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Volumn 34, Issue 3, 2012, Pages 200-211

The inhibitor of apoptosis (IAP) proteins are critical regulators of signaling pathways and targets for anti-cancer therapy

Author keywords

Apoptosis; BIR; Cancer; IAP; NF kB; RING; Smac; TNF; Ubiquitin

Indexed keywords

ANTINEOPLASTIC AGENT; BIRINAPANT; BV 6; CISPLATIN; CYTARABINE; ENZYME INHIBITOR; ETOPOSIDE; FLUOROURACIL; GDC 0152; GEMCITABINE; HGS 1029; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN 1; INHIBITOR OF APOPTOSIS PROTEIN 2; INHIBITOR OF APOPTOSIS PROTEIN ANTAGONIST; IRINOTECAN; LCL 161; LIVIN; MV 1; NAVELBINE; PROTEIN INHIBITOR; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; UBIQUITIN; UNCLASSIFIED DRUG; X LINKED INHIBITOR OF APOPTOSIS;

EID: 84872462277     PISSN: 18129269     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (162)

References (138)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell 2011; 144: 646-74.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 84255210700 scopus 로고    scopus 로고
    • Molecular definitions of cell death subroutines: Recommendations of the Nomenclature Committee on Cell Death 2012
    • Galluzzi L, Vitale I, Abrams JM, et al. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ 2012; 19: 107-20.
    • (2012) Cell Death Differ , vol.19 , pp. 107-120
    • Galluzzi, L.1    Vitale, I.2    Abrams, J.M.3
  • 3
    • 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
  • 4
    • 78649635741 scopus 로고    scopus 로고
    • To fight or die - Inhibitor of apoptosis proteins at the crossroad of innate immunity and death
    • Lopez J, Meier P. To fight or die - inhibitor of apoptosis proteins at the crossroad of innate immunity and death. Curr Opin Cell Biol 2010; 22: 872-81.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 872-881
    • Lopez, J.1    Meier, P.2
  • 5
    • 0033179212 scopus 로고    scopus 로고
    • An exegesis of IAPs: Salvation and surprises from BIR motifs
    • Miller LK. An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol 1999; 9: 323-8.
    • (1999) Trends Cell Biol , vol.9 , pp. 323-328
    • Miller, L.K.1
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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, et al. Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes. Nature 1996; 379: 349-53.
    • (1996) Nature , vol.379 , pp. 349-353
    • Liston, P.1    Roy, N.2    Tamai, K.3
  • 9
    • 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, et al. 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
  • 10
    • 0037427441 scopus 로고    scopus 로고
    • Mammalian mitochondrial IAP binding proteins
    • Vaux DL, Silke J. Mammalian mitochondrial IAP binding proteins. Biochem Biophys Res Commun 2003; 304: 499-504.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 499-504
    • Vaux, D.L.1    Silke, J.2
  • 11
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science 1998; 281: 1312-6.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 12
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: Functions and regulation of caspases
    • Chang HY, Yang X. Proteases for cell suicide: functions and regulation of caspases. Microbiol Mol Biol Rev 2000; 64: 821-46.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 13
    • 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
  • 15
    • 44749085513 scopus 로고    scopus 로고
    • Targeting the extrinsic apoptosis pathway in cancer
    • Ashkenazi A. Targeting the extrinsic apoptosis pathway in cancer. Cytokine Growth Factor Rev 2008; 19: 325-31.
    • (2008) Cytokine Growth Factor Rev , vol.19 , pp. 325-331
    • Ashkenazi, A.1
  • 16
    • 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, et al. A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Cell 2000; 101: 777-87.
    • (2000) Cell , vol.101 , pp. 777-787
    • Park, Y.C.1    Ye, H.2    Hsia, C.3
  • 17
    • 0029122732 scopus 로고
    • Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast
    • Stutz F, Neville M, Rosbash M. Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast. Cell 1995; 82: 495-506.
    • (1995) Cell , vol.82 , pp. 495-506
    • Stutz, F.1    Neville, M.2    Rosbash, M.3
  • 18
    • 76749132616 scopus 로고    scopus 로고
    • RIPK1 is not essential for TNFR1-induced activation of NF-kappaB
    • Wong WW, Gentle IE, Nachbur U, et al. RIPK1 is not essential for TNFR1-induced activation of NF-kappaB. Cell Death Differ 2010; 17: 482-7.
    • (2010) Cell Death Differ , vol.17 , pp. 482-487
    • Wong, W.W.1    Gentle, I.E.2    Nachbur, U.3
  • 19
    • 79959539790 scopus 로고    scopus 로고
    • Ubiquitylation in apoptosis: A post-translational modification at the edge of life and death
    • Vucic D, Dixit VM, Wertz IE. Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death. Nat Rev Mol Cell Biol 2011; 12: 439-52.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 439-452
    • Vucic, D.1    Dixit, V.M.2    Wertz, I.E.3
  • 20
    • 44949240664 scopus 로고    scopus 로고
    • cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand MJ, Milutinovic S, Dickson KM, et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell 2008; 30: 689-700.
    • (2008) Mol Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.1    Milutinovic, S.2    Dickson, K.M.3
  • 21
    • 54049155149 scopus 로고    scopus 로고
    • c-IAP1 and c-IAP2 Are Critical Mediators of Tumor Necrosis Factor alpha (TNFα)-induced NF-kB Activation
    • Varfolomeev E, Goncharov T, Fedorova AV, et al. c-IAP1 and c-IAP2 Are Critical Mediators of Tumor Necrosis Factor alpha (TNFα)-induced NF-kB Activation. J Biol Chem 2008; 283: 24295-9.
    • (2008) J Biol Chem , vol.283 , pp. 24295-24299
    • Varfolomeev, E.1    Goncharov, T.2    Fedorova, A.V.3
  • 22
    • 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
  • 23
    • 62849093368 scopus 로고    scopus 로고
    • Death receptor signal transducers: Nodes of coordination in immune signaling networks
    • Wilson NS, Dixit V, Ashkenazi A. Death receptor signal transducers: nodes of coordination in immune signaling networks. Nat Immunol 2009; 10: 348-55.
    • (2009) Nat Immunol , vol.10 , pp. 348-355
    • Wilson, N.S.1    Dixit, V.2    Ashkenazi, A.3
  • 24
    • 33746886979 scopus 로고    scopus 로고
    • Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy
    • Fulda S, Debatin KM. Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene 2006; 25: 4798-811.
    • (2006) Oncogene , vol.25 , pp. 4798-4811
    • Fulda, S.1    Debatin, K.M.2
  • 25
    • 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
  • 26
    • 0035156848 scopus 로고    scopus 로고
    • Identification of XAF1 as an antagonist of XIAP anti-caspase activity
    • Liston P, Fong WG, Kelly NL, et al. Identification of XAF1 as an antagonist of XIAP anti-caspase activity. Nat Cell Biol 2001; 3: 128-33.
    • (2001) Nat Cell Biol , vol.3 , pp. 128-133
    • Liston, P.1    Fong, W.G.2    Kelly, N.L.3
  • 27
    • 34548817572 scopus 로고    scopus 로고
    • Degradation of survivin by the X-linked inhibitor of apoptosis (XIAP)-XAF1 complex
    • Arora V, Cheung HH, Plenchette S, et al. Degradation of survivin by the X-linked inhibitor of apoptosis (XIAP)-XAF1 complex. J Biol Chem 2007; 282: 26202-9.
    • (2007) J Biol Chem , vol.282 , pp. 26202-26209
    • Arora, V.1    Cheung, H.H.2    Plenchette, S.3
  • 28
    • 33645640920 scopus 로고    scopus 로고
    • The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases
    • Eckelman BP, Salvesen GS. The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases. J Biol Chem 2006; 281: 3254-60.
    • (2006) J Biol Chem , vol.281 , pp. 3254-3260
    • Eckelman, B.P.1    Salvesen, G.S.2
  • 29
    • 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, Labbe K, et al. Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2. Immunity 2009; 30: 789-801.
    • (2009) Immunity , vol.30 , pp. 789-801
    • Bertrand, M.J.1    Doiron, K.2    Labbe, K.3
  • 30
    • 77449147556 scopus 로고    scopus 로고
    • Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs
    • Silke J, Brink R. Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs. Cell Death Differ 2010; 17: 35-45.
    • (2010) Cell Death Differ , vol.17 , pp. 35-45
    • Silke, J.1    Brink, R.2
  • 31
    • 45849120966 scopus 로고    scopus 로고
    • (Un)expected roles of c-IAPs in apoptotic and NF-kB signaling pathways
    • Varfolomeev E, Vucic D. (Un)expected roles of c-IAPs in apoptotic and NF-kB signaling pathways. Cell Cycle 2008; 7: 1511-21.
    • (2008) Cell Cycle , vol.7 , pp. 1511-1521
    • Varfolomeev, E.1    Vucic, D.2
  • 32
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux QL, Takahashi R, Salvesen GS, Reed JC. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 1997; 388: 300-4.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 33
    • 84856495152 scopus 로고    scopus 로고
    • Targeting IAP proteins for therapeutic intervention in cancer
    • Fulda S, Vucic D. Targeting IAP proteins for therapeutic intervention in cancer. Nat Rev Drug Discov 2012; 11: 109-24.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 109-124
    • Fulda, S.1    Vucic, D.2
  • 34
    • 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, et al. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J 1999; 18: 5242-51.
    • (1999) EMBO J , vol.18 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicke, H.R.3
  • 35
    • 0034278085 scopus 로고    scopus 로고
    • The IAP family: Endogenous caspase inhibitors with multiple biological activities
    • Yang YL, Li XM. The IAP family: endogenous caspase inhibitors with multiple biological activities. Cell Res 2000; 10: 169-77.
    • (2000) Cell Res , vol.10 , pp. 169-177
    • Yang, Y.L.1    Li, X.M.2
  • 36
    • 0033056850 scopus 로고    scopus 로고
    • Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat
    • Hinds MG, Norton RS, Vaux DL, Day CL. Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat. Nat Struct Biol 1999; 6: 648-51.
    • (1999) Nat Struct Biol , vol.6 , pp. 648-651
    • Hinds, M.G.1    Norton, R.S.2    Vaux, D.L.3    Day, C.L.4
  • 37
    • 34249799878 scopus 로고    scopus 로고
    • XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization
    • Lu M, Lin SC, Huang Y, et al. XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization. Mol Cell 2007; 26: 689-702.
    • (2007) Mol Cell , vol.26 , pp. 689-702
    • Lu, M.1    Lin, S.C.2    Huang, Y.3
  • 38
    • 33644853217 scopus 로고    scopus 로고
    • Distinct BIR domains of cIAP1 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, et al. Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases. J Biol Chem 2006; 281: 1080-90.
    • (2006) J Biol Chem , vol.281 , pp. 1080-1090
    • Samuel, T.1    Welsh, K.2    Lober, T.3
  • 39
    • 33749389926 scopus 로고    scopus 로고
    • The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-kB activation independently of TRAF1 and TRAF2
    • Varfolomeev E, Wayson SM, Dixit VM, et al. The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-kB activation independently of TRAF1 AND TRAF2. J Biol Chem 2006; 281: 29022-9.
    • (2006) J Biol Chem , vol.281 , pp. 29022-29029
    • Varfolomeev, E.1    Wayson, S.M.2    Dixit, V.M.3
  • 40
    • 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, et al. Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation. Mol Cell 2010; 38: 101-13.
    • (2010) Mol Cell , vol.38 , pp. 101-113
    • Zheng, C.1    Kabaleeswaran, V.2    Wang, Y.3
  • 41
    • 0035831019 scopus 로고    scopus 로고
    • Structural basis for the inhibition of caspase-3 by XIAP
    • Riedl SJ, Renatus M, Schwarzenbacher R, et al. Structural basis for the inhibition of caspase-3 by XIAP. Cell 2001; 104: 791-800.
    • (2001) Cell , vol.104 , pp. 791-800
    • Riedl, S.J.1    Renatus, M.2    Schwarzenbacher, R.3
  • 42
    • 0035920126 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes
    • Suzuki Y, Nakabayashi Y, Nakata K, et al. X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes. J Biol Chem 2001; 276: 27058-63.
    • (2001) J Biol Chem , vol.276 , pp. 27058-27063
    • Suzuki, Y.1    Nakabayashi, Y.2    Nakata, K.3
  • 43
    • 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, et al. 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
  • 44
    • 14844323968 scopus 로고    scopus 로고
    • XIAP inhibits caspase-3 and -7 using two binding sites: Evolutionarily conserved mechanism of IAPs
    • Scott FL, Denault JB, Riedl SJ, et al. XIAP inhibits caspase-3 and -7 using two binding sites: evolutionarily conserved mechanism of IAPs. EMBO J 2005; 24: 645-55.
    • (2005) EMBO J , vol.24 , pp. 645-655
    • Scott, F.L.1    Denault, J.B.2    Riedl, S.J.3
  • 45
    • 0037291737 scopus 로고    scopus 로고
    • Mechanism of XIAP-mediated inhibition of caspase-9
    • Shiozaki EN, Chai J, Rigotti DJ, et al. Mechanism of XIAP-mediated inhibition of caspase-9. Mol Cell 2003; 11: 519-27.
    • (2003) Mol Cell , vol.11 , pp. 519-527
    • Shiozaki, E.N.1    Chai, J.2    Rigotti, D.J.3
  • 46
    • 0035282570 scopus 로고    scopus 로고
    • A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis
    • Srinivasula SM, Hegde R, Saleh A, et al. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis. Nature 2001; 410: 112-6.
    • (2001) Nature , vol.410 , pp. 112-116
    • Srinivasula, S.M.1    Hegde, R.2    Saleh, A.3
  • 47
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs, NF-kB activation, and TNFα-dependent apoptosis
    • Varfolomeev E, Blankenship JW, Wayson SM, et al. IAP antagonists induce autoubiquitination of c-IAPs, NF-kB activation, and TNFα-dependent apoptosis. Cell 2007; 131: 669-81.
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1    Blankenship, J.W.2    Wayson, S.M.3
  • 48
    • 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, et al. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102: 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3
  • 49
    • 1542782158 scopus 로고    scopus 로고
    • Requirement of both the second and third BIR domains for the relief of X-linked inhibitor of apoptosis protein (XIAP)-mediated caspase inhibition by Smac
    • Huang Y, Rich RL, Myszka DG, Wu H. Requirement of both the second and third BIR domains for the relief of X-linked inhibitor of apoptosis protein (XIAP)-mediated caspase inhibition by Smac. J Biol Chem 2003; 278: 49517-22.
    • (2003) J Biol Chem , vol.278 , pp. 49517-49522
    • Huang, Y.1    Rich, R.L.2    Myszka, D.G.3    Wu, H.4
  • 50
  • 51
    • 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, et al. Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance. Proc Natl Acad Sci USA 2005; 102: 16182-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16182-16187
    • Silke, J.1    Kratina, T.2    Chu, D.3
  • 52
    • 77449084943 scopus 로고    scopus 로고
    • Assembling the building blocks: Structure and function of inhibitor of apoptosis proteins
    • Mace PD, Shirley S, Day CL. Assembling the building blocks: structure and function of inhibitor of apoptosis proteins. Cell Death Differ 2010; 17: 46-53.
    • (2010) Cell Death Differ , vol.17 , pp. 46-53
    • Mace, P.D.1    Shirley, S.2    Day, C.L.3
  • 53
    • 78650300883 scopus 로고    scopus 로고
    • c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling
    • Dynek JN, Goncharov T, Dueber EC, et al. c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling. EMBO J 2010; 29: 4198-209.
    • (2010) EMBO J , vol.29 , pp. 4198-4209
    • Dynek, J.N.1    Goncharov, T.2    Dueber, E.C.3
  • 54
    • 50049110244 scopus 로고    scopus 로고
    • Regulation of apoptosis by XIAP ubiquitin-ligase activity
    • Schile AJ, Garcia-Fernandez M, Steller H. Regulation of apoptosis by XIAP ubiquitin-ligase activity. Genes Dev 2008; 22: 2256-66.
    • (2008) Genes Dev , vol.22 , pp. 2256-2266
    • Schile, A.J.1    Garcia-Fernandez, M.2    Steller, H.3
  • 55
    • 0036300214 scopus 로고    scopus 로고
    • The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis
    • Wilson R, Goyal L, Ditzel M, et al. The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis. Nat Cell Biol 2002; 4: 445-50.
    • (2002) Nat Cell Biol , vol.4 , pp. 445-450
    • Wilson, R.1    Goyal, L.2    Ditzel, M.3
  • 56
    • 58249086500 scopus 로고    scopus 로고
    • Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2(1)
    • Blankenship JW, Varfolomeev E, Goncharov T, et al. Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2(1). Biochem J 2009; 417: 149-60.
    • (2009) Biochem J , vol.417 , pp. 149-160
    • Blankenship, J.W.1    Varfolomeev, E.2    Goncharov, T.3
  • 57
    • 55549140475 scopus 로고    scopus 로고
    • IAPs contain an evolutionarily conserved ubiquitin-binding domain that regulates NF-kappaB as well as cell survival and oncogenesis
    • Gyrd-Hansen M, Darding M, Miasari M, et al. IAPs contain an evolutionarily conserved ubiquitin-binding domain that regulates NF-kappaB as well as cell survival and oncogenesis. Nat Cell Biol 2008; 10: 1309-17.
    • (2008) Nat Cell Biol , vol.10 , pp. 1309-1317
    • Gyrd-Hansen, M.1    Darding, M.2    Miasari, M.3
  • 59
    • 78650090605 scopus 로고    scopus 로고
    • Ubiquitin makes its mark on immune regulation
    • Malynn BA, Ma A. Ubiquitin makes its mark on immune regulation. Immunity 2010; 33: 843-52.
    • (2010) Immunity , vol.33 , pp. 843-852
    • Malynn, B.A.1    Ma, A.2
  • 61
    • 0033607313 scopus 로고    scopus 로고
    • The NF-kappaB activation pathway: A paradigm in information transfer from membrane to nucleus
    • Rothwarf DM, Karin M. The NF-kappaB activation pathway: a paradigm in information transfer from membrane to nucleus. Sci STKE 1999; 1999: RE1.
    • (1999) Sci STKE , vol.1999
    • Rothwarf, D.M.1    Karin, M.2
  • 62
    • 33750443289 scopus 로고    scopus 로고
    • IκB kinase complexes: Gateways to NF-κB activation and transcription
    • Scheidereit C. IκB kinase complexes: gateways to NF-κB activation and transcription. Oncogene 2006; 25: 6685-705.
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 63
    • 84858627919 scopus 로고    scopus 로고
    • Cellular Inhibitors of apoptosis are global regulators of NF-kappaB and MAPK activation by members of the TNF family of receptors
    • Varfolomeev E, Goncharov T, Maecker H, et al. Cellular Inhibitors of apoptosis are global regulators of NF-kappaB and MAPK activation by members of the TNF family of receptors. Sci Signal 2012; 5: ra22.
    • (2012) Sci Signal , vol.5
    • Varfolomeev, E.1    Goncharov, T.2    Maecker, H.3
  • 64
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP, et al. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 2006; 22: 245-57.
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3
  • 65
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex
    • Tokunaga F, Nakagawa T, Nakahara M, et al. SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex. Nature 2011; 471: 633-6.
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1    Nakagawa, T.2    Nakahara, M.3
  • 66
    • 79952623655 scopus 로고    scopus 로고
    • cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production
    • Vanlangenakker N, Vanden Berghe T, Bogaert P, et al. cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production. Cell Death Differ 2011; 18: 656-65.
    • (2011) Cell Death Differ , vol.18 , pp. 656-665
    • Vanlangenakker, N.1    Vanden Berghe, T.2    Bogaert, P.3
  • 67
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach B, Cordier SM, Schmukle AC, et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 2011; 471: 591-6.
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1    Cordier, S.M.2    Schmukle, A.C.3
  • 68
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis
    • Ikeda F, Deribe YL, Skanland SS, et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis. Nature 2011; 471: 637-41.
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1    Deribe, Y.L.2    Skanland, S.S.3
  • 69
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis
    • Ting AT, Pimentel-Muinos FX, Seed B. RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis. EMBO J 1996; 15: 6189-96.
    • (1996) EMBO J , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muinos, F.X.2    Seed, B.3
  • 70
    • 0035021123 scopus 로고    scopus 로고
    • The alpha and beta subunits of IkappaB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF
    • Devin A, Lin Y, Yamaoka S, et al. The alpha and beta subunits of IkappaB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF. Mol Cell Biol 2001; 21: 3986-94.
    • (2001) Mol Cell Biol , vol.21 , pp. 3986-3994
    • Devin, A.1    Lin, Y.2    Yamaoka, S.3
  • 71
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C, Deng L, Hong M, et al. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 2001; 412: 346-51.
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3
  • 72
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato J, Mercurio F, Rosette C, et al. Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation. Mol Cell Biol 1996; 16: 1295-304.
    • (1996) Mol Cell Biol , vol.16 , pp. 1295-1304
    • DiDonato, J.1    Mercurio, F.2    Rosette, C.3
  • 73
    • 17944401842 scopus 로고    scopus 로고
    • Identification of the receptor component of the IkappaBalpha-ubiquitin ligase
    • Yaron A, Hatzubai A, Davis M, et al. Identification of the receptor component of the IkappaBalpha-ubiquitin ligase. Nature 1998; 396: 590-4.
    • (1998) Nature , vol.396 , pp. 590-594
    • Yaron, A.1    Hatzubai, A.2    Davis, M.3
  • 74
    • 44749088134 scopus 로고    scopus 로고
    • Crosstalk via the NF-kappaB signaling system
    • Basak S, Hoffmann A. Crosstalk via the NF-kappaB signaling system. Cytokine Growth Factor Rev 2008; 19: 187-97.
    • (2008) Cytokine Growth Factor Rev , vol.19 , pp. 187-197
    • Basak, S.1    Hoffmann, A.2
  • 75
    • 33947506490 scopus 로고    scopus 로고
    • Specificity of TRAF3 in its negative regulation of the noncanonical NF-kappa B pathway
    • He JQ, Saha SK, Kang JR, et al. Specificity of TRAF3 in its negative regulation of the noncanonical NF-kappa B pathway. J Biol Chem 2007; 282: 3688-94.
    • (2007) J Biol Chem , vol.282 , pp. 3688-3694
    • He, J.Q.1    Saha, S.K.2    Kang, J.R.3
  • 76
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1
    • Malinin NL, Boldin MP, Kovalenko AV, Wallach D. MAP3K-related kinase involved in NF-kappaB 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
  • 77
    • 56349164232 scopus 로고    scopus 로고
    • Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling
    • Vallabhapurapu S, Matsuzawa A, Zhang W, et al. Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling. Nat Immunol 2008; 9: 1364-70.
    • (2008) Nat Immunol , vol.9 , pp. 1364-1370
    • Vallabhapurapu, S.1    Matsuzawa, A.2    Zhang, W.3
  • 78
    • 0034745420 scopus 로고    scopus 로고
    • NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100
    • Xiao G, Harhaj EW, Sun SC. NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100. Mol Cell 2001; 7: 401-9.
    • (2001) Mol Cell , vol.7 , pp. 401-409
    • Xiao, G.1    Harhaj, E.W.2    Sun, S.C.3
  • 79
    • 0035266318 scopus 로고    scopus 로고
    • XIAP regulates Akt activity and caspase-3-dependent cleavage during cisplatin-induced apoptosis in human ovarian epithelial cancer cells
    • Asselin E, Mills GB, Tsang BK. XIAP regulates Akt activity and caspase-3-dependent cleavage during cisplatin-induced apoptosis in human ovarian epithelial cancer cells. Cancer Res 2001; 61: 1862-8.
    • (2001) Cancer Res , vol.61 , pp. 1862-1868
    • Asselin, E.1    Mills, G.B.2    Tsang, B.K.3
  • 80
    • 0035854738 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein functions as a cofactor in transforming growth factor-beta signaling
    • Birkey Reffey S, Wurthner JU, Parks WT, et al. X-linked inhibitor of apoptosis protein functions as a cofactor in transforming growth factor-beta signaling. J Biol Chem 2001; 276: 26542-9.
    • (2001) J Biol Chem , vol.276 , pp. 26542-26549
    • Birkey Reffey, S.1    Wurthner, J.U.2    Parks, W.T.3
  • 81
    • 0036178047 scopus 로고    scopus 로고
    • IAP suppression of apoptosis involves distinct mechanisms: The TAK1/JNK1 signaling cascade and caspase inhibition
    • Sanna MG, da Silva Correia J, Ducrey O, et al. IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1 signaling cascade and caspase inhibition. Mol Cell Biol 2002; 22: 1754-66.
    • (2002) Mol Cell Biol , vol.22 , pp. 1754-1766
    • Sanna, M.G.1    Da Silva Correia, J.2    Ducrey, O.3
  • 82
    • 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. J Biol Chem 2007; 282: 7777-82.
    • (2007) J Biol Chem , vol.282 , pp. 7777-7782
    • Zhao, Y.1    Conze, D.B.2    Hanover, J.A.3    Ashwell, J.D.4
  • 83
    • 36749047445 scopus 로고    scopus 로고
    • c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for Mad1
    • Xu L, Zhu J, Hu X, et al. c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for Mad1. Mol Cell 2007; 28: 914-22.
    • (2007) Mol Cell , vol.28 , pp. 914-922
    • Xu, L.1    Zhu, J.2    Hu, X.3
  • 84
    • 61849157254 scopus 로고    scopus 로고
    • TNFR signaling: Ubiquitin-conjugated TRAFfic signals control stop-and-go for MAPK signaling complexes
    • Karin M, Gallagher E. TNFR signaling: ubiquitin-conjugated TRAFfic signals control stop-and-go for MAPK signaling complexes. Immunol Rev 2009; 228: 225-40.
    • (2009) Immunol Rev , vol.228 , pp. 225-240
    • Karin, M.1    Gallagher, E.2
  • 85
    • 79954583057 scopus 로고    scopus 로고
    • Deletion of cIAP1 and cIAP2 in murine B lymphocytes constitutively activates cell survival pathways and inactivates the germinal center response
    • Gardam S, Turner VM, Anderton H, et al. Deletion of cIAP1 and cIAP2 in murine B lymphocytes constitutively activates cell survival pathways and inactivates the germinal center response. Blood 2011; 117: 4041-51.
    • (2011) Blood , vol.117 , pp. 4041-4051
    • Gardam, S.1    Turner, V.M.2    Anderton, H.3
  • 86
    • 34250888664 scopus 로고    scopus 로고
    • Nod1/RICK and TLR signaling regulate chemokine and antimicrobial innate immune responses in mesothelial cells
    • Park JH, Kim YG, Shaw M, et al. Nod1/RICK and TLR signaling regulate chemokine and antimicrobial innate immune responses in mesothelial cells. J Immunol 2007; 179: 514-21.
    • (2007) J Immunol , vol.179 , pp. 514-521
    • Park, J.H.1    Kim, Y.G.2    Shaw, M.3
  • 87
    • 38549084725 scopus 로고    scopus 로고
    • A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation
    • Hasegawa M, Fujimoto Y, Lucas PC, et al. A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation. EMBO J 2008; 27: 373-83.
    • (2008) EMBO J , vol.27 , pp. 373-383
    • Hasegawa, M.1    Fujimoto, Y.2    Lucas, P.C.3
  • 88
    • 0034698053 scopus 로고    scopus 로고
    • Activation of NF-kappa B by XIAP, the X chromosome-linked inhibitor of apoptosis, in endothelial cells involves TAK1
    • Hofer-Warbinek R, Schmid JA, Stehlik C, et al. Activation of NF-kappa B by XIAP, the X chromosome-linked inhibitor of apoptosis, in endothelial cells involves TAK1. J Biol Chem 2000; 275: 22064-8.
    • (2000) J Biol Chem , vol.275 , pp. 22064-22068
    • Hofer-Warbinek, R.1    Schmid, J.A.2    Stehlik, C.3
  • 89
    • 70149099161 scopus 로고    scopus 로고
    • XIAP mediates NOD signaling via interaction with RIP2
    • Krieg A, Correa RG, Garrison JB, et al. XIAP mediates NOD signaling via interaction with RIP2. Proc Natl Acad Sci USA 2009; 106: 14524-9.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14524-14529
    • Krieg, A.1    Correa, R.G.2    Garrison, J.B.3
  • 90
    • 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, et al. The Ubiquitin Ligase XIAP Recruits LUBAC for NOD2 Signaling in Inflammation and Innate Immunity. Mol Cell 2012; 46: 746-58.
    • (2012) Mol Cell , vol.46 , pp. 746-758
    • Damgaard, R.B.1    Nachbur, U.2    Yabal, M.3
  • 91
    • 77951247349 scopus 로고    scopus 로고
    • Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response
    • Mao AP, Li S, Zhong B, et al. Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response. J Biol Chem 2010; 285: 9470-6.
    • (2010) J Biol Chem , vol.285 , pp. 9470-9476
    • Mao, A.P.1    Li, S.2    Zhong, B.3
  • 92
    • 84857404572 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation
    • Vince JE, Wong WW, Gentle I, et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity 2012; 36: 215-27.
    • (2012) Immunity , vol.36 , pp. 215-227
    • Vince, J.E.1    Wong, W.W.2    Gentle, I.3
  • 93
    • 84856812315 scopus 로고    scopus 로고
    • IkappaB kinase epsilon- Dependent phosphorylation and degradation of X-linked inhibitor of apoptosis sensitizes cells to virus-induced apoptosis
    • Nakhaei P, Sun Q, Solis M, et al. IkappaB kinase epsilon- dependent phosphorylation and degradation of X-linked inhibitor of apoptosis sensitizes cells to virus-induced apoptosis. J Virol 2012; 86: 726-37.
    • (2012) J Virol , vol.86 , pp. 726-737
    • Nakhaei, P.1    Sun, Q.2    Solis, M.3
  • 94
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: Crucial integrators of cellular stress
    • Meylan E, Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem Sci 2005; 30: 151-9.
    • (2005) Trends Biochem Sci , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 96
    • 84859467770 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
    • Zhao J, Jitkaew S, Cai Z, et al. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc Natl Acad Sci USA 2012; 109: 5322-7.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5322-5327
    • Zhao, J.1    Jitkaew, S.2    Cai, Z.3
  • 97
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • Sun L, Wang H, Wang Z, et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 2012; 148: 213-27.
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1    Wang, H.2    Wang, Z.3
  • 98
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang Z, Jiang H, Chen S, et al. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 2012; 148: 228-43.
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.1    Jiang, H.2    Chen, S.3
  • 100
    • 80054750078 scopus 로고    scopus 로고
    • In vivo and in vitro determination of cell death markers in neurons
    • Naniche N, Sau D, Pasinelli P. In vivo and in vitro determination of cell death markers in neurons. Methods Mol Biol 2011; 793: 9-21.
    • (2011) Methods Mol Biol , vol.793 , pp. 9-21
    • Naniche, N.1    Sau, D.2    Pasinelli, P.3
  • 101
  • 102
    • 17144438370 scopus 로고    scopus 로고
    • Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias
    • Tamm I, Kornblau SM, Segall H, et al. Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin Cancer Res 2000; 6: 1796-803.
    • (2000) Clin Cancer Res , vol.6 , pp. 1796-1803
    • Tamm, I.1    Kornblau, S.M.2    Segall, H.3
  • 103
    • 79951655008 scopus 로고    scopus 로고
    • Inhibitor of apoptosis protein family as diagnostic markers and therapeutic targets of colorectal cancer
    • Miura K, Fujibuchi W, Ishida K, et al. Inhibitor of apoptosis protein family as diagnostic markers and therapeutic targets of colorectal cancer. Surg Today 2011; 41: 175-82.
    • (2011) Surg Today , vol.41 , pp. 175-182
    • Miura, K.1    Fujibuchi, W.2    Ishida, K.3
  • 104
    • 34248195931 scopus 로고    scopus 로고
    • Immunohistochemical detection of antiapoptotic protein X-linked inhibitor of apoptosis in mammary carcinoma
    • Jaffer S, Orta L, Sunkara S, et al. Immunohistochemical detection of antiapoptotic protein X-linked inhibitor of apoptosis in mammary carcinoma. Hum Pathol 2007; 38: 864-70.
    • (2007) Hum Pathol , vol.38 , pp. 864-870
    • Jaffer, S.1    Orta, L.2    Sunkara, S.3
  • 105
    • 33846973344 scopus 로고    scopus 로고
    • The X-linked inhibitor of apoptosis protein (XIAP) is up-regulated in metastatic melanoma, and XIAP cleavage by Phenoxodiol is associated with Carboplatin sensitization
    • Kluger HM, McCarthy MM, Alvero AB, et al. The X-linked inhibitor of apoptosis protein (XIAP) is up-regulated in metastatic melanoma, and XIAP cleavage by Phenoxodiol is associated with Carboplatin sensitization. J Transl Med 2007; 5: 6.
    • (2007) J Transl Med , vol.5 , pp. 6
    • Kluger, H.M.1    McCarthy, M.M.2    Alvero, A.B.3
  • 106
    • 0034885949 scopus 로고    scopus 로고
    • Expression of X-linked inhibitor of apoptosis as a novel prognostic marker in radically resected non-small cell lung cancer patients
    • Ferreira CG, van der Valk P, Span SW, et al. Expression of X-linked inhibitor of apoptosis as a novel prognostic marker in radically resected non-small cell lung cancer patients. Clin Cancer Res 2001; 7: 2468-74.
    • (2001) Clin Cancer Res , vol.7 , pp. 2468-2474
    • Ferreira, C.G.1    Van Der Valk, P.2    Span, S.W.3
  • 107
    • 0036733756 scopus 로고    scopus 로고
    • Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy
    • Imoto I, Tsuda H, Hirasawa A, et al. Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy. Cancer Res 2002; 62: 4860-6.
    • (2002) Cancer Res , vol.62 , pp. 4860-4866
    • Imoto, I.1    Tsuda, H.2    Hirasawa, A.3
  • 108
    • 33750589355 scopus 로고    scopus 로고
    • IAP family protein expression correlates with poor outcome of multiple myeloma patients in association with chemotherapy-induced overexpression of multidrug resistance genes
    • Nakagawa Y, Abe S, Kurata M, et al. IAP family protein expression correlates with poor outcome of multiple myeloma patients in association with chemotherapy-induced overexpression of multidrug resistance genes. Am J Hematol 2006; 81: 824-31.
    • (2006) Am J Hematol , vol.81 , pp. 824-831
    • Nakagawa, Y.1    Abe, S.2    Kurata, M.3
  • 109
    • 0033151510 scopus 로고    scopus 로고
    • The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas
    • Dierlamm J, Baens M, Wlodarska I, et al. The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas. Blood 1999; 93: 3601-9.
    • (1999) Blood , vol.93 , pp. 3601-3609
    • Dierlamm, J.1    Baens, M.2    Wlodarska, I.3
  • 110
    • 70449715589 scopus 로고    scopus 로고
    • Masking MALT1: The paracaspase's potential for cancer therapy
    • Vucic D, Dixit VM. Masking MALT1: the paracaspase's potential for cancer therapy. J Exp Med 2009; 206: 2309-12.
    • (2009) J Exp Med , vol.206 , pp. 2309-2312
    • Vucic, D.1    Dixit, V.M.2
  • 111
    • 26244446246 scopus 로고    scopus 로고
    • Melanoma inhibitor of apoptosis protein is expressed differentially in melanoma and melanocytic naevus, but similarly in primary and metastatic melanomas
    • Gong J, Chen N, Zhou Q, et al. Melanoma inhibitor of apoptosis protein is expressed differentially in melanoma and melanocytic naevus, but similarly in primary and metastatic melanomas. J Clin Pathol 2005; 58: 1081-5.
    • (2005) J Clin Pathol , vol.58 , pp. 1081-1085
    • Gong, J.1    Chen, N.2    Zhou, Q.3
  • 112
    • 33751086477 scopus 로고    scopus 로고
    • The anti-apoptotic livin gene is an important determinant for the apoptotic resistance of non-small cell lung cancer cells
    • Crnkovic-Mertens I, Muley T, Meister M, et al. The anti-apoptotic livin gene is an important determinant for the apoptotic resistance of non-small cell lung cancer cells. Lung Cancer 2006; 54: 135-42.
    • (2006) Lung Cancer , vol.54 , pp. 135-142
    • Crnkovic-Mertens, I.1    Muley, T.2    Meister, M.3
  • 113
    • 84862500452 scopus 로고    scopus 로고
    • Immunity to the melanoma inhibitor of apoptosis protein (ML-IAP; livin) in patients with malignant melanoma
    • Zhou J, Yuen NK, Zhan Q, et al. Immunity to the melanoma inhibitor of apoptosis protein (ML-IAP; livin) in patients with malignant melanoma. Cancer Immunol Immunother 2012; 61: 655-65.
    • (2012) Cancer Immunol Immunother , vol.61 , pp. 655-665
    • Zhou, J.1    Yuen, N.K.2    Zhan, Q.3
  • 114
    • 44849094211 scopus 로고    scopus 로고
    • Microphthalmia-associated transcription factor is a critical transcriptional regulator of melanoma inhibitor of apoptosis in melanomas
    • Dynek JN, Chan SM, Liu J, et al. Microphthalmia-associated transcription factor is a critical transcriptional regulator of melanoma inhibitor of apoptosis in melanomas. Cancer Res 2008; 68: 3124-32.
    • (2008) Cancer Res , vol.68 , pp. 3124-3132
    • Dynek, J.N.1    Chan, S.M.2    Liu, J.3
  • 116
    • 70349309831 scopus 로고    scopus 로고
    • Intracellular localization of survivin determines biological behavior in colorectal cancer
    • Qi G, Tuncel H, Aoki E, et al. Intracellular localization of survivin determines biological behavior in colorectal cancer. Oncol Rep 2009; 22: 557-62.
    • (2009) Oncol Rep , vol.22 , pp. 557-562
    • Qi, G.1    Tuncel, H.2    Aoki, E.3
  • 117
    • 70349329714 scopus 로고    scopus 로고
    • Smac mimetics as new cancer therapeutics
    • Chen DJ, Huerta S. Smac mimetics as new cancer therapeutics. Anticancer Drugs 2009; 20: 646-58.
    • (2009) Anticancer Drugs , vol.20 , pp. 646-658
    • Chen, D.J.1    Huerta, S.2
  • 118
    • 76149118435 scopus 로고    scopus 로고
    • Small-molecule pan-IAP antagonists: A patent review
    • Flygare JA, Fairbrother WJ. Small-molecule pan-IAP antagonists: a patent review. Expert Opin Ther Pat 2010; 20: 251-67.
    • (2010) Expert Opin Ther Pat , vol.20 , pp. 251-267
    • Flygare, J.A.1    Fairbrother, W.J.2
  • 119
    • 37749037799 scopus 로고    scopus 로고
    • Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs
    • Zobel K, Wang L, Varfolomeev E, et al. Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs. ACS Chem Biol 2006; 1: 525-33.
    • (2006) ACS Chem Biol , vol.1 , pp. 525-533
    • Zobel, K.1    Wang, L.2    Varfolomeev, E.3
  • 120
    • 37049019494 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a potent, nonpeptide, cell-permeable, bivalent Smac mimetic that concurrently targets both the BIR2 and BIR3 domains in XIAP
    • Sun H, Nikolovska-Coleska Z, Lu J, et al. Design, synthesis, and characterization of a potent, nonpeptide, cell-permeable, bivalent Smac mimetic that concurrently targets both the BIR2 and BIR3 domains in XIAP. J Am Chem Soc 2007; 129: 15279-94.
    • (2007) J Am Chem Soc , vol.129 , pp. 15279-15294
    • Sun, H.1    Nikolovska-Coleska, Z.2    Lu, J.3
  • 121
    • 71749083634 scopus 로고    scopus 로고
    • X Chromosome- Linked inhibitor of apoptosis regulates cell death induction by proapoptotic receptor agonists
    • Varfolomeev E, Alicke B, Elliott JM, et al. X Chromosome- linked inhibitor of apoptosis regulates cell death induction by proapoptotic receptor agonists. J Biol Chem 2009; 284: 34553-60.
    • (2009) J Biol Chem , vol.284 , pp. 34553-34560
    • Varfolomeev, E.1    Alicke, B.2    Elliott, J.M.3
  • 122
    • 36148954336 scopus 로고    scopus 로고
    • IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis
    • Vince JE, Wong WW, Khan N, et al. IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis. Cell 2007; 131: 682-93.
    • (2007) Cell , vol.131 , pp. 682-693
    • Vince, J.E.1    Wong, W.W.2    Khan, N.3
  • 123
    • 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, et al. Autocrine TNFalpha signaling renders human cancer cells susceptible to smac-mimetic-induced apoptosis. Cancer Cell 2007; 12: 445-56.
    • (2007) Cancer Cell , vol.12 , pp. 445-456
    • Petersen, S.L.1    Wang, L.2    Yalcin-Chin, A.3
  • 124
    • 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, et al. A Smac mimetic rescue screen reveals roles for inhibitor of apoptosis proteins in tumor necrosis factor-alpha signaling. Cancer Res 2007; 67: 11493-8.
    • (2007) Cancer Res , vol.67 , pp. 11493-11498
    • Gaither, A.1    Porter, D.2    Yao, Y.3
  • 125
    • 80054837173 scopus 로고    scopus 로고
    • Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination
    • Dueber EC, Schoeffler AJ, Lingel A, et al. Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination. Science 2011; 334: 376-80.
    • (2011) Science , vol.334 , pp. 376-380
    • Dueber, E.C.1    Schoeffler, A.J.2    Lingel, A.3
  • 126
    • 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, et al. Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization. J Biol Chem 2011; 286: 17015-28.
    • (2011) J Biol Chem , vol.286 , pp. 17015-17028
    • Feltham, R.1    Bettjeman, B.2    Budhidarmo, R.3
  • 127
    • 80054817975 scopus 로고    scopus 로고
    • Smac mimetic bypasses apoptosis resistance in FADD- Or caspase-8-deficient cells by priming for tumor necrosis factor alpha-induced necroptosis
    • Laukens B, Jennewein C, Schenk B, et al. Smac mimetic bypasses apoptosis resistance in FADD- or caspase-8-deficient cells by priming for tumor necrosis factor alpha-induced necroptosis. Neoplasia 2011; 13: 971-9.
    • (2011) Neoplasia , vol.13 , pp. 971-979
    • Laukens, B.1    Jennewein, C.2    Schenk, B.3
  • 128
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • He S, Wang L, Miao L, et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 2009; 137: 1100-11.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3
  • 129
    • 56449103218 scopus 로고    scopus 로고
    • SM-164: A novel, bivalent Smac mimetic that induces apoptosis and tumor regression by concurrent removal of the blockade of cIAP-1/2 and XIAP
    • Lu J, Bai L, Sun H, Nikolovska-Coleska Z, et al. SM-164: a novel, bivalent Smac mimetic that induces apoptosis and tumor regression by concurrent removal of the blockade of cIAP-1/2 and XIAP. Cancer Res 2008; 68: 9384-93.
    • (2008) Cancer Res , vol.68 , pp. 9384-9393
    • Lu, J.1    Bai, L.2    Sun, H.3    Nikolovska-Coleska, Z.4
  • 130
    • 77955376177 scopus 로고    scopus 로고
    • Overcoming cancer cell resistance to Smac mimetic induced apoptosis by modulating cIAP-2 expression
    • Petersen SL, Peyton M, Minna JD, Wang X. Overcoming cancer cell resistance to Smac mimetic induced apoptosis by modulating cIAP-2 expression. Proc Natl Acad Sci USA 2010; 107: 11936-41.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11936-11941
    • Petersen, S.L.1    Peyton, M.2    Minna, J.D.3    Wang, X.4
  • 131
    • 69249208481 scopus 로고    scopus 로고
    • XIAP discriminates between type i and type II FAS-induced apoptosis
    • Jost PJ, Grabow S, Gray D, et al. XIAP discriminates between type I and type II FAS-induced apoptosis. Nature 2009; 460: 1035-9.
    • (2009) Nature , vol.460 , pp. 1035-1039
    • Jost, P.J.1    Grabow, S.2    Gray, D.3
  • 132
    • 67650787318 scopus 로고    scopus 로고
    • Antagonism of c-IAP and XIAP proteins is required for efficient induction of cell death by small-molecule IAP antagonists
    • Ndubaku C, Varfolomeev E, Wang L, et al. Antagonism of c-IAP and XIAP proteins is required for efficient induction of cell death by small-molecule IAP antagonists. ACS Chem Biol 2009; 4: 557-66.
    • (2009) ACS Chem Biol , vol.4 , pp. 557-566
    • Ndubaku, C.1    Varfolomeev, E.2    Wang, L.3
  • 133
    • 84861034546 scopus 로고    scopus 로고
    • Discovery of a potent small-molecule antagonist of inhibitor of apoptosis (IAP) proteins and clinical candidate for the treatment of cancer (GDC-0152)
    • Flygare JA, Beresini M, Budha N, et al. Discovery of a potent small-molecule antagonist of inhibitor of apoptosis (IAP) proteins and clinical candidate for the treatment of cancer (GDC-0152). J Med Chem 2012; 55: 4101-13.
    • (2012) J Med Chem , vol.55 , pp. 4101-4113
    • Flygare, J.A.1    Beresini, M.2    Budha, N.3
  • 134
    • 84861151960 scopus 로고    scopus 로고
    • Smac mimetic LBW242 sensitizes XIAP-overexpressing neuroblastoma cells for TNF-alpha-independent apoptosis
    • Eschenburg G, Eggert A, Schramm A, et al. Smac mimetic LBW242 sensitizes XIAP-overexpressing neuroblastoma cells for TNF-alpha-independent apoptosis. Cancer Res 2012; 72: 2645-56.
    • (2012) Cancer Res , vol.72 , pp. 2645-2656
    • Eschenburg, G.1    Eggert, A.2    Schramm, A.3
  • 135
    • 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, et al. cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol Cell 2011; 43: 449-63.
    • (2011) Mol Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1    Geserick, P.2    Kellert, B.3
  • 136
    • 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, et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol Cell 2011; 43: 432-48.
    • (2011) Mol Cell , vol.43 , pp. 432-448
    • Tenev, T.1    Bianchi, K.2    Darding, M.3
  • 137
    • 80053933840 scopus 로고    scopus 로고
    • NF-kappaB is required for Smac mimetic-mediated sensitization of glioblastoma cells for gamma-irradiation-induced apoptosis
    • Berger R, Jennewein C, Marschall V, et al. NF-kappaB is required for Smac mimetic-mediated sensitization of glioblastoma cells for gamma-irradiation- induced apoptosis. Mol Cancer Ther 2011; 10: 1867-75.
    • (2011) Mol Cancer Ther , vol.10 , pp. 1867-1875
    • Berger, R.1    Jennewein, C.2    Marschall, V.3
  • 138
    • 70749151909 scopus 로고    scopus 로고
    • A Smac-mimetic sensitizes prostate cancer cells to TRAIL-induced apoptosis via modulating both IAPs and NF-kappaB
    • Dai Y, Liu M, Tang W, et al. A Smac-mimetic sensitizes prostate cancer cells to TRAIL-induced apoptosis via modulating both IAPs and NF-kappaB. BMC Cancer 2009; 9: 392.
    • (2009) BMC Cancer , vol.9 , pp. 392
    • Dai, Y.1    Liu, M.2    Tang, W.3


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