메뉴 건너뛰기




Volumn 7, Issue 11, 2008, Pages 1511-1521

(Un)expected roles of c-IAPs in apoptotic and NFκB signaling pathways

Author keywords

Apoptosis; c IAP; IAP; NF B; NIK; TNF

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN 1; INHIBITOR OF APOPTOSIS PROTEIN 2; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2;

EID: 45849120966     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.7.11.5959     Document Type: Review
Times cited : (113)

References (157)
  • 1
    • 0028929328 scopus 로고
    • Mechanisms and genes of cellular suicide
    • Steller H. Mechanisms and genes of cellular suicide. Science 1995; 267:1445-9.
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 2
    • 0028943734 scopus 로고    scopus 로고
    • Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science 1995; 267:1456-62.
    • Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science 1995; 267:1456-62.
  • 3
    • 0038786580 scopus 로고    scopus 로고
    • Apoptosis-targeted therapies for cancer
    • Reed JC. Apoptosis-targeted therapies for cancer. Cancer Cell 2003; 3:17-22.
    • (2003) Cancer Cell , vol.3 , pp. 17-22
    • Reed, J.C.1
  • 4
    • 33645784245 scopus 로고    scopus 로고
    • Genetic disorders of programmed cell death in the immune system
    • Bidere N, Su HC, Lenardo MJ. Genetic disorders of programmed cell death in the immune system. Annual review of immunology 2006; 24:321-52.
    • (2006) Annual review of immunology , vol.24 , pp. 321-352
    • Bidere, N.1    Su, H.C.2    Lenardo, M.J.3
  • 5
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science 1998; 281:1305-8.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 7
    • 0344393783 scopus 로고    scopus 로고
    • Alterations in the apoptotic machinery and their potential role in anticancer drug resistance
    • Kaufmann SH, Vaux DL. Alterations in the apoptotic machinery and their potential role in anticancer drug resistance. Oncogene 2003; 22:7414-30.
    • (2003) Oncogene , vol.22 , pp. 7414-7430
    • Kaufmann, S.H.1    Vaux, D.L.2
  • 8
    • 2442547741 scopus 로고    scopus 로고
    • Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies
    • Salvesen GS, Abrams JM. Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies. Oncogene 2004; 23:2774-84.
    • (2004) Oncogene , vol.23 , pp. 2774-2784
    • Salvesen, G.S.1    Abrams, J.M.2
  • 9
    • 37549048249 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A. The Bcl-2 protein family: opposing activities that mediate cell death. Nature reviews 2008; 9:47-59.
    • (2008) Nature reviews , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 11
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • Riedl SJ, Salvesen GS. The apoptosome: signalling platform of cell death. Nature reviews 2007; 8:405-13.
    • (2007) Nature reviews , vol.8 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 12
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi A. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nat Rev Cancer 2002; 2:420-30.
    • (2002) Nat Rev Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 14
    • 34247842740 scopus 로고    scopus 로고
    • The death domain superfamily in intracellular signaling of apoptosis and inflammation
    • Park HH, Lo YC, Lin SC, Wang L, Yang JK, Wu H. The death domain superfamily in intracellular signaling of apoptosis and inflammation. Annual review of immunology 2007; 25:561-86.
    • (2007) Annual review of immunology , vol.25 , pp. 561-586
    • Park, H.H.1    Lo, Y.C.2    Lin, S.C.3    Wang, L.4    Yang, J.K.5    Wu, H.6
  • 15
    • 0036009115 scopus 로고    scopus 로고
    • NFκB at the crossroads of life and death
    • Karin M, Lin A. NFκB at the crossroads of life and death. Nature immunology 2002; 3:221-7.
    • (2002) Nature immunology , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 16
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003; 114:181-90.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 17
    • 0027537461 scopus 로고
    • An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif
    • Crook NE, Clem RJ, Miller LK. An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif. J Virol 1993; 67:2168-74.
    • (1993) J Virol , vol.67 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 18
    • 0028274132 scopus 로고
    • An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs
    • Birnbaum MJ, Clem RJ, Miller LK. An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs. J Virol 1994; 68:2521-8.
    • (1994) J Virol , vol.68 , pp. 2521-2528
    • Birnbaum, M.J.1    Clem, R.J.2    Miller, L.K.3
  • 19
    • 17144377113 scopus 로고    scopus 로고
    • IAPs, RINGs and ubiquitylation
    • Vaux DL, Silke J. IAPs, RINGs and ubiquitylation. Nature reviews 2005; 6:287-97.
    • (2005) Nature reviews , vol.6 , pp. 287-297
    • Vaux, D.L.1    Silke, J.2
  • 20
    • 34547126428 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) as cancer targets
    • Hunter AM, Lacasse EC, Korneluk RG. The inhibitors of apoptosis (IAPs) as cancer targets. Apoptosis 2007; 12:1543-68.
    • (2007) Apoptosis , vol.12 , pp. 1543-1568
    • Hunter, A.M.1    Lacasse, E.C.2    Korneluk, R.G.3
  • 23
    • 33645640920 scopus 로고    scopus 로고
    • The human anti-apoptotic proteins c-IAP1 and c-IAP2 bind but do not inhibit caspases
    • Eckelman BP, Salvesen GS. The human anti-apoptotic proteins c-IAP1 and c-IAP2 bind but do not inhibit caspases. The Journal of biological chemistry 2006; 281:3254-60.
    • (2006) The Journal of biological chemistry , vol.281 , pp. 3254-3260
    • Eckelman, B.P.1    Salvesen, G.S.2
  • 24
    • 33749252583 scopus 로고    scopus 로고
    • Human inhibitor of apoptosis proteins: Why XIAP is the black sheep of the family
    • Eckelman BP, Salvesen GS, Scott FL. Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family. EMBO Rep 2006; 7:988-94.
    • (2006) EMBO Rep , vol.7 , pp. 988-994
    • Eckelman, B.P.1    Salvesen, G.S.2    Scott, F.L.3
  • 27
    • 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, Myszka DG, Wu H. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell 2001; 104:781-90.
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4    Myszka, D.G.5    Wu, H.6
  • 30
    • 0034616945 scopus 로고    scopus 로고
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102:33-42.
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102:33-42.
  • 34
    • 45849089789 scopus 로고    scopus 로고
    • Requirement of both the BIR2 and BIR3 domains for the relief of XIAP-mediated caspase inhibition by Smac
    • Huang Y, Rich RL, Myszka DG, Wu H. Requirement of both the BIR2 and BIR3 domains for the relief of XIAP-mediated caspase inhibition by Smac. The Journal of biological chemistry 2003; 278:9517-22.
    • (2003) The Journal of biological chemistry , vol.278 , pp. 9517-9522
    • Huang, Y.1    Rich, R.L.2    Myszka, D.G.3    Wu, H.4
  • 39
    • 0038722727 scopus 로고    scopus 로고
    • Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis
    • Yang QH, Church-Hajduk R, Ren J, Newton ML, Du C. Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis. Genes & development 2003; 17:1487-96.
    • (2003) Genes & development , vol.17 , pp. 1487-1496
    • Yang, Q.H.1    Church-Hajduk, R.2    Ren, J.3    Newton, M.L.4    Du, C.5
  • 45
    • 0035895597 scopus 로고    scopus 로고
    • xIAP induces cell cycle arrest and activates nuclear factorκB: New survival pathways disabled by caspase-mediated cleavage during apoptosis of human endothelial cells
    • Levkau B, Garton KJ, Ferri N, Kloke K, Nofer JR, Baba HA, Raines EW, Breithardt G. xIAP induces cell cycle arrest and activates nuclear factorκB: new survival pathways disabled by caspase-mediated cleavage during apoptosis of human endothelial cells. Circulation research 2001; 88:282-90.
    • (2001) Circulation research , vol.88 , pp. 282-290
    • Levkau, B.1    Garton, K.J.2    Ferri, N.3    Kloke, K.4    Nofer, J.R.5    Baba, H.A.6    Raines, E.W.7    Breithardt, G.8
  • 51
    • 21244460672 scopus 로고    scopus 로고
    • Naip5/Birc1e and susceptibility to Legionella pneumophila
    • Fortier A, Diez E, Gros P. Naip5/Birc1e and susceptibility to Legionella pneumophila. Trends in microbiology 2005; 13:328-35.
    • (2005) Trends in microbiology , vol.13 , pp. 328-335
    • Fortier, A.1    Diez, E.2    Gros, P.3
  • 54
    • 33645791082 scopus 로고    scopus 로고
    • Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity
    • Ren T, Zamboni DS, Roy CR, Dietrich WF, Vance RE. Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity. PLoS pathogens 2006; 2:18.
    • (2006) PLoS pathogens , vol.2 , pp. 18
    • Ren, T.1    Zamboni, D.S.2    Roy, C.R.3    Dietrich, W.F.4    Vance, R.E.5
  • 55
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 1995; 83:1243-52.
    • (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
  • 56
    • 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. The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex. PNAS 1996; 93:13973-8.
    • (1996) PNAS , vol.93 , pp. 13973-13978
    • Shu, H.B.1    Takeuchi, M.2    Goeddel, D.V.3
  • 58
    • 0032508414 scopus 로고    scopus 로고
    • NFκB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang CY, Mayo MW, Korneluk RG, Goeddel DV, Baldwin AS Jr. NFκB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 1998; 281:1680-3.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin Jr, A.S.5
  • 59
    • 34548857955 scopus 로고    scopus 로고
    • Ubiquitin ligases in cancer: Ushers for degradation
    • Newton K, Vucic D. Ubiquitin ligases in cancer: ushers for degradation. Cancer investigation 2007; 25:502-13.
    • (2007) Cancer investigation , vol.25 , pp. 502-513
    • Newton, K.1    Vucic, D.2
  • 61
    • 0033980888 scopus 로고    scopus 로고
    • Diverse Domains of THREAD/DIAP1 Are Required to Inhibit Apoptosis Induced by REAPER and HID in Drosophila
    • Lisi S, Mazzon I, White K. Diverse Domains of THREAD/DIAP1 Are Required to Inhibit Apoptosis Induced by REAPER and HID in Drosophila. Genetics 2000; 154:669-78.
    • (2000) Genetics , vol.154 , pp. 669-678
    • Lisi, S.1    Mazzon, I.2    White, K.3
  • 63
    • 0036712650 scopus 로고    scopus 로고
    • Reaper-mediated inhibition of DIAP1-induced DTRAF1 degradation results in activation of JNK in Drosophila
    • Kuranaga E, Kanuka H, Igaki T, Sawamoto K, Ichijo H, Okano H, Miura M. Reaper-mediated inhibition of DIAP1-induced DTRAF1 degradation results in activation of JNK in Drosophila. Nature cell biology 2002; 4:705-10.
    • (2002) Nature cell biology , vol.4 , pp. 705-710
    • Kuranaga, E.1    Kanuka, H.2    Igaki, T.3    Sawamoto, K.4    Ichijo, H.5    Okano, H.6    Miura, M.7
  • 67
    • 45849147211 scopus 로고    scopus 로고
    • Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition
    • Holley CL, Olson MR, Colon Ramos DA, Kornbluth S. Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition. Nature cell biology 2002; 14:14.
    • (2002) Nature cell biology , vol.14 , pp. 14
    • Holley, C.L.1    Olson, M.R.2    Colon Ramos, D.A.3    Kornbluth, S.4
  • 69
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • MacFarlane M, Merrison W, Bratton SB, Cohen GM. Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro. The Journal of biological chemistry 2002; 277:36611-6.
    • (2002) The Journal of biological chemistry , vol.277 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 70
    • 0037855783 scopus 로고    scopus 로고
    • Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO
    • Hu S, Yang X. Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO. The Journal of biological chemistry 2003; 278:10055-60.
    • (2003) The Journal of biological chemistry , vol.278 , pp. 10055-10060
    • Hu, S.1    Yang, X.2
  • 71
    • 17044368875 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO
    • Morizane Y, Honda R, Fukami K, Yasuda H. X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO. J Biochem (Tokyo) 2005; 137:125-32.
    • (2005) J Biochem (Tokyo) , vol.137 , pp. 125-132
    • Morizane, Y.1    Honda, R.2    Fukami, K.3    Yasuda, H.4
  • 72
    • 33644853217 scopus 로고    scopus 로고
    • Distinct BIR domains of c-IAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases
    • Samuel T, Welsh K, Lober T, Togo SH, Zapata JM, Reed JC. Distinct BIR domains of c-IAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases. The Journal of biological chemistry 2006; 281:1080-90.
    • (2006) The Journal of biological chemistry , vol.281 , pp. 1080-1090
    • Samuel, T.1    Welsh, K.2    Lober, T.3    Togo, S.H.4    Zapata, J.M.5    Reed, J.C.6
  • 74
    • 2342445559 scopus 로고    scopus 로고
    • Smac/DIABLO selectively reduces the levels of c-IAP1 and c-IAP2 but not that of XIAP and livin in HeLa cells
    • Yang QH, Du C. Smac/DIABLO selectively reduces the levels of c-IAP1 and c-IAP2 but not that of XIAP and livin in HeLa cells. The Journal of biological chemistry 2004; 279:16963-70.
    • (2004) The Journal of biological chemistry , vol.279 , pp. 16963-16970
    • Yang, Q.H.1    Du, C.2
  • 75
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, c-IAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7
    • Huang H, Joazeiro CA, Bonfoco E, Kamada S, Leverson JD, Hunter T. The inhibitor of apoptosis, c-IAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. The Journal of biological chemistry 2000; 275:26661-4.
    • (2000) The Journal of biological chemistry , vol.275 , pp. 26661-26664
    • Huang, H.1    Joazeiro, C.A.2    Bonfoco, E.3    Kamada, S.4    Leverson, J.D.5    Hunter, T.6
  • 76
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • Suzuki Y, Nakabayashi Y, Takahashi R. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. PNAS 2001; 98:8662-7.
    • (2001) PNAS , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 79
    • 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. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 2000; 288:874-7.
    • (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
  • 81
    • 28044469866 scopus 로고    scopus 로고
    • Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance
    • Silke J, Kratina T, Chu D, Ekert PG, Day CL, Pakusch M, Huang DC, Vaux DL. Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance. PNAS 2005; 102:16182-7.
    • (2005) PNAS , vol.102 , pp. 16182-16187
    • Silke, J.1    Kratina, T.2    Chu, D.3    Ekert, P.G.4    Day, C.L.5    Pakusch, M.6    Huang, D.C.7    Vaux, D.L.8
  • 83
    • 0037149542 scopus 로고    scopus 로고
    • TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2
    • Li X, Yang Y, Ashwell JD. TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. Nature 2002; 416:345-7.
    • (2002) Nature , vol.416 , pp. 345-347
    • Li, X.1    Yang, Y.2    Ashwell, J.D.3
  • 84
    • 0036629347 scopus 로고    scopus 로고
    • Apoptotic crosstalk of TNF receptors: TNF-R2-induces depletion of TRAF2 and IAP proteins and accelerates TNF-R1-dependent activation of caspase-8
    • Fotin-Mleczek M, Henkler F, Samel D, Reichwein M, Hausser A, Parmryd I, Scheurich P, Schmid JA, Wajant H. Apoptotic crosstalk of TNF receptors: TNF-R2-induces depletion of TRAF2 and IAP proteins and accelerates TNF-R1-dependent activation of caspase-8. J Cell Sci 2002; 115:2757-70.
    • (2002) J Cell Sci , vol.115 , pp. 2757-2770
    • Fotin-Mleczek, M.1    Henkler, F.2    Samel, D.3    Reichwein, M.4    Hausser, A.5    Parmryd, I.6    Scheurich, P.7    Schmid, J.A.8    Wajant, H.9
  • 85
    • 20044387665 scopus 로고    scopus 로고
    • TNFalpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination
    • Wu CJ, Conze DB, Li X, Ying SX, Hanover JA, Ashwell JD. TNFalpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination. The EMBO journal 2005; 24:1886-98.
    • (2005) The EMBO journal , vol.24 , pp. 1886-1898
    • Wu, C.J.1    Conze, D.B.2    Li, X.3    Ying, S.X.4    Hanover, J.A.5    Ashwell, J.D.6
  • 86
    • 2442559290 scopus 로고    scopus 로고
    • Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro
    • Park SM, Yoon JB, Lee TH. Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro. FEBS Lett 2004; 566:151-6.
    • (2004) FEBS Lett , vol.566 , pp. 151-156
    • Park, S.M.1    Yoon, J.B.2    Lee, T.H.3
  • 92
    • 0142188706 scopus 로고    scopus 로고
    • Coexistence of high levels of apoptotic signaling and inhibitor of apoptosis proteins in human tumor cells: Implication for cancer specific therapy
    • Yang L, Cao Z, Yan H, Wood WC. Coexistence of high levels of apoptotic signaling and inhibitor of apoptosis proteins in human tumor cells: implication for cancer specific therapy. Cancer Res 2003; 63:6815-24.
    • (2003) Cancer Res , vol.63 , pp. 6815-6824
    • Yang, L.1    Cao, Z.2    Yan, H.3    Wood, W.C.4
  • 94
    • 34948871492 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins as targets for anticancer therapy
    • Fulda S. Inhibitor of apoptosis proteins as targets for anticancer therapy. Expert Rev Anticancer Ther 2007; 7:1255-64.
    • (2007) Expert Rev Anticancer Ther , vol.7 , pp. 1255-1264
    • Fulda, S.1
  • 95
    • 35948950248 scopus 로고    scopus 로고
    • The inhibitor of apoptosis proteins as therapeutic targets in cancer
    • Vucic D, Fairbrother WJ. The inhibitor of apoptosis proteins as therapeutic targets in cancer. Clin Cancer Res 2007; 13:5995-6000.
    • (2007) Clin Cancer Res , vol.13 , pp. 5995-6000
    • Vucic, D.1    Fairbrother, W.J.2
  • 96
    • 0041913978 scopus 로고    scopus 로고
    • Development and characterization of nonpeptidic small molecule inhibitors of the XIAP/caspase-3 interaction
    • Wu TY, Wagner KW, Bursulaya B, Schultz PG, Deveraux QL. Development and characterization of nonpeptidic small molecule inhibitors of the XIAP/caspase-3 interaction. Chem Biol 2003; 10:759-67.
    • (2003) Chem Biol , vol.10 , pp. 759-767
    • Wu, T.Y.1    Wagner, K.W.2    Bursulaya, B.3    Schultz, P.G.4    Deveraux, Q.L.5
  • 97
    • 0037442965 scopus 로고    scopus 로고
    • Predominant suppression of apoptosome by inhibitor of apoptosis protein in non-small cell lung cancer H460 cells: Therapeutic effect of a novel polyarginine-conjugated Smac peptide
    • Yang L, Mashima T, Sato S, Mochizuki M, Sakamoto H, Yamori T, Oh-Hara T, Tsuruo T. Predominant suppression of apoptosome by inhibitor of apoptosis protein in non-small cell lung cancer H460 cells: therapeutic effect of a novel polyarginine-conjugated Smac peptide. Cancer Res 2003; 63:831-7.
    • (2003) Cancer Res , vol.63 , pp. 831-837
    • Yang, L.1    Mashima, T.2    Sato, S.3    Mochizuki, M.4    Sakamoto, H.5    Yamori, T.6    Oh-Hara, T.7    Tsuruo, T.8
  • 99
    • 4444243683 scopus 로고    scopus 로고
    • A small molecule Smac mimic potentiates TRAIL- and TNFα-mediated cell death
    • Li L, Thomas RM, Suzuki H, De Brabander JK, Wang X, Harran PG. A small molecule Smac mimic potentiates TRAIL- and TNFα-mediated cell death. Science 2004; 305:1471-4.
    • (2004) Science , vol.305 , pp. 1471-1474
    • Li, L.1    Thomas, R.M.2    Suzuki, H.3    De Brabander, J.K.4    Wang, X.5    Harran, P.G.6
  • 100
    • 2342448582 scopus 로고    scopus 로고
    • Discovery of embelin as a cell-permeable, small-molecular weight inhibitor of XIAP through structure-based computational screening of a traditional herbal medicine three-dimensional structure database
    • Nikolovska-Coleska Z, Xu L, Hu Z, Tomita Y, Li P, Roller PP, Wang R, Fang X, Guo R, Zhang M, Lippman ME, Yang D, Wang S. Discovery of embelin as a cell-permeable, small-molecular weight inhibitor of XIAP through structure-based computational screening of a traditional herbal medicine three-dimensional structure database. J Med Chem 2004; 47:2430-40.
    • (2004) J Med Chem , vol.47 , pp. 2430-2440
    • Nikolovska-Coleska, Z.1    Xu, L.2    Hu, Z.3    Tomita, Y.4    Li, P.5    Roller, P.P.6    Wang, R.7    Fang, X.8    Guo, R.9    Zhang, M.10    Lippman, M.E.11    Yang, D.12    Wang, S.13
  • 101
    • 33845919012 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a potent, cell-permeable, conformationally constrained second mitochondria derived activator of caspase (Smac) mimetic
    • Sun H, Nikolovska Coleska Z, Lu J, Qiu S, Yang CY, Gao W, Meagher J, Stuckey J, Wang S. Design, synthesis, and evaluation of a potent, cell-permeable, conformationally constrained second mitochondria derived activator of caspase (Smac) mimetic. J Med Chem 2006; 49:7916-20.
    • (2006) J Med Chem , vol.49 , pp. 7916-7920
    • Sun, H.1    Nikolovska Coleska, Z.2    Lu, J.3    Qiu, S.4    Yang, C.Y.5    Gao, W.6    Meagher, J.7    Stuckey, J.8    Wang, S.9
  • 104
    • 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. Smac agonists sensitize for Apo2L/TRAIL- or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo. Nat Med 2002; 8:808-15.
    • (2002) Nat Med , vol.8 , pp. 808-815
    • Fulda, S.1    Wick, W.2    Weller, M.3    Debatin, K.M.4
  • 105
    • 0036565885 scopus 로고    scopus 로고
    • Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis
    • Guo F, Nimmanapalli R, Paranawithana S, Wittman S, Griffin D, Bali P, O'Bryan E, Fumero C, Wang HG, Bhalla K. Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis. Blood 2002; 99:3419-26.
    • (2002) Blood , vol.99 , pp. 3419-3426
    • Guo, F.1    Nimmanapalli, R.2    Paranawithana, S.3    Wittman, S.4    Griffin, D.5    Bali, P.6    O'Bryan, E.7    Fumero, C.8    Wang, H.G.9    Bhalla, K.10
  • 107
    • 27744526342 scopus 로고    scopus 로고
    • A small molecule Smac-mimic compound induces apoptosis and sensitizes TRAIL- and etoposide-induced apoptosis in breast cancer cells
    • Bockbrader KM, Tan M, Sun Y. A small molecule Smac-mimic compound induces apoptosis and sensitizes TRAIL- and etoposide-induced apoptosis in breast cancer cells. Oncogene 2005; 24:7381-8.
    • (2005) Oncogene , vol.24 , pp. 7381-7388
    • Bockbrader, K.M.1    Tan, M.2    Sun, Y.3
  • 117
    • 42149105590 scopus 로고    scopus 로고
    • Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
    • epub ahead of print
    • Linke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL. Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans. Cell death and differentiation 2008; epub ahead of print.
    • (2008) Cell death and differentiation
    • Linke, K.1    Mace, P.D.2    Smith, C.A.3    Vaux, D.L.4    Silke, J.5    Day, C.L.6
  • 122
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • Baud V, Karin M. Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol 2001; 11:372-7.
    • (2001) Trends Cell Biol , vol.11 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 123
    • 33750443289 scopus 로고    scopus 로고
    • IκB kinase complexes: Gateways to NFκB activation and transcription
    • Scheidereit C. IκB kinase complexes: gateways to NFκB activation and transcription. Oncogene 2006; 25:6685-705.
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 124
    • 33749265867 scopus 로고    scopus 로고
    • The alternative NFκB pathway from biochemistry to biology: Pitfalls and promises for future drug development
    • Dejardin E. The alternative NFκB pathway from biochemistry to biology: pitfalls and promises for future drug development. Biochemical pharmacology 2006; 72:1161-79.
    • (2006) Biochemical pharmacology , vol.72 , pp. 1161-1179
    • Dejardin, E.1
  • 125
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases
    • Hacker H, Karin M. Regulation and function of IKK and IKK-related kinases. Sci STKE 2006; 2006:13.
    • (2006) Sci STKE 2006 , pp. 13
    • Hacker, H.1    Karin, M.2
  • 126
    • 37449033866 scopus 로고    scopus 로고
    • Positive and negative signaling components involved in TNFalpha-induced NFkappaB activation
    • Li H, Lin X. Positive and negative signaling components involved in TNFalpha-induced NFkappaB activation. Cytokine 2008; 41:1-8.
    • (2008) Cytokine , vol.41 , pp. 1-8
    • Li, H.1    Lin, X.2
  • 127
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NFκB
    • Brummelkamp TR, Nijman SM, Dirac AM, Bernards R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NFκB. Nature 2003; 424:797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 129
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NFκB activation by TNFR family members
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A, Mosialos G. CYLD is a deubiquitinating enzyme that negatively regulates NFκB activation by TNFR family members. Nature 2003; 424:793-6.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 131
    • 0034745420 scopus 로고    scopus 로고
    • NFκB-inducing kinase regulates the processing of NFκB2 p100
    • Xiao G, Harhaj EW, Sun SC. NFκB-inducing kinase regulates the processing of NFκB2 p100. Molecular cell 2001; 7:401-9.
    • (2001) Molecular cell , vol.7 , pp. 401-409
    • Xiao, G.1    Harhaj, E.W.2    Sun, S.C.3
  • 134
    • 84934436838 scopus 로고    scopus 로고
    • Physiological roles and mechanisms of signaling by TRAF2 and TRAF5
    • Au PY, Yeh WC. Physiological roles and mechanisms of signaling by TRAF2 and TRAF5. Advances in experimental medicine and biology 2007; 597:32-47.
    • (2007) Advances in experimental medicine and biology , vol.597 , pp. 32-47
    • Au, P.Y.1    Yeh, W.C.2
  • 135
    • 2942731516 scopus 로고    scopus 로고
    • Regulation of the NFκB-inducing kinase by tumor necrosis factor receptor-associated factor 3-induced degradation
    • Liao G, Zhang M, Harhaj EW, Sun SC. Regulation of the NFκB-inducing kinase by tumor necrosis factor receptor-associated factor 3-induced degradation. The Journal of biological chemistry 2004; 279:26243-50.
    • (2004) The Journal of biological chemistry , vol.279 , pp. 26243-26250
    • Liao, G.1    Zhang, M.2    Harhaj, E.W.3    Sun, S.C.4
  • 136
    • 8444220390 scopus 로고    scopus 로고
    • TRAF2 differentially regulates the canonical and noncanonical pathways of NFκB activation in mature B cells
    • Grech AP, Amesbury M, Chan T, Gardam S, Basten A, Brink R. TRAF2 differentially regulates the canonical and noncanonical pathways of NFκB activation in mature B cells. Immunity 2004; 21:629-42.
    • (2004) Immunity , vol.21 , pp. 629-642
    • Grech, A.P.1    Amesbury, M.2    Chan, T.3    Gardam, S.4    Basten, A.5    Brink, R.6
  • 139
    • 34548014506 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factor 3 is a critical regulator of B cell homeostasis in secondary lymphoid organs
    • Xie P, Stunz LL, Larison KD, Yang B, Bishop GA. Tumor necrosis factor receptor-associated factor 3 is a critical regulator of B cell homeostasis in secondary lymphoid organs. Immunity 2007; 27:253-67.
    • (2007) Immunity , vol.27 , pp. 253-267
    • Xie, P.1    Stunz, L.L.2    Larison, K.D.3    Yang, B.4    Bishop, G.A.5
  • 140
    • 0037114130 scopus 로고    scopus 로고
    • TNFR-associated factor-3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NFκB activation and IL-10 production
    • Xu LG, Shu HB. TNFR-associated factor-3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NFκB activation and IL-10 production. J Immunol 2002; 169:6883-9.
    • (2002) J Immunol , vol.169 , pp. 6883-6889
    • Xu, L.G.1    Shu, H.B.2
  • 141
    • 15444379092 scopus 로고    scopus 로고
    • An atypical tumor necrosis factor (TNF) receptor-associated factor-binding motif of B cell-activating factor belonging to the TNF family (BAFF) receptor mediates induction of the noncanonical NFκB signaling pathway
    • Morrison MD, Reiley W, Zhang M, Sun SC. An atypical tumor necrosis factor (TNF) receptor-associated factor-binding motif of B cell-activating factor belonging to the TNF family (BAFF) receptor mediates induction of the noncanonical NFκB signaling pathway. The Journal of biological chemistry 2005; 280:10018-24.
    • (2005) The Journal of biological chemistry , vol.280 , pp. 10018-10024
    • Morrison, M.D.1    Reiley, W.2    Zhang, M.3    Sun, S.C.4
  • 142
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NFκB induction by TNF, CD95 and IL-1
    • Malinin NL, Boldin MP, Kovalenko AV, Wallach D. MAP3K-related kinase involved in NFκB induction by TNF, CD95 and IL-1. Nature 1997; 385:540-4.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 144
    • 11244334124 scopus 로고    scopus 로고
    • TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NFκB activation
    • He L, Grammer AC, Wu X, Lipsky PE. TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NFκB activation. The Journal of biological chemistry 2004; 279:55855-65.
    • (2004) The Journal of biological chemistry , vol.279 , pp. 55855-55865
    • He, L.1    Grammer, A.C.2    Wu, X.3    Lipsky, P.E.4
  • 145
    • 0038150358 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2)
    • Shi CS, Kehrl JH. Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2). The Journal of biological chemistry 2003; 278:15429-34.
    • (2003) The Journal of biological chemistry , vol.278 , pp. 15429-15434
    • Shi, C.S.1    Kehrl, J.H.2
  • 147
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: A beautiful pathway
    • Chen G, Goeddel DV. TNF-R1 signaling: a beautiful pathway. Science 2002; 296:1634-5.
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 148
    • 1342285692 scopus 로고    scopus 로고
    • Tumor necrosis factor: An apoptosis
    • Varfolomeev EE, Ashkenazi A. Tumor necrosis factor: an apoptosis JuNKie? Cell 2004; 116:491-7.
    • (2004) JuNKie? Cell , vol.116 , pp. 491-497
    • Varfolomeev, E.E.1    Ashkenazi, A.2
  • 149
    • 0034730713 scopus 로고    scopus 로고
    • Failure to regulate TNF-induced NFκB and cell death responses in A20-deficient mice
    • Lee EG, Boone DL, Chai S, Libby SL, Chien M, Lodolce JP, Ma A. Failure to regulate TNF-induced NFκB and cell death responses in A20-deficient mice. Science 2000; 289:2350-4.
    • (2000) Science , vol.289 , pp. 2350-2354
    • Lee, E.G.1    Boone, D.L.2    Chai, S.3    Libby, S.L.4    Chien, M.5    Lodolce, J.P.6    Ma, A.7
  • 150
    • 35648935968 scopus 로고    scopus 로고
    • Birc2 (c-Iap1) regulates endothelial cell integrity and blood vessel homeostasis
    • Santoro MM, Samuel T, Mitchell T, Reed JC, Stainier DY. Birc2 (c-Iap1) regulates endothelial cell integrity and blood vessel homeostasis. Nat Genet 2007; 39:1397-402.
    • (2007) Nat Genet , vol.39 , pp. 1397-1402
    • Santoro, M.M.1    Samuel, T.2    Mitchell, T.3    Reed, J.C.4    Stainier, D.Y.5
  • 151
    • 0141621240 scopus 로고    scopus 로고
    • A role for NFkappaB essential modifier/IκB kinase-gamma (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α
    • Tang ED, Wang CY, Xiong Y, Guan KL. A role for NFkappaB essential modifier/IκB kinase-gamma (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α. The Journal of biological chemistry 2003; 278:37297-305.
    • (2003) The Journal of biological chemistry , vol.278 , pp. 37297-37305
    • Tang, E.D.1    Wang, C.Y.2    Xiong, Y.3    Guan, K.L.4
  • 152
    • 34247191196 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor 2 signaling induces selective c-IAP1-dependent ASK1 ubiquitination and terminates mitogen-activated protein kinase signaling
    • Zhao Y, Conze DB, Hanover JA, Ashwell JD. Tumor necrosis factor receptor 2 signaling induces selective c-IAP1-dependent ASK1 ubiquitination and terminates mitogen-activated protein kinase signaling. The Journal of biological chemistry 2007; 282:7777-82.
    • (2007) The Journal of biological chemistry , vol.282 , pp. 7777-7782
    • Zhao, Y.1    Conze, D.B.2    Hanover, J.A.3    Ashwell, J.D.4
  • 157
    • 5644302162 scopus 로고    scopus 로고
    • Receptor-specific signaling for both the alternative and the canonical NFκB activation pathways by NFκB-inducing kinase
    • Ramakrishnan P, Wang W, Wallach D. Receptor-specific signaling for both the alternative and the canonical NFκB activation pathways by NFκB-inducing kinase. Immunity 2004; 21:477-89.
    • (2004) Immunity , vol.21 , pp. 477-489
    • Ramakrishnan, P.1    Wang, W.2    Wallach, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.