메뉴 건너뛰기




Volumn 4, Issue 12, 2003, Pages 721-729

Anticancer therapy targeting the apoptotic pathway

Author keywords

[No Author keywords available]

Indexed keywords

AAG 17; ADAPTOR PROTEIN; ADVEXIN; ANTINEOPLASTIC AGENT; BORTEZOMIB; CANFOSFAMIDE; CASPASE; DOCETAXEL; FAS LIGAND; GEFITINIB; GLUTATHIONE DERIVATIVE; HEAT SHOCK PROTEIN 70; IMATINIB; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MONOCLONAL ANTIBODY; NEW DRUG; OBLIMERSEN; ONYX 015; PLATINUM DERIVATIVE; PROTEASOME INHIBITOR; PROTEIN BCL 2; PROTEIN FARNESYLTRANSFERASE INHIBITOR; PROTEIN INHIBITOR; PROTEIN P53; SURVIVIN; TAXANE DERIVATIVE; TIPIFARNIB; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 0346873049     PISSN: 14702045     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1470-2045(03)01277-4     Document Type: Review
Times cited : (476)

References (98)
  • 1
    • 0036910734 scopus 로고    scopus 로고
    • Programmed cell death: Many ways for cells to die decently
    • Jaattela M. Programmed cell death: many ways for cells to die decently. Ann Med 2002; 34: 480-88.
    • (2002) Ann. Med. , vol.34 , pp. 480-488
    • Jaattela, M.1
  • 2
    • 0036463649 scopus 로고    scopus 로고
    • Apoptosis-based therapies
    • Reed JC. Apoptosis-based therapies. Nat Rev Drug Discov 2002; 1: 111-21.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 111-121
    • Reed, J.C.1
  • 3
    • 0034523818 scopus 로고    scopus 로고
    • Proapoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer SJ, Wei MC, Saito M, et al. Proapoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ 2000; 7: 1166-73.
    • (2000) Cell Death Differ. , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3
  • 4
    • 0033582526 scopus 로고    scopus 로고
    • Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis
    • Sun XM, MacFarlane M, Zhuang J, et al. Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis. J Biol Chem 1999; 274: 5053-60.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5053-5060
    • Sun, X.M.1    MacFarlane, M.2    Zhuang, J.3
  • 5
    • 0034278085 scopus 로고    scopus 로고
    • The IAP family: Endogenous caspase inhibitors with multiple biological activities
    • Yang YL, Li XM. The IAP family: endogenous caspase inhibitors with multiple biological activities. Cell Res 2000; 10: 169-77.
    • (2000) Cell Res. , vol.10 , pp. 169-177
    • Yang, Y.L.1    Li, X.M.2
  • 6
    • 0036449793 scopus 로고    scopus 로고
    • Current status of the molecular mechanisms of anticancer drug-induced apoptosis: The contribution of molecular-level analysis to cancer chemotherapy
    • Kim R, Tanabe K, Uchida Y, et al. Current status of the molecular mechanisms of anticancer drug-induced apoptosis: the contribution of molecular-level analysis to cancer chemotherapy. Cancer Chemother Pharmacol 2002; 50: 343-52.
    • (2002) Cancer Chemother. Pharmacol. , vol.50 , pp. 343-352
    • Kim, R.1    Tanabe, K.2    Uchida, Y.3
  • 7
    • 0035930905 scopus 로고    scopus 로고
    • Alternative splicing variants of c-FLIP transduce the differential signal through the Raf or TRAF2 in TNF-induced cell proliferation
    • Park SJ, Kim YY, Ju JW, et al. Alternative splicing variants of c-FLIP transduce the differential signal through the Raf or TRAF2 in TNF-induced cell proliferation. Biochem Biophys Res Commun 2001; 289: 1205-10.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 1205-1210
    • Park, S.J.1    Kim, Y.Y.2    Ju, J.W.3
  • 8
  • 9
    • 0037274017 scopus 로고    scopus 로고
    • Signaling and transcriptional control of Fas ligand gene expression
    • Kavurma MM, Khachigian LM. Signaling and transcriptional control of Fas ligand gene expression. Cell Death Differ 2003; 10: 36-44.
    • (2003) Cell Death Differ. , vol.10 , pp. 36-44
    • Kavurma, M.M.1    Khachigian, L.M.2
  • 10
    • 0037273848 scopus 로고    scopus 로고
    • Apo2L/TRAIL and its death and decoy receptors
    • LeBlanc HN, Ashkenazi A. Apo2L/TRAIL and its death and decoy receptors. Cell Death Differ 2003; 10: 66-75.
    • (2003) Cell Death Differ. , vol.10 , pp. 66-75
    • LeBlanc, H.N.1    Ashkenazi, A.2
  • 11
    • 17944379442 scopus 로고    scopus 로고
    • CD95 and TRAIL receptor-mediated activation of protein kinase C and NF-kappaB contributes to apoptosis resistance in ductal pancreatic adenocarcinoma cells
    • Trauzold A, Wermann H, Arlt A, et al. CD95 and TRAIL receptor-mediated activation of protein kinase C and NF-kappaB contributes to apoptosis resistance in ductal pancreatic adenocarcinoma cells. Oncogene 2001; 20: 4258-69.
    • (2001) Oncogene , vol.20 , pp. 4258-4269
    • Trauzold, A.1    Wermann, H.2    Arlt, A.3
  • 13
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams JM, Cory S. The Bcl-2 protein family: arbiters of cell survival. Science 1998; 281: 1322-26.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 14
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91: 479-89.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 15
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature 2000; 407: 770-76.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 16
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 1997; 275: 1132-36.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 17
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH, et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001; 292: 727-30.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 18
    • 0030614915 scopus 로고    scopus 로고
    • Structure of Bcl-xL-Bak peptide complex: Recognition between regulators of apoptosis
    • Sattler M, Liang H, Nettesheim D, et al. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 1997; 275: 983-86.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3
  • 19
    • 9044225527 scopus 로고    scopus 로고
    • BCL2 family proteins: Regulators of cell death involved in the pathogenesis of cancer and resistance to therapy
    • Reed JC, Miyashita T, Takayama S, et al. BCL2 family proteins: regulators of cell death involved in the pathogenesis of cancer and resistance to therapy. J Cell Biochem 1996; 60: 23-32.
    • (1996) J. Cell Biochem. , vol.60 , pp. 23-32
    • Reed, J.C.1    Miyashita, T.2    Takayama, S.3
  • 20
    • 0033616709 scopus 로고    scopus 로고
    • Deletion of the loop region of Bcl-2 completely blocks paclitaxel-induced apoptosis
    • Srivastava RK, Mi QS, Hardwick JM, Longo DL. Deletion of the loop region of Bcl-2 completely blocks paclitaxel-induced apoptosis. Proc Natl Acad Sci USA 1999; 96: 3775-80.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3775-3780
    • Srivastava, R.K.1    Mi, Q.S.2    Hardwick, J.M.3    Longo, D.L.4
  • 21
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T, Reed JC. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 1995; 80: 293-99.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 22
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM, Korsmeyer SJ. BCL-2 family members and the mitochondria in apoptosis. Genes Dev 1999; 13: 1899-911.
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 23
    • 85047696563 scopus 로고    scopus 로고
    • Regulation of the mitochondrial checkpoint in p53-mediated apoptosis confers resistance to cell death
    • Henry H, Thomas A, Shen Y, White E. Regulation of the mitochondrial checkpoint in p53-mediated apoptosis confers resistance to cell death. Oncogene 2002; 21: 748-60.
    • (2002) Oncogene , vol.21 , pp. 748-760
    • Henry, H.1    Thomas, A.2    Shen, Y.3    White, E.4
  • 24
    • 0037372013 scopus 로고    scopus 로고
    • Apoptosis and melanoma: Molecular mechanisms
    • Hussein MR, Haemel AK, Wood GS. Apoptosis and melanoma: molecular mechanisms. J Pathol 2003; 199: 275-88.
    • (2003) J. Pathol. , vol.199 , pp. 275-288
    • Hussein, M.R.1    Haemel, A.K.2    Wood, G.S.3
  • 25
    • 0037377269 scopus 로고    scopus 로고
    • The p53 tumor suppressor gene and nuclear protein: Basic science review and relevance in the management of bladder cancer
    • Smith ND, Rubenstein JN, Eggener SE, Kozlowski JM. The p53 tumor suppressor gene and nuclear protein: basic science review and relevance in the management of bladder cancer. J Urol 2003; 169: 1219-28.
    • (2003) J. Urol. , vol.169 , pp. 1219-1228
    • Smith, N.D.1    Rubenstein, J.N.2    Eggener, S.E.3    Kozlowski, J.M.4
  • 26
    • 0037131519 scopus 로고    scopus 로고
    • Dueling activities of AIF in cell death versus survival: DNA binding and redox activity
    • Lipton SA, Bossy-Wetzel E. Dueling activities of AIF in cell death versus survival: DNA binding and redox activity. Cell 2002; 111: 147-50.
    • (2002) Cell , vol.111 , pp. 147-150
    • Lipton, S.A.1    Bossy-Wetzel, E.2
  • 27
    • 0033215040 scopus 로고    scopus 로고
    • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    • Deveraux QL, Leo E, Stennicke HR, et al. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. Embo J 1999; 18: 5242-51.
    • (1999) Embo J. , vol.18 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicke, H.R.3
  • 28
    • 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, et al. IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. Embo J 1998; 17: 2215-23.
    • (1998) Embo J. , vol.17 , pp. 2215-2223
    • Deveraux, Q.L.1    Roy, N.2    Stennicke, H.R.3
  • 29
    • 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, et al. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. Embo J 1997; 16: 6914-25.
    • (1997) Embo J. , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3
  • 30
    • 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, 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: 131-46.
    • (2002) Drug Resist. Updat. , vol.5 , pp. 131-146
    • Cheng, J.Q.1    Jiang, X.2    Fraser, M.3
  • 31
    • 0034905394 scopus 로고    scopus 로고
    • XIAP: Apoptotic brake and promising therapeutic target
    • Holcik M, Gibson H, Korneluk RG. XIAP: apoptotic brake and promising therapeutic target. Apoptosis 2001; 6: 253-61.
    • (2001) Apoptosis , vol.6 , pp. 253-261
    • Holcik, M.1    Gibson, H.2    Korneluk, R.G.3
  • 32
    • 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, 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: 445-54.
    • (2002) J. Biol. Chem. , vol.277 , pp. 445-454
    • Verhagen, A.M.1    Silke, J.2    Ekert, P.G.3
  • 33
    • 0032506524 scopus 로고    scopus 로고
    • Control of apoptosis and mitotic spindle checkpoint by survivin
    • Li F, Ambrosini G, Chu EY, et al. Control of apoptosis and mitotic spindle checkpoint by survivin. Nature 1998; 396: 580-84.
    • (1998) Nature , vol.396 , pp. 580-584
    • Li, F.1    Ambrosini, G.2    Chu, E.Y.3
  • 34
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini G, Adida C, Altieri DC. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997; 3: 917-21.
    • (1997) Nat. Med. , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.C.3
  • 35
    • 0035738740 scopus 로고    scopus 로고
    • The role of survivin as a new target of diagnosis and treatment in human cancer
    • Yamamoto T, Tanigawa N. The role of survivin as a new target of diagnosis and treatment in human cancer. Med Electron Microsc 2001; 34: 207-12.
    • (2001) Med. Electron Microsc. , vol.34 , pp. 207-212
    • Yamamoto, T.1    Tanigawa, N.2
  • 36
    • 0036358584 scopus 로고    scopus 로고
    • Survivin: Anti-apoptosis protein and a prognostic marker for tumor progression and recurrence
    • 123
    • Sela B. Survivin: anti-apoptosis protein and a prognostic marker for tumor progression and recurrence. Harefuah 2002; 141: 103-07, 123.
    • (2002) Harefuah , vol.141 , pp. 103-107
    • Sela, B.1
  • 37
    • 0037414775 scopus 로고    scopus 로고
    • Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells
    • Chen J, Jin S, Tahir SK, et al. Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells. J Biol Chem 2003; 278: 486-90.
    • (2003) J. Biol. Chem. , vol.278 , pp. 486-490
    • Chen, J.1    Jin, S.2    Tahir, S.K.3
  • 38
    • 0034885358 scopus 로고    scopus 로고
    • New insights into the role of nuclear factor-kappaB in cell growth regulation
    • Chen F, Castranova V, Shi X. New insights into the role of nuclear factor-kappaB in cell growth regulation. Am J Pathol 2001; 159: 387-97.
    • (2001) Am. J. Pathol. , vol.159 , pp. 387-397
    • Chen, F.1    Castranova, V.2    Shi, X.3
  • 39
    • 0035437171 scopus 로고    scopus 로고
    • TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: Therapeutic applications
    • Mitsiades CS, Treon SP, Mitsiades N, et al. TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: therapeutic applications. Blood 2001; 98: 795-804.
    • (2001) Blood , vol.98 , pp. 795-804
    • Mitsiades, C.S.1    Treon, S.P.2    Mitsiades, N.3
  • 41
    • 0033944777 scopus 로고    scopus 로고
    • Heat shock proteins-modulators of apoptosis in tumour cells
    • Creagh EM, Sheehan D, Cotter TG. Heat shock proteins-modulators of apoptosis in tumour cells. Leukemia 2000; 14: 1161-73.
    • (2000) Leukemia , vol.14 , pp. 1161-1173
    • Creagh, E.M.1    Sheehan, D.2    Cotter, T.G.3
  • 42
    • 0033830374 scopus 로고    scopus 로고
    • The chaperone function of hsp70 is required for protection against stress-induced apoptosis
    • Mosser DD, Caron AW, Bourget L, et al. The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol Cell Biol 2000; 20: 7146-59.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7146-7159
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3
  • 43
    • 0034253474 scopus 로고    scopus 로고
    • Negative regulation of the Apaf-1 apoptosome by Hsp70
    • Saleh A, Srinivasula SM, Balkir L, et al. Negative regulation of the Apaf-1 apoptosome by Hsp70. Nat Cell Biol 2000; 2: 476-83.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 476-483
    • Saleh, A.1    Srinivasula, S.M.2    Balkir, L.3
  • 44
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM, Wolf BB, Cain K, et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2000; 2: 469-75.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3
  • 45
    • 0026779422 scopus 로고
    • Interaction of heat-shock protein 70 with p53 translated in vitro: Evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation
    • Hainaut P, Milner J. Interaction of heat-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation. Embo J 1992; 11: 3513-20.
    • (1992) Embo J. , vol.11 , pp. 3513-3520
    • Hainaut, P.1    Milner, J.2
  • 46
    • 0025966492 scopus 로고
    • Nuclear colocalization of cellular and viral myc proteins with HSP70 in myc-overexpressing cells
    • Koskinen PJ, Sistonen L, Evan G, Morimoto R, Alitalo K. Nuclear colocalization of cellular and viral myc proteins with HSP70 in myc-overexpressing cells. J Virol 1991; 65: 842-51.
    • (1991) J. Virol. , vol.65 , pp. 842-851
    • Koskinen, P.J.1    Sistonen, L.2    Evan, G.3    Morimoto, R.4    Alitalo, K.5
  • 47
    • 0030871891 scopus 로고    scopus 로고
    • BAG1 modulates the chaperone activity of Hsp70/Hsc70
    • Takayama S, Bimston DN, Matsuzawa S, et al. BAG1 modulates the chaperone activity of Hsp70/Hsc70. Embo J 1997; 16: 4887-96.
    • (1997) Embo J. , vol.16 , pp. 4887-4896
    • Takayama, S.1    Bimston, D.N.2    Matsuzawa, S.3
  • 48
    • 17944366977 scopus 로고    scopus 로고
    • Heat-shock protein 70 antagonizes apoptosis-inducing factor
    • Ravagnan L, Gurbuxani S, Susin SA, et al. Heat-shock protein 70 antagonizes apoptosis-inducing factor. Nat Cell Biol 2001; 3: 839-43.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 839-843
    • Ravagnan, L.1    Gurbuxani, S.2    Susin, S.A.3
  • 49
    • 0242496212 scopus 로고    scopus 로고
    • Molecular sequelae of proteasome inhibition in human multiple myeloma cells
    • Mitsiades N, Mitsiades CS, Poulaki V, et al. Molecular sequelae of proteasome inhibition in human multiple myeloma cells. Proc Natl Acad Sci USA 2002; 99: 14374-79.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14374-14379
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 50
    • 0142213549 scopus 로고    scopus 로고
    • Proteomic identification of Heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor
    • In press
    • Hu W, Wu WG, Chen L, et al. Proteomic identification of Heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor. Proteomics 2003; in press.
    • (2003) Proteomics
    • Hu, W.1    Wu, W.G.2    Chen, L.3
  • 51
    • 0033636080 scopus 로고    scopus 로고
    • A new method of antitumor therapy with a high dose of TNF perfusion for unresectable liver tumors
    • Nakamoto T, Inagawa H, Takagi K, Soma G. A new method of antitumor therapy with a high dose of TNF perfusion for unresectable liver tumors. Anticancer Res 2000; 20: 4087-96.
    • (2000) Anticancer Res. , vol.20 , pp. 4087-4096
    • Nakamoto, T.1    Inagawa, H.2    Takagi, K.3    Soma, G.4
  • 52
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak H, Miller RE, Ariail K, et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med 1999; 5: 157-63.
    • (1999) Nat. Med. , vol.5 , pp. 157-163
    • Walczak, H.1    Miller, R.E.2    Ariail, K.3
  • 53
    • 0032693143 scopus 로고    scopus 로고
    • Apoptosis regulating proteins as targets of therapy for haematological malignancies
    • Kornblau SM, Konopleva M, Andreeff M. Apoptosis regulating proteins as targets of therapy for haematological malignancies. Expert Opin Investig Drugs 1999; 8: 2027-57.
    • (1999) Expert. Opin. Investig. Drugs , vol.8 , pp. 2027-2057
    • Kornblau, S.M.1    Konopleva, M.2    Andreeff, M.3
  • 54
    • 0035216008 scopus 로고    scopus 로고
    • TRAIL/Apo-2L: Mechanisms and clinical applications in cancer
    • Srivastava RK. TRAIL/Apo-2L: mechanisms and clinical applications in cancer. Neoplasia 2001; 3: 535-46.
    • (2001) Neoplasia , vol.3 , pp. 535-546
    • Srivastava, R.K.1
  • 56
    • 0035866369 scopus 로고    scopus 로고
    • Anticancer agents sensitize tumor cells to tumor necrosis factor-related apoptosis-inducing ligand-mediated caspase-8 activation and apoptosis
    • Lacour S, Hammann A, Wotawa A, et al. Anticancer agents sensitize tumor cells to tumor necrosis factor-related apoptosis-inducing ligand-mediated caspase-8 activation and apoptosis. Cancer Res 2001; 61: 1645-51.
    • (2001) Cancer Res. , vol.61 , pp. 1645-1651
    • Lacour, S.1    Hammann, A.2    Wotawa, A.3
  • 57
    • 0037118590 scopus 로고    scopus 로고
    • Enhanced tumor killing by Apo2L/TRAIL and CPT-11 co-treatment is associated with p21 cleavage and differential regulation of Apo2L/TRAIL ligand and its receptors
    • Xiang H, Fox JA, Totpal K, et al. Enhanced tumor killing by Apo2L/TRAIL and CPT-11 co-treatment is associated with p21 cleavage and differential regulation of Apo2L/TRAIL ligand and its receptors. Oncogene 2002; 21: 3611-19.
    • (2002) Oncogene , vol.21 , pp. 3611-3619
    • Xiang, H.1    Fox, J.A.2    Totpal, K.3
  • 58
    • 0034022160 scopus 로고    scopus 로고
    • Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand
    • Jo M, Kim TH, Seol DW, et al. Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand. Nat Med 2000; 6: 564-67.
    • (2000) Nat. Med. , vol.6 , pp. 564-567
    • Jo, M.1    Kim, T.H.2    Seol, D.W.3
  • 59
    • 0036234117 scopus 로고    scopus 로고
    • Inhibition of bcl-2 as cancer therapy
    • Ciardiello F, Tortora G. Inhibition of bcl-2 as cancer therapy. Ann Oncol 2002; 13: 501-02.
    • (2002) Ann. Oncol. , vol.13 , pp. 501-502
    • Ciardiello, F.1    Tortora, G.2
  • 60
    • 0034794290 scopus 로고    scopus 로고
    • Preliminary phase I results of G3139 (bcl-2 antisense oligonucleoticle) therapy in combination with docetaxel in hormone-refractory prostate cancer
    • Tolcher AW. Preliminary phase I results of G3139 (bcl-2 antisense oligonucleoticle) therapy in combination with docetaxel in hormone-refractory prostate cancer. Semin Oncol 2001; 28 (4 suppl 15): 67-70.
    • (2001) Semin. Oncol. , vol.28 , Issue.4 SUPPL. 15 , pp. 67-70
    • Tolcher, A.W.1
  • 61
    • 0035869667 scopus 로고    scopus 로고
    • Synergistic chemosensitization and inhibition of progression to androgen independence by antisense Bcl-2 oligodeoxynucleotide and paclitaxel in the LNCaP prostate tumor model
    • Leung S, Miyake H, Zellweger T, et al. Synergistic chemosensitization and inhibition of progression to androgen independence by antisense Bcl-2 oligodeoxynucleotide and paclitaxel in the LNCaP prostate tumor model. Int J Cancer 2001; 91: 846-50.
    • (2001) Int. J. Cancer , vol.91 , pp. 846-850
    • Leung, S.1    Miyake, H.2    Zellweger, T.3
  • 62
    • 0036303535 scopus 로고    scopus 로고
    • Phase I trial of BCL-2 antisense oligonucleotide (G3139) administered by continuous intravenous infusion in patients with advanced cancer
    • Morris MJ, Tong WP, Cordon-Cardo C, et al. Phase I trial of BCL-2 antisense oligonucleotide (G3139) administered by continuous intravenous infusion in patients with advanced cancer. Clin Cancer Res 2002; 8: 679-83.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 679-683
    • Morris, M.J.1    Tong, W.P.2    Cordon-Cardo, C.3
  • 63
    • 0036236808 scopus 로고    scopus 로고
    • A pilot trial of G3139, a bcl-2 antisense oligonucleotide, and paclitaxel in patients with chemorefractory small-cell lung cancer
    • Rudin CM, Otterson GA, Mauer AM, et al. A pilot trial of G3139, a bcl-2 antisense oligonucleotide, and paclitaxel in patients with chemorefractory small-cell lung cancer. Ann Oncol 2002; 13: 539-45.
    • (2002) Ann. Oncol. , vol.13 , pp. 539-545
    • Rudin, C.M.1    Otterson, G.A.2    Mauer, A.M.3
  • 64
    • 0034015672 scopus 로고    scopus 로고
    • Phase I clinical and pharmacokinetic study of bcl-2 antisense oligonucleotide therapy in patients with non-Hodgkins lymphoma
    • Waters JS, Webb A, Cunningham D, et al. Phase I clinical and pharmacokinetic study of bcl-2 antisense oligonucleotide therapy in patients with non-Hodgkins lymphoma. J Clin Oncol 2000; 18: 1812-23.
    • (2000) J. Clin. Oncol. , vol.18 , pp. 1812-1823
    • Waters, J.S.1    Webb, A.2    Cunningham, D.3
  • 65
    • 0029863194 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of latent alkylating agents activated by glutathione S-transferase
    • Satyam A, Hocker MD, Kane-Maguire KA, et al. Design, synthesis, and evaluation of latent alkylating agents activated by glutathione S-transferase. J Med Chem 1996; 39: 1736-47.
    • (1996) J. Med. Chem. , vol.39 , pp. 1736-1747
    • Satyam, A.1    Hocker, M.D.2    Kane-Maguire, K.A.3
  • 66
    • 0033917834 scopus 로고    scopus 로고
    • Cellular response to a glutathione S-transferase P1-1 activated prodrug
    • Rosario LA, O'Brien ML, Henderson CJ, et al. Cellular response to a glutathione S-transferase P1-1 activated prodrug. Mol Pharmacol 2000; 58: 167-74.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 167-174
    • Rosario, L.A.1    O'Brien, M.L.2    Henderson, C.J.3
  • 67
    • 0031011245 scopus 로고    scopus 로고
    • Activity of TER286 against human tumor colony-forming units
    • Izbicka E, Lawrence R, Cerna C, et al. Activity of TER286 against human tumor colony-forming units. Anticancer Drugs 1997; 8: 345-48.
    • (1997) Anticancer Drugs , vol.8 , pp. 345-348
    • Izbicka, E.1    Lawrence, R.2    Cerna, C.3
  • 68
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell 2000; 103: 239-52.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 69
    • 0035212589 scopus 로고    scopus 로고
    • The ups and downs of MEK kinase interactions
    • Hagemann C, Blank JL. The ups and downs of MEK kinase interactions. Cell Signal 2001; 13: 863-75.
    • (2001) Cell Signal , vol.13 , pp. 863-875
    • Hagemann, C.1    Blank, J.L.2
  • 70
    • 0347293099 scopus 로고    scopus 로고
    • Phase 2 study of TLK 286 (GST p1-1 activated glutathione analog) in patients with platinum and paclitaxel refractory/resistant advanced epithelial ovarian cancer
    • (abstr)
    • Kavanagh J, Kudelka, AP, Spriggs DR, et al. Phase 2 study of TLK 286 (GST p1-1 activated glutathione analog) in patients with platinum and paclitaxel refractory/resistant advanced epithelial ovarian cancer. ASCO 2002; 831 (abstr).
    • (2002) ASCO , pp. 831
    • Kavanagh, J.1    Kudelka, A.P.2    Spriggs, D.R.3
  • 71
    • 0036735298 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model
    • LeBlanc R, Catley LP, Hideshima T, et al. Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model. Cancer Res 2002; 62: 4996-5000.
    • (2002) Cancer Res. , vol.62 , pp. 4996-5000
    • LeBlanc, R.1    Catley, L.P.2    Hideshima, T.3
  • 72
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: A novel class of potent and effective antitumor agents
    • Adams J, Palombella VJ, Sausville EA, et al. Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Res 1999; 59: 2615-22.
    • (1999) Cancer Res. , vol.59 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 73
    • 0036181371 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor PS-341
    • Adams J. Development of the proteasome inhibitor PS-341. Oncologist 2002; 7: 9-16.
    • (2002) Oncologist , vol.7 , pp. 9-16
    • Adams, J.1
  • 74
    • 0037252480 scopus 로고    scopus 로고
    • High-dose therapy and immunomodulatory drugs in multiple myeloma
    • Barlogie B, Shaughnessy J, Zangari M, Tricot G. High-dose therapy and immunomodulatory drugs in multiple myeloma. Semin Oncol 2002; 29 (6 Suppl 17): 26-33.
    • (2002) Semin. Oncol. , vol.29 , Issue.6 SUPPL. 17 , pp. 26-33
    • Barlogie, B.1    Shaughnessy, J.2    Zangari, M.3    Tricot, G.4
  • 75
    • 0036217332 scopus 로고    scopus 로고
    • Proteasome inhibition: A novel approach to cancer therapy
    • Adams J. Proteasome inhibition: a novel approach to cancer therapy. Trends Mol Med 2002; 8 (4 Suppl): S49-54.
    • (2002) Trends Mol. Med. , vol.8 , Issue.4 SUPPL.
    • Adams, J.1
  • 76
    • 18344412545 scopus 로고    scopus 로고
    • Update on the proteasome inhibitor PS341
    • L'Allemain G. Update on the proteasome inhibitor PS341. Bull Cancer 2002; 89: 29-30.
    • (2002) Bull. Cancer , vol.89 , pp. 29-30
    • L'Allemain, G.1
  • 77
    • 0035215395 scopus 로고    scopus 로고
    • Proteasome inhibition in cancer: Development of PS-341
    • Adams J. Proteasome inhibition in cancer: development of PS-341. Semin Oncol 2001; 28: 613-19.
    • (2001) Semin. Oncol. , vol.28 , pp. 613-619
    • Adams, J.1
  • 78
    • 0035736099 scopus 로고    scopus 로고
    • The proteasome: A new target for novel drug therapies
    • Elliott PJ, Ross JS. The proteasome: a new target for novel drug therapies. Am J Clin Pathol 2001; 116: 637-46.
    • (2001) Am. J. Clin. Pathol. , vol.116 , pp. 637-646
    • Elliott, P.J.1    Ross, J.S.2
  • 79
    • 0034820022 scopus 로고    scopus 로고
    • Cell cycle regulation in the G1 phase: A promising target for the development of new chemotherapeutic anticancer agents
    • Owa T, Yoshino H, Yoshimatsu K, Nagasu T. Cell cycle regulation in the G1 phase: a promising target for the development of new chemotherapeutic anticancer agents. Curr Med Chem 2001; 8: 1487-503.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1487-1503
    • Owa, T.1    Yoshino, H.2    Yoshimatsu, K.3    Nagasu, T.4
  • 80
    • 0034321816 scopus 로고    scopus 로고
    • Clinical trials referral resource. Current clinical trials for the proteasome inhibitor PS-341
    • 1593-94 1597
    • Wright J, Hillsamer VL, Gore-Langton RE, Cheson BD. Clinical trials referral resource. Current clinical trials for the proteasome inhibitor PS-341. Oncology 2000; 14: 1589-90, 1593-94, 1597.
    • (2000) Oncology , vol.14 , pp. 1589-1590
    • Wright, J.1    Hillsamer, V.L.2    Gore-Langton, R.E.3    Cheson, B.D.4
  • 81
    • 0034062989 scopus 로고    scopus 로고
    • Proteasome inhibition: A new strategy in cancer treatment
    • Adams J, Palombella VJ, Elliott PJ. Proteasome inhibition: a new strategy in cancer treatment. Invest New Drugs 2000; 18: 109-21.
    • (2000) Invest. New Drugs , vol.18 , pp. 109-121
    • Adams, J.1    Palombella, V.J.2    Elliott, P.J.3
  • 82
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, bid and p53 in the apoptotic response triggered by histone deacetylase inhibitors TSA and SAHA
    • Henderson C, Mizzau M, Paroni G, et al. Role of caspases, bid and p53 in the apoptotic response triggered by histone deacetylase inhibitors TSA and SAHA. J Biol Chem 2003; 278: 12579-89.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3
  • 83
    • 0030796349 scopus 로고    scopus 로고
    • Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): Dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway
    • Medina V, Edmonds B, Young GP, et al. Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. Cancer Res 1997; 57: 3697-707.
    • (1997) Cancer Res. , vol.57 , pp. 3697-3707
    • Medina, V.1    Edmonds, B.2    Young, G.P.3
  • 84
    • 0032539890 scopus 로고    scopus 로고
    • A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
    • Richon VM, Emiliani S, Verdin E, et al. A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. Proc Natl Acad Sci USA 1998; 95: 3003-07.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3003-3007
    • Richon, V.M.1    Emiliani, S.2    Verdin, E.3
  • 85
    • 0036014986 scopus 로고    scopus 로고
    • Histone deacetylases as therapeutic targets in hematologic malignancies
    • Melnick A, Licht JD. Histone deacetylases as therapeutic targets in hematologic malignancies. Curr Opin Hematol 2002; 9: 322-32.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 322-332
    • Melnick, A.1    Licht, J.D.2
  • 86
    • 0035755974 scopus 로고    scopus 로고
    • Histone deacetylases and cancer: Causes and therapies
    • Marks P, Rifkind RA, Richon VM, et al. Histone deacetylases and cancer: causes and therapies. Nat Rev Cancer 2001; 1: 194-202.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 194-202
    • Marks, P.1    Rifkind, R.A.2    Richon, V.M.3
  • 87
    • 0003251972 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor for the treatment of pheripheral or cutaneous T-cell lymphoma
    • Piekarz R. Histone deacetylase inhibitor for the treatment of pheripheral or cutaneous T-cell lymphoma. Proc Am Soc Clin Oncol 2001; 20: 323B.
    • (2001) Proc. Am. Soc. Clin. Oncol. , vol.20
    • Piekarz, R.1
  • 90
    • 0035686546 scopus 로고    scopus 로고
    • INGN-201. Introgen Therapeutics
    • Brukner I. INGN-201. Introgen Therapeutics. Curr Opin Investig Drugs 2001; 2: 1776-85.
    • (2001) Curr. Opin. Investig. Drugs , vol.2 , pp. 1776-1785
    • Brukner, I.1
  • 91
    • 0031750168 scopus 로고    scopus 로고
    • Adenovirus-mediated p53 gene transfer in patients with advanced recurrent head and neck squamous cell carcinoma
    • Clayman GL, EI-Naggar AK, Lippman SM, et al. Adenovirus-mediated p53 gene transfer in patients with advanced recurrent head and neck squamous cell carcinoma. J Clin Oncol 1998; 16: 2221-32.
    • (1998) J. Clin. Oncol. , vol.16 , pp. 2221-2232
    • Clayman, G.L.1    EI-Naggar, A.K.2    Lippman, S.M.3
  • 92
    • 0037340739 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitors in the treatment of breast cancer
    • Kelland LR. Farnesyl transferase inhibitors in the treatment of breast cancer. Expert Opin Investig Drugs 2003; 12: 413-21.
    • (2003) Expert. Opin. Investig. Drugs , vol.12 , pp. 413-421
    • Kelland, L.R.1
  • 94
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein I, Robertson D, DiStefano F, et al. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res 2001; 61: 4003-09.
    • (2001) Cancer Res. , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3
  • 95
    • 0037265586 scopus 로고    scopus 로고
    • Development of small molecule hsp90 inhibitors: Utilizing both forward and reverse chemical genomics for drug identification
    • Neckers L. Development of small molecule hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification. Curr Med Chem 2003; 10: 733-39.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 733-739
    • Neckers, L.1
  • 96
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • Neckers L, Schulte TW, Mimnaugh E. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest New Drugs 1999; 17: 361-73.
    • (1999) Invest. New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 97
    • 0035810742 scopus 로고    scopus 로고
    • Measurement of the novel antitumor agent 17-(allylamino) A 7-demethoxygeldanamycin in human plasma by high-performance liquid chromatography
    • Agnew EB, Wilson RH, Grem JL, et al. Measurement of the novel antitumor agent 17-(allylamino) A 7-demethoxygeldanamycin in human plasma by high-performance liquid chromatography. J Chromatogr B Biomed Sci Appl 2001; 755: 237-43.
    • (2001) J. Chromatogr. B Biomed. Sci. Appl. , vol.755 , pp. 237-243
    • Agnew, E.B.1    Wilson, R.H.2    Grem, J.L.3
  • 98
    • 0037439578 scopus 로고    scopus 로고
    • Anticancer drugs of tomorrow: Apoptotic pathways as targets for drug design
    • Los M, Burek CJ, Stroh C, et al. Anticancer drugs of tomorrow: apoptotic pathways as targets for drug design. Drug Discov Today 2003; 8: 67-77.
    • (2003) Drug Discov. Today , vol.8 , pp. 67-77
    • Los, M.1    Burek, C.J.2    Stroh, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.