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Volumn 247, Issue , 2005, Pages 35-88

Survivin: A protein with dual roles in mitosis and apoptosis

Author keywords

Apoptosis; Cancer; Cell division; Mitosis; Survivin

Indexed keywords

PACLITAXEL; PROTEIN P53; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SURVIVIN;

EID: 28844469941     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(05)47002-3     Document Type: Review
Times cited : (156)

References (192)
  • 1
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan D., Jiang X.J., Morgan D.G., Heuser J.E., Wang X.D., and Akey C.W. Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation Mol. Cell 9 2002 423 432
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.J.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.D.5    Akey, C.W.6
  • 3
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini G., Adida C., and Altieri D. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma Nat. Med. 3 1997 917 921
    • (1997) Nat. Med. , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.3
  • 4
    • 0032080335 scopus 로고    scopus 로고
    • Induction of apoptosis and inhibition of proliferation by survivin gene targeting
    • Ambrosini G., Adida C., Sirugo G., and Altieri D. Induction of apoptosis and inhibition of proliferation by survivin gene targeting J. Biol. Chem. 273 1998 11177 11182
    • (1998) J. Biol. Chem. , vol.273 , pp. 11177-11182
    • Ambrosini, G.1    Adida, C.2    Sirugo, G.3    Altieri, D.4
  • 8
    • 0347895102 scopus 로고    scopus 로고
    • Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAPI in situ
    • Arnt C.R., Chiorean M.V., Heldebrant M.P., Gores G.J., and Kaufmann S.H. Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAPI in situ J. Biol. Chem. 277 2002 44236 44243
    • (2002) J. Biol. Chem. , vol.277 , pp. 44236-44243
    • Arnt, C.R.1    Chiorean, M.V.2    Heldebrant, M.P.3    Gores, G.J.4    Kaufmann, S.H.5
  • 13
    • 2942674780 scopus 로고    scopus 로고
    • Dual Role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase
    • Bartke T., Pohl C., Pyrowolakis G., and Jentsch S. Dual Role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase Mol. Cell 14 2004 801 811
    • (2004) Mol. Cell , vol.14 , pp. 801-811
    • Bartke, T.1    Pohl, C.2    Pyrowolakis, G.3    Jentsch, S.4
  • 14
    • 4944250023 scopus 로고    scopus 로고
    • 2/M phase transition and is regulated by microtubule-attachment and Aurora B kinase activity
    • 2/M phase transition and is regulated by microtubule-attachment and Aurora B kinase activity J. Cell Sci. 117 2004 4033 4042
    • (2004) J. Cell Sci. , vol.117 , pp. 4033-4042
    • Beardmore, V.A.1    Ahonen, L.J.2    Gorbsky, G.J.3    Kallio, M.J.4
  • 15
    • 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 J.C., Duckett C.S., and Altieri D.C. Acute ablation of survivin uncovers p53-dependent mitotic checkpoint functions and control of mitochondrial apoptosis J. Biol. Chem. 279 2004 2077 2084
    • (2004) J. Biol. Chem. , vol.279 , pp. 2077-2084
    • Beltrami, E.1    Plescia, J.2    Wilkinson, J.C.3    Duckett, C.S.4    Altieri, D.C.5
  • 16
    • 0035577762 scopus 로고    scopus 로고
    • The budding yeast protein kinase Ipl1/Aurora allows the absence of tension to activate the spindle checkpoint
    • Biggins S., and Murray A.W. The budding yeast protein kinase Ipl1/Aurora allows the absence of tension to activate the spindle checkpoint Genes Dev. 15 2001 3118 3129
    • (2001) Genes Dev. , vol.15 , pp. 3118-3129
    • Biggins, S.1    Murray, A.W.2
  • 17
    • 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 O.P., Mesri M., Wall N.R., Plescia J., Dohi T., and Altieri D.C. Therapeutic targeting of the survivin pathway in cancer: Initiation of mitochondrial apoptosis and suppression of tumor-associated angiogenesis Clin. Cancer Res. 9 2003 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
  • 20
    • 0036732808 scopus 로고    scopus 로고
    • Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation
    • Bolton M.A., Lan W., Powers S.E., McCleland M.L., Kuang J., and Stukenberg P.T. Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation Mol. Biol. Cell 13 2002 3064 3077
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3064-3077
    • Bolton, M.A.1    Lan, W.2    Powers, S.E.3    McCleland, M.L.4    Kuang, J.5    Stukenberg, P.T.6
  • 21
    • 0037415571 scopus 로고    scopus 로고
    • The budding yeast Ipl1/aurora protein kinase regulates spindle disassembly
    • Buvelot S., Tatsutani S.Y., Vermaak D., and Biggins S. The budding yeast Ipl1/aurora protein kinase regulates spindle disassembly J. Cell Biol. 160 2003 329 339
    • (2003) J. Cell Biol. , vol.160 , pp. 329-339
    • Buvelot, S.1    Tatsutani, S.Y.2    Vermaak, D.3    Biggins, S.4
  • 23
    • 12244268624 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): Key to the conserved caspase-independent pathways of cell death?
    • Cande C., Cecconi F., Dessen P., and Kroemer G. Apoptosis-inducing factor (AIF): Key to the conserved caspase-independent pathways of cell death? J. Cell Sci. 115 2002 4727 4734
    • (2002) J. Cell Sci. , vol.115 , pp. 4727-4734
    • Cande, C.1    Cecconi, F.2    Dessen, P.3    Kroemer, G.4
  • 26
    • 0042170180 scopus 로고    scopus 로고
    • Survivin is required for stable checkpoint activation in response to loss of spindle tension in HeLa cells
    • Carvalho A., Carmena M., Sambade C., Earnshaw W.C., and Wheatley S.P. Survivin is required for stable checkpoint activation in response to loss of spindle tension in HeLa cells J. Cell Sci. 116 2003 2987 2998
    • (2003) J. Cell Sci. , vol.116 , pp. 2987-2998
    • Carvalho, A.1    Carmena, M.2    Sambade, C.3    Earnshaw, W.C.4    Wheatley, S.P.5
  • 28
    • 0033635270 scopus 로고    scopus 로고
    • Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual α-helical extensions
    • Chantalat L., Skoufias D.A., Kleman J.P., Jung B., Dideberg O., and Margolis R.L. Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual α-helical extensions Mol. Cell 6 2000 183 189
    • (2000) Mol. Cell , vol.6 , pp. 183-189
    • Chantalat, L.1    Skoufias, D.A.2    Kleman, J.P.3    Jung, B.4    Dideberg, O.5    Margolis, R.L.6
  • 29
    • 0035816553 scopus 로고    scopus 로고
    • Apaf-1/cytochrome c-independent and Smac-dependent induction of apoptosis in multiple myeloma (MM) cells
    • Chauhan D., Hideshima T., Rosen S., Reed J.C., Kharbanda S., and Anderson K.C. Apaf-1/cytochrome c-independent and Smac-dependent induction of apoptosis in multiple myeloma (MM) cells J. Biol. Chem. 276 2001 24453 24456
    • (2001) J. Biol. Chem. , vol.276 , pp. 24453-24456
    • Chauhan, D.1    Hideshima, T.2    Rosen, S.3    Reed, J.C.4    Kharbanda, S.5    Anderson, K.C.6
  • 30
    • 4344660599 scopus 로고    scopus 로고
    • Downregulation of Bcl-2, FLIP or IAPs (XIAP and survivin) by siRNAs sensitizes resistant melanoma cells to Apo2L/TRAIL-induced apoptosis
    • Chawla-Sarkar M., Bae S.I., Reu F.J., Jacobs B.S., Lindner D.J., and Borden E.C. Downregulation of Bcl-2, FLIP or IAPs (XIAP and survivin) by siRNAs sensitizes resistant melanoma cells to Apo2L/TRAIL-induced apoptosis Cell Death Differ. 11 2004 915 923
    • (2004) Cell Death Differ. , vol.11 , pp. 915-923
    • Chawla-sarkar, M.1    Bae, S.I.2    Reu, F.J.3    Jacobs, B.S.4    Lindner, D.J.5    Borden, E.C.6
  • 33
    • 0038457729 scopus 로고    scopus 로고
    • Survivin expression in ovarian carcinoma: Correlation with apoptotic markers and prognosis
    • Cohen C., Lohmann C.M., Cotsonis G., Lawson D., and Santoianni R. Survivin expression in ovarian carcinoma: Correlation with apoptotic markers and prognosis Mod. Pathol. 16 2003 574 583
    • (2003) Mod. Pathol. , vol.16 , pp. 574-583
    • Cohen, C.1    Lohmann, C.M.2    Cotsonis, G.3    Lawson, D.4    Santoianni, R.5
  • 35
    • 0027537461 scopus 로고
    • An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif
    • Crook N.E., Clem R.J., and Miller L.K. An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif J. Virol. 67 1993 2168 2174
    • (1993) J. Virol. , vol.67 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 36
    • 0036141029 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO
    • Deng Y., Lin Y., and Wu X. TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO Genes Dev. 16 2002 33 45
    • (2002) Genes Dev. , vol.16 , pp. 33-45
    • Deng, Y.1    Lin, Y.2    Wu, X.3
  • 37
    • 85047693458 scopus 로고    scopus 로고
    • Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: Cause or effect?
    • Dickson D.W. Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: Cause or effect? J. Clin. Invest. 114 2004 23 27
    • (2004) J. Clin. Invest. , vol.114 , pp. 23-27
    • Dickson, D.W.1
  • 39
    • 9644278114 scopus 로고    scopus 로고
    • Mitochondrial survivin inhibits apoptosis and promotes tumorigenesis
    • Dohi T., Beltrami E., Wall N.R., Plescia J., and Altieri D.C. Mitochondrial survivin inhibits apoptosis and promotes tumorigenesis J. Clin. Invest. 114 2004 1117 1127
    • (2004) J. Clin. Invest. , vol.114 , pp. 1117-1127
    • Dohi, T.1    Beltrami, E.2    Wall, N.R.3    Plescia, J.4    Altieri, D.C.5
  • 40
    • 0037291890 scopus 로고    scopus 로고
    • Insights into the regulatory mechanism for caspase-8 activation
    • Donepudi M., Sweeney A.M., Briand C., and Grutter M.G. Insights into the regulatory mechanism for caspase-8 activation Mol. Cell 11 2003 543 549
    • (2003) Mol. Cell , vol.11 , pp. 543-549
    • Donepudi, M.1    Sweeney, A.M.2    Briand, C.3    Grutter, M.G.4
  • 41
    • 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., and Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition Cell 102 2000 33 42
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 43
    • 0035809172 scopus 로고    scopus 로고
    • Diablo promotes apoptosis by removing MIHA/XIAP from processed caspase 9
    • Ekert P., Silke J., Hawkins C., Verhagen A., and Vaux D. Diablo promotes apoptosis by removing MIHA/XIAP from processed caspase 9 J. Cell Biol. 152 2001 483 490
    • (2001) J. Cell Biol. , vol.152 , pp. 483-490
    • Ekert, P.1    Silke, J.2    Hawkins, C.3    Verhagen, A.4    Vaux, D.5
  • 45
    • 0031001092 scopus 로고    scopus 로고
    • Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE
    • Fraser A.G., and Evan G.I. Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE EMBO J. 16 1997 2805 2813
    • (1997) EMBO J. , vol.16 , pp. 2805-2813
    • Fraser, A.G.1    Evan, G.I.2
  • 46
    • 0033602489 scopus 로고    scopus 로고
    • Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis
    • Fraser A.G., James C., Evan G.I., and Hengartner M.O. Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis Curr. Biol. 9 1999 292 301
    • (1999) Curr. Biol. , vol.9 , pp. 292-301
    • Fraser, A.G.1    James, C.2    Evan, G.I.3    Hengartner, M.O.4
  • 47
    • 0036236068 scopus 로고    scopus 로고
    • Immunohistochemical localization of survivin in benign cervical mucosa, cervical dysplasia, and invasive squamous cell carcinoma
    • Frost M., Jarboe E.A., Orlicky D., Gianani R., Thompson L.C., Enomoto T., and Shroyer K.R. Immunohistochemical localization of survivin in benign cervical mucosa, cervical dysplasia, and invasive squamous cell carcinoma Am. J. Clin. Pathol. 117 2002 738 744
    • (2002) Am. J. Clin. Pathol. , vol.117 , pp. 738-744
    • Frost, M.1    Jarboe, E.A.2    Orlicky, D.3    Gianani, R.4    Thompson, L.C.5    Enomoto, T.6    Shroyer, K.R.7
  • 49
    • 3142598843 scopus 로고    scopus 로고
    • A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration
    • Geisbrecht E.R., and Montell D.J. A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration Cell 118 2004 111 125
    • (2004) Cell , vol.118 , pp. 111-125
    • Geisbrecht, E.R.1    Montell, D.J.2
  • 50
    • 0037189527 scopus 로고    scopus 로고
    • Identification of aurora kinases as RasGAP Src homology 3 domain-binding proteins
    • Gigoux V., L'Hoste S., Raynaud F., Camonis J., and Garbay C. Identification of aurora kinases as RasGAP Src homology 3 domain-binding proteins J. Biol. Chem. 277 2002 23742 23746
    • (2002) J. Biol. Chem. , vol.277 , pp. 23742-23746
    • Gigoux, V.1    L'Hoste, S.2    Raynaud, F.3    Camonis, J.4    Garbay, C.5
  • 52
    • 0023943432 scopus 로고
    • Independent prognostic significance of a nuclear proliferation antigen in diffuse large cell lymphomas as determined by the monoclonal antibody Ki-67
    • Grogan T.M., Lippman S.M., Spier C.M., Slymen D.J., Rybski J.A., Rangel C.S., Richter L.C., and Miller T.P. Independent prognostic significance of a nuclear proliferation antigen in diffuse large cell lymphomas as determined by the monoclonal antibody Ki-67 Blood 71 1988 1157 1160
    • (1988) Blood , vol.71 , pp. 1157-1160
    • Grogan, T.M.1    Lippman, S.M.2    Spier, C.M.3    Slymen, D.J.4    Rybski, J.A.5    Rangel, C.S.6    Richter, L.C.7    Miller, T.P.8
  • 57
    • 0038746733 scopus 로고    scopus 로고
    • The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint
    • Hauf S., Cole R.W., La Terre S., Zimmer C., Schnapp G., Walter R., Heckel A., van Meel J., Rieder C.L., and Peters J.M. The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint J. Cell Biol. 161 2003 281 294
    • (2003) J. Cell Biol. , vol.161 , pp. 281-294
    • Hauf, S.1    Cole, R.W.2    La Terre, S.3    Zimmer, C.4    Schnapp, G.5    Walter, R.6    Heckel, A.7    Van Meel, J.8    Rieder, C.L.9    Peters, J.M.10
  • 58
    • 0029583176 scopus 로고
    • Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death
    • Hay B.A., Wassarman D.A., and Rubin G.M. Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death Cell 83 1995 1253 1262
    • (1995) Cell , vol.83 , pp. 1253-1262
    • Hay, B.A.1    Wassarman, D.A.2    Rubin, G.M.3
  • 59
    • 0034698053 scopus 로고    scopus 로고
    • Activation of NF-κB by XIAP, the X chromosome-linked inhibitor of apoptosis, in endothelial cells involves TAK1
    • Hofer-Warbinek R., Schmid J.A., Stehlik C., Binder B.R., Lipp J., and de Martin R. Activation of NF-κB by XIAP, the X chromosome-linked inhibitor of apoptosis, in endothelial cells involves TAK1 J. Biol. Chem. 275 2000 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
  • 60
    • 0036479115 scopus 로고    scopus 로고
    • Transcriptional repression of the anti-apoptotic survivin gene by wild type p53
    • Hoffman W.H., Biade S., Zilfou J.T., Chen J.D., and Murphy M. Transcriptional repression of the anti-apoptotic survivin gene by wild type p53 J. Biol. Chem. 277 2002 3247 3257
    • (2002) J. Biol. Chem. , vol.277 , pp. 3247-3257
    • Hoffman, W.H.1    Biade, S.2    Zilfou, J.T.3    Chen, J.D.4    Murphy, M.5
  • 61
    • 0041968963 scopus 로고    scopus 로고
    • Exploring the functional interactions between aurora B, INCENP, and survivin in mitosis
    • Honda R., Korner R., and Nigg E.A. Exploring the functional interactions between aurora B, INCENP, and survivin in mitosis Mol. Biol. Cell 14 2003 3325 3341
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3325-3341
    • Honda, R.1    Korner, R.2    Nigg, E.A.3
  • 62
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP. Differential roles of the linker versus the BIR domain
    • Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., and Wu H. Structural basis of caspase inhibition by XIAP. Differential roles of the linker versus the BIR domain Cell 104 2001 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
  • 63
    • 1442310961 scopus 로고    scopus 로고
    • Role of Bcl-2 family members in invertebrates
    • Igaki T., and Miura M. Role of Bcl-2 family members in invertebrates Biochim. Biophys. Acta 1644 2004 73 81
    • (2004) Biochim. Biophys. Acta , vol.1644 , pp. 73-81
    • Igaki, T.1    Miura, M.2
  • 64
    • 0033661699 scopus 로고    scopus 로고
    • Role of survivin, whose gene is mapped to 17q25, in human neuroblastoma and identification of a novel dominant-negative isoform, survivin-β/2B
    • Islam A., Kageyama H., Hashizume K., Kaneko Y., and Nakagawara A. Role of survivin, whose gene is mapped to 17q25, in human neuroblastoma and identification of a novel dominant-negative isoform, survivin-β/2B Med. Pediatr. Oncol. 35 2000 550 553
    • (2000) Med. Pediatr. Oncol. , vol.35 , pp. 550-553
    • Islam, A.1    Kageyama, H.2    Hashizume, K.3    Kaneko, Y.4    Nakagawara, A.5
  • 65
    • 0034822324 scopus 로고    scopus 로고
    • Participation of survivin in mitotic and apoptotic activities of normal and tumor-derived cells
    • Jiang X., Wilford C., Duensing S., Munger K., Jones G., and Jones D. Participation of survivin in mitotic and apoptotic activities of normal and tumor-derived cells J. Biol. Chem. 83 2001 342 354
    • (2001) J. Biol. Chem. , vol.83 , pp. 342-354
    • Jiang, X.1    Wilford, C.2    Duensing, S.3    Munger, K.4    Jones, G.5    Jones, D.6
  • 67
    • 0034698097 scopus 로고    scopus 로고
    • Deterin, a new inhibitor of apoptosis from Drosophila melanogaster
    • Jones G., Jones D., Zhou L., Stellar H., and Chu Y. Deterin, a new inhibitor of apoptosis from Drosophila melanogaster J. Biol. Chem. 275 2000 22157 22165
    • (2000) J. Biol. Chem. , vol.275 , pp. 22157-22165
    • Jones, G.1    Jones, D.2    Zhou, L.3    Stellar, H.4    Chu, Y.5
  • 68
    • 0037018844 scopus 로고    scopus 로고
    • Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis
    • Kallio M.J., McCleland M.L., Stukenberg P.T., and Gorbsky G.J. Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis Curr. Biol. 12 2002 900 905
    • (2002) Curr. Biol. , vol.12 , pp. 900-905
    • Kallio, M.J.1    McCleland, M.L.2    Stukenberg, P.T.3    Gorbsky, G.J.4
  • 70
    • 0033231614 scopus 로고    scopus 로고
    • Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator
    • Kanuka H., Sawamoto K., Inohara N., Matsuno K., Okano H., and Miura M. Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator Mol. Cell 4 1999 757 769
    • (1999) Mol. Cell , vol.4 , pp. 757-769
    • Kanuka, H.1    Sawamoto, K.2    Inohara, N.3    Matsuno, K.4    Okano, H.5    Miura, M.6
  • 71
    • 10744227367 scopus 로고    scopus 로고
    • Knockdown of survivin expression by small interfering RNA reduces the clonogenic survival of human sarcoma cell lines independently of p53
    • Kappler M., Bache M., Bartel F., Kotzsch M., Panian M., Wurl P., Blumke K., Schmidt H., Meye A., and Taubert H. Knockdown of survivin expression by small interfering RNA reduces the clonogenic survival of human sarcoma cell lines independently of p53 Cancer Gene Ther. 11 2004 186 193
    • (2004) Cancer Gene Ther. , vol.11 , pp. 186-193
    • Kappler, M.1    Bache, M.2    Bartel, F.3    Kotzsch, M.4    Panian, M.5    Wurl, P.6    Blumke, K.7    Schmidt, H.8    Meye, A.9    Taubert, H.10
  • 73
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F.R., Wyllie A.H., and Currie A.R. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics British J. Cancer 26 1972 239 257
    • (1972) British J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 74
  • 76
    • 4444361250 scopus 로고    scopus 로고
    • Survivin expression is an independent prognostic factor in rectal cancer patients with and without preoperative radiotherapy
    • Knutsen A., Adell G., and Sun X.F. Survivin expression is an independent prognostic factor in rectal cancer patients with and without preoperative radiotherapy Int. J. Radiat. Oncol. Biol. Phys. 60 2004 149 155
    • (2004) Int. J. Radiat. Oncol. Biol. Phys. , vol.60 , pp. 149-155
    • Knutsen, A.1    Adell, G.2    Sun, X.F.3
  • 77
    • 0033573905 scopus 로고    scopus 로고
    • Expression of a murine homologue of the inhibitor of apoptosis protein is related to cell proliferation
    • Kobayashi K., Hatano M., Otaki M., Ogasawara T., and Tokuhisa T. Expression of a murine homologue of the inhibitor of apoptosis protein is related to cell proliferation Proc. Natl. Acad. Sci. USA 96 1999 1457 1462
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1457-1462
    • Kobayashi, K.1    Hatano, M.2    Otaki, M.3    Ogasawara, T.4    Tokuhisa, T.5
  • 80
    • 2342584674 scopus 로고    scopus 로고
    • Clearance of apoptotic cells: Getting rid of the corpses
    • Lauber K., Blumenthal S.G., Waibel M., and Wesselborg S. Clearance of apoptotic cells: Getting rid of the corpses Mol. Cell 14 2004 277 287
    • (2004) Mol. Cell , vol.14 , pp. 277-287
    • Lauber, K.1    Blumenthal, S.G.2    Waibel, M.3    Wesselborg, S.4
  • 81
    • 2342528439 scopus 로고    scopus 로고
    • The survivin/Aurora B complex: Its role in coordinating tension and attachment
    • Lens S.M., and Medema R.H. The survivin/Aurora B complex: Its role in coordinating tension and attachment Cell Cycle 2 2003 507 510
    • (2003) Cell Cycle , vol.2 , pp. 507-510
    • Lens, S.M.1    Medema, R.H.2
  • 83
    • 0036223874 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis
    • Leverson J.D., Huang H., Forsburg S.L., and Hunter T. The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis Mol. Biol. Cell 13 2002 1132 1143
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1132-1143
    • Leverson, J.D.1    Huang, H.2    Forsburg, S.L.3    Hunter, T.4
  • 84
    • 1542335506 scopus 로고    scopus 로고
    • Uncoupling of the signaling and caspase-inhibitory properties of X-linked inhibitor of apoptosis
    • Lewis J., Burstein E., Reffey S.B., Bratton S.B., Roberts A.B., and Duckett C.S. Uncoupling of the signaling and caspase-inhibitory properties of X-linked inhibitor of apoptosis J. Biol. Chem. 279 2004 9023 9029
    • (2004) J. Biol. Chem. , vol.279 , pp. 9023-9029
    • Lewis, J.1    Burstein, E.2    Reffey, S.B.3    Bratton, S.B.4    Roberts, A.B.5    Duckett, C.S.6
  • 85
    • 14844313647 scopus 로고    scopus 로고
    • Role of survivin and its splice variants in tumorigenesis
    • Li F. Role of survivin and its splice variants in tumorigenesis Br. J. Cancer 92 2004 212 216
    • (2004) Br. J. Cancer , vol.92 , pp. 212-216
    • Li, F.1
  • 88
    • 0033168929 scopus 로고    scopus 로고
    • The cancer antiapoptosis mouse survivin gene: Characterization of locus and transcriptional requirements of basal and cell cycle-dependent expression
    • Li F.Z., and Altieri D.C. The cancer antiapoptosis mouse survivin gene: Characterization of locus and transcriptional requirements of basal and cell cycle-dependent expression Cancer Res. 59 1999 3143 3151
    • (1999) Cancer Res. , vol.59 , pp. 3143-3151
    • Li, F.Z.1    Altieri, D.C.2
  • 89
    • 0033436285 scopus 로고    scopus 로고
    • Transcriptional analysis of human survivin gene expression
    • Li F.Z., and Altieri D.C. Transcriptional analysis of human survivin gene expression Biochem. J. 344 1999 305 311
    • (1999) Biochem. J. , vol.344 , pp. 305-311
    • Li, F.Z.1    Altieri, D.C.2
  • 90
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li L.Y., Luo X., and Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria Nature 412 2001 95 99
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 93
    • 1542375910 scopus 로고    scopus 로고
    • Silencing of antiapoptotic survivin gene by multiple approaches of RNA interference technology
    • Ling X., and Li F. Silencing of antiapoptotic survivin gene by multiple approaches of RNA interference technology Biotechniques 36 2004 456 460
    • (2004) Biotechniques , vol.36 , pp. 456-460
    • Ling, X.1    Li, F.2
  • 94
    • 0942290423 scopus 로고    scopus 로고
    • Rapid induction of mitochondrial events and caspase-independent apoptosis in Survivin-targeted melanoma cells
    • Liu T., Brouha B., and Grossman D. Rapid induction of mitochondrial events and caspase-independent apoptosis in Survivin-targeted melanoma cells Oncogene 23 2004 39 48
    • (2004) Oncogene , vol.23 , pp. 39-48
    • Liu, T.1    Brouha, B.2    Grossman, D.3
  • 97
    • 0041857759 scopus 로고    scopus 로고
    • P21/CDKN1A mediates negative regulation of transcription by p53
    • Lohr K., Moritz C., Contente A., and Dobbelstein M. p21/CDKN1A mediates negative regulation of transcription by p53 J. Biol. Chem. 278 2003 32507 32516
    • (2003) J. Biol. Chem. , vol.278 , pp. 32507-32516
    • Lohr, K.1    Moritz, C.2    Contente, A.3    Dobbelstein, M.4
  • 98
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., and Wang X.D. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors Cell 94 1998 481 490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.D.5
  • 99
    • 0037137188 scopus 로고    scopus 로고
    • A highly conserved arginine is critical for the functional folding of inhibitor of apoptosis (IAP) BIR domains
    • Luque L.E., Grape K.P., and Junker M. A highly conserved arginine is critical for the functional folding of inhibitor of apoptosis (IAP) BIR domains Biochemistry 41 2002 13663 13671
    • (2002) Biochemistry , vol.41 , pp. 13663-13671
    • Luque, L.E.1    Grape, K.P.2    Junker, M.3
  • 101
    • 0033571983 scopus 로고    scopus 로고
    • Survivin-ΔEx3 and Survivin-2B: Two novel splice variants of the apoptosis inhibitor survivin with different antiapoptotic properties
    • Mahotka C., Wenzel M., Springer E., Gabbert H.E., and Gerharz C.D. Survivin-ΔEx3 and Survivin-2B: Two novel splice variants of the apoptosis inhibitor survivin with different antiapoptotic properties Cancer Res. 59 1999 6097 6102
    • (1999) Cancer Res. , vol.59 , pp. 6097-6102
    • Mahotka, C.1    Wenzel, M.2    Springer, E.3    Gabbert, H.E.4    Gerharz, C.D.5
  • 103
    • 2542457495 scopus 로고    scopus 로고
    • Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases
    • Martinon F., and Tschopp J. Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases Cell 117 2004 561 574
    • (2004) Cell , vol.117 , pp. 561-574
    • Martinon, F.1    Tschopp, J.2
  • 104
    • 0037784054 scopus 로고    scopus 로고
    • Pro-caspase-3 expression in ovarian carcinoma cells increases survivin transcription which can be countered with a dominant negative mutant, survivin T34A: A combination gene therapy strategy
    • McKay T.R., Bell S., Tenev T., Stoll V., Lopes R., Lemoine N.R., and McNeish I.A. Pro-caspase-3 expression in ovarian carcinoma cells increases survivin transcription which can be countered with a dominant negative mutant, survivin T34A: A combination gene therapy strategy Oncogene 22 2003 3539 3547
    • (2003) Oncogene , vol.22 , pp. 3539-3547
    • McKay, T.R.1    Bell, S.2    Tenev, T.3    Stoll, V.4    Lopes, R.5    Lemoine, N.R.6    McNeish, I.A.7
  • 105
    • 0038297558 scopus 로고    scopus 로고
    • Expression of Smac/DIABLO in ovarian carcinoma cells induces apoptosis via a caspase-9-mediated pathway
    • McNeish I.A., Bell S., McKay T., Tenev T., Marani M., and Lemoine N.R. Expression of Smac/DIABLO in ovarian carcinoma cells induces apoptosis via a caspase-9-mediated pathway Exp. Cell Res. 286 2003 186 198
    • (2003) Exp. Cell Res. , vol.286 , pp. 186-198
    • McNeish, I.A.1    Bell, S.2    McKay, T.3    Tenev, T.4    Marani, M.5    Lemoine, N.R.6
  • 107
    • 7744234871 scopus 로고    scopus 로고
    • Prognostic significance and different properties of survivin splicing variants in gastric cancer
    • Meng H., Lu C., Mabuchi H., and Tanigawa N. Prognostic significance and different properties of survivin splicing variants in gastric cancer Cancer Lett. 216 2004 147 155
    • (2004) Cancer Lett. , vol.216 , pp. 147-155
    • Meng, H.1    Lu, C.2    Mabuchi, H.3    Tanigawa, N.4
  • 110
    • 0034820448 scopus 로고    scopus 로고
    • Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is required for condensation, spindle elongation and repair
    • Morishita J., Matsusaka T., Goshima G., Nakamura T., Tatebe H., and Yanagida M. Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is required for condensation, spindle elongation and repair Genes Cells 6 2001 743 763
    • (2001) Genes Cells , vol.6 , pp. 743-763
    • Morishita, J.1    Matsusaka, T.2    Goshima, G.3    Nakamura, T.4    Tatebe, H.5    Yanagida, M.6
  • 112
    • 0037018843 scopus 로고    scopus 로고
    • The kinase activity of Aurora B is required for kinetochore-microtubule interactions during mitosis
    • Murata-Hori M., and Wang Y. The kinase activity of Aurora B is required for kinetochore-microtubule interactions during mitosis Curr. Biol. 12 2002 894 899
    • (2002) Curr. Biol. , vol.12 , pp. 894-899
    • Murata-hori, M.1    Wang, Y.2
  • 113
    • 0036894075 scopus 로고    scopus 로고
    • Survivin mRNA is down-regulated during early Xenopus laevis embryogenesis
    • Murphy C.R., Sabel J.L., Sandler A.D., and Dagle J.M. Survivin mRNA is down-regulated during early Xenopus laevis embryogenesis Dev. Dyn. 225 2002 597 601
    • (2002) Dev. Dyn. , vol.225 , pp. 597-601
    • Murphy, C.R.1    Sabel, J.L.2    Sandler, A.D.3    Dagle, J.M.4
  • 115
    • 0041941573 scopus 로고    scopus 로고
    • An inner centromere protein that stimulates the microtubule depolymerising activity of a KinI kinase
    • Ohi R., Coughlin M.L., Lane W.S., and Mitchison T.J. An inner centromere protein that stimulates the microtubule depolymerising activity of a KinI kinase Dev. Cell 5 2003 309 321
    • (2003) Dev. Cell , vol.5 , pp. 309-321
    • Ohi, R.1    Coughlin, M.L.2    Lane, W.S.3    Mitchison, T.J.4
  • 118
    • 0342657718 scopus 로고    scopus 로고
    • A novel antisense oligonucleotide targeting survivin expression induces apoptosis and sensitizes lung cancer cells to chemotherapy
    • Olie R.A., Simoes-Wust A.P., Baumann B., Leech S.H., Fabbro D., Stahel R.A., and Zangemeister-Wittke U. A novel antisense oligonucleotide targeting survivin expression induces apoptosis and sensitizes lung cancer cells to chemotherapy Cancer Res. 60 2000 2805 2809
    • (2000) Cancer Res. , vol.60 , pp. 2805-2809
    • Olie, R.A.1    Simoes-wust, A.P.2    Baumann, B.3    Leech, S.H.4    Fabbro, D.5    Stahel, R.A.6    Zangemeister-wittke, U.7
  • 122
    • 0037380133 scopus 로고    scopus 로고
    • S. pombe aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response
    • Petersen J., and Hagan I.M. S. pombe aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response Curr. Biol. 13 2003 590 597
    • (2003) Curr. Biol. , vol.13 , pp. 590-597
    • Petersen, J.1    Hagan, I.M.2
  • 123
    • 0032852181 scopus 로고    scopus 로고
    • S. pombe Pbh1p: An inhibitor of apoptosis domain containing protein is essential for chromosome segregation
    • Rajagopalan S., and Balasubramanian M.K. S. pombe Pbh1p: An inhibitor of apoptosis domain containing protein is essential for chromosome segregation FEBS Letts. 460 1999 187 190
    • (1999) FEBS Letts. , vol.460 , pp. 187-190
    • Rajagopalan, S.1    Balasubramanian, M.K.2
  • 124
    • 0036189157 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe Bir1p, a nuclear protein that localizes to kinetochores and the spindle midzone, is essential for chromosome condensation and spindle elongation during mitosis
    • Rajagopalan S., and Balasubramanian M.K. Schizosaccharomyces pombe Bir1p, a nuclear protein that localizes to kinetochores and the spindle midzone, is essential for chromosome condensation and spindle elongation during mitosis Genetics 160 2002 445 456
    • (2002) Genetics , vol.160 , pp. 445-456
    • Rajagopalan, S.1    Balasubramanian, M.K.2
  • 125
    • 0032877668 scopus 로고    scopus 로고
    • Dysregulation of apoptosis in cancer
    • Reed J.C. Dysregulation of apoptosis in cancer J. Clin. Oncol. 17 1999 2941 2953
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2941-2953
    • Reed, J.C.1
  • 126
    • 0034794571 scopus 로고    scopus 로고
    • The Survivin saga goes in vivo
    • Reed J.C. The Survivin saga goes in vivo J. Clin. Invest. 108 2001 965 969
    • (2001) J. Clin. Invest. , vol.108 , pp. 965-969
    • Reed, J.C.1
  • 127
    • 0035854738 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein functions as a cofactor in transforming growth factor-β signaling
    • Reffey S.B., Wurthner J.U., Parks W.T., Roberts A.B., and Duckett C.S. X-linked inhibitor of apoptosis protein functions as a cofactor in transforming growth factor-β signaling J. Biol. Chem. 276 2001 26542 26549
    • (2001) J. Biol. Chem. , vol.276 , pp. 26542-26549
    • Reffey, S.B.1    Wurthner, J.U.2    Parks, W.T.3    Roberts, A.B.4    Duckett, C.S.5
  • 129
    • 0036343736 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export determines the cytoplasmic localization of the antiapoptotic protein survivin
    • Rodriguez J.A., Span S.W., Ferreira C.G.M., Kruyt F.A.E., and Giaccone G. CRM1-mediated nuclear export determines the cytoplasmic localization of the antiapoptotic protein survivin Exp. Cell Res. 275 2002 44 53
    • (2002) Exp. Cell Res. , vol.275 , pp. 44-53
    • Rodriguez, J.A.1    Span, S.W.2    Ferreira, C.G.M.3    Kruyt, F.A.E.4    Giaccone, G.5
  • 130
    • 0038070181 scopus 로고    scopus 로고
    • CSC1: A subunit of the aurora B kinase complex that binds to the survivin-like protein BIR-1 and the Incenp-like protein ICP-1
    • Romano A., Guse A., Krascenicova I., Schnabel H., Schnabel R., and Glotzer M. CSC1: A subunit of the aurora B kinase complex that binds to the survivin-like protein BIR-1 and the Incenp-like protein ICP-1 J. Cell Biol. 161 2003 229 236
    • (2003) J. Cell Biol. , vol.161 , pp. 229-236
    • Romano, A.1    Guse, A.2    Krascenicova, I.3    Schnabel, H.4    Schnabel, R.5    Glotzer, M.6
  • 131
    • 0027275992 scopus 로고
    • Identification of seven new cut genes involved in Schizosaccharomyces pombe mitosis
    • Samejima I., Matsumoto T., Nakeseko Y., Beach D., and Yanagida M. Identification of seven new cut genes involved in Schizosaccharomyces pombe mitosis J. Cell Sci. 105 1993 135 143
    • (1993) J. Cell Sci. , vol.105 , pp. 135-143
    • Samejima, I.1    Matsumoto, T.2    Nakeseko, Y.3    Beach, D.4    Yanagida, M.5
  • 132
    • 3242657509 scopus 로고    scopus 로고
    • The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly
    • Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A., and Funabiki H. The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly Cell 118 2004 187 202
    • (2004) Cell , vol.118 , pp. 187-202
    • Sampath, S.C.1    Ohi, R.2    Leismann, O.3    Salic, A.4    Pozniakovski, A.5    Funabiki, H.6
  • 135
    • 0035039678 scopus 로고    scopus 로고
    • A structural view of mitochondria-mediated apoptosis
    • Shi Y.G. A structural view of mitochondria-mediated apoptosis Nat. Struct. Biol. 8 2001 394 401
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 394-401
    • Shi, Y.G.1
  • 136
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S., Narita M., and Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC Nature 399 1999 483 487
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 139
    • 0034993758 scopus 로고    scopus 로고
    • Two kinds of BIR-containing protein: Inhibitors of apoptosis, or required for mitosis
    • Silke J., and Vaux D. Two kinds of BIR-containing protein: Inhibitors of apoptosis, or required for mitosis J. Cell Sci. 114 2001 1821 1827
    • (2001) J. Cell Sci. , vol.114 , pp. 1821-1827
    • Silke, J.1    Vaux, D.2
  • 142
    • 1542283797 scopus 로고    scopus 로고
    • A single amino acid change (Asp53-Ala53) converts survivin from anti-apoptotic to pro-apoptotic
    • Song Z., Liu S., He H., Hoti N., Wang Y., Feng S., and Wu M. A single amino acid change (Asp53-Ala53) converts survivin from anti-apoptotic to pro-apoptotic Mol. Biol. Cell 15 2004 1287 1296
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1287-1296
    • Song, Z.1    Liu, S.2    He, H.3    Hoti, N.4    Wang, Y.5    Feng, S.6    Wu, M.7
  • 143
    • 0033637849 scopus 로고    scopus 로고
    • The survivin-like C. elegans BIR-1 protein acts with the aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone
    • Speliotes E.K., Uren A., Vaux D., and Horvitz H.R. The survivin-like C. elegans BIR-1 protein acts with the aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone Mol. Cell 6 2000 211 223
    • (2000) Mol. Cell , vol.6 , pp. 211-223
    • Speliotes, E.K.1    Uren, A.2    Vaux, D.3    Horvitz, H.R.4
  • 144
    • 0032490670 scopus 로고    scopus 로고
    • Nuclear factor (NF)-κB-regulated X-chromosome-linked IAP gene expression protects endothelial cells from tumor necrosis factor α-induced apoptosis
    • Stehlik C., de Martin R., Kumabashiri I., Schmid J.A., Binder B.R., and Lipp J. Nuclear factor (NF)-κB-regulated X-chromosome-linked IAP gene expression protects endothelial cells from tumor necrosis factor α-induced apoptosis J. Exp. Med. 188 1998 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
  • 146
    • 11844252553 scopus 로고    scopus 로고
    • Solution structure of human survivin and its binding interface with Smac/DIABLO
    • Sun C., Nettesheim D., Liu Z., and Olejniczak E.T. Solution structure of human survivin and its binding interface with Smac/DIABLO Biochemistry 44 2005 11 17
    • (2005) Biochemistry , vol.44 , pp. 11-17
    • Sun, C.1    Nettesheim, D.2    Liu, Z.3    Olejniczak, E.T.4
  • 148
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • Suzuki Y., Nakabayashi Y., and Takahashi R. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death Proc. Natl. Acad. Sci. USA 98 2001 8662 8667
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 149
    • 2542549018 scopus 로고    scopus 로고
    • High expression levels of X-linked inhibitor of apoptosis protein and survivin correlate with poor overall survival in childhood de novo acute myeloid leukemia
    • Tamm I., Richter S., Oltersdorf D., Creutzig U., Harbott J., Scholz F., Karawajew L., Ludwig W.D., and Wuchter C. High expression levels of X-linked inhibitor of apoptosis protein and survivin correlate with poor overall survival in childhood de novo acute myeloid leukemia Clin. Cancer Res. 10 2004 3737 3744
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3737-3744
    • Tamm, I.1    Richter, S.2    Oltersdorf, D.3    Creutzig, U.4    Harbott, J.5    Scholz, F.6    Karawajew, L.7    Ludwig, W.D.8    Wuchter, C.9
  • 150
    • 0032403126 scopus 로고    scopus 로고
    • IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases and anticancer drugs
    • Tamm I., Wang Y., Sausville E., Scudiero D., Vigna N., Oltersdorf T., and Reed J. IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases and anticancer drugs Cancer Res. 58 1998 5315 5320
    • (1998) Cancer Res. , vol.58 , pp. 5315-5320
    • Tamm, I.1    Wang, Y.2    Sausville, E.3    Scudiero, D.4    Vigna, N.5    Oltersdorf, T.6    Reed, J.7
  • 151
    • 0036178929 scopus 로고    scopus 로고
    • Evidence that the Ipl1-Sli15 (aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections
    • Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Scheibel E., Stark M.J.R., and Nasmyth K. Evidence that the Ipl1-Sli15 (aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections Cell 108 2002 317 329
    • (2002) Cell , vol.108 , pp. 317-329
    • Tanaka, T.U.1    Rachidi, N.2    Janke, C.3    Pereira, G.4    Galova, M.5    Scheibel, E.6    Stark, M.J.R.7    Nasmyth, K.8
  • 154
    • 12344300349 scopus 로고    scopus 로고
    • IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms
    • Tenev T., Zachariou A., Wilson R., Ditzel M., and Meier P. IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms Nat. Cell Biol. 7 2005 70 77
    • (2005) Nat. Cell Biol. , vol.7 , pp. 70-77
    • Tenev, T.1    Zachariou, A.2    Wilson, R.3    Ditzel, M.4    Meier, P.5
  • 155
    • 0035496099 scopus 로고    scopus 로고
    • Regulation of lymphocyte proliferation and death by FLIP
    • Thome M., and Tschopp J. Regulation of lymphocyte proliferation and death by FLIP Nat. Rev. Immunol. 1 2001 50 58
    • (2001) Nat. Rev. Immunol. , vol.1 , pp. 50-58
    • Thome, M.1    Tschopp, J.2
  • 156
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N., and Lazebnik Y. Caspases: Enemies within Science 281 1998 1312 1316
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.1    Lazebnik, Y.2
  • 157
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: More than scavengers Biochim. Biophys. Acta 1477 2000 98 111
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 159
    • 2942679807 scopus 로고    scopus 로고
    • Cell cycle progression after cleavage failure: Mammalian somatic cells do not possess a "tetraploidy checkpoint."
    • Uetake Y., and Sluder G. Cell cycle progression after cleavage failure: Mammalian somatic cells do not possess a "tetraploidy checkpoint." J. Cell Biol. 165 2004 609 615
    • (2004) J. Cell Biol. , vol.165 , pp. 609-615
    • Uetake, Y.1    Sluder, G.2
  • 161
    • 0034597594 scopus 로고    scopus 로고
    • Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype
    • Uren A.G., Wong L., Pakusch M., Fowler K.J., Burrows F.J., Vaux D.L., and Choo K.H.A. Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype Curr. Biol. 10 2000 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    Choo, K.H.A.7
  • 162
    • 7744222944 scopus 로고    scopus 로고
    • Chromosomal passengers: The four-dimensional regulation of mitotic events
    • Vagnarelli P., and Earnshaw W.C. Chromosomal passengers: The four-dimensional regulation of mitotic events Chromosoma 113 2004 211 222
    • (2004) Chromosoma , vol.113 , pp. 211-222
    • Vagnarelli, P.1    Earnshaw, W.C.2
  • 164
    • 0033923368 scopus 로고    scopus 로고
    • Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement
    • Verdecia M., Huang H.-K., Dutil E., Kaiser D., Hunter T., and Noel J. Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement Nat. Struct. Biol. 7 2000 602 608
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 602-608
    • Verdecia, M.1    Huang, H.-K.2    Dutil, E.3    Kaiser, D.4    Hunter, T.5    Noel, J.6
  • 165
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen A., Ekert P., Pakusch M., Silke J., Connolly L., Reid G., Moritz R., Simpson R., and Vaux D. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins Cell 102 2000 43 53
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.1    Ekert, P.2    Pakusch, M.3    Silke, J.4    Connolly, L.5    Reid, G.6    Moritz, R.7    Simpson, R.8    Vaux, D.9
  • 166
    • 0034921727 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs
    • Verhagen A.M., Coulson E.J., and Vaux D.L. Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs Genome Biol. 2 2001 3009.1 3009.10
    • (2001) Genome Biol. , vol.2 , pp. 30091-300910
    • Verhagen, A.M.1    Coulson, E.J.2    Vaux, D.L.3
  • 168
    • 0037228959 scopus 로고    scopus 로고
    • Suppression of survivin phosphorylation on Thr34 by flavopiridol enhances tumor cell apoptosis
    • Wall N.R., O'Connor D.S., Plescia J., Pommier Y., and Altieri D.C. Suppression of survivin phosphorylation on Thr34 by flavopiridol enhances tumor cell apoptosis Cancer Res. 63 2003 230 235
    • (2003) Cancer Res. , vol.63 , pp. 230-235
    • Wall, N.R.1    O'Connor, D.S.2    Plescia, J.3    Pommier, Y.4    Altieri, D.C.5
  • 169
    • 0037013894 scopus 로고    scopus 로고
    • Characterization of an anti-apoptotic glycoprotein encoded by Kaposi's sarcoma-associated herpesvirus which resembles a spliced variant of human survivin
    • Wang H.-W., Sharp T.V., Koumi A., Koentges G., and Boshoff C. Characterization of an anti-apoptotic glycoprotein encoded by Kaposi's sarcoma-associated herpesvirus which resembles a spliced variant of human survivin EMBO J. 21 2002 2602 2615
    • (2002) EMBO J. , vol.21 , pp. 2602-2615
    • Wang, H.-W.1    Sharp, T.V.2    Koumi, A.3    Koentges, G.4    Boshoff, C.5
  • 170
    • 4544334875 scopus 로고    scopus 로고
    • Survivin regulates the p53 tumor suppressor gene family
    • Wang Z., Fukuda S., and Pelus L. Survivin regulates the p53 tumor suppressor gene family Oncogene 23 2004 8146 8153
    • (2004) Oncogene , vol.23 , pp. 8146-8153
    • Wang, Z.1    Fukuda, S.2    Pelus, L.3
  • 171
    • 0035810919 scopus 로고    scopus 로고
    • INCENP is required for proper targeting of survivin to the centromeres and the anaphase spindle during mitosis
    • Wheatley S.P., Carvalho A., Vagnarelli P., and Earnshaw W.C. INCENP is required for proper targeting of survivin to the centromeres and the anaphase spindle during mitosis Curr. Biol. 11 2001 886 890
    • (2001) Curr. Biol. , vol.11 , pp. 886-890
    • Wheatley, S.P.1    Carvalho, A.2    Vagnarelli, P.3    Earnshaw, W.C.4
  • 172
    • 1242339630 scopus 로고    scopus 로고
    • Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to INCENP in vivo
    • Wheatley S.P., Henzing A.J., Dodson H., Khaled W., and Earnshaw W.C. Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to INCENP in vivo J. Biol. Chem. 279 2004 5655 5660
    • (2004) J. Biol. Chem. , vol.279 , pp. 5655-5660
    • Wheatley, S.P.1    Henzing, A.J.2    Dodson, H.3    Khaled, W.4    Earnshaw, W.C.5
  • 173
    • 3543011331 scopus 로고    scopus 로고
    • Upstream regulatory role for XIAP in receptor-mediated apoptosis
    • Wilkinson J.C., Cepero E., Boise L.H., and Duckett C.S. Upstream regulatory role for XIAP in receptor-mediated apoptosis Mol. Cell. Biol. 24 2004 7003 7014
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7003-7014
    • Wilkinson, J.C.1    Cepero, E.2    Boise, L.H.3    Duckett, C.S.4
  • 175
    • 15744368221 scopus 로고    scopus 로고
    • Molecular mechanism of inhibition of survivin transcription by the GC-rich sequence selective DNA-binding antitumor agent, hedamycin: Evidence of survivin downregulation associated with drug sensitivity
    • Wu J., Ling X., Pan D., Apontes P., Song L., Liang P., Altieri D.C., Beerman T., and Li F. Molecular mechanism of inhibition of survivin transcription by the GC-rich sequence selective DNA-binding antitumor agent, hedamycin: Evidence of survivin downregulation associated with drug sensitivity J. Biol. Chem. 280 2005 9745 9751
    • (2005) J. Biol. Chem. , vol.280 , pp. 9745-9751
    • Wu, J.1    Ling, X.2    Pan, D.3    Apontes, P.4    Song, L.5    Liang, P.6    Altieri, D.C.7    Beerman, T.8    Li, F.9
  • 176
    • 0032522223 scopus 로고    scopus 로고
    • Detection of programmed cell death using fluorescence energy transfer
    • Xu X., Gerard A., Huang B., Anderson D., Payan D., and Luo Y. Detection of programmed cell death using fluorescence energy transfer Nucleic Acids Res. 26 1998 2034 2035
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2034-2035
    • Xu, X.1    Gerard, A.2    Huang, B.3    Anderson, D.4    Payan, D.5    Luo, Y.6
  • 177
    • 4544260238 scopus 로고    scopus 로고
    • A mutation found in the promoter region of the human survivin gene is correlated with overexpression of survivin in cancer cells
    • Xu Y., Fang F., Ludewig G., Jones G., and Jones D. A mutation found in the promoter region of the human survivin gene is correlated with overexpression of survivin in cancer cells DNA Cell Biol. 9 2004 527 537
    • (2004) DNA Cell Biol. , vol.9 , pp. 527-537
    • Xu, Y.1    Fang, F.2    Ludewig, G.3    Jones, G.4    Jones, D.5
  • 178
    • 1242271228 scopus 로고    scopus 로고
    • Translational regulation of X-linked inhibitor of apoptosis protein by interleukin-6: A novel mechanism of tumor cell survival
    • Yamagiwa Y., Marienfeld C., Meng F., Holcik M., and Patel T. Translational regulation of X-linked inhibitor of apoptosis protein by interleukin-6: A novel mechanism of tumor cell survival Cancer Res. 64 2004 1293 1298
    • (2004) Cancer Res. , vol.64 , pp. 1293-1298
    • Yamagiwa, Y.1    Marienfeld, C.2    Meng, F.3    Holcik, M.4    Patel, T.5
  • 180
    • 6344221309 scopus 로고    scopus 로고
    • Cell division and cell survival in the absence of survivin
    • Yang D., Welm A., and Bishop J.M. Cell division and cell survival in the absence of survivin Proc. Natl. Acad. Sci. USA 101 2004 15100 15105
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15100-15105
    • Yang, D.1    Welm, A.2    Bishop, J.M.3
  • 181
    • 4243182684 scopus 로고    scopus 로고
    • Tumor-specific gene expression using the survivin promoter is further increased by hypoxia
    • Yang L., Cao Z., Li F., Post D.E., Van Meir E.G., Zhong H., and Wood W.C. Tumor-specific gene expression using the survivin promoter is further increased by hypoxia Gene Ther. 11 2004 1215 1223
    • (2004) Gene Ther. , vol.11 , pp. 1215-1223
    • Yang, L.1    Cao, Z.2    Li, F.3    Post, D.E.4    Van Meir, E.G.5    Zhong, H.6    Wood, W.C.7
  • 182
    • 0035132464 scopus 로고    scopus 로고
    • Reconstitution of caspase 3 sensitizes MCF-7 breast cancer cells to doxorubicin- and etoposide-induced apoptosis
    • Yang X.-H., Sladek T.L., Liu X., Butler B.R., Froelich C.J., and Thor A.D. Reconstitution of caspase 3 sensitizes MCF-7 breast cancer cells to doxorubicin- and etoposide-induced apoptosis Cancer Res. 61 2001 348 354
    • (2001) Cancer Res. , vol.61 , pp. 348-354
    • Yang, X.-H.1    Sladek, T.L.2    Liu, X.3    Butler, B.R.4    Froelich, C.J.5    Thor, A.D.6
  • 183
    • 0033539663 scopus 로고    scopus 로고
    • Participation of Bir1p, a member of the inhibitor of apoptosis family, in yeast chromosome segregation events
    • Yoon H., and Carbon J. Participation of Bir1p, a member of the inhibitor of apoptosis family, in yeast chromosome segregation events Proc. Natl. Acad. Sci. USA 96 1999 13208 13213
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13208-13213
    • Yoon, H.1    Carbon, J.2
  • 184
    • 13144290928 scopus 로고    scopus 로고
    • Methylation profiles of thirty four promoter-CpG islands and concordant methylation behaviours of sixteen genes that may contribute to carcinogenesis of astrocytoma
    • Yu J., Zhang H., Gu J., Lin S., Li J., Lu W., Wang Y., and Zhu J. Methylation profiles of thirty four promoter-CpG islands and concordant methylation behaviours of sixteen genes that may contribute to carcinogenesis of astrocytoma BMC Cancer 4 2004 65
    • (2004) BMC Cancer , vol.4 , pp. 65
    • Yu, J.1    Zhang, H.2    Gu, J.3    Lin, S.4    Li, J.5    Lu, W.6    Wang, Y.7    Zhu, J.8
  • 185
    • 0345732684 scopus 로고    scopus 로고
    • IAP-antagonists exhibit non-redundant modes of action through differential DIAP1 binding
    • Zachariou A., Tenev T., Goyal L., Agapite J., Steller H., and Meier P. IAP-antagonists exhibit non-redundant modes of action through differential DIAP1 binding EMBO J. 22 2003 6642 6652
    • (2003) EMBO J. , vol.22 , pp. 6642-6652
    • Zachariou, A.1    Tenev, T.2    Goyal, L.3    Agapite, J.4    Steller, H.5    Meier, P.6
  • 187
    • 2342527764 scopus 로고    scopus 로고
    • Aberrant quantity and localization of aurora-B/AIM1 and survivin during megakarocyte polyploidization and the consequences of aurora-B/AIM1-deregulated expression
    • Zhang Y., Nagata Y., Yu G., Nguyen H.G., Jones M.R., Toselli P., Jackson C.W., Tatsuka M., Todokoro K., and Ravid K. Aberrant quantity and localization of aurora-B/AIM1 and survivin during megakarocyte polyploidization and the consequences of aurora-B/AIM1-deregulated expression Blood 103 2004 3717 3726
    • (2004) Blood , vol.103 , pp. 3717-3726
    • Zhang, Y.1    Nagata, Y.2    Yu, G.3    Nguyen, H.G.4    Jones, M.R.5    Toselli, P.6    Jackson, C.W.7    Tatsuka, M.8    Todokoro, K.9    Ravid, K.10
  • 188
    • 0034532701 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway regulates survivin degradation in a cell cycle-dependent manner
    • Zhao J., Tenev T., Martins L.M., Downward J., and Lemoine N.R. The ubiquitin-proteasome pathway regulates survivin degradation in a cell cycle-dependent manner J. Cell Sci. 113 2000 4363 4371
    • (2000) J. Cell Sci. , vol.113 , pp. 4363-4371
    • Zhao, J.1    Tenev, T.2    Martins, L.M.3    Downward, J.4    Lemoine, N.R.5
  • 189
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • Zhao M., Antunes F., Eaton J.W., and Brunk U.T. Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis Eur. J. Biochem. 270 2003 3778 3786
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3778-3786
    • Zhao, M.1    Antunes, F.2    Eaton, J.W.3    Brunk, U.T.4
  • 190
    • 9244225689 scopus 로고    scopus 로고
    • Survivin deregulation in β-tubulin mutant ovarian cancer cells underlies their compromised mitotic response to Taxol
    • Zhou J., O'Brate A., Zelnak A., and Giannakakou P. Survivin deregulation in β-tubulin mutant ovarian cancer cells underlies their compromised mitotic response to Taxol Cancer Res. 64 2004 8708 8714
    • (2004) Cancer Res. , vol.64 , pp. 8708-8714
    • Zhou, J.1    O'Brate, A.2    Zelnak, A.3    Giannakakou, P.4
  • 191
    • 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 W.G., and Findley H.W. DNA damage induces a novel p53-survivin signaling pathway regulating cell cycle and apoptosis in acute lymphoblastic leukemia cells J. Pharmacol. Exp. Ther. 303 2002 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


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