobuloalveolar development in the mammary gland
    • Olayioye MA, Kaufmann H, Pakusch M, Vaux DL et al (2005) XIAP-deficiency leads to delayed lobuloalveolar development in the mammary gland. Cell Death Differ 12:87-90
    • (2005) Cell Death Differ , vol.12 , pp. 87-90
    • Olayioye, M.A.1    Kaufmann, H.2    Pakusch, M.3    Vaux, D.L.4
  • 93
    • 0035399637 scopus 로고    scopus 로고
    • Programmed cell death of developing mammalian neurons after genetic deletion of caspases
    • Oppenheim RW, Flavell RA, Vinsant S, Prevette D et al (2001) Programmed cell death of developing mammalian neurons after genetic deletion of caspases. J Neurosci 21:4752-4760
    • (2001) J Neurosci , vol.21 , pp. 4752-4760
    • Oppenheim, R.W.1    Flavell, R.A.2    Vinsant, S.3    Prevette, D.4
  • 94
    • 84960904302 scopus 로고    scopus 로고
    • The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles
    • Orme MH, Liccardi G, Moderau N, Feltham R et al (2016) The unconventional myosin CRINKLED and its mammalian orthologue MYO7A regulate caspases in their signalling roles. Nat Commun 7:10972
    • (2016) Nat Commun , vol.7 , pp. 10972
    • Orme, M.H.1    Liccardi, G.2    Moderau, N.3    Feltham, R.4
  • 95
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park YC, Burkitt V, Villa AR, Tong L, Wu H (1999) Structural basis for self-association and receptor recognition of human TRAF2. Nature 398:533-538
    • (1999) Nature , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3    Tong, L.4    Wu, H.5
  • 96
    • 0034705271 scopus 로고    scopus 로고
    • A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction
    • Park YC, Ye H, Hsia C, Segal D et al (2000) A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Cell 101:777-787
    • (2000) Cell , vol.101 , pp. 777-787
    • Park, Y.C.1    Ye, H.2    Hsia, C.3    Segal, D.4
  • 97
    • 84922602504 scopus 로고    scopus 로고
    • Necroptosis and its role in inflammation
    • Pasparakis M, Vandenabeele P (2015) Necroptosis and its role in inflammation. Nature 517:311-320
    • (2015) Nature , vol.517 , pp. 311-320
    • Pasparakis, M.1    Vandenabeele, P.2
  • 98
    • 84907995994 scopus 로고    scopus 로고
    • HOIP deficiency causes embryonic lethality by aberrant TNFR1-mediated endothelial cell death
    • Peltzer N, Rieser E, Taraborrelli L, Draber P et al (2014) HOIP deficiency causes embryonic lethality by aberrant TNFR1-mediated endothelial cell death. Cell Rep 9:153-165
    • (2014) Cell Rep , vol.9 , pp. 153-165
    • Peltzer, N.1    Rieser, E.2    Taraborrelli, L.3    Draber, P.4
  • 99
    • 35948994157 scopus 로고    scopus 로고
    • Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis
    • Petersen SL, Wang L, Yalcin-Chin A, Li L et al (2007) Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis. Cancer Cell 12:445-456
    • (2007) Cancer Cell , vol.12 , pp. 445-456
    • Petersen, S.L.1    Wang, L.2    Yalcin-Chin, A.3    Li, L.4
  • 100
    • 50149089360 scopus 로고    scopus 로고
    • The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors
    • Pobezinskaya YL, Kim YS, Choksi S, Morgan MJ et al (2008) The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors. Nat Immunol 9:1047-1054
    • (2008) Nat Immunol , vol.9 , pp. 1047-1054
    • Pobezinskaya, Y.L.1    Kim, Y.S.2    Choksi, S.3    Morgan, M.J.4
  • 101
    • 84901422731 scopus 로고    scopus 로고
    • RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis
    • Rickard JA, O’Donnell JA, Evans JM, Lalaoui N et al (2014) RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis. Cell 157:1175-1188
    • (2014) Cell , vol.157 , pp. 1175-1188
    • Rickard, J.A.1    O’Donnell, J.A.2    Evans, J.M.3    Lalaoui, N.4
  • 102
    • 0035831019 scopus 로고    scopus 로고
    • Structural basis for the inhibition of caspase-3 by XIAP
    • Riedl SJ, Renatus M, Schwarzenbacher R, Zhou Q et al (2001) Structural basis for the inhibition of caspase-3 by XIAP. Cell 104:791-800
    • (2001) Cell , vol.104 , pp. 791-800
    • Riedl, S.J.1    Renatus, M.2    Schwarzenbacher, R.3    Zhou, Q.4
  • 103
    • 33750597717 scopus 로고    scopus 로고
    • XIAP deficiency in humans causes an X-linked lymphoproliferative syndrome
    • Rigaud S, Fondanèche MC, Lambert N, Pasquier B et al (2006) XIAP deficiency in humans causes an X-linked lymphoproliferative syndrome. Nature 444:110-114
    • (2006) Nature , vol.444 , pp. 110-114
    • Rigaud, S.1    Fondanèche, M.C.2    Lambert, N.3    Pasquier, B.4
  • 104
    • 84919898250 scopus 로고    scopus 로고
    • Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA
    • Rongvaux A, Jackson R, Harman CC, Li T et al (2014) Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA. Cell 159:1563-1577
    • (2014) Cell , vol.159 , pp. 1563-1577
    • Rongvaux, A.1    Jackson, R.2    Harman, C.C.3    Li, T.4
  • 105
    • 0029595282 scopus 로고
    • The TNF-R2-TRAF signaling complex contains two novel proteins related to baculoviral-inhibitor of apoptosis proteins
    • Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV (1995) The TNF-R2-TRAF signaling complex contains two novel proteins related to baculoviral-inhibitor of apoptosis proteins. Cell 83:1243-1252
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 106
    • 0030698127 scopus 로고    scopus 로고
    • The c-iap-1 and c-iap-2 proteins are direct inhibitors of specific caspases
    • Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC (1997) The c-iap-1 and c-iap-2 proteins are direct inhibitors of specific caspases. EMBO J 16:6914-6925
    • (1997) EMBO J , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 107
    • 33644853217 scopus 로고    scopus 로고
    • Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of TRAF2 and Smac
    • Samuel T, Welsh K, Lober T, Togo SH et al (2006) Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of TRAF2 and Smac. J Biol Chem 281:1080-1090
    • (2006) J Biol Chem , vol.281 , pp. 1080-1090
    • Samuel, T.1    Welsh, K.2    Lober, T.3    Togo, S.H.4
  • 108
    • 50049110244 scopus 로고    scopus 로고
    • Regulation of apoptosis by XIAP ubiquitin-ligase activity
    • Schile AJ, García-Fernández M, Steller H (2008) Regulation of apoptosis by XIAP ubiquitin-ligase activity. Genes Dev 22:2256-2266
    • (2008) Genes Dev , vol.22 , pp. 2256-2266
    • Schile, A.J.1    García-Fernández, M.2    Steller, H.3
  • 109
    • 84945568831 scopus 로고    scopus 로고
    • An apoptotic ‘Eat Me’ signal: Phosphatidylserine exposure
    • Segawa K, Nagata S (2015) An apoptotic ‘Eat Me’ signal: phosphatidylserine exposure. Trends Cell Biol 25:639-650
    • (2015) Trends Cell Biol , vol.25 , pp. 639-650
    • Segawa, K.1    Nagata, S.2
  • 110
    • 84942892037 scopus 로고    scopus 로고
    • Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
    • Shi J, Zhao Y, Wang K, Shi X et al (2015) Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 526:660-665
    • (2015) Nature , vol.526 , pp. 660-665
    • Shi, J.1    Zhao, Y.2    Wang, K.3    Shi, X.4
  • 111
    • 0030447483 scopus 로고    scopus 로고
    • The tumor necrosis factor receptor 2 signal transducers traf2 and c-iap1 are components of the tumor necrosis factor receptor 1 signaling complex
    • Shu HB, Takeuchi M, Goeddel DV (1996) The tumor necrosis factor receptor 2 signal transducers traf2 and c-iap1 are components of the tumor necrosis factor receptor 1 signaling complex. Proc Natl Acad Sci USA 93:13973-13978
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13973-13978
    • Shu, H.B.1    Takeuchi, M.2    Goeddel, D.V.3
  • 112
    • 77449147556 scopus 로고    scopus 로고
    • Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs
    • Silke J, Brink R (2010) Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs. Cell Death Differ 17:35-45
    • (2010) Cell Death Differ , vol.17 , pp. 35-45
    • Silke, J.1    Brink, R.2
  • 113
    • 85003520631 scopus 로고    scopus 로고
    • In the midst of life-cell death: What is it, what is it good for, and how to study it
    • pdb.top070508
    • Silke J, Johnstone RW (2016) In the midst of life-cell death: what is it, what is it good for, and how to study it. Cold Spring Harb Protoc 2016:pdb.top070508
    • (2016) Cold Spring Harb Protoc
    • Silke, J.1    Johnstone, R.W.2
  • 114
    • 84875138006 scopus 로고    scopus 로고
    • Inhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammation
    • (United States)
    • Silke J, Meier P (2013) Inhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammation. Cold Spring Harb Perspect Biol 5:2 (United States)
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , pp. 2
    • Silke, J.1    Meier, P.2
  • 115
    • 84925364966 scopus 로고    scopus 로고
    • IAPs and necroptotic cell death
    • Shen HM, Vandenabeele P (eds), Springer, New York
    • Silke J, Vaux D (2014) IAPs and necroptotic cell death. In: Shen HM, Vandenabeele P (eds) Necrotic cell death. Springer, New York, pp 57-77
    • (2014) Necrotic Cell Death , pp. 57-77
    • Silke, J.1    Vaux, D.2
  • 116
    • 84928204838 scopus 로고    scopus 로고
    • IAP gene deletion and conditional knockout models
    • Silke J, Vaux DL (2015) IAP gene deletion and conditional knockout models. Semin Cell Dev Biol 39:97-105
    • (2015) Semin Cell Dev Biol , vol.39 , pp. 97-105
    • Silke, J.1    Vaux, D.L.2
  • 117
    • 17744369252 scopus 로고    scopus 로고
    • Sequence as well as functional similarity for DIABLO/smac and grim, reaper and hid
    • Silke J, Verhagen AM, Ekert PG, Vaux DL (2000) Sequence as well as functional similarity for DIABLO/smac and grim, reaper and hid? Cell Death Differ 7:1275
    • (2000) Cell Death Differ , vol.7 , pp. 1275
    • Silke, J.1    Verhagen, A.M.2    Ekert, P.G.3    Vaux, D.L.4
  • 118
    • 0035876176 scopus 로고    scopus 로고
    • Direct inhibition of caspase 3 is dispensable for the anti-apoptotic activity of XIAP
    • Silke J, Ekert PG, Day CL, Hawkins CJ et al (2001) Direct inhibition of caspase 3 is dispensable for the anti-apoptotic activity of XIAP. EMBO J 20:3114-3123
    • (2001) EMBO J , vol.20 , pp. 3114-3123
    • Silke, J.1    Ekert, P.G.2    Day, C.L.3    Hawkins, C.J.4
  • 119
    • 0034680876 scopus 로고    scopus 로고
    • Molecular determinants of the caspase-promoting activity of smac/DIABLO and its role in the death receptor pathway
    • Srinivasula SM, Datta P, Fan XJ, Fernandes-Alnemri T et al (2000) Molecular determinants of the caspase-promoting activity of smac/DIABLO and its role in the death receptor pathway. J Biol Chem 275:36152-36157
    • (2000) J Biol Chem , vol.275 , pp. 36152-36157
    • Srinivasula, S.M.1    Datta, P.2    Fan, X.J.3    Fernandes-Alnemri, T.4
  • 120
    • 84885015530 scopus 로고    scopus 로고
    • Smac mimetic and demethylating agents synergistically trigger cell death in acute myeloid leukemia cells and overcome apoptosis resistance by inducing necroptosis
    • Steinhart L, Belz K, Fulda S (2013) Smac mimetic and demethylating agents synergistically trigger cell death in acute myeloid leukemia cells and overcome apoptosis resistance by inducing necroptosis. Cell Death Dis 4:e802
    • (2013) Cell Death Dis , pp. 4
    • Steinhart, L.1    Belz, K.2    Fulda, S.3
  • 121
    • 84937519269 scopus 로고    scopus 로고
    • Identification of a novel synergistic induction of cell death by Smac mimetic and HDAC inhibitors in acute myeloid leukemia cells
    • Steinwascher S, Nugues AL, Schoeneberger H, Fulda S (2015) Identification of a novel synergistic induction of cell death by Smac mimetic and HDAC inhibitors in acute myeloid leukemia cells. Cancer Lett 366:32-43
    • (2015) Cancer Lett , vol.366 , pp. 32-43
    • Steinwascher, S.1    Nugues, A.L.2    Schoeneberger, H.3    Fulda, S.4
  • 122
    • 0033592470 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP
    • Sun C, Cai M, Gunasekera AH, Meadows RP et al (1999) NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP. Nature 401:818-821
    • (1999) Nature , vol.401 , pp. 818-821
    • Sun, C.1    Cai, M.2    Gunasekera, A.H.3    Meadows, R.P.4
  • 123
    • 57349147782 scopus 로고    scopus 로고
    • Design of small-molecule peptidic and nonpeptidic Smac mimetics
    • Sun H, Nikolovska-Coleska Z, Yang CY, Qian D et al (2008) Design of small-molecule peptidic and nonpeptidic Smac mimetics. Acc Chem Res 41:1264-1277
    • (2008) Acc Chem Res , vol.41 , pp. 1264-1277
    • Sun, H.1    Nikolovska-Coleska, Z.2    Yang, C.Y.3    Qian, D.4
  • 124
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y, Imai Y, Nakayama H, Takahashi K et al (2001) A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell 8:613-621
    • (2001) Mol Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4
  • 125
    • 0035965232 scopus 로고    scopus 로고
    • Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-j B activation and protection from cell death
    • Tada K, Okazaki T, Sakon S, Kobarai T et al (2001) Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-j B activation and protection from cell death. J Biol Chem 276:36530-36534
    • (2001) J Biol Chem , vol.276 , pp. 36530-36534
    • Tada, K.1    Okazaki, T.2    Sakon, S.3    Kobarai, T.4
  • 126
    • 0032478717 scopus 로고    scopus 로고
    • A single BIR domain of XIAP sufficient for inhibiting caspases
    • Takahashi R, Deveraux Q, Tamm I, Welsh K et al (1998) A single BIR domain of XIAP sufficient for inhibiting caspases. J Biol Chem 273:7787-7790
    • (1998) J Biol Chem , vol.273 , pp. 7787-7790
    • Takahashi, R.1    Deveraux, Q.2    Tamm, I.3    Welsh, K.4
  • 127
    • 84907197966 scopus 로고    scopus 로고
    • RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis
    • Takahashi N, Vereecke L, Bertrand MJM, Duprez L et al (2014) RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis. Nature 513:95-99
    • (2014) Nature , vol.513 , pp. 95-99
    • Takahashi, N.1    Vereecke, L.2    Bertrand, M.3    Duprez, L.4
  • 128
    • 79960921946 scopus 로고    scopus 로고
    • The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • Tenev T, Bianchi K, Darding M, Broemer M et al (2011) The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol Cell 43:432-448
    • (2011) Mol Cell , vol.43 , pp. 432-448
    • Tenev, T.1    Bianchi, K.2    Darding, M.3    Broemer, M.4
  • 129
    • 84979523727 scopus 로고    scopus 로고
    • More to life than NF-jB in TNFR1 signaling
    • Ting AT, Bertrand MJ (2016) More to life than NF-jB in TNFR1 signaling. Trends Immunol 37:535-545
    • (2016) Trends Immunol , vol.37 , pp. 535-545
    • Ting, A.T.1    Bertrand, M.J.2
  • 130
    • 0029953942 scopus 로고    scopus 로고
    • Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind TRAFs
    • Uren AG, Pakusch M, Hawkins CJ, Puls KL, Vaux DL (1996) Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind TRAFs. Proc Natl Acad Sci USA 93:4974-4978
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4974-4978
    • Uren, A.G.1    Pakusch, M.2    Hawkins, C.J.3    Puls, K.L.4    Vaux, D.L.5
  • 131
    • 33749389926 scopus 로고    scopus 로고
    • The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-jB activation independently of TRAF1 and TRAF2
    • Varfolomeev E, Wayson SM, Dixit VM, Fairbrother WJ, Vucic D (2006) The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-jB activation independently of TRAF1 and TRAF2. J Biol Chem 281:29022-29029
    • (2006) J Biol Chem , vol.281 , pp. 29022-29029
    • Varfolomeev, E.1    Wayson, S.M.2    Dixit, V.M.3    Fairbrother, W.J.4    Vucic, D.5
  • 132
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs, NF-jB activation, and TNFa-dependent apoptosis
    • Varfolomeev E, Blankenship JW, Wayson SM, Fedorova AV et al (2007) IAP antagonists induce autoubiquitination of c-IAPs, NF-jB activation, and TNFa-dependent apoptosis. Cell 131:669-681
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1    Blankenship, J.W.2    Wayson, S.M.3    Fedorova, A.V.4
  • 133
    • 54049155149 scopus 로고    scopus 로고
    • C-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFa)-induced NF-jB activation
    • Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN et al (2008) c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFa)-induced NF-jB activation. J Biol Chem 283:24295-24299
    • (2008) J Biol Chem , vol.283 , pp. 24295-24299
    • Varfolomeev, E.1    Goncharov, T.2    Fedorova, A.V.3    Dynek, J.N.4
  • 134
    • 84858627919 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis are global regulators of NF-jB and MAPK activation by members of the TNF family of receptors
    • Varfolomeev E, Goncharov T, Maecker H, Zobel K et al (2012) Cellular inhibitors of apoptosis are global regulators of NF-jB and MAPK activation by members of the TNF family of receptors. Sci Signal 5:ra22
    • (2012) Sci Signal , vol.5
    • Varfolomeev, E.1    Goncharov, T.2    Maecker, H.3    Zobel, K.4
  • 135
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M, Silke J et al (2000) Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102:42-53
    • (2000) Cell , vol.102 , pp. 42-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4
  • 136
    • 0037016686 scopus 로고    scopus 로고
    • HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins
    • Verhagen AM, Silke J, Ekert PG, Pakusch M et al (2002) HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins. J Biol Chem 277:445-454
    • (2002) J Biol Chem , vol.277 , pp. 445-454
    • Verhagen, A.M.1    Silke, J.2    Ekert, P.G.3    Pakusch, M.4
  • 137
    • 33846251849 scopus 로고    scopus 로고
    • Identification of mammalian mitochondrial proteins that interact with IAPs via N-terminal IAP binding motifs
    • Verhagen AM, Kratina TK, Hawkins CJ, Silke J et al (2007) Identification of mammalian mitochondrial proteins that interact with IAPs via N-terminal IAP binding motifs. Cell Death Diff 14:348-357
    • (2007) Cell Death Diff , vol.14 , pp. 348-357
    • Verhagen, A.M.1    Kratina, T.K.2    Hawkins, C.J.3    Silke, J.4
  • 138
    • 36148954336 scopus 로고    scopus 로고
    • IAP antagonists target cIAP1 to induce TNFa-dependent apoptosis
    • Vince JE, Wong WW, Khan N, Feltham R et al (2007) IAP antagonists target cIAP1 to induce TNFa-dependent apoptosis. Cell 131:682-693
    • (2007) Cell , vol.131 , pp. 682-693
    • Vince, J.E.1    Wong, W.W.2    Khan, N.3    Feltham, R.4
  • 139
    • 72149117664 scopus 로고    scopus 로고
    • TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-{j}B and to prevent TNF-induced apoptosis
    • Vince JE, Pantaki D, Feltham R, Mace PD et al (2009) TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-{j}B and to prevent TNF-induced apoptosis. J Biol Chem 284:35906-35915
    • (2009) J Biol Chem , vol.284 , pp. 35906-35915
    • Vince, J.E.1    Pantaki, D.2    Feltham, R.3    Mace, P.D.4
  • 140
    • 84857404572 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation
    • Vince JE, Wong WW, Gentle I, Lawlor KE et al (2012) Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity 36:215-227
    • (2012) Immunity , vol.36 , pp. 215-227
    • Vince, J.E.1    Wong, W.W.2    Gentle, I.3    Lawlor, K.E.4
  • 141
    • 0030928651 scopus 로고    scopus 로고
    • Inhibition of reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs)
    • Vucic D, Kaiser WJ, Harvey AJ, Miller LK (1997) Inhibition of reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs). Proc Natl Acad Sci USA 94:10183-10188
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10183-10188
    • Vucic, D.1    Kaiser, W.J.2    Harvey, A.J.3    Miller, L.K.4
  • 142
    • 84878258373 scopus 로고    scopus 로고
    • Cytokine profiles in children with primary Epstein-Barr virus infection
    • Wada T, Muraoka M, Yokoyama T, Toma T et al (2013) Cytokine profiles in children with primary Epstein-Barr virus infection. Pediatr Blood Cancer 60:E46-E48
    • (2013) Pediatr Blood Cancer , vol.60
    • Wada, T.1    Muraoka, M.2    Yokoyama, T.3    Toma, T.4
  • 143
    • 84984904321 scopus 로고    scopus 로고
    • SPATA2 links CYLD to the TNF-a receptor signaling complex and modulates the receptor signaling outcomes
    • Wagner SA, Satpathy S, Beli P, Choudhary C (2016) SPATA2 links CYLD to the TNF-a receptor signaling complex and modulates the receptor signaling outcomes. EMBO J 35:1868-1884
    • (2016) EMBO J , vol.35 , pp. 1868-1884
    • Wagner, S.A.1    Satpathy, S.2    Beli, P.3    Choudhary, C.4
  • 144
    • 0028200532 scopus 로고
    • Genetic control of programmed cell death in Drosophila
    • White K, Grether ME, Abrams JM, Young L et al (1994) Genetic control of programmed cell death in Drosophila. Science 264:677-683
    • (1994) Science , vol.264 , pp. 677-683
    • White, K.1    Grether, M.E.2    Abrams, J.M.3    Young, L.4
  • 145
    • 84919884654 scopus 로고    scopus 로고
    • Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production
    • White MJ, McArthur K, Metcalf D, Lane RM et al (2014) Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production. Cell 159:1549-1562
    • (2014) Cell , vol.159 , pp. 1549-1562
    • White, M.J.1    McArthur, K.2    Metcalf, D.3    Lane, R.M.4
  • 146
    • 85019078783 scopus 로고    scopus 로고
    • Loss of XIAP facilitates switch to TNFa-induced necroptosis in mouse neutrophils
    • Wicki S, Gurzeler U, Wei-Lynn Wong W, Jost PJ et al (2016) Loss of XIAP facilitates switch to TNFa-induced necroptosis in mouse neutrophils. Cell Death Dis 7:e2422
    • (2016) Cell Death Dis , pp. 7
    • Wicki, S.1    Gurzeler, U.2    Wei-Lynn Wong, W.3    Jost, P.J.4
  • 147
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley SR, Schooley K, Smolak PJ, Din WS et al (1995) Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 3:673-682
    • (1995) Immunity , vol.3 , pp. 673-682
    • Wiley, S.R.1    Schooley, K.2    Smolak, P.J.3    Din, W.S.4
  • 148
    • 76749132616 scopus 로고    scopus 로고
    • RIPK1 is not essential for TNFR1-induced activation of NF-jB
    • Wong WW, Gentle IE, Nachbur U, Anderton H et al (2010) RIPK1 is not essential for TNFR1-induced activation of NF-jB. Cell Death Differ 17:482-487
    • (2010) Cell Death Differ , vol.17 , pp. 482-487
    • Wong, W.W.1    Gentle, I.E.2    Nachbur, U.3    Erton, H.4
  • 149
    • 84899112438 scopus 로고    scopus 로고
    • CIAPs and XIAP regulate myelopoiesis through cytokine production in an RIPK1-and RIPK3-dependent manner
    • Wong WW, Vince JE, Lalaoui N, Lawlor KE et al (2014) cIAPs and XIAP regulate myelopoiesis through cytokine production in an RIPK1-and RIPK3-dependent manner. Blood 123:2562-2572
    • (2014) Blood , vol.123 , pp. 2562-2572
    • Wong, W.W.1    Vince, J.E.2    Lalaoui, N.3    Lawlor, K.E.4
  • 150
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • Wu G, Chai JJ, Suber TL, Wu JW et al (2000) Structural basis of IAP recognition by Smac/DIABLO. Nature 408:1008-1012
    • (2000) Nature , vol.408 , pp. 1008-1012
    • Wu, G.1    Chai, J.J.2    Suber, T.L.3    Wu, J.W.4
  • 151
    • 84903480849 scopus 로고    scopus 로고
    • XIAP restricts TNF-and RIP3-dependent cell death and inflammasome activation
    • Yabal M, Müller N, Adler H, Knies N et al (2014) XIAP restricts TNF-and RIP3-dependent cell death and inflammasome activation. Cell Rep 7:1796-1808
    • (2014) Cell Rep , vol.7 , pp. 1796-1808
    • Yabal, M.1    Müller, N.2    Adler, H.3    Knies, N.4
  • 152
    • 84923241393 scopus 로고    scopus 로고
    • Programmed cell death in neurodevelopment
    • Yamaguchi Y, Miura M (2015) Programmed cell death in neurodevelopment. Dev Cell 32:478-490
    • (2015) Dev Cell , vol.32 , pp. 478-490
    • Yamaguchi, Y.1    Miura, M.2
  • 153
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang Y, Fang S, Jensen JP, Weissman AM, Ashwell JD (2000) Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288:874-877
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 154
    • 0033197872 scopus 로고    scopus 로고
    • The structural basis for the recognition of diverse receptor sequences by TRAF2
    • Ye H, Park YC, Kreishman M, Kieff E, Wu H (1999) The structural basis for the recognition of diverse receptor sequences by TRAF2. Mol Cell 4:321-330
    • (1999) Mol Cell , vol.4 , pp. 321-330
    • Ye, H.1    Park, Y.C.2    Kreishman, M.3    Kieff, E.4    Wu, H.5
  • 155
    • 0031463025 scopus 로고    scopus 로고
    • Early lethality, functional nf-kb activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice
    • Yeh WC, Shahinian A, Speiser D, Kraunus J et al (1997) Early lethality, functional nf-kb activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity 7:715-725
    • (1997) Immunity , vol.7 , pp. 715-725
    • Yeh, W.C.1    Shahinian, A.2    Speiser, D.3    Kraunus, J.4
  • 156
    • 84964434465 scopus 로고    scopus 로고
    • An endogenous caspase-11 ligand elicits interleukin-1 release from living dendritic cells
    • Zanoni I, Tan Y, Di Gioia M, Broggi A et al (2016) An endogenous caspase-11 ligand elicits interleukin-1 release from living dendritic cells. Science 352:1232-1236
    • (2016) Science , vol.352 , pp. 1232-1236
    • Zanoni, I.1    Tan, Y.2    Di Gioia, M.3    Broggi, A.4
  • 157
    • 79952780505 scopus 로고    scopus 로고
    • Functional complementation between FADD and RIP1 in embryos and lymphocytes
    • Zhang H, Zhou X, McQuade T, Li J et al (2011) Functional complementation between FADD and RIP1 in embryos and lymphocytes. Nature 471:373-376
    • (2011) Nature , vol.471 , pp. 373-376
    • Zhang, H.1    Zhou, X.2    McQuade, T.3    Li, J.4
  • 158
    • 84964045814 scopus 로고    scopus 로고
    • TRAF2 exerts opposing effects on basal and TNFa-induced activation of the classic IKK complex in hematopoietic cells in mice
    • Zhang L, Blackwell K, Workman LM, Gibson-Corley KN et al (2016) TRAF2 exerts opposing effects on basal and TNFa-induced activation of the classic IKK complex in hematopoietic cells in mice. J Cell Sci 129:1455-1467
    • (2016) J Cell Sci , vol.129 , pp. 1455-1467
    • Zhang, L.1    Blackwell, K.2    Workman, L.M.3    Gibson-Corley, K.N.4
  • 160
    • 77950352082 scopus 로고    scopus 로고
    • Crystal structures of the TRAF2: CIAP2 and the TRAF1: TRAF2: CIAP2 complexes: Affinity, specificity, and regulation
    • Zheng C, Kabaleeswaran V, Wang Y, Cheng G, Wu H (2010) Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation. Mol Cell 38:101-113
    • (2010) Mol Cell , vol.38 , pp. 101-113
    • Zheng, C.1    Kabaleeswaran, V.2    Wang, Y.3    Cheng, G.4    Wu, H.5
  • 161
    • 0032575309 scopus 로고    scopus 로고
    • Interaction of the baculovirus anti-apoptotic protein p35 with caspases—specificity, kinetics, and characterization of the caspase/p35 complex
    • Zhou Q, Krebs JF, Snipas SJ, Price A et al (1998) Interaction of the baculovirus anti-apoptotic protein p35 with caspases—specificity, kinetics, and characterization of the caspase/p35 complex. Biochemistry 37:10757-10765
    • (1998) Biochemistry , vol.37 , pp. 10757-10765
    • Zhou, Q.1    Krebs, J.F.2    Snipas, S.J.3    Price, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.