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Volumn 18, Issue 11, 2004, Pages 1751-1759

Inhibitor of apoptosis proteins: New therapeutic targets in hematological cancer?

Author keywords

Apoptosis; IAP; Inhibitor od apoptosis; Leukemia; Lymphoma; NF B

Indexed keywords

ANTINEOPLASTIC AGENT; ANTISENSE OLIGONUCLEOTIDE; APOPTOSIS INHIBITOR; BORTEZOMIB; CASPASE; IMMUNOMODULATING AGENT; LIVIN; PROTEASOME INHIBITOR; PROTEIN BCL 2; PROTEIN INHIBITOR; REGULATOR PROTEIN; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SMALL INTERFERING RNA; SURVIVIN; UNCLASSIFIED DRUG;

EID: 8844244753     PISSN: 08876924     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.leu.2403493     Document Type: Review
Times cited : (56)

References (158)
  • 1
    • 0033152340 scopus 로고    scopus 로고
    • Biochemical and genetic control of apoptosis: Relevance to normal hematopoiesis and hematological malignancies
    • Wickremasinghe RG, Hoffbrand AV. Biochemical and genetic control of apoptosis: relevance to normal hematopoiesis and hematological malignancies. Blood 1999; 93: 3587-3600.
    • (1999) Blood , vol.93 , pp. 3587-3600
    • Wickremasinghe, R.G.1    Hoffbrand, A.V.2
  • 2
    • 0036234468 scopus 로고    scopus 로고
    • Pathways of apoptosis in lymphocyte development, homeostasis, and disease
    • Rathmell JC, Thompson CB. Pathways of apoptosis in lymphocyte development, homeostasis, and disease. Cell 2002; 109 (Suppl): S97-S107.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Rathmell, J.C.1    Thompson, C.B.2
  • 3
    • 0038393112 scopus 로고    scopus 로고
    • Apoptosis in the development and maintenance of the immune system
    • Opferman JT, Korsmeyer SJ. Apoptosis in the development and maintenance of the immune system. Nat Immunol 2003; 4: 410-415.
    • (2003) Nat. Immunol. , vol.4 , pp. 410-415
    • Opferman, J.T.1    Korsmeyer, S.J.2
  • 4
    • 0022546957 scopus 로고
    • Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma
    • Tsujimoto Y, Croce CM. Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc Natl Acad Sci USA 1986; 83: 5214-5218.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 5
    • 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, Stefanova-Ouzounova M, Hernandez JM, Hossfeld DK 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: 3601-3609.
    • (1999) Blood , vol.93 , pp. 3601-3609
    • Dierlamm, J.1    Baens, M.2    Wlodarska, I.3    Stefanova-Ouzounova, M.4    Hernandez, J.M.5    Hossfeld, D.K.6
  • 6
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell 1997; 88 355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 7
    • 0642283970 scopus 로고    scopus 로고
    • Regulation of proliferation, survival and apoptosis by members of the TNF superfamily
    • Gaur U, Aggarwal BB. Regulation of proliferation, survival and apoptosis by members of the TNF superfamily. Biochem Pharmacol 2003; 66: 1403-1408.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1403-1408
    • Gaur, U.1    Aggarwal, B.B.2
  • 8
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S, Adams JM. The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2002; 2: 647-656.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 9
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD, Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 2003; 112 481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 10
    • 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 2168-2174.
    • (1993) J. Virol. , vol.67 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 11
    • 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: 2521-2528.
    • (1994) J. Virol. , vol.68 , pp. 2521-2528
    • Birnbaum, M.J.1    Clem, R.J.2    Miller, L.K.3
  • 12
    • 13344278692 scopus 로고    scopus 로고
    • Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes
    • Liston P, Roy N, Tamai K, Lefebvre C, Baird S, Cherton-Horvat G et al. Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes. Nature 1996; 379: 349-353.
    • (1996) Nature , vol.379 , pp. 349-353
    • Liston, P.1    Roy, N.2    Tamai, K.3    Lefebvre, C.4    Baird, S.5    Cherton-Horvat, G.6
  • 13
    • 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: 1243-1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 14
    • 0029953942 scopus 로고    scopus 로고
    • Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors
    • Uren AG, Pakusch M, Hawkins CJ, Puls KL, Vaux DL. Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors. Proc Natl Acad Sci USA 1996; 93: 4974-4978.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4974-4978
    • Uren, A.G.1    Pakusch, M.2    Hawkins, C.J.3    Puls, K.L.4    Vaux, D.L.5
  • 15
    • 15844425961 scopus 로고    scopus 로고
    • A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors
    • Duckett CS, Nava VE, Gedrich RW, Clem RJ, Van Dongen JL, Gilfillan MC et al. A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors. EMBO J 1996; 15: 2685-2694.
    • (1996) EMBO J. , vol.15 , pp. 2685-2694
    • Duckett, C.S.1    Nava, V.E.2    Gedrich, R.W.3    Clem, R.J.4    Van Dongen, J.L.5    Gilfillan, M.C.6
  • 16
    • 0030746636 scopus 로고    scopus 로고
    • A novel antiapoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini G, Adida C, Altieri DC. A novel antiapoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997; 3: 917-921.
    • (1997) Nat. Med. , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.C.3
  • 17
    • 0034597630 scopus 로고    scopus 로고
    • ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas
    • Vucic D, Stennicke HR, Pisabarro MT, Salvesen GS, Dixit VM. ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas. Curr Biol 2000; 10: 1359-1366.
    • (2000) Curr. Biol. , vol.10 , pp. 1359-1366
    • Vucic, D.1    Stennicke, H.R.2    Pisabarro, M.T.3    Salvesen, G.S.4    Dixit, V.M.5
  • 18
    • 0035793557 scopus 로고    scopus 로고
    • Livin, a novel inhibitor of apoptosis protein family member
    • Kasof CM, Gomes BC. Livin, a novel inhibitor of apoptosis protein family member. J Biol Chem 2001; 276: 3238-3246.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3238-3246
    • Kasof, C.M.1    Gomes, B.C.2
  • 19
    • 0032526948 scopus 로고    scopus 로고
    • A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors
    • Hauser HP, Bardroff M, Pyrowolakis G, Jentsch S. A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. J Cell Biol 1998; 141: 1415-1422.
    • (1998) J. Cell Biol. , vol.141 , pp. 1415-1422
    • Hauser, H.P.1    Bardroff, M.2    Pyrowolakis, G.3    Jentsch, S.4
  • 21
    • 0034967005 scopus 로고    scopus 로고
    • Molecular cloning of ILP-2, a novel member of the inhibitor of apoptosis protein family
    • Richter BW, Mir SS, Eiben LJ, Lewis J, Reffey SB, Frattini A et al. Molecular cloning of ILP-2, a novel member of the inhibitor of apoptosis protein family. Mol Cell Biol 2001; 21: 4292-4301.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 4292-4301
    • Richter, B.W.1    Mir, S.S.2    Eiben, L.J.3    Lewis, J.4    Reffey, S.B.5    Frattini, A.6
  • 22
    • 0032410818 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) and their emerging role in cancer
    • LaCasse EC, Baird S, Korneluk RG, MacKenzie AE. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene 1998; 17: 3247-3259.
    • (1998) Oncogene , vol.17 , pp. 3247-3259
    • LaCasse, E.C.1    Baird, S.2    Korneluk, R.G.3    MacKenzie, A.E.4
  • 23
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins - Suppressors of apoptosis
    • Deveraux QL, Reed JC. IAP family proteins - suppressors of apoptosis. Genes Dev 1999; 13: 239-252.
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 24
    • 0346880501 scopus 로고    scopus 로고
    • The inhibitors of apoptosis: There is more to life than Bcl2
    • Liston P, Fong WG, Korneluk RG. The inhibitors of apoptosis: there is more to life than Bcl2. Oncogene 2003; 22: 8568-8580.
    • (2003) Oncogene , vol.22 , pp. 8568-8580
    • Liston, P.1    Fong, W.G.2    Korneluk, R.G.3
  • 25
    • 0032522738 scopus 로고    scopus 로고
    • IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases
    • Deveraux QL, Roy N, Stennicke HR, Van Arsdale T, Zhou Q, Srinivasula SM et al. IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. EMBO J 1998; 17: 2215-2223.
    • (1998) EMBO J. , vol.17 , pp. 2215-2223
    • Deveraux, Q.L.1    Roy, N.2    Stennicke, H.R.3    Van Arsdale, T.4    Zhou, Q.5    Srinivasula, S.M.6
  • 27
    • 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, Datta P, Shiozaki E, Chai J et al. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis. Nature 2001; 410: 112-116.
    • (2001) Nature , vol.410 , pp. 112-116
    • Srinivasula, S.M.1    Hegde, R.2    Saleh, A.3    Datta, P.4    Shiozaki, E.5    Chai, J.6
  • 29
    • 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: 781-790.
    • (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
  • 31
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J 1997; 16: 6914-6925.
    • (1997) EMBO J. , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 32
    • 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, Reed JC, Takahashi R. X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes. J Biol Chem 2001; 276: 27058-27063.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27058-27063
    • Suzuki, Y.1    Nakabayashi, Y.2    Nakata, K.3    Reed, J.C.4    Takahashi, R.5
  • 33
    • 0035969963 scopus 로고    scopus 로고
    • An antiapoptotic protein human survivin is a direct inhibitor of caspase-3 and -7
    • Shin S, Sung BJ, Cho YS, Kim HJ, Ha NC, Hwang JI et al. An antiapoptotic protein human survivin is a direct inhibitor of caspase-3 and -7. Biochemistry 2001; 40: 1117-1123.
    • (2001) Biochemistry , vol.40 , pp. 1117-1123
    • Shin, S.1    Sung, B.J.2    Cho, Y.S.3    Kim, H.J.4    Ha, N.C.5    Hwang, J.I.6
  • 34
    • 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; 388 300-304.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 35
    • 0033592470 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP
    • Sun C, Cai M, Gunasekera AH, Meadows RP, Wang H, Chen J et al. NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP. Nature 1999; 401: 818-822.
    • (1999) Nature , vol.401 , pp. 818-822
    • Sun, C.1    Cai, M.2    Gunasekera, A.H.3    Meadows, R.P.4    Wang, H.5    Chen, J.6
  • 36
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM. RING finger proteins: mediators of ubiquitin ligase activity. Cell 2000; 102: 549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 37
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, cIAP2, 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, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. J Biol Chem 2000; 275: 26661-26664.
    • (2000) J. Biol. Chem. , 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
  • 38
    • 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 antiapoptotic 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 antiapoptotic effect in Fas-induced cell death. Proc Natl Acad Sci USA 2001; 98: 8662-8667.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 39
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac uhiquitination in vitro
    • MacFarlane M, Merrison W, Bratton SB, Cohen GM. Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac uhiquitination in vitro. J Biol Chem 2002; 277: 36611-36616.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 40
    • 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. J Biol Chem 2003; 278: 10055-10060.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10055-10060
    • Hu, S.1    Yang, X.2
  • 41
    • 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: 874-877.
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 42
    • 0033215040 scopus 로고    scopus 로고
    • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    • Deveraux QL, Leo E, Stennicke HR, Welsh K, Salvesen GS, Reed JC. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J 1999; 18: 5242-5251.
    • (1999) EMBO J. , vol.18 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicke, H.R.3    Welsh, K.4    Salvesen, G.S.5    Reed, J.C.6
  • 43
    • 0034032963 scopus 로고    scopus 로고
    • Inhibitor of apoptosis protein hILP undergoes caspase-mediated cleavage during T lymphocyte apoptosis
    • Johnson DE, Gastman BR, Wieckowski E, Wang GQ, Amoscato A, Delach SM et al. Inhibitor of apoptosis protein hILP undergoes caspase-mediated cleavage during T lymphocyte apoptosis. Cancer Res 2000; 60: 1818-1823.
    • (2000) Cancer Res. , vol.60 , pp. 1818-1823
    • Johnson, D.E.1    Gastman, B.R.2    Wieckowski, E.3    Wang, G.Q.4    Amoscato, A.5    Delach, S.M.6
  • 44
    • 0035895597 scopus 로고    scopus 로고
    • xIAP induces cell-cycle arrest and activates nuclear factor-kappaB: 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 et al. xIAP induces cell-cycle arrest and activates nuclear factor-kappaB: new survival pathways disabled by caspase-mediated cleavage during apoptosis of human endothelial cells. Circ Res 2001; 88: 282-290.
    • (2001) Circ. Res. , 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
  • 46
    • 0141954004 scopus 로고    scopus 로고
    • Caspase-mediated cleavage converts Livin from an antiapoptotic to a proapoptotic factor: Implications for drug-resistant melanoma
    • Nachmias B, Ashhab Y, Bucholtz V, Drize O, Kadouri L, Lotem M et al. Caspase-mediated cleavage converts Livin from an antiapoptotic to a proapoptotic factor: implications for drug-resistant melanoma. Cancer Res 2003; 63: 6340-6349.
    • (2003) Cancer Res. , vol.63 , pp. 6340-6349
    • Nachmias, B.1    Ashhab, Y.2    Bucholtz, V.3    Drize, O.4    Kadouri, L.5    Lotem, M.6
  • 47
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. 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    Li, L.4    Wang, X.5
  • 48
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PC, Pakusch M, Silke J, Connolly LM, Reid GE et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 2000; 102: 43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.C.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6
  • 49
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y, Imai Y, Nakayama H, Takahashi K, Takio K, Takahashi R. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell 2001; 8: 613-621.
    • (2001) Mol. Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 50
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
    • Hegde R, Srinivasula SM, Zhang Z, Wassell R, Mukattash R, Cilenti L et al. Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction. J Biol Chem 2002; 277: 432-438.
    • (2002) J. Biol. Chem. , vol.277 , pp. 432-438
    • Hegde, R.1    Srinivasula, S.M.2    Zhang, Z.3    Wassell, R.4    Mukattash, R.5    Cilenti, L.6
  • 52
    • 18244386261 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity
    • van Loo G, van Gurp M, Depuydt B, Srinivasula SM, Rodriguez I, Alnemri ES et al. The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity. Cell Death Differ 2002; 9 20-26.
    • (2002) Cell Death Differ. , vol.9 , pp. 20-26
    • van Loo, G.1    van Gurp, M.2    Depuydt, B.3    Srinivasula, S.M.4    Rodriguez, I.5    Alnemri, E.S.6
  • 54
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai J, Du C, Wu JW, Kyin S, Wang X, Shi Y. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 2000; 406: 855-862.
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3    Kyin, S.4    Wang, X.5    Shi, Y.6
  • 55
    • 0034700495 scopus 로고    scopus 로고
    • Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
    • Liu Z, Sun C, Olejniczak ET, Meadows RP, Betz SF, Oost T et al. Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain. Nature 2000; 408: 1004-1008.
    • (2000) Nature , vol.408 , pp. 1004-1008
    • Liu, Z.1    Sun, C.2    Olejniczak, E.T.3    Meadows, R.P.4    Betz, S.F.5    Oost, T.6
  • 56
    • 0034680876 scopus 로고    scopus 로고
    • Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway
    • Srinivasula SM, Datta P, Fan XJ, Fernandes-Alnemri T, Huang Z, Alnemri ES. Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway. J Biol Chem 2000; 275: 36152-36157.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36152-36157
    • Srinivasula, S.M.1    Datta, P.2    Fan, X.J.3    Fernandes-Alnemri, T.4    Huang, Z.5    Alnemri, E.S.6
  • 57
    • 0037016686 scopus 로고    scopus 로고
    • HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins
    • Verhagen AM, Silke J, Ekert PG, Pakusch M, Kaufmann H, Connolly LM et al. HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins. J Biol Chem 2002; 277: 445-454.
    • (2002) J. Biol. Chem. , vol.277 , pp. 445-454
    • Verhagen, A.M.1    Silke, J.2    Ekert, P.G.3    Pakusch, M.4    Kaufmann, H.5    Connolly, L.M.6
  • 58
    • 1542571796 scopus 로고    scopus 로고
    • Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi
    • Martins LM, Turk BE, Cowling V, Borg A, Jarrell ET, Cantley LC et al. Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi. J Biol Chem 2003; 278: 49417-49427.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49417-49427
    • Martins, L.M.1    Turk, B.E.2    Cowling, V.3    Borg, A.4    Jarrell, E.T.5    Cantley, L.C.6
  • 60
    • 0041355416 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2
    • Srinivasula SM, Gupta S, Datta P, Zhang Z, Hegde R, Cheong N et al. Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2. J Biol Chem 2003; 278 31469-31472.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31469-31472
    • Srinivasula, S.M.1    Gupta, S.2    Datta, P.3    Zhang, Z.4    Hegde, R.5    Cheong, N.6
  • 61
    • 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 Dev 2003; 17: 1487-1496.
    • (2003) Genes Dev. , vol.17 , pp. 1487-1496
    • Yang, Q.H.1    Church-Hajduk, R.2    Ren, J.3    Newton, M.L.4    Du, C.5
  • 64
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 1998; 16: 225-260.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 65
    • 0344845002 scopus 로고    scopus 로고
    • Dying for NF-kappaB? Control of cell death by transcriptional regulation of the apoptotic machinery
    • Burstein E, Duckett CS. Dying for NF-kappaB? Control of cell death by transcriptional regulation of the apoptotic machinery. Curr Opin Cell Biol 2003; 15: 732-737.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 732-737
    • Burstein, E.1    Duckett, C.S.2
  • 67
    • 0035895414 scopus 로고    scopus 로고
    • Nuclear factor-kappaB and cell survival: IAPs call for support
    • Lee R, Collins T. Nuclear factor-kappaB and cell survival: IAPs call for support. Circ Res 2001; 88: 262-264.
    • (2001) Circ. Res. , vol.88 , pp. 262-264
    • Lee, R.1    Collins, T.2
  • 68
    • 0033153009 scopus 로고    scopus 로고
    • Overexpression of A1, an NF-kappaB-inducible antiapoptotic bcl gene, inhibits endothelial cell activation
    • Stroka DM, Badrichani AZ, Bach FH, Ferran C. Overexpression of A1, an NF-kappaB-inducible antiapoptotic bcl gene, inhibits endothelial cell activation. Blood 1999; 93: 3803-3810.
    • (1999) Blood , vol.93 , pp. 3803-3810
    • Stroka, D.M.1    Badrichani, A.Z.2    Bach, F.H.3    Ferran, C.4
  • 69
    • 0033558215 scopus 로고    scopus 로고
    • The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis
    • Zong WX, Edelstein LC, Chen C, Bash J, Gelinas C. The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis. Genes Dev 1999; 13: 382-387.
    • (1999) Genes Dev. , vol.13 , pp. 382-387
    • Zong, W.X.1    Edelstein, L.C.2    Chen, C.3    Bash, J.4    Gelinas, C.5
  • 70
    • 0033529416 scopus 로고    scopus 로고
    • NF-kappaB-mediated up-regulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signaling in B lymphocytes
    • Lee HH, Dadgostar H, Cheng Q, Shu J, Cheng G. NF-kappaB-mediated up-regulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signaling in B lymphocytes. Proc Natl Acad Sci USA 1999; 96: 9136-9141.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9136-9141
    • Lee, H.H.1    Dadgostar, H.2    Cheng, Q.3    Shu, J.4    Cheng, G.5
  • 71
    • 0033621956 scopus 로고    scopus 로고
    • The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L)
    • Chen C, Edelstein LC, Gelinas C. The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L). Mol Cell Biol 2000; 20: 2687-2695.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2687-2695
    • Chen, C.1    Edelstein, L.C.2    Gelinas, C.3
  • 72
    • 0034423508 scopus 로고    scopus 로고
    • The antiapoptotic activities of Rel and RelA required during B-cell maturation involve the regulation of Bcl-2 expression
    • Grossmann M, O'Reilly LA, Gugasyan R, Strasser A, Adams JM, Gerondakis S. The antiapoptotic activities of Rel and RelA required during B-cell maturation involve the regulation of Bcl-2 expression. EMBO J 2000; 19: 6351-6360.
    • (2000) EMBO J. , vol.19 , pp. 6351-6360
    • Grossmann, M.1    O'Reilly, L.A.2    Gugasyan, R.3    Strasser, A.4    Adams, J.M.5    Gerondakis, S.6
  • 74
    • 0035920230 scopus 로고    scopus 로고
    • Rel/NF-kappaB transcription factors protect against tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-induced apoptosis by up-regulating the TRAIL decoy receptor DcR1
    • Bernard D, Quatannens B, Vandenbunder B, Abbadie C. Rel/NF-kappaB transcription factors protect against tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-induced apoptosis by up-regulating the TRAIL decoy receptor DcR1. J Biol Chem 2001; 276: 27322-27328.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27322-27328
    • Bernard, D.1    Quatannens, B.2    Vandenbunder, B.3    Abbadie, C.4
  • 75
    • 0035137882 scopus 로고    scopus 로고
    • Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB
    • Baldwin AS. Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB. J Clin Invest 2001; 107: 241-246.
    • (2001) J. Clin. Invest. , vol.107 , pp. 241-246
    • Baldwin, A.S.1
  • 76
    • 0031833431 scopus 로고    scopus 로고
    • The regulation and roles of Rel/NF-kappa B transcription factors during lymphocyte activation
    • Gerondakis S, Grumont R, Rourke I, Grossmann M. The regulation and roles of Rel/NF-kappa B transcription factors during lymphocyte activation. Curr Opin Immunol 1998; 10: 353-359.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 353-359
    • Gerondakis, S.1    Grumont, R.2    Rourke, I.3    Grossmann, M.4
  • 77
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control
    • Chu ZL, McKinsey TA, Liu L, Gentry JJ, Malim MH, Ballard DW. Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control. Proc Natl Acad Sci USA 1997; 94: 10057-10062.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10057-10062
    • Chu, Z.L.1    McKinsey, T.A.2    Liu, L.3    Gentry, J.J.4    Malim, M.H.5    Ballard, D.W.6
  • 78
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB 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 Jr AS. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 1998; 281: 1680-1683.
    • (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
  • 79
    • 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, Binder BR, Lipp J, de Martin R. Activation of NF-kappa B by XIAP, the X chromosome-linked inhibitor of apoptosis, in endothelial cells involves TAK1. J Biol Chem 2000; 275: 22064-22068.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22064-22068
    • Hofer-Warbinek, R.1    Schmid, J.A.2    Stehlik, C.3    Binder, B.R.4    Lipp, J.5    de Martin, R.6
  • 80
    • 0032490670 scopus 로고    scopus 로고
    • Nuclear factor (NF)-kappaB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor alpha-induced apoptosis
    • Stehlik C, de Martin R, Kumabashiri I, Schmid JA, Binder BR, Lipp J. Nuclear factor (NF)-kappaB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor alpha-induced apoptosis. J Exp Med 1998; 188: 211-216.
    • (1998) J. Exp. Med. , vol.188 , pp. 211-216
    • Stehlik, C.1    de Martin, R.2    Kumabashiri, I.3    Schmid, J.A.4    Binder, B.R.5    Lipp, J.6
  • 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 CJ, Ducrey O, Lee J, Nomoto K, Schrantz N et al. IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1 signaling cascade and caspase inhibition. Mol Cell Biol 2002; 22: 1754-1766.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 1754-1766
    • Sanna, M.G.1    da Silva, C.J.2    Ducrey, O.3    Lee, J.4    Nomoto, K.5    Schrantz, N.6
  • 82
    • 0036619301 scopus 로고    scopus 로고
    • Role of X-linked inhibitor of apoptosis protein in chemoresistance in ovarian cancer: Possible involvement of the phosphoinositide-3 kinase/Akt pathway
    • Cheng JQ, Jiang X, Fraser M, Li M, Dan HC, Sun M et al. Role of X-linked inhibitor of apoptosis protein in chemoresistance in ovarian cancer: possible involvement of the phosphoinositide-3 kinase/Akt pathway. Drug Resist Updat 2002; 5: 131-146.
    • (2002) Drug Resist. Updat. , vol.5 , pp. 131-146
    • Cheng, J.Q.1    Jiang, X.2    Fraser, M.3    Li, M.4    Dan, H.C.5    Sun, M.6
  • 83
    • 10744228158 scopus 로고    scopus 로고
    • Regulation and targeting of antiapoptotic XIAP in acute myeloid leukemia
    • Carter BZ, Milella M, Tsao T, McQueen T, Schober WD, Hu W et al. Regulation and targeting of antiapoptotic XIAP in acute myeloid leukemia. Leukemia 2003; 17: 2081-2089.
    • (2003) Leukemia , vol.17 , pp. 2081-2089
    • Carter, B.Z.1    Milella, M.2    Tsao, T.3    McQueen, T.4    Schober, W.D.5    Hu, W.6
  • 84
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100: 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 85
    • 0035902115 scopus 로고    scopus 로고
    • Proliferation, cell cycle and apoptosis in cancer
    • Evan GI, Vousden KH. Proliferation, cell cycle and apoptosis in cancer. Nature 2001; 411: 342-348.
    • (2001) Nature , vol.411 , pp. 342-348
    • Evan, G.I.1    Vousden, K.H.2
  • 86
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • Johnstone RW, Ruefli AA, Lowe SW. Apoptosis: a link between cancer genetics and chemotherapy. Cell 2002; 108: 153-164.
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 87
    • 0346250160 scopus 로고    scopus 로고
    • Survivin, versatile modulation of cell division and apoptosis in cancer
    • Altieri DC. Survivin, versatile modulation of cell division and apoptosis in cancer. Oncogene 2003; 22: 8581-8589.
    • (2003) Oncogene , vol.22 , pp. 8581-8589
    • Altieri, D.C.1
  • 88
    • 0034284050 scopus 로고    scopus 로고
    • Prognostic significance of survivin expression in diffuse large B-cell lymphomas
    • Adida C, Haioun C, Gaulard P, Lepage E, Morel P, Briere J et al. Prognostic significance of survivin expression in diffuse large B-cell lymphomas. Blood 2000; 96: 1921-1925.
    • (2000) Blood , vol.96 , pp. 1921-1925
    • Adida, C.1    Haioun, C.2    Gaulard, P.3    Lepage, E.4    Morel, P.5    Briere, J.6
  • 89
    • 85014269563 scopus 로고    scopus 로고
    • Relationship between expression of genes involved in cell cycle control and apoptosis in diffuse large B cell lymphoma: A preferential survivin-cyclin B link
    • Kuttler F, Valnet-Rabier MB, Angonin R, Ferrand C, Deconinck E, Mougin C et al. Relationship between expression of genes involved in cell cycle control and apoptosis in diffuse large B cell lymphoma: a preferential survivin-cyclin B link. Leukemia 2002; 16: 726-735.
    • (2002) Leukemia , vol.16 , pp. 726-735
    • Kuttler, F.1    Valnet-Rabier, M.B.2    Angonin, R.3    Ferrand, C.4    Deconinck, E.5    Mougin, C.6
  • 92
    • 0035353163 scopus 로고    scopus 로고
    • Cytokine-regulated expression of survivin in myeloid leukemia
    • Carter BZ, Milella M, Altieri DC, Andreeff M. Cytokine-regulated expression of survivin in myeloid leukemia. Blood 2001; 97: 2784-2790.
    • (2001) Blood , vol.97 , pp. 2784-2790
    • Carter, B.Z.1    Milella, M.2    Altieri, D.C.3    Andreeff, M.4
  • 93
    • 0034933717 scopus 로고    scopus 로고
    • Aberrant expression of caspase cascade regulatory genes in adult T-cell leukaemia: Survivin is an important determinant for prognosis
    • Kamihira S, Yamada Y, Hirakata Y, Tomonaga M, Sugahara K, Hayashi T et al. Aberrant expression of caspase cascade regulatory genes in adult T-cell leukaemia: survivin is an important determinant for prognosis. Br J Haematol 2001; 114: 63-69.
    • (2001) Br. J. Haematol. , vol.114 , pp. 63-69
    • Kamihira, S.1    Yamada, Y.2    Hirakata, Y.3    Tomonaga, M.4    Sugahara, K.5    Hayashi, T.6
  • 95
    • 0034598797 scopus 로고    scopus 로고
    • High expression of Survivin, mapped to 17q25, is significantly associated with poor prognostic factors and promotes cell survival in human neuroblastoma
    • Islam A, Kageyama H, Takada N, Kawamoto T, Takayasu H, Isogai E et al. High expression of Survivin, mapped to 17q25, is significantly associated with poor prognostic factors and promotes cell survival in human neuroblastoma. Oncogene 2000; 19: 617-623.
    • (2000) Oncogene , vol.19 , pp. 617-623
    • Islam, A.1    Kageyama, H.2    Takada, N.3    Kawamoto, T.4    Takayasu, H.5    Isogai, E.6
  • 96
    • 0035964487 scopus 로고    scopus 로고
    • DNA demethylase is expressed in ovarian cancers and the expression correlates with demethylation of CpG sites in the promoter region of c-erbB-2 and survivin genes
    • Hattori M, Sakamoto H, Satoh K, Yamamoto T. DNA demethylase is expressed in ovarian cancers and the expression correlates with demethylation of CpG sites in the promoter region of c-erbB-2 and survivin genes. Cancer Lett 2001; 169: 155-164.
    • (2001) Cancer Lett. , vol.169 , pp. 155-164
    • Hattori, M.1    Sakamoto, H.2    Satoh, K.3    Yamamoto, T.4
  • 97
    • 0036479115 scopus 로고    scopus 로고
    • Transcriptional repression of the antiapoptotic survivin gene by wild type p53
    • Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M. Transcriptional repression of the antiapoptotic survivin gene by wild type p53. J Biol Chem 2002; 277: 3247-3257.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3247-3257
    • Hoffman, W.H.1    Biade, S.2    Zilfou, J.T.3    Chen, J.4    Murphy, M.5
  • 98
    • 18344369169 scopus 로고    scopus 로고
    • Human survivin is negatively regulated by wild-type p53 and participates in p53-dependent apoptotic pathway
    • Mirza A, McGuirk M, Hockenberry TN, Wu Q, Ashar H, Black S et al. Human survivin is negatively regulated by wild-type p53 and participates in p53-dependent apoptotic pathway. Oncogene 2002; 21: 2613-2622.
    • (2002) Oncogene , vol.21 , pp. 2613-2622
    • Mirza, A.1    McGuirk, M.2    Hockenberry, T.N.3    Wu, Q.4    Ashar, H.5    Black, S.6
  • 99
    • 0036785525 scopus 로고    scopus 로고
    • DNA damage induces a novel p53-survivin signaling pathway regulating cell cycle and apoptosis in acute lymphoblastic leukemia cells
    • Zhou M, Gu L, Li F, Zhu Y, Woods WG, Findley HW. DNA damage induces a novel p53-survivin signaling pathway regulating cell cycle and apoptosis in acute lymphoblastic leukemia cells. J Pharmacol Exp Ther 2002; 303: 124-131.
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 124-131
    • Zhou, M.1    Gu, L.2    Li, F.3    Zhu, Y.4    Woods, W.G.5    Findley, H.W.6
  • 100
  • 101
    • 0345826036 scopus 로고    scopus 로고
    • Acute ablation of survivin uncovers p53-dependent mitotic checkpoint functions and control of mitochondrial apoptosis
    • Beltrami E, Plescia J, Wilkinson JC, Duckett CS, Altieri DC. Acute ablation of survivin uncovers p53-dependent mitotic checkpoint functions and control of mitochondrial apoptosis. J Biol Chem 2003; 279: 2077-2083.
    • (2003) J. Biol. Chem. , vol.279 , pp. 2077-2083
    • Beltrami, E.1    Plescia, J.2    Wilkinson, J.C.3    Duckett, C.S.4    Altieri, D.C.5
  • 102
    • 0037817310 scopus 로고    scopus 로고
    • Therapeutic targeting of the survivin pathway in cancer: Initiation of mitochondrial apoptosis and suppression of tumor-associated angiogenesis
    • Blanc-Brude OP, Mesri M, Wall NR, Plescia J, Dohi T, Altieri DC. Therapeutic targeting of the survivin pathway in cancer: initiation of mitochondrial apoptosis and suppression of tumor-associated angiogenesis. Clin Cancer Res 2003; 9: 2683-2692.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 2683-2692
    • Blanc-Brude, O.P.1    Mesri, M.2    Wall, N.R.3    Plescia, J.4    Dohi, T.5    Altieri, D.C.6
  • 103
    • 0344974238 scopus 로고    scopus 로고
    • Targeting Survivin expression induces cell proliferation defect and subsequent cell death involving mitochondrial pathway in myeloid leukemic cells
    • Carter BZ, Wang RY, Schober WD, Milella M, Chism D, Andreeff M. Targeting Survivin expression induces cell proliferation defect and subsequent cell death involving mitochondrial pathway in myeloid leukemic cells. Cell Cycle 2003; 2: 488-493.
    • (2003) Cell Cycle , vol.2 , pp. 488-493
    • Carter, B.Z.1    Wang, R.Y.2    Schober, W.D.3    Milella, M.4    Chism, D.5    Andreeff, M.6
  • 104
    • 0034597594 scopus 로고    scopus 로고
    • Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype
    • Uren AG, Wong L, Pakusch M, Fowler KJ, Burrows FJ, Vaux DL et al. Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype. Curr Biol 2000; 10: 1319-1328.
    • (2000) Curr. Biol. , vol.10 , pp. 1319-1328
    • Uren, A.G.1    Wong, L.2    Pakusch, M.3    Fowler, K.J.4    Burrows, F.J.5    Vaux, D.L.6
  • 105
    • 0036472994 scopus 로고    scopus 로고
    • Survivin exists in immunochemically distinct subcellular pools and is involved in spindle microtubule function
    • Fortugno P, Wall NR, Giodini A, O'Connor DS, Plescia J, Padgett KM et al. Survivin exists in immunochemically distinct subcellular pools and is involved in spindle microtubule function. J Cell Sci 2002; 115 (Part 3): 575-585.
    • (2002) J. Cell Sci. , vol.115 , Issue.PART 3 , pp. 575-585
    • Fortugno, P.1    Wall, N.R.2    Giodini, A.3    O'Connor, D.S.4    Plescia, J.5    Padgett, K.M.6
  • 107
    • 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, Krajewski S, Welsh K, Kitada S et al. Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin Cancer Res 2000; 6 1796-1803.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 1796-1803
    • Tamm, I.1    Kornblau, S.M.2    Segall, H.3    Krajewski, S.4    Welsh, K.5    Kitada, S.6
  • 109
    • 0037211252 scopus 로고    scopus 로고
    • Role of XIAP in the malignant phenotype of transitional cell cancer (TCC) and therapeutic activity of XIAP antisense oligonucleotides against multidrug-resistant TCC in vitro
    • Bilim V, Kasahara T, Hara N, Takahashi K, Tomita Y. Role of XIAP in the malignant phenotype of transitional cell cancer (TCC) and therapeutic activity of XIAP antisense oligonucleotides against multidrug-resistant TCC in vitro. Int J Cancer 2003; 103: 29-37.
    • (2003) Int. J. Cancer , vol.103 , pp. 29-37
    • Bilim, V.1    Kasahara, T.2    Hara, N.3    Takahashi, K.4    Tomita, Y.5
  • 110
    • 17744379360 scopus 로고    scopus 로고
    • Human ovarian cancer and cisplatin resistance: Possible role of inhibitor of apoptosis proteins
    • Li J, Feng Q, Kim JM, Schneiderman D, Liston P, Li M et al. Human ovarian cancer and cisplatin resistance: possible role of inhibitor of apoptosis proteins. Endocrinology 2001; 142: 370-380.
    • (2001) Endocrinology , vol.142 , pp. 370-380
    • Li, J.1    Feng, Q.2    Kim, J.M.3    Schneiderman, D.4    Liston, P.5    Li, M.6
  • 111
    • 0842284092 scopus 로고    scopus 로고
    • Cisplatin resistance in an ovarian carcinoma is associated with a defect in programmed cell death control through XIAP regulation
    • Mansouri A, Zhang Q, Ridgway LD, Tian L, Claret FX. Cisplatin resistance in an ovarian carcinoma is associated with a defect in programmed cell death control through XIAP regulation. Oncol Res 2003; 13: 399-404.
    • (2003) Oncol. Res. , vol.13 , pp. 399-404
    • Mansouri, A.1    Zhang, Q.2    Ridgway, L.D.3    Tian, L.4    Claret, F.X.5
  • 112
    • 0032917709 scopus 로고    scopus 로고
    • Expression and biological activity of X-linked inhibitor of apoptosis (XIAP) in human malignant glioma
    • Wagenknecht B, Glaser T, Naumann U, Kugler S, Isenmann S, Bahr M et al. Expression and biological activity of X-linked inhibitor of apoptosis (XIAP) in human malignant glioma. Cell Death Differ 1999; 6: 370-376.
    • (1999) Cell Death Differ. , vol.6 , pp. 370-376
    • Wagenknecht, B.1    Glaser, T.2    Naumann, U.3    Kugler, S.4    Isenmann, S.5    Bahr, M.6
  • 113
    • 0036800343 scopus 로고    scopus 로고
    • Up-regulation of XIAP by M-CSF is associated with resistance of myeloid leukemia cells to apoptosis
    • Zhang J, Li Y, Shen B. Up-regulation of XIAP by M-CSF is associated with resistance of myeloid leukemia cells to apoptosis. Leukemia 2002; 16: 2163-2165.
    • (2002) Leukemia , vol.16 , pp. 2163-2165
    • Zhang, J.1    Li, Y.2    Shen, B.3
  • 114
    • 0242442595 scopus 로고    scopus 로고
    • Hypermethylation of XIAP-associated factor 1, a putative tumor suppressor gene from the 17p13.2 locus, in human gastric adenocarcinomas
    • Byun DS, Cho K, Ryu BK, Lee MG, Kang MJ, Kim HR et al. Hypermethylation of XIAP-associated factor 1, a putative tumor suppressor gene from the 17p13.2 locus, in human gastric adenocarcinomas. Cancer Res 2003; 63: 7068-7075.
    • (2003) Cancer Res. , vol.63 , pp. 7068-7075
    • Byun, D.S.1    Cho, K.2    Ryu, B.K.3    Lee, M.G.4    Kang, M.J.5    Kim, H.R.6
  • 115
    • 0037388691 scopus 로고    scopus 로고
    • A comprehensive search for DNA amplification in lung cancer identifies inhibitors of apoptosis cIAP1 and cIAP2 as candidate oncogenes
    • Dai Z, Zhu WG, Morrison CD, Brena RM, Smiraglia DJ, Raval A et al. A comprehensive search for DNA amplification in lung cancer identifies inhibitors of apoptosis cIAP1 and cIAP2 as candidate oncogenes. Hum Mol Genet 2003; 12: 791-801.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 791-801
    • Dai, Z.1    Zhu, W.G.2    Morrison, C.D.3    Brena, R.M.4    Smiraglia, D.J.5    Raval, A.6
  • 116
    • 0035884398 scopus 로고    scopus 로고
    • Identification of cIAP1 as a candidate target gene within an amplicon at 11q22 in esophageal squamous cell carcinomas
    • Imoto I, Yang ZQ, Pimkhaokham A, Tsuda H, Shimada Y, Imamura M et al. Identification of cIAP1 as a candidate target gene within an amplicon at 11q22 in esophageal squamous cell carcinomas. Cancer Res 2001; 61: 6629-6634.
    • (2001) Cancer Res. , vol.61 , pp. 6629-6634
    • Imoto, I.1    Yang, Z.Q.2    Pimkhaokham, A.3    Tsuda, H.4    Shimada, Y.5    Imamura, M.6
  • 117
    • 0034279817 scopus 로고    scopus 로고
    • p21WAF1 prevents down-modulation of the apoptotic inhibitor protein c-IAP1 and inhibits leukemic apoptosis
    • Steinman RA, Johnson DE. p21WAF1 prevents down-modulation of the apoptotic inhibitor protein c-IAP1 and inhibits leukemic apoptosis. Mol Med 2000; 6: 736-749.
    • (2000) Mol. Med. , vol.6 , pp. 736-749
    • Steinman, R.A.1    Johnson, D.E.2
  • 118
    • 2942545582 scopus 로고    scopus 로고
    • Akt activity in endometrial cancer cells: Regulation of cell survival through cIAP-1
    • Gagnon V, St Germain ME, Parent S, Asselin E. Akt activity in endometrial cancer cells: regulation of cell survival through cIAP-1. Int J Oncol 2003; 23: 803-810.
    • (2003) Int. J. Oncol. , vol.23 , pp. 803-810
    • Gagnon, V.1    St Germain, M.E.2    Parent, S.3    Asselin, E.4
  • 119
    • 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, Miura M, Sakamoto M, Hirohashi S et al. Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy. Cancer Res 2002; 62: 4860-4866.
    • (2002) Cancer Res. , vol.62 , pp. 4860-4866
    • Imoto, I.1    Tsuda, H.2    Hirasawa, A.3    Miura, M.4    Sakamoto, M.5    Hirohashi, S.6
  • 120
    • 8844255654 scopus 로고    scopus 로고
    • Expression of c-IAP1, c-IAP2 and Survivin discriminates different types of lymphoid malignancies
    • Submitted
    • de Graaf A, van Krieken H, Tönnissen E, Wissink W, van de Locht L, Overes I et al. Expression of c-IAP1, c-IAP2 and Survivin discriminates different types of lymphoid malignancies. Submitted.
    • de Graaf, A.1    van Krieken, H.2    Tönnissen, E.3    Wissink, W.4    van de Locht, L.5    Overes, I.6
  • 121
    • 0037307753 scopus 로고    scopus 로고
    • Expression of the inhibitor of apoptosis (IAP) family members in human neutrophils: Up-regulation of cIAP2 by granulocyte colony-stimulating factor and overexpression of cIAP2 in chronic neutrophilic leukemia
    • Hasegawa T, Suzuki K, Sakamoto C, Ohta K, Nishiki S, Hino M et al. Expression of the inhibitor of apoptosis (IAP) family members in human neutrophils: up-regulation of cIAP2 by granulocyte colony-stimulating factor and overexpression of cIAP2 in chronic neutrophilic leukemia. Blood 2003; 101: 1164-1171.
    • (2003) Blood , vol.101 , pp. 1164-1171
    • Hasegawa, T.1    Suzuki, K.2    Sakamoto, C.3    Ohta, K.4    Nishiki, S.5    Hino, M.6
  • 122
    • 0042530178 scopus 로고    scopus 로고
    • cIAP-2 block apoptotic events in bladder cancer cells
    • Jonsson G, Paulie S, Grandien A. cIAP-2 block apoptotic events in bladder cancer cells. Anticancer Res 2003; 23: 3311-3316.
    • (2003) Anticancer Res. , vol.23 , pp. 3311-3316
    • Jonsson, G.1    Paulie, S.2    Grandien, A.3
  • 123
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren AG, O'Rourke K, Aravind LA, Pisabarro MT, Seshagiri S, Koonin EV et al. Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol Cell 2000; 6: 961-967.
    • (2000) Mol. Cell , vol.6 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.A.3    Pisabarro, M.T.4    Seshagiri, S.5    Koonin, E.V.6
  • 124
    • 0033847542 scopus 로고    scopus 로고
    • The product of the t(11;18), an API2-MLT fusion, marks nearly half of gastric MALT type lymphomas without large cell proliferation
    • Baens M, Maes B, Steyls A, Geboes K, Marynen P, Wolf-Peeters C. The product of the t(11;18), an API2-MLT fusion, marks nearly half of gastric MALT type lymphomas without large cell proliferation. Am J Pathol 2000; 156: 1433-1439.
    • (2000) Am. J. Pathol. , vol.156 , pp. 1433-1439
    • Baens, M.1    Maes, B.2    Steyls, A.3    Geboes, K.4    Marynen, P.5    Wolf-Peeters, C.6
  • 125
    • 0033870289 scopus 로고    scopus 로고
    • API2-MALT1 chimeric transcripts involved in mucosa-associated lymphoid tissue type lymphoma predict heterogeneous products
    • Motegi M, Yonezumi M, Suzuki H, Suzuki R, Hosokawa Y, Hosaka S et al. API2-MALT1 chimeric transcripts involved in mucosa-associated lymphoid tissue type lymphoma predict heterogeneous products. Am J Pathol 2000; 156: 807-812.
    • (2000) Am. J. Pathol. , vol.156 , pp. 807-812
    • Motegi, M.1    Yonezumi, M.2    Suzuki, H.3    Suzuki, R.4    Hosokawa, Y.5    Hosaka, S.6
  • 126
    • 0035883045 scopus 로고    scopus 로고
    • T(11;18)(q21;q21) is associated with advanced mucosa-associated lymphoid tissue lymphoma that expresses nuclear BCL10
    • Liu H, Ye H, Dogan A, Ranaldi R, Hamoudi RA, Bearzi I et al. T(11;18)(q21;q21) is associated with advanced mucosa-associated lymphoid tissue lymphoma that expresses nuclear BCL10. Blood 2001; 98: 1182-1187.
    • (2001) Blood , vol.98 , pp. 1182-1187
    • Liu, H.1    Ye, H.2    Dogan, A.3    Ranaldi, R.4    Hamoudi, R.A.5    Bearzi, I.6
  • 127
    • 0033534627 scopus 로고    scopus 로고
    • Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types
    • Willis TG, Jadayel DM, Du MQ, Peng H, Perry AR, Abdul-Rauf M et al. Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types. Cell 1999; 96: 35-45.
    • (1999) Cell , vol.96 , pp. 35-45
    • Willis, T.G.1    Jadayel, D.M.2    Du, M.Q.3    Peng, H.4    Perry, A.R.5    Abdul-Rauf, M.6
  • 128
    • 0033596124 scopus 로고    scopus 로고
    • Aberrant rel/nfkb genes and activity in human cancer
    • Rayet B, Gelinas C. Aberrant rel/nfkb genes and activity in human cancer. Oncogene 1999; 18: 6938-6947.
    • (1999) Oncogene , vol.18 , pp. 6938-6947
    • Rayet, B.1    Gelinas, C.2
  • 129
    • 0035207110 scopus 로고    scopus 로고
    • The role of nuclear factor-kappaB in the biology and treatment of multiple myeloma
    • Berenson JR, Ma HM, Vescio R. The role of nuclear factor-kappaB in the biology and treatment of multiple myeloma. Semin Oncol 2001; 28: 626-633.
    • (2001) Semin. Oncol. , vol.28 , pp. 626-633
    • Berenson, J.R.1    Ma, H.M.2    Vescio, R.3
  • 130
    • 0038206722 scopus 로고    scopus 로고
    • Inhibition of constitutive NF-kappa B activation in mantle cell lymphoma B cells leads to induction of cell cycle arrest and apoptosis
    • Pham LV, Tamayo AT, Yoshimura LC, Lo P, Ford RJ. Inhibition of constitutive NF-kappa B activation in mantle cell lymphoma B cells leads to induction of cell cycle arrest and apoptosis. J Immunol 2003; 171: 88-95.
    • (2003) J. Immunol. , vol.171 , pp. 88-95
    • Pham, L.V.1    Tamayo, A.T.2    Yoshimura, L.C.3    Lo, P.4    Ford, R.J.5
  • 131
    • 0035905313 scopus 로고    scopus 로고
    • Constitutive nuclear factor kappaB activity is required for survival of activated B cell-like diffuse large B cell lymphoma cells
    • Davis RE, Brown KD, Siebenlist U, Staudt LM. Constitutive nuclear factor kappaB activity is required for survival of activated B cell-like diffuse large B cell lymphoma cells. J Exp Med 2001; 194: 1861-1874.
    • (2001) J. Exp. Med. , vol.194 , pp. 1861-1874
    • Davis, R.E.1    Brown, K.D.2    Siebenlist, U.3    Staudt, L.M.4
  • 132
    • 0037224547 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase/AKT1 pathway involvement in drug and all-trans-retinoic acid resistance of leukemia cells
    • Neri LM, Borgatti P, Tazzari PL, Bortul R, Cappellini A, Tabellini G et al. The phosphoinositide 3-kinase/AKT1 pathway involvement in drug and all-trans-retinoic acid resistance of leukemia cells. Mol Cancer Res 2003; 1: 234-246.
    • (2003) Mol. Cancer Res. , vol.1 , pp. 234-246
    • Neri, L.M.1    Borgatti, P.2    Tazzari, P.L.3    Bortul, R.4    Cappellini, A.5    Tabellini, G.6
  • 133
    • 0035889120 scopus 로고    scopus 로고
    • Transformation of interleukin-3-dependent cells without participation of Stat5/bcl-xL: Cooperation of akt with raf/erk leads to p65 nuclear factor kappaB-mediated antiapoptosis involving c-IAP2
    • Gelfanov VM, Burgess GS, Litz-Jackson S, King AJ, Marshall MS, Nakshatri H et al. Transformation of interleukin-3-dependent cells without participation of Stat5/bcl-xL: cooperation of akt with raf/erk leads to p65 nuclear factor kappaB-mediated antiapoptosis involving c-IAP2. Blood 2001; 98: 2508-2517.
    • (2001) Blood , vol.98 , pp. 2508-2517
    • Gelfanov, V.M.1    Burgess, G.S.2    Litz-Jackson, S.3    King, A.J.4    Marshall, M.S.5    Nakshatri, H.6
  • 135
    • 0034015672 scopus 로고    scopus 로고
    • Phase I clinical and pharmacokinetic study of bcl-2 antisense oligonucleotide therapy in patients with non-Hodgkin's lymphoma
    • Waters JS, Webb A, Cunningham D, Clarke PA, Raynaud F, di Stefano F et al. Phase I clinical and pharmacokinetic study of bcl-2 antisense oligonucleotide therapy in patients with non-Hodgkin's lymphoma. J Clin Oncol 2000; 18: 1812-1823.
    • (2000) J. Clin. Oncol. , vol.18 , pp. 1812-1823
    • Waters, J.S.1    Webb, A.2    Cunningham, D.3    Clarke, P.A.4    Raynaud, F.5    di Stefano, F.6
  • 136
    • 0037438586 scopus 로고    scopus 로고
    • Phase 1 and pharmacodynamic studies of G3139, a Bcl-2 antisense oligonucleotide, in combination with chemotherapy in refractory or relapsed acute leukemia
    • Marcucci G, Byrd JC, Dai G, Klisovic MI, Kourlas PJ, Young DC et al. Phase 1 and pharmacodynamic studies of G3139, a Bcl-2 antisense oligonucleotide, in combination with chemotherapy in refractory or relapsed acute leukemia. Blood 2003; 101: 425-432.
    • (2003) Blood , vol.101 , pp. 425-432
    • Marcucci, G.1    Byrd, J.C.2    Dai, G.3    Klisovic, M.I.4    Kourlas, P.J.5    Young, D.C.6
  • 137
    • 1542608418 scopus 로고    scopus 로고
    • Inhibition of survivin expression suppresses the growth of aggressive non-Hodgkin's lymphoma
    • Ansell SM, Arendt BK, Grote DM, Jelinek DF, Novak AJ, Wellik LE et al. Inhibition of survivin expression suppresses the growth of aggressive non-Hodgkin's lymphoma. Leukemia 2004; 18: 616-623.
    • (2004) Leukemia , vol.18 , pp. 616-623
    • Ansell, S.M.1    Arendt, B.K.2    Grote, D.M.3    Jelinek, D.F.4    Novak, A.J.5    Wellik, L.E.6
  • 138
    • 0035904376 scopus 로고    scopus 로고
    • Effects of survivin antagonists on growth of established tumors and B7-1 immunogene therapy
    • Kanwar JR, Shen WP, Kanwar RK, Berg RW, Krissansen GW. Effects of survivin antagonists on growth of established tumors and B7-1 immunogene therapy. J Natl Cancer Inst 2001; 93: 1541-1552.
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 1541-1552
    • Kanwar, J.R.1    Shen, W.P.2    Kanwar, R.K.3    Berg, R.W.4    Krissansen, G.W.5
  • 139
    • 0037267333 scopus 로고    scopus 로고
    • Validating survivin as a cancer therapeutic target
    • Altieri DC. Validating survivin as a cancer therapeutic target. Nat Rev Cancer 2003; 3: 46-54.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 46-54
    • Altieri, D.C.1
  • 140
    • 0034074562 scopus 로고    scopus 로고
    • Antibody response to the tumor-associated inhibitor of apoptosis protein survivin in cancer patients
    • Rohayem J, Diestelkoetter P, Weigle B, Oehmichen A, Schmitz M, Mehlhorn J et al. Antibody response to the tumor-associated inhibitor of apoptosis protein survivin in cancer patients. Cancer Res 2000; 60: 1815-1817.
    • (2000) Cancer Res. , vol.60 , pp. 1815-1817
    • Rohayem, J.1    Diestelkoetter, P.2    Weigle, B.3    Oehmichen, A.4    Schmitz, M.5    Mehlhorn, J.6
  • 141
    • 0035881885 scopus 로고    scopus 로고
    • Spontaneous cytotoxic T-cell responses against survivin-derived MHC class I-restricted T-cell epitopes in situ as well as ex vivo in cancer patients
    • Andersen MH, Pedersen LO, Capeller B, Brocker EB, Becker JC, Thor SP. Spontaneous cytotoxic T-cell responses against survivin-derived MHC class I-restricted T-cell epitopes in situ as well as ex vivo in cancer patients. Cancer Res 2001; 61: 5964-5968.
    • (2001) Cancer Res. , vol.61 , pp. 5964-5968
    • Andersen, M.H.1    Pedersen, L.O.2    Capeller, B.3    Brocker, E.B.4    Becker, J.C.5    Thor, S.P.6
  • 142
    • 0035107985 scopus 로고    scopus 로고
    • Identification of a cytotoxic T lymphocyte response to the apoptosis inhibitor protein survivin in cancer patients
    • Andersen MH, Pedersen LO, Becker JC, Straten PT. Identification of a cytotoxic T lymphocyte response to the apoptosis inhibitor protein survivin in cancer patients. Cancer Res 2001; 61: 869-872.
    • (2001) Cancer Res. , vol.61 , pp. 869-872
    • Andersen, M.H.1    Pedersen, L.O.2    Becker, J.C.3    Straten, P.T.4
  • 143
    • 0141763655 scopus 로고    scopus 로고
    • Induction of antitumour immunity using survivin peptide-pulsed dendritic cells in a murine lymphoma model
    • Siegel S, Wagner A, Schmitz N, Zeis M. Induction of antitumour immunity using survivin peptide-pulsed dendritic cells in a murine lymphoma model. Br J Haematol 2003; 122: 911-914.
    • (2003) Br. J. Haematol. , vol.122 , pp. 911-914
    • Siegel, S.1    Wagner, A.2    Schmitz, N.3    Zeis, M.4
  • 144
    • 0038528582 scopus 로고    scopus 로고
    • Generation of cytotoxic responses in mice and human individuals against hematological malignancies using survivin-RNA-transfected dendritic cells
    • Zeis M, Siegel S, Wagner A, Schmitz M, Marget M, Kuhl-Burmeister R et al. Generation of cytotoxic responses in mice and human individuals against hematological malignancies using survivin-RNA-transfected dendritic cells. J Immunol 2003; 170 5391-5397.
    • (2003) J. Immunol. , vol.170 , pp. 5391-5397
    • Zeis, M.1    Siegel, S.2    Wagner, A.3    Schmitz, M.4    Marget, M.5    Kuhl-Burmeister, R.6
  • 147
    • 0037500905 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis (XIAP) blocks Apo2 ligand/tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis of prostate cancer cells in the presence of mitochondrial activation: Sensitization by over-expression of second mitochondria-derived activator of caspase/direct IAP-binding protein with low pl (Smac/DIABLO)
    • Ng CP, Bonavida B. X-linked inhibitor of apoptosis (XIAP) blocks Apo2 ligand/tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis of prostate cancer cells in the presence of mitochondrial activation: sensitization by over-expression of second mitochondria-derived activator of caspase/direct IAP-binding protein with low pl (Smac/DIABLO). Mol Cancer Ther 2002; 1: 1051-1058.
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 1051-1058
    • Ng, C.P.1    Bonavida, B.2
  • 148
    • 0037470027 scopus 로고    scopus 로고
    • A novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLO
    • Hunter AM, Kottachchi D, Lewis J, Duckett CS, Korneluk RG, Liston P. A novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLO. J Biol Chem 2003; 278 7494-7499.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7494-7499
    • Hunter, A.M.1    Kottachchi, D.2    Lewis, J.3    Duckett, C.S.4    Korneluk, R.G.5    Liston, P.6
  • 149
    • 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 et al. 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: 831-837.
    • (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
  • 150
    • 0034651739 scopus 로고    scopus 로고
    • Modulation of NF-kappa B activity and apoptosis in chronic lymphocytic leukemia B cells
    • Furman RR, Asgary Z, Mascarenhas JO, Liou HC, Schattner EJ. Modulation of NF-kappa B activity and apoptosis in chronic lymphocytic leukemia B cells. J Immunol 2000; 164: 2200-2206.
    • (2000) J. Immunol. , vol.164 , pp. 2200-2206
    • Furman, R.R.1    Asgary, Z.2    Mascarenhas, J.O.3    Liou, H.C.4    Schattner, E.J.5
  • 151
    • 0037443459 scopus 로고    scopus 로고
    • Potentiation of TRAIL-induced apoptosis in primary effusion lymphoma through azidothymidine-mediated inhibition of NF-kappa B
    • Ghosh SK, Wood C, Boise LH, Mian AM, Deyev VV, Feuer G et al. Potentiation of TRAIL-induced apoptosis in primary effusion lymphoma through azidothymidine-mediated inhibition of NF-kappa B. Blood 2003; 101: 2321-2327.
    • (2003) Blood , vol.101 , pp. 2321-2327
    • Ghosh, S.K.1    Wood, C.2    Boise, L.H.3    Mian, A.M.4    Deyev, V.V.5    Feuer, G.6
  • 152
    • 0034744586 scopus 로고    scopus 로고
    • Characterization of NF-kappaB expression in Hodgkin's disease: Inhibition of constitutively expressed NF-kappaB results in spontaneous caspase-independent apoptosis in Hodgkin and Reed-Sternberg cells
    • Izban KF, Ergin M, Huang Q, Qin JZ, Martinez RL, Schnitzer B et al. Characterization of NF-kappaB expression in Hodgkin's disease: inhibition of constitutively expressed NF-kappaB results in spontaneous caspase-independent apoptosis in Hodgkin and Reed-Sternberg cells. Mod Pathol 2001; 14: 297-310.
    • (2001) Mod. Pathol. , vol.14 , pp. 297-310
    • Izban, K.F.1    Ergin, M.2    Huang, Q.3    Qin, J.Z.4    Martinez, R.L.5    Schnitzer, B.6
  • 153
    • 0036624741 scopus 로고    scopus 로고
    • Biologic sequelae of nuclear factor-kappaB blockade in multiple myeloma: Therapeutic applications
    • Mitsiades N, Mitsiades CS, Poulaki V, Chauhan D, Richardson PG, Hideshima T et al. Biologic sequelae of nuclear factor-kappaB blockade in multiple myeloma: therapeutic applications. Blood 2002; 99: 4079-4086.
    • (2002) Blood , vol.99 , pp. 4079-4086
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3    Chauhan, D.4    Richardson, P.G.5    Hideshima, T.6
  • 154
    • 0035725855 scopus 로고    scopus 로고
    • Analysis of expression of nuclear factor kappa B (NF-kappa B) in multiple myeloma: Downregulation of NF-kappa B induces apoptosis
    • Ni H, Ergin M, Huang Q, Qin JZ, Amin HM, Martinez RL et al. Analysis of expression of nuclear factor kappa B (NF-kappa B) in multiple myeloma: downregulation of NF-kappa B induces apoptosis. Br J Haematol 2001; 115: 279-286.
    • (2001) Br. J. Haematol. , vol.115 , pp. 279-286
    • Ni, H.1    Ergin, M.2    Huang, Q.3    Qin, J.Z.4    Amin, H.M.5    Martinez, R.L.6
  • 155
    • 0036104603 scopus 로고    scopus 로고
    • Not just research tools - Proteasome inhibitors offer therapeutic promise
    • Goldberg AL, Rock K. Not just research tools - proteasome inhibitors offer therapeutic promise. Nat Med 2002; 8: 338-340.
    • (2002) Nat. Med. , vol.8 , pp. 338-340
    • Goldberg, A.L.1    Rock, K.2
  • 156
    • 0037443551 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: Therapeutic applications
    • Mitsiades N, Mitsiades CS, Richardson PG, Poulaki V, Tai YT, Chauhan D et al. The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: therapeutic applications. Blood 2003; 101: 2377-2380.
    • (2003) Blood , vol.101 , pp. 2377-2380
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3    Poulaki, V.4    Tai, Y.T.5    Chauhan, D.6
  • 157
    • 0038528620 scopus 로고    scopus 로고
    • Clinical update: Proteasome inhibitors in hematologic malignancies
    • Richardson P. Clinical update: proteasome inhibitors in hematologic malignancies. Cancer Treat Rev 2003; 29 (Suppl 1): 33-39.
    • (2003) Cancer Treat. Rev. , vol.29 , Issue.SUPPL. 1 , pp. 33-39
    • Richardson, P.1
  • 158
    • 0036348365 scopus 로고    scopus 로고
    • Proteasome inhibitors in the treatment of B-cell malignancies
    • Schenkein D. Proteasome inhibitors in the treatment of B-cell malignancies. Clin Lymphoma 2002; 3: 49-55.
    • (2002) Clin. Lymphoma , vol.3 , pp. 49-55
    • Schenkein, D.1


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