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Volumn 42, Issue 14, 2006, Pages 2233-2240

The clinical trail of TRAIL

Author keywords

Antibody; Apoptosis; RhTRAIL; Therapy; TRAIL

Indexed keywords

ALANINE AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; BILIRUBIN; CARBOPLATIN; CASPASE 8; CISPLATIN; DEATH RECEPTOR 4; DEATH RECEPTOR 5; DNA; GEMCITABINE; HISTONE DEACETYLASE INHIBITOR; MAPATUMUMAB; MONOCLONAL ANTIBODY; OSTEOPROTEGERIN; PACLITAXEL; PROTEIN BCL 2; RECOMBINANT PROTEIN; RECOMBINANT TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; TRASTUZUMAB; UNCLASSIFIED DRUG;

EID: 33748100542     PISSN: 09598049     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejca.2006.03.018     Document Type: Article
Times cited : (161)

References (66)
  • 1
    • 0027291205 scopus 로고
    • Lethal effect of the anti-Fas antibody in mice
    • Ogasawara J., Watanabefukunaga R., Adachi M., et al. Lethal effect of the anti-Fas antibody in mice. Nature 364 (1993) 806-809
    • (1993) Nature , vol.364 , pp. 806-809
    • Ogasawara, J.1    Watanabefukunaga, R.2    Adachi, M.3
  • 2
    • 0023684531 scopus 로고
    • A phase-I trial of intravenously-administered recombinant tumor necrosis factor-alpha in cancer-patients
    • Feinberg B., Kurzrock R., Talpaz M., et al. A phase-I trial of intravenously-administered recombinant tumor necrosis factor-alpha in cancer-patients. J Clin Oncol 6 (1988) 1328-1334
    • (1988) J Clin Oncol , vol.6 , pp. 1328-1334
    • Feinberg, B.1    Kurzrock, R.2    Talpaz, M.3
  • 3
    • 0035164903 scopus 로고    scopus 로고
    • Isolated limb perfusion: the European experience
    • [ix]
    • Lejeune F.J., Kroon B.B., Di Filippo F., et al. Isolated limb perfusion: the European experience. Surg Oncol Clin N Am 10 (2001) 821-832 [ix]
    • (2001) Surg Oncol Clin N Am , vol.10 , pp. 821-832
    • Lejeune, F.J.1    Kroon, B.B.2    Di Filippo, F.3
  • 4
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi A. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nat Rev Cancer 2 (2002) 420-430
    • (2002) Nat Rev Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 5
    • 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
  • 6
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: signaling and modulation
    • Ashkenazi A., and 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
  • 7
    • 2942565827 scopus 로고    scopus 로고
    • Enhancement of therapeutic potential of TRAIL by cancer chemotherapy and irradiation: mechanisms and clinical implications
    • Shankar S., and Srivastava R.K. Enhancement of therapeutic potential of TRAIL by cancer chemotherapy and irradiation: mechanisms and clinical implications. Drug Resist Updat 7 (2004) 139-156
    • (2004) Drug Resist Updat , vol.7 , pp. 139-156
    • Shankar, S.1    Srivastava, R.K.2
  • 8
    • 0034725664 scopus 로고    scopus 로고
    • Temperature-sensitive differential affinity of TRAIL for its receptors. DR5 is the highest affinity receptor
    • Truneh A., Sharma S., Silverman C., et al. Temperature-sensitive differential affinity of TRAIL for its receptors. DR5 is the highest affinity receptor. J Biol Chem 275 (2000) 23319-23325
    • (2000) J Biol Chem , vol.275 , pp. 23319-23325
    • Truneh, A.1    Sharma, S.2    Silverman, C.3
  • 9
    • 0035735753 scopus 로고    scopus 로고
    • Potential and caveats of TRAIL in cancer therapy
    • Held J., and Schulze-Osthoff K. Potential and caveats of TRAIL in cancer therapy. Drug Resist Updat 4 (2001) 243-252
    • (2001) Drug Resist Updat , vol.4 , pp. 243-252
    • Held, J.1    Schulze-Osthoff, K.2
  • 10
    • 3042784478 scopus 로고    scopus 로고
    • Modulation of TRAIL signaling for cancer therapy
    • Fulda S., and Debatin K.M. Modulation of TRAIL signaling for cancer therapy. Vitam Horm 67 (2004) 275-290
    • (2004) Vitam Horm , vol.67 , pp. 275-290
    • Fulda, S.1    Debatin, K.M.2
  • 11
    • 0001203366 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of the mouse homologue of the KILLER/DR5 tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) death receptor
    • Wu G.S., Burns T.F., Zhan Y., Alnemri E.S., and El Deiry W.S. Molecular cloning and functional analysis of the mouse homologue of the KILLER/DR5 tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) death receptor. Cancer Res 59 (1999) 2770-2775
    • (1999) Cancer Res , vol.59 , pp. 2770-2775
    • Wu, G.S.1    Burns, T.F.2    Zhan, Y.3    Alnemri, E.S.4    El Deiry, W.S.5
  • 12
    • 0037240850 scopus 로고    scopus 로고
    • Nature's TRAIL-on a path to cancer immunotherapy
    • Smyth M.J., Takeda K., Hayakawa Y., et al. Nature's TRAIL-on a path to cancer immunotherapy. Immunity 18 (2003) 1-6
    • (2003) Immunity , vol.18 , pp. 1-6
    • Smyth, M.J.1    Takeda, K.2    Hayakawa, Y.3
  • 13
    • 0036467427 scopus 로고    scopus 로고
    • Increased susceptibility to tumor initiation and metastasis in TNF-related apoptosis-inducing ligand-deficient mice
    • Cretney E., Takeda K., Yagita H., et al. Increased susceptibility to tumor initiation and metastasis in TNF-related apoptosis-inducing ligand-deficient mice. J Immunol 168 (2002) 1356-1361
    • (2002) J Immunol , vol.168 , pp. 1356-1361
    • Cretney, E.1    Takeda, K.2    Yagita, H.3
  • 14
    • 2542610615 scopus 로고    scopus 로고
    • Tissue distribution of the death ligand TRAIL and its receptors
    • Spierings D.C., de Vries E.G., Vellenga E., et al. Tissue distribution of the death ligand TRAIL and its receptors. J Histochem Cytochem 52 (2004) 821-831
    • (2004) J Histochem Cytochem , vol.52 , pp. 821-831
    • Spierings, D.C.1    de Vries, E.G.2    Vellenga, E.3
  • 15
    • 0037148518 scopus 로고    scopus 로고
    • Critical role for tumor necrosis factor-related apoptosis-inducing ligand in immune surveillance against tumor development
    • Takeda K., Smyth M.J., Cretney E., et al. Critical role for tumor necrosis factor-related apoptosis-inducing ligand in immune surveillance against tumor development. J Exp Med 195 (2002) 161-169
    • (2002) J Exp Med , vol.195 , pp. 161-169
    • Takeda, K.1    Smyth, M.J.2    Cretney, E.3
  • 16
    • 33645091240 scopus 로고    scopus 로고
    • TNF-related apoptosis-inducing ligand as a therapeutic agent in autoimmunity and cancer
    • Cretney E., Shanker A., Yagita H., Smyth M.J., and Sayers T.J. TNF-related apoptosis-inducing ligand as a therapeutic agent in autoimmunity and cancer. Immunol Cell Biol 84 (2006) 87-98
    • (2006) Immunol Cell Biol , vol.84 , pp. 87-98
    • Cretney, E.1    Shanker, A.2    Yagita, H.3    Smyth, M.J.4    Sayers, T.J.5
  • 17
    • 11444253174 scopus 로고    scopus 로고
    • Endotoxin increases plasma soluble tumor necrosis factor-related apoptosis-inducing ligand level mediated by the p38 mitogen-activated protein kinase signaling pathway
    • Lub-de Hooge M.N., de Jong S., Vermot-Desroches C., et al. Endotoxin increases plasma soluble tumor necrosis factor-related apoptosis-inducing ligand level mediated by the p38 mitogen-activated protein kinase signaling pathway. Shock 22 (2004) 186-188
    • (2004) Shock , vol.22 , pp. 186-188
    • Lub-de Hooge, M.N.1    de Jong, S.2    Vermot-Desroches, C.3
  • 18
    • 19544390527 scopus 로고    scopus 로고
    • Soluble TRAIL concentrations are raised in patients with systemic lupus erythematosus
    • Lub-de Hooge M.N., de Vries E.G., de Jong S., and Bijl M. Soluble TRAIL concentrations are raised in patients with systemic lupus erythematosus. Ann Rheum Dis 64 (2005) 854-858
    • (2005) Ann Rheum Dis , vol.64 , pp. 854-858
    • Lub-de Hooge, M.N.1    de Vries, E.G.2    de Jong, S.3    Bijl, M.4
  • 19
    • 0037273848 scopus 로고    scopus 로고
    • Apo2L/TRAIL and its death and decoy receptors
    • LeBlanc H.N., and Ashkenazi A. Apo2L/TRAIL and its death and decoy receptors. Cell Death Differ 10 (2003) 66-75
    • (2003) Cell Death Differ , vol.10 , pp. 66-75
    • LeBlanc, H.N.1    Ashkenazi, A.2
  • 21
    • 0037621450 scopus 로고    scopus 로고
    • Silencing of death receptor and caspase-8 expression in small cell lung carcinoma cell lines and tumors by DNA methylation
    • Hopkins-Donaldson S., Ziegler A., Kurtz S., et al. Silencing of death receptor and caspase-8 expression in small cell lung carcinoma cell lines and tumors by DNA methylation. Cell Death Differ 10 (2003) 356-364
    • (2003) Cell Death Differ , vol.10 , pp. 356-364
    • Hopkins-Donaldson, S.1    Ziegler, A.2    Kurtz, S.3
  • 22
    • 21344474349 scopus 로고    scopus 로고
    • Contribution of epigenetic silencing of tumor necrosis factor-related apoptosis inducing ligand receptor 1 (DR4) to TRAIL resistance and ovarian cancer
    • Horak P., Pils D., Haller G., et al. Contribution of epigenetic silencing of tumor necrosis factor-related apoptosis inducing ligand receptor 1 (DR4) to TRAIL resistance and ovarian cancer. Mol Cancer Res 3 (2005) 335-343
    • (2005) Mol Cancer Res , vol.3 , pp. 335-343
    • Horak, P.1    Pils, D.2    Haller, G.3
  • 23
    • 14844288360 scopus 로고    scopus 로고
    • Lessons from TRAIL-resistance mechanisms in colorectal cancer cells: paving the road to patient-tailored therapy
    • Van Geelen C.M., de Vries E.G., and de Jong S. Lessons from TRAIL-resistance mechanisms in colorectal cancer cells: paving the road to patient-tailored therapy. Drug Resist Updat 7 (2004) 345-358
    • (2004) Drug Resist Updat , vol.7 , pp. 345-358
    • Van Geelen, C.M.1    de Vries, E.G.2    de Jong, S.3
  • 24
    • 30144434107 scopus 로고    scopus 로고
    • Potentiation of neuroblastoma metastasis by loss of caspase-8
    • Stupack D.G., Teitz T., Potter M.D., et al. Potentiation of neuroblastoma metastasis by loss of caspase-8. Nature 439 (2006) 95-99
    • (2006) Nature , vol.439 , pp. 95-99
    • Stupack, D.G.1    Teitz, T.2    Potter, M.D.3
  • 25
    • 19544382901 scopus 로고    scopus 로고
    • The caspase-8 modulator c-FLIP
    • Kataoka T. The caspase-8 modulator c-FLIP. Crit Rev Immunol 25 (2005) 31-58
    • (2005) Crit Rev Immunol , vol.25 , pp. 31-58
    • Kataoka, T.1
  • 26
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., and Reed J.C. Mitochondria and apoptosis. Science 281 (1998) 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 27
    • 0036792475 scopus 로고    scopus 로고
    • The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet
    • Van Loo G., Saelens X., van Gurp M., et al. The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet. Cell Death Differ 9 (2002) 1031-1042
    • (2002) Cell Death Differ , vol.9 , pp. 1031-1042
    • Van Loo, G.1    Saelens, X.2    van Gurp, M.3
  • 28
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 29
    • 2342453921 scopus 로고    scopus 로고
    • Death receptors in chemotherapy and cancer
    • Debatin K.M., and Krammer P.H. Death receptors in chemotherapy and cancer. Oncogene 23 (2004) 2950-2966
    • (2004) Oncogene , vol.23 , pp. 2950-2966
    • Debatin, K.M.1    Krammer, P.H.2
  • 30
    • 0037379739 scopus 로고    scopus 로고
    • Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: differential regulation of cytochrome c and Smac/DIABLO release
    • Kandasamy K., Srinivasula S.M., Alnemri E.S., et al. Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: differential regulation of cytochrome c and Smac/DIABLO release. Cancer Res 63 (2003) 1712-1721
    • (2003) Cancer Res , vol.63 , pp. 1712-1721
    • Kandasamy, K.1    Srinivasula, S.M.2    Alnemri, E.S.3
  • 31
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
    • Lindsten T., Ross A.J., King A., et al. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol Cell 6 (2000) 1389-1399
    • (2000) Mol Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1    Ross, A.J.2    King, A.3
  • 32
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death
    • Wei M.C., Zong W.X., Cheng E.H., et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292 (2001) 727-730
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 33
    • 0036131142 scopus 로고    scopus 로고
    • Tumor-cell resistance to death receptor-induced apoptosis through mutational inactivation of the proapoptotic Bcl-2 homolog Bax
    • LeBlanc H., Lawrence D., Varfolomeev E., et al. Tumor-cell resistance to death receptor-induced apoptosis through mutational inactivation of the proapoptotic Bcl-2 homolog Bax. Nat Med 8 (2002) 274-281
    • (2002) Nat Med , vol.8 , pp. 274-281
    • LeBlanc, H.1    Lawrence, D.2    Varfolomeev, E.3
  • 34
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux Q.L., Takahashi R., Salvesen G.S., and Reed J.C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388 (1997) 300-304
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 35
    • 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
  • 36
    • 17144377113 scopus 로고    scopus 로고
    • IAPs, RINGs and ubiquitylation
    • Vaux D.L., and Silke J. IAPs, RINGs and ubiquitylation. Nat Rev Mol Cell Biol 6 (2005) 287-297
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 287-297
    • Vaux, D.L.1    Silke, J.2
  • 37
    • 33645640920 scopus 로고    scopus 로고
    • The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases
    • Eckelman B.P., and Salvesen G.S. The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases. J Biol Chem 281 (2006) 3254-3260
    • (2006) J Biol Chem , vol.281 , pp. 3254-3260
    • Eckelman, B.P.1    Salvesen, G.S.2
  • 38
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: blocking the road to death's door
    • Salvesen G.S., and Duckett C.S. IAP proteins: blocking the road to death's door. Nat Rev Mol Cell Biol 3 (2002) 401-410
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 39
    • 0037418619 scopus 로고    scopus 로고
    • TRAIL-induced signalling and apoptosis
    • MacFarlane M. TRAIL-induced signalling and apoptosis. Toxicol Lett 139 (2003) 89-97
    • (2003) Toxicol Lett , vol.139 , pp. 89-97
    • MacFarlane, M.1
  • 40
    • 31544470589 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin synergistically potentiates tumor necrosis factor-induced lung cancer cell death by blocking the nuclear factor-kappaB pathway
    • Wang X., Ju W., Renouard J., et al. 17-Allylamino-17-demethoxygeldanamycin synergistically potentiates tumor necrosis factor-induced lung cancer cell death by blocking the nuclear factor-kappaB pathway. Cancer Res 66 (2006) 1089-1095
    • (2006) Cancer Res , vol.66 , pp. 1089-1095
    • Wang, X.1    Ju, W.2    Renouard, J.3
  • 42
    • 1242317030 scopus 로고    scopus 로고
    • Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP)
    • Dan H.C., Sun M., Kaneko S., et al. Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP). J Biol Chem 279 (2004) 5405-5412
    • (2004) J Biol Chem , vol.279 , pp. 5405-5412
    • Dan, H.C.1    Sun, M.2    Kaneko, S.3
  • 43
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco I., and Sawyers C.L. The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat Rev Cancer 2 (2002) 489-501
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 44
    • 0032713075 scopus 로고    scopus 로고
    • Safety and antitumor activity of recombinant soluble Apo2 ligand
    • Ashkenazi A., Pai R.C., Fong S., et al. Safety and antitumor activity of 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
  • 45
    • 0034812659 scopus 로고    scopus 로고
    • Preclinical studies to predict the disposition of Apo2L/tumor necrosis factor-related apoptosis-inducing ligand in humans: characterization of in vivo efficacy, pharmacokinetics, and safety
    • Kelley S.K., Harris L.A., Xie D., et al. Preclinical studies to predict the disposition of Apo2L/tumor necrosis factor-related apoptosis-inducing ligand in humans: characterization of in vivo efficacy, pharmacokinetics, and safety. J Pharmacol Exp Ther 299 (2001) 31-38
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 31-38
    • Kelley, S.K.1    Harris, L.A.2    Xie, D.3
  • 46
    • 0035050960 scopus 로고    scopus 로고
    • Differential hepatocyte toxicity of recombinant Apo2L/TRAIL versions
    • Lawrence D., Shahrokh Z., Marsters S., et al. Differential hepatocyte toxicity of recombinant Apo2L/TRAIL versions. Nat Med 7 (2001) 383-385
    • (2001) Nat Med , vol.7 , pp. 383-385
    • Lawrence, D.1    Shahrokh, Z.2    Marsters, S.3
  • 47
    • 20244378961 scopus 로고    scopus 로고
    • Enhanced apoptosis and tumor regression induced by a direct agonist antibody to tumor necrosis factor-related apoptosis-inducing ligand receptor 2
    • Motoki K., Mori E., Matsumoto A., et al. Enhanced apoptosis and tumor regression induced by a direct agonist antibody to tumor necrosis factor-related apoptosis-inducing ligand receptor 2. Clin Cancer Res 11 (2005) 3126-3135
    • (2005) Clin Cancer Res , vol.11 , pp. 3126-3135
    • Motoki, K.1    Mori, E.2    Matsumoto, A.3
  • 48
    • 33646393448 scopus 로고    scopus 로고
    • HGS-ETR1, a fully human agonistic monoclonal antibody to the tumor necrosis factor-related apoptosis-inducing ligand receptor 1 (TRAIL-R1) in patients with advanced solid cancer: results of a phase 1 trial
    • [abstr C22]
    • Hirte H.W., Hotte S.J., Chen E.X., et al. HGS-ETR1, a fully human agonistic monoclonal antibody to the tumor necrosis factor-related apoptosis-inducing ligand receptor 1 (TRAIL-R1) in patients with advanced solid cancer: results of a phase 1 trial. Clin Cancer Res 11 (2005) 9104s [abstr C22]
    • (2005) Clin Cancer Res , vol.11
    • Hirte, H.W.1    Hotte, S.J.2    Chen, E.X.3
  • 49
    • 33646397515 scopus 로고    scopus 로고
    • A phase I, pharmacokinetic (PK) study of HGS-ETR1, an agonist monoclonal antibody to TRAIL-R1, in patients with solid tumors
    • Mita M.T., Tolcher A.W., Patnaik A., et al. A phase I, pharmacokinetic (PK) study of HGS-ETR1, an agonist monoclonal antibody to TRAIL-R1, in patients with solid tumors. Proc Am Assoc Cancer Res 46 (2005) 544
    • (2005) Proc Am Assoc Cancer Res , vol.46 , pp. 544
    • Mita, M.T.1    Tolcher, A.W.2    Patnaik, A.3
  • 50
    • 33646390886 scopus 로고    scopus 로고
    • Results of a phase 2 trial of HGS-ETR1 (agonistic human monoclonal antibody to TRAIL receptor 1) in subjects with relapsed/refractory non-Hodgkin's lymphoma (NHL) (ETR1-HM01)
    • Younes A., Vose J., Zelenetz A.D., et al. Results of a phase 2 trial of HGS-ETR1 (agonistic human monoclonal antibody to TRAIL receptor 1) in subjects with relapsed/refractory non-Hodgkin's lymphoma (NHL) (ETR1-HM01). Blood (ASH Annual Meeting Abstracts) 106 (2005) 489
    • (2005) Blood (ASH Annual Meeting Abstracts) , vol.106 , pp. 489
    • Younes, A.1    Vose, J.2    Zelenetz, A.D.3
  • 51
    • 31744446823 scopus 로고    scopus 로고
    • Results of a phase 2 trial of HGS-ETR1 (agonistic human monoclonal antibody to TRAIL receptor 1) in subjects with relapsed/recurrent non-small cell lung cancer (NSCLC)
    • [abstr P460]
    • Bonomi P., Greco F.A., Crawford J., et al. Results of a phase 2 trial of HGS-ETR1 (agonistic human monoclonal antibody to TRAIL receptor 1) in subjects with relapsed/recurrent non-small cell lung cancer (NSCLC). Lung Cancer 49 Suppl. 2 (2005) S237 [abstr P460]
    • (2005) Lung Cancer , vol.49 , Issue.SUPPL. 2
    • Bonomi, P.1    Greco, F.A.2    Crawford, J.3
  • 52
    • 33646415571 scopus 로고    scopus 로고
    • Results of a phase 2 trial of HGS-ETR1 (agonistic human monoclonal antibody to TRAIL receptor 1) in subjects with relapsed or refractory colorectal cancer (CRC)
    • [abstr 630]
    • Kanzler S., Trarbach T., Heinemann V., et al. Results of a phase 2 trial of HGS-ETR1 (agonistic human monoclonal antibody to TRAIL receptor 1) in subjects with relapsed or refractory colorectal cancer (CRC). Eur J Cancer 3 Suppl. (2005) 177 [abstr 630]
    • (2005) Eur J Cancer , vol.3 , Issue.SUPPL , pp. 177
    • Kanzler, S.1    Trarbach, T.2    Heinemann, V.3
  • 53
    • 33646434448 scopus 로고    scopus 로고
    • A phase 1 and pharmacological study of HGS-ETR1, an antibody targeting TRAIL-R1, in combination with paclitaxel and carboplatin in patients with advanced solid malignancies
    • [abstr B109]
    • Hariharan S., Gore L., Eckhardt S.G., et al. A phase 1 and pharmacological study of HGS-ETR1, an antibody targeting TRAIL-R1, in combination with paclitaxel and carboplatin in patients with advanced solid malignancies. Clin Cancer Res 11 (2005) 9058s [abstr B109]
    • (2005) Clin Cancer Res , vol.11
    • Hariharan, S.1    Gore, L.2    Eckhardt, S.G.3
  • 54
    • 33646410356 scopus 로고    scopus 로고
    • A phase 1 study of HGS-ETR1, a fully human agonistic monoclonal antibody to the TRAIL-R1, in combination with gemcitabine and cisplatin in subjects with advanced solid malignancies
    • [abstr C74]
    • Mom C.H., Sleijfer S., Gietema J.A., et al. A phase 1 study of HGS-ETR1, a fully human agonistic monoclonal antibody to the TRAIL-R1, in combination with gemcitabine and cisplatin in subjects with advanced solid malignancies. Clin Cancer Res 11 (2005) 9117s [abstr C74]
    • (2005) Clin Cancer Res , vol.11
    • Mom, C.H.1    Sleijfer, S.2    Gietema, J.A.3
  • 55
    • 33646390332 scopus 로고    scopus 로고
    • HGS-ETR2-ST02: a phase 1 clinical trial of HGS-ETR2, a fully human activating monoclonal antibody to TRAIL-R2, in patients with advanced solid tumors
    • [abstr C21]
    • Sarantopoulos J., Wakelee H., Mita M.T., et al. HGS-ETR2-ST02: a phase 1 clinical trial of HGS-ETR2, a fully human activating monoclonal antibody to TRAIL-R2, in patients with advanced solid tumors. Clin Cancer Res 11 (2005) 9104s [abstr C21]
    • (2005) Clin Cancer Res , vol.11
    • Sarantopoulos, J.1    Wakelee, H.2    Mita, M.T.3
  • 56
    • 33646416396 scopus 로고    scopus 로고
    • Phase 1 and pharmakinetic study of HGS-ETR2, a fully human agonistic monoclonal antibody to TRAIL-R2, in patients with advanced solid malignancies
    • [abstr B114]
    • Attard G., Plummer R.E., De Bono J.S., et al. Phase 1 and pharmakinetic study of HGS-ETR2, a fully human agonistic monoclonal antibody to TRAIL-R2, in patients with advanced solid malignancies. Clin Cancer Res 11 (2005) 9060s [abstr B114]
    • (2005) Clin Cancer Res , vol.11
    • Attard, G.1    Plummer, R.E.2    De Bono, J.S.3
  • 57
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: novel drugs for the treatment of cancer
    • Johnstone R.W. Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discov 1 (2002) 287-299
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 58
    • 22744437647 scopus 로고    scopus 로고
    • HDAC inhibitors enhance the apoptosis-inducing potential of TRAIL in breast carcinoma
    • Singh T.R., Shankar S., and Srivastava R.K. HDAC inhibitors enhance the apoptosis-inducing potential of TRAIL in breast carcinoma. Oncogene 24 (2005) 4609-4623
    • (2005) Oncogene , vol.24 , pp. 4609-4623
    • Singh, T.R.1    Shankar, S.2    Srivastava, R.K.3
  • 59
    • 28944449421 scopus 로고    scopus 로고
    • Combining proteasome inhibition with TNF-related apoptosis-inducing ligand (Apo2L/TRAIL) for cancer therapy
    • Sayers T.J., and Murphy W.J. Combining proteasome inhibition with TNF-related apoptosis-inducing ligand (Apo2L/TRAIL) for cancer therapy. Cancer Immunol Immunother 55 (2006) 76-84
    • (2006) Cancer Immunol Immunother , vol.55 , pp. 76-84
    • Sayers, T.J.1    Murphy, W.J.2
  • 60
    • 10044282921 scopus 로고    scopus 로고
    • Apoptosis pathway-targeted drugs - from the bench to the clinic
    • Cummings J., Ward T.H., Ranson M., and Dive C. Apoptosis pathway-targeted drugs - from the bench to the clinic. Biochim Biophys Acta 1705 (2004) 53-66
    • (2004) Biochim Biophys Acta , vol.1705 , pp. 53-66
    • Cummings, J.1    Ward, T.H.2    Ranson, M.3    Dive, C.4
  • 61
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl-2 family proteins induces regression of solid tumours
    • Oltersdorf T., Elmore S.W., Shoemaker A.R., et al. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature 435 (2005) 677-681
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1    Elmore, S.W.2    Shoemaker, A.R.3
  • 62
    • 26444560914 scopus 로고    scopus 로고
    • mTOR controls FLIPS translation and TRAIL sensitivity in glioblastoma multiforme cells
    • Panner A., James C.D., Berger M.S., and Pieper R.O. mTOR controls FLIPS translation and TRAIL sensitivity in glioblastoma multiforme cells. Mol Cell Biol 25 (2005) 8809-8823
    • (2005) Mol Cell Biol , vol.25 , pp. 8809-8823
    • Panner, A.1    James, C.D.2    Berger, M.S.3    Pieper, R.O.4
  • 63
    • 31544454764 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function by 17-allylamino-17-demethoxy-geldanamycin in Hodgkin's lymphoma cells down-regulates Akt kinase, dephosphorylates extracellular signal-regulated kinase, and induces cell cycle arrest and cell death
    • Georgakis G.V., Li Y., Rassidakis G.Z., et al. Inhibition of heat shock protein 90 function by 17-allylamino-17-demethoxy-geldanamycin in Hodgkin's lymphoma cells down-regulates Akt kinase, dephosphorylates extracellular signal-regulated kinase, and induces cell cycle arrest and cell death. Clin Cancer Res 12 (2006) 584-590
    • (2006) Clin Cancer Res , vol.12 , pp. 584-590
    • Georgakis, G.V.1    Li, Y.2    Rassidakis, G.Z.3
  • 64
    • 33644857988 scopus 로고    scopus 로고
    • Sensitization of TRAIL-resistant cells by inhibition of heat shock protein 90 with low-dose geldanamycin
    • Ma Y., Lakshmikanthan V., Lewis R.W., and Kumar M.V. Sensitization of TRAIL-resistant cells by inhibition of heat shock protein 90 with low-dose geldanamycin. Mol Cancer Ther 5 (2006) 170-178
    • (2006) Mol Cancer Ther , vol.5 , pp. 170-178
    • Ma, Y.1    Lakshmikanthan, V.2    Lewis, R.W.3    Kumar, M.V.4
  • 65
    • 0035874898 scopus 로고    scopus 로고
    • Down-regulation of the erbB-2 receptor by trastuzumab (herceptin) enhances tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis in breast and ovarian cancer cell lines that overexpress erbB-2
    • Cuello M., Ettenberg S.A., Clark A.S., et al. Down-regulation of the erbB-2 receptor by trastuzumab (herceptin) enhances tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis in breast and ovarian cancer cell lines that overexpress erbB-2. Cancer Res 61 (2001) 4892-4900
    • (2001) Cancer Res , vol.61 , pp. 4892-4900
    • Cuello, M.1    Ettenberg, S.A.2    Clark, A.S.3
  • 66
    • 0036064773 scopus 로고    scopus 로고
    • Regulation of Akt by EGF-R inhibitors, a possible mechanism of EGF-R inhibitor-enhanced TRAIL-induced apoptosis
    • Park S.Y., and Seol D.W. Regulation of Akt by EGF-R inhibitors, a possible mechanism of EGF-R inhibitor-enhanced TRAIL-induced apoptosis. Biochem Biophys Res Commun 295 (2002) 515-518
    • (2002) Biochem Biophys Res Commun , vol.295 , pp. 515-518
    • Park, S.Y.1    Seol, D.W.2


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