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Volumn 2, Issue 1, 2001, Pages 33-42

Apoptosis: Implications of basic research for clinical oncology

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS REGULATORY PROTEIN; BCL 2 BINDING PROTEIN, BIM; BCL-2-BINDING PROTEIN, BIM; CARRIER PROTEIN; CASPASE; HEAT SHOCK PROTEIN; MEMBRANE PROTEIN; ONCOPROTEIN;

EID: 0035240260     PISSN: 14702045     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1470-2045(00)00193-5     Document Type: Review
Times cited : (141)

References (69)
  • 1
    • 0033026714 scopus 로고    scopus 로고
    • Mechanisms of apoptosis avoidance in cancer
    • Reed J.C. Mechanisms of apoptosis avoidance in cancer. Curr Opin Oncol. 11:1999;68-75.
    • (1999) Curr Opin Oncol , vol.11 , pp. 68-75
    • Reed, J.C.1
  • 2
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F.R., Wyllie A.H., Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer. 26:1972;239-306.
    • (1972) Br J Cancer , vol.26 , pp. 239-306
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
  • 4
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates and functions during apoptosis
    • Earnshaw W.C., Martins L.M., Kaufmann S.H. Mammalian caspases: structure, activation, substrates and functions during apoptosis. Annu Rev Biochem. 68:1999;383-424.
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 5
    • 0032440288 scopus 로고    scopus 로고
    • Mechanisms and control of programmed cell death in invertebrates
    • Bergmann A., Agapite J., Steller H. Mechanisms and control of programmed cell death in invertebrates. Oncogene. 17:1998;3215-3223.
    • (1998) Oncogene , vol.17 , pp. 3215-3223
    • Bergmann, A.1    Agapite, J.2    Steller, H.3
  • 6
    • 0033119367 scopus 로고    scopus 로고
    • Genetic control of programmed cell death in the nematode Caenorhabditis elegans
    • Horvitz H.R. Genetic control of programmed cell death in the nematode Caenorhabditis elegans. Cancer Res. 59:(suppl):1999;1701s-1706s.
    • (1999) Cancer Res , vol.59 , Issue.SUPPL
    • Horvitz, H.R.1
  • 7
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H., Henzel W.J., Liu X., et al. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 90:1997;405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3
  • 9
    • 0032930312 scopus 로고    scopus 로고
    • Dr Josef Steiner cancer research prize lecture: The role of physiological cell death in neoplastic transformation and in anti-cancer therapy
    • Strasser A. Dr Josef Steiner cancer research prize lecture: the role of physiological cell death in neoplastic transformation and in anti-cancer therapy. Int J Cancer. 81:1999;505-511.
    • (1999) Int J Cancer , vol.81 , pp. 505-511
    • Strasser, A.1
  • 10
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., Reed J.C. Mitochondrial control of cell death. Nat Med. 6:2000;513-519.
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 11
    • 0034660892 scopus 로고    scopus 로고
    • The Pezcoller lecture: Cancer cell cycle revisited
    • Sherr C.J. The Pezcoller lecture: cancer cell cycle revisited. Cancer Res. 60:2000;3689-3695.
    • (2000) Cancer Res , vol.60 , pp. 3689-3695
    • Sherr, C.J.1
  • 12
    • 0033786378 scopus 로고    scopus 로고
    • Rb function in cell-cycle regulation and apoptosis
    • Harbour J.W., Dean D.C. Rb function in cell-cycle regulation and apoptosis. Nat Cell Biol. 2:2000;E65-67.
    • (2000) Nat Cell Biol , vol.2 , pp. 65-67
    • Harbour, J.W.1    Dean, D.C.2
  • 14
    • 0032575688 scopus 로고    scopus 로고
    • The bcl-2 protein family: Arbiters of cell survival
    • Adams J.M., Cory S. The bcl-2 protein family: arbiters of cell survival. Science. 281:1998;1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 15
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.1    Reed, J.C.2
  • 16
    • 0034658350 scopus 로고    scopus 로고
    • Apoptotic protease activating factor 1 (Apaf-1)-independent cell death suppression by bcl-2
    • Haraguchi M., Torii S., Matsuzawa S., et al. Apoptotic protease activating factor 1 (Apaf-1)-independent cell death suppression by bcl-2. J Exp Med. 191:2000;1709-1720.
    • (2000) J Exp Med , vol.191 , pp. 1709-1720
    • Haraguchi, M.1    Torii, S.2    Matsuzawa, S.3
  • 17
    • 0028972616 scopus 로고
    • Regulation of apoptosis by bcl-2 family proteins and its role in cancer and chemoresistance
    • Reed J.C. Regulation of apoptosis by bcl-2 family proteins and its role in cancer and chemoresistance. Curr Opin Oncol. 7:1995;541-546.
    • (1995) Curr Opin Oncol , vol.7 , pp. 541-546
    • Reed, J.C.1
  • 18
    • 0034176085 scopus 로고    scopus 로고
    • Elucidating cell signalling mechanisms using antisense technology
    • Koller E., Gaarde W.A., Monia B.P. Elucidating cell signalling mechanisms using antisense technology. Trends Pharmacol Sci. 21:2000;142-148.
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 142-148
    • Koller, E.1    Gaarde, W.A.2    Monia, B.P.3
  • 19
    • 0029871942 scopus 로고    scopus 로고
    • Bcl-2 expression in chronic lymphocytic leukemia and its correlation with the induction of apoptosis and clinical outcome
    • Robertson L.E., Plunkett W., McConnell K., et al. Bcl-2 expression in chronic lymphocytic leukemia and its correlation with the induction of apoptosis and clinical outcome. Leukemia. 10:1996;456-459.
    • (1996) Leukemia , vol.10 , pp. 456-459
    • Robertson, L.E.1    Plunkett, W.2    McConnell, K.3
  • 20
    • 0026346883 scopus 로고
    • Differential expression of the Bcl-2 proto-oncogene in neuroblastomas and other human neural tumors
    • Reed J., Meister L., Cuddy M., et al. Differential expression of the Bcl-2 proto-oncogene in neuroblastomas and other human neural tumors. Cancer Res. 5l:1991;6529-6538.
    • (1991) Cancer Res , vol.5 , pp. 6529-6538
    • Reed, J.1    Meister, L.2    Cuddy, M.3
  • 21
    • 0032863163 scopus 로고    scopus 로고
    • All along the watchtower: On the regulation of apoptosis regulators
    • Fadeel B., Zhivotovsky B., Orrenius S. All along the watchtower: on the regulation of apoptosis regulators. FASEB J. 13:1999;1647-1657.
    • (1999) FASEB J , vol.13 , pp. 1647-1657
    • Fadeel, B.1    Zhivotovsky, B.2    Orrenius, S.3
  • 22
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of bax into the outer mitochondrial membrane
    • Eskes R., Deshagher S., Antonsson B., Martinou J.C. Bid induces the oligomerization and insertion of bax into the outer mitochondrial membrane. Mol Cell Biol. 20:2000;929-935.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Deshagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 23
    • 0032574761 scopus 로고    scopus 로고
    • Bax directly induces release of cytochrome c from isolated mitochondria
    • Jurgensmeier J.M., Xie Z., Deveraux Q., et al. Bax directly induces release of cytochrome c from isolated mitochondria. Proc Natl Acad Sci USA. 5:1998;4997-5002.
    • (1998) Proc Natl Acad Sci USA , vol.5 , pp. 4997-5002
    • Jurgensmeier, J.M.1    Xie, Z.2    Deveraux, Q.3
  • 24
    • 0030838164 scopus 로고    scopus 로고
    • The caspase family of cysteine proteases
    • Thornberry N. The caspase family of cysteine proteases. Br Med Bull. 53:1997;478-790.
    • (1997) Br Med Bull , vol.53 , pp. 478-790
    • Thornberry, N.1
  • 25
    • 0033832629 scopus 로고    scopus 로고
    • Noncaspase proteases in apoptosis
    • Johnson D.E. Noncaspase proteases in apoptosis. Leukemia. 14:2000;1695-1703.
    • (2000) Leukemia , vol.14 , pp. 1695-1703
    • Johnson, D.E.1
  • 26
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins - Suppressors of apoptosis
    • Deveraux Q., Reed J.C. IAP family proteins - suppressors of apoptosis. Genes Dev. 13:1998;239-252.
    • (1998) Genes Dev , vol.13 , pp. 239-252
    • Deveraux, Q.1    Reed, J.C.2
  • 27
    • 17144438370 scopus 로고    scopus 로고
    • Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias
    • Tamm I., Kornblau S.M., Segall H., et al. Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin Cancer Res. 6:2000;1796-1803.
    • (2000) Clin Cancer Res , vol.6 , pp. 1796-1803
    • Tamm, I.1    Kornblau, S.M.2    Segall, H.3
  • 28
    • 0032478717 scopus 로고    scopus 로고
    • A single BIR domain of XIAP sufficient for inhibiting caspases
    • Takahashi R., Deveraux Q., Tamm I., et al. A single BIR domain of XIAP sufficient for inhibiting caspases. J Biol Chem. 273:1998;7787-7790.
    • (1998) J Biol Chem , vol.273 , pp. 7787-7790
    • Takahashi, R.1    Deveraux, Q.2    Tamm, I.3
  • 29
    • 0029992609 scopus 로고    scopus 로고
    • Suppression of TNF-α-induced apoptosis by NF-κB
    • Antwerp D.J., Martin S.J., Kafri T., et al. Suppression of TNF-α-induced apoptosis by NF-κB. Science. 274:1996;787-789.
    • (1996) Science , vol.274 , pp. 787-789
    • Antwerp, D.J.1    Martin, S.J.2    Kafri, T.3
  • 30
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini G., Adida C., Altieri D.C. 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.C.3
  • 31
    • 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., et al. 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
  • 32
    • 0032410818 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) and their emerging role in cancer
    • LaCasse E.C., Baird S., Korneluk R.G., MacKenzie A.E. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene. 17:1998;3247-3259.
    • (1998) Oncogene , vol.17 , pp. 3247-3259
    • Lacasse, E.C.1    Baird, S.2    Korneluk, R.G.3    MacKenzie, A.E.4
  • 33
    • 0032506524 scopus 로고    scopus 로고
    • Control of apoptosis and mitotic spindle checkpoint by survivin
    • Li F., Ambrosini G., Chu E.Y., et al. Control of apoptosis and mitotic spindle checkpoint by survivin. Nature. 396:1998;580-584.
    • (1998) Nature , vol.396 , pp. 580-584
    • Li, F.1    Ambrosini, G.2    Chu, E.Y.3
  • 34
    • 0034612594 scopus 로고    scopus 로고
    • Survivin initiates cell cycle entry by the competitive interaction with Cdk-4/p16INK4a and Cdk2/cyclin E complex activation
    • Suzuki A., Hayashida M., Ito T., et al. Survivin initiates cell cycle entry by the competitive interaction with Cdk-4/p16INK4a and Cdk2/cyclin E complex activation. Oncogene. 19:2000;3225-3234.
    • (2000) Oncogene , vol.19 , pp. 3225-3234
    • Suzuki, A.1    Hayashida, M.2    Ito, T.3
  • 35
    • 0033258321 scopus 로고    scopus 로고
    • Survivin cell-separation anxiety
    • Reed J.C. Survivin cell-separation anxiety. Nat Cell Biol. 1:1999;199-200.
    • (1999) Nat Cell Biol , vol.1 , pp. 199-200
    • Reed, J.C.1
  • 36
    • 0033258543 scopus 로고    scopus 로고
    • Pleiotropic cell-division defects and apoptosis induced by interference with survivin function
    • Li F., Ackermann E.J., Bennett C.F., et al. Pleiotropic cell-division defects and apoptosis induced by interference with survivin function. Nat Cell Biol. 1:1999;461-466.
    • (1999) Nat Cell Biol , vol.1 , pp. 461-466
    • Li, F.1    Ackermann, E.J.2    Bennett, C.F.3
  • 37
    • 0033151510 scopus 로고    scopus 로고
    • The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas
    • Dierlamm J., Baens M., Wlodarska I., et al. The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas. Blood. 93:1999;3601-3609.
    • (1999) Blood , vol.93 , pp. 3601-3609
    • Dierlamm, J.1    Baens, M.2    Wlodarska, I.3
  • 38
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Irmler M., Thome M., Hahne M., et al. Inhibition of death receptor signals by cellular FLIP. Nature. 388:1997;190-195.
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1    Thome, M.2    Hahne, M.3
  • 39
    • 0032532013 scopus 로고    scopus 로고
    • FLIP prevents apoptosis induced by death receptors but not by perforin/granzyme B, chemotherapeutic drugs, and gamma irradiation
    • Kataoka T., Schroter M., Hahne M., et al. FLIP prevents apoptosis induced by death receptors but not by perforin/granzyme B, chemotherapeutic drugs, and gamma irradiation. J Immunol. 161:1998;3936-3942.
    • (1998) J Immunol , vol.161 , pp. 3936-3942
    • Kataoka, T.1    Schroter, M.2    Hahne, M.3
  • 40
    • 18744425429 scopus 로고    scopus 로고
    • The caspase-8 inhibitor FLIP promotes activation of NF-κB and Erk signaling pathways
    • Kataoka T., Budd R.C., Holler N., et al. The caspase-8 inhibitor FLIP promotes activation of NF-κB and Erk signaling pathways. Curr Biol. 10:2000;640-648.
    • (2000) Curr Biol , vol.10 , pp. 640-648
    • Kataoka, T.1    Budd, R.C.2    Holler, N.3
  • 41
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A., Dixit V.M. Death receptors: signaling and modulation. Science. 281:1998;1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 42
    • 0032807406 scopus 로고    scopus 로고
    • The modular nature of apoptotic signaling proteins
    • Hofmann K. The modular nature of apoptotic signaling proteins. Cell Mol Life Sci. 55:1999;1113-1128.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1113-1128
    • Hofmann, K.1
  • 43
    • 0031786658 scopus 로고    scopus 로고
    • The CD95/CD95 ligand system is not the major effector in anticancer drug-mediated apoptosis
    • Tolomeo M., Dusonchet L., Meli M., et al. The CD95/CD95 ligand system is not the major effector in anticancer drug-mediated apoptosis. Cell Death Differ. 5:1998;735-742.
    • (1998) Cell Death Differ , vol.5 , pp. 735-742
    • Tolomeo, M.1    Dusonchet, L.2    Meli, M.3
  • 44
    • 0029935682 scopus 로고    scopus 로고
    • Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug induced apoptosis in leukemia cells
    • Friesen C., Herr I., Krammer P.H., Debatin K.-M. Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug induced apoptosis in leukemia cells. Nat Med. 2:1996;574-577.
    • (1996) Nat Med , vol.2 , pp. 574-577
    • Friesen, C.1    Herr, I.2    Krammer, P.H.3    Debatin, K.-M.4
  • 45
    • 0033135406 scopus 로고    scopus 로고
    • Anticancer drugs induce caspase-8/FLICE activation and apoptosis in the absence of CD95 receptor/ligand interaction
    • Wesselborg S., Engels I.H., Rossmann E., et al. Anticancer drugs induce caspase-8/FLICE activation and apoptosis in the absence of CD95 receptor/ligand interaction. Blood. 93:1999;3053-3063.
    • (1999) Blood , vol.93 , pp. 3053-3063
    • Wesselborg, S.1    Engels, I.H.2    Rossmann, E.3
  • 46
    • 0034699353 scopus 로고    scopus 로고
    • Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis
    • Engels I.H., Stepczynska A., Stroh C., et al. Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis. Oncogene. 19:2000;4563-4573.
    • (2000) Oncogene , vol.19 , pp. 4563-4573
    • Engels, I.H.1    Stepczynska, A.2    Stroh, C.3
  • 48
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
    • Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J Biol Chem. 271:1996;12687-12690.
    • (1996) J Biol Chem , vol.271 , pp. 12687-12690
    • Pitti, R.M.1    Marsters, S.A.2    Ruppert, S.3    Donahue, C.J.4    Moore, A.5    Ashkenazi, A.6
  • 49
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley S.R., Schooley K., Smolak P.J., et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity. 3:1995;673-682.
    • (1995) Immunity , vol.3 , pp. 673-682
    • Wiley, S.R.1    Schooley, K.2    Smolak, P.J.3
  • 50
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak H., Miller R.E., Ariail K., et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med. 5:1999;157-163.
    • (1999) Nat Med , vol.5 , pp. 157-163
    • Walczak, H.1    Miller, R.E.2    Ariail, K.3
  • 51
    • 0032713075 scopus 로고    scopus 로고
    • Safety and antitumor activityof recombinant soluble Apo2 ligand
    • Ashkenazi A., Pai R.C., Fong S., et al. Safety and antitumor activityof recombinant soluble Apo2 ligand. J Clin Invest. 104:1999;155-162.
    • (1999) J Clin Invest , vol.104 , pp. 155-162
    • Ashkenazi, A.1    Pai, R.C.2    Fong, S.3
  • 52
    • 0034022160 scopus 로고    scopus 로고
    • Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand
    • Jo M., Kim T.-H., Seoul D.-W., et al. Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand. Nat Med. 6:2000;564-567.
    • (2000) Nat Med , vol.6 , pp. 564-567
    • Jo, M.1    Kim, T.-H.2    Seoul, D.-W.3
  • 53
    • 0034026719 scopus 로고    scopus 로고
    • Steering anti-cancer drugs away from the TRAIL
    • Nagata S. Steering anti-cancer drugs away from the TRAIL. Nat Med. 6:2000;502-503.
    • (2000) Nat Med , vol.6 , pp. 502-503
    • Nagata, S.1
  • 54
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jaattela M. Escaping cell death: survival proteins in cancer. Exp Cell Res. 248:1999;30-43.
    • (1999) Exp Cell Res , vol.248 , pp. 30-43
    • Jaattela, M.1
  • 55
    • 0026703222 scopus 로고
    • Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity
    • Jaattela M., Wissing D., Bauer P.A., Li G.C. Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity. EMBO J. 11:1992;3507-3512.
    • (1992) EMBO J , vol.11 , pp. 3507-3512
    • Jaattela, M.1    Wissing, D.2    Bauer, P.A.3    Li, G.C.4
  • 56
    • 0029586916 scopus 로고
    • Expression of the heat shock protein HSP27 in human ovarian cancer
    • Langdon S.P., Rabiasz G.J., Hirst G.L., et al. Expression of the heat shock protein HSP27 in human ovarian cancer. Clin Cancer Res. 1:1995;1603-1609.
    • (1995) Clin Cancer Res , vol.1 , pp. 1603-1609
    • Langdon, S.P.1    Rabiasz, G.J.2    Hirst, G.L.3
  • 57
    • 0030902367 scopus 로고    scopus 로고
    • Overexpression of resistance-related proteins (metallothioneins, glutathione-S-transferase pi, heat shock protein 27, and lung resistance-related protein) in osteosarcoma. Relationship with poor prognosis
    • Uozaki H., Horiuchi H., Ishida T., et al. Overexpression of resistance-related proteins (metallothioneins, glutathione-S-transferase pi, heat shock protein 27, and lung resistance-related protein) in osteosarcoma. Relationship with poor prognosis. Cancer. 79:1997;2336-2344.
    • (1997) Cancer , vol.79 , pp. 2336-2344
    • Uozaki, H.1    Horiuchi, H.2    Ishida, T.3
  • 58
    • 0021821903 scopus 로고
    • Involvement of the bcl-2 gene in human follicular lymphoma
    • Tsujimoto Y., Cossman J., Croce C. Involvement of the bcl-2 gene in human follicular lymphoma. Science. 228:1985;1440-1443.
    • (1985) Science , vol.228 , pp. 1440-1443
    • Tsujimoto, Y.1    Cossman, J.2    Croce, C.3
  • 59
    • 0027164144 scopus 로고
    • High expression of bcl-2-protein in acute myeloid leukemia is associated with poor response to chemotherapy
    • Campos L., Rouault J.P., Sabido O., et al. High expression of bcl-2-protein in acute myeloid leukemia is associated with poor response to chemotherapy. Blood. 81:1993;3091-3096.
    • (1993) Blood , vol.81 , pp. 3091-3096
    • Campos, L.1    Rouault, J.P.2    Sabido, O.3
  • 60
    • 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 J.S., Webb A., Cunningham D., et al. Phase I clinical and pharmacokinetic study of bcl-2 antisense oligonucleotide therapy in patients with non-Hodgkin's lymphoma. J Clin Oncol. 18:2000;1812-1823.
    • (2000) J Clin Oncol , vol.18 , pp. 1812-1823
    • Waters, J.S.1    Webb, A.2    Cunningham, D.3
  • 61
    • 0032523945 scopus 로고    scopus 로고
    • Modulation of bcl-2 protein levels by an intracellular anti-bcl-2 single-chain antibody increases drug-induced cytotoxicity in the breast cancer cell line MCF-7
    • Piche A., Grim J., Rancourt C., Gomez-Navarro J., Reed J.C., Curiel D.T. Modulation of bcl-2 protein levels by an intracellular anti-bcl-2 single-chain antibody increases drug-induced cytotoxicity in the breast cancer cell line MCF-7. Cancer Res. 58:1998;2134-2140.
    • (1998) Cancer Res , vol.58 , pp. 2134-2140
    • Piche, A.1    Grim, J.2    Rancourt, C.3    Gomez-Navarro, J.4    Reed, J.C.5    Curiel, D.T.6
  • 62
    • 0032817236 scopus 로고    scopus 로고
    • A recombinant defective adenoviral agent expressing anti-bcl-2 ribozyme promotes apoptosis of bcl-2-expressing human prostate cancer cells
    • Dorai T., Perlman H., Walsh K., et al. A recombinant defective adenoviral agent expressing anti-bcl-2 ribozyme promotes apoptosis of bcl-2-expressing human prostate cancer cells. Int J Cancer. 82:1999;846-852.
    • (1999) Int J Cancer , vol.82 , pp. 846-852
    • Dorai, T.1    Perlman, H.2    Walsh, K.3
  • 63
    • 0030964037 scopus 로고    scopus 로고
    • ICE-protease inhibitors block murine liver injury and apoptosis caused by CD95 or by TNF-α
    • Kunstle G., Leist M., Uhlig S., et al. ICE-protease inhibitors block murine liver injury and apoptosis caused by CD95 or by TNF-α Immunol Lett. 55:1997;5-10.
    • (1997) Immunol Lett , vol.55 , pp. 5-10
    • Kunstle, G.1    Leist, M.2    Uhlig, S.3
  • 64
    • 0031782909 scopus 로고    scopus 로고
    • TRAIL: A molecule with multiplereceptors and control mechanisms
    • Griffith T.S., Lynch D.H. TRAIL: a molecule with multiplereceptors and control mechanisms. Curr Opin Immunol. 10:1998;559-563.
    • (1998) Curr Opin Immunol , vol.10 , pp. 559-563
    • Griffith, T.S.1    Lynch, D.H.2
  • 65
    • 0031815071 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM
    • Vucic D., Kaiser W.J., Miller L.K. Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM. Mol Cell Biol. 18:1998;3300-3309.
    • (1998) Mol Cell Biol , vol.18 , pp. 3300-3309
    • Vucic, D.1    Kaiser, W.J.2    Miller, L.K.3
  • 66
    • 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. 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
  • 67
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai J., Du C., Wu J.-W., Kyin S., Wang X., Shi Y. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature. 406:2000;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
  • 68
    • 0032905030 scopus 로고    scopus 로고
    • Control of inducible chemoresistance: Enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-kappaB
    • Wang C.Y., Cusack J.C., Liu R., Baldwin A.S. Control of inducible chemoresistance: enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-kappaB. Nat Med. 5:1999;412-417.
    • (1999) Nat Med , vol.5 , pp. 412-417
    • Wang, C.Y.1    Cusack, J.C.2    Liu, R.3    Baldwin, A.S.4
  • 69
    • 9544244796 scopus 로고    scopus 로고
    • Retrovirus-mediated wild-type p53 gene transfer to tumors of patients with lung cancer
    • Roth J.A., Nguyen D., Lawrence D.D., et al. Retrovirus-mediated wild-type p53 gene transfer to tumors of patients with lung cancer. Nat Med. 2:1996;985-991.
    • (1996) Nat Med , vol.2 , pp. 985-991
    • Roth, J.A.1    Nguyen, D.2    Lawrence, D.D.3


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