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Volumn 5, Issue APR, 2015, Pages

Trailing TRAIL resistance: Novel targets for TRAIL sensitization in cancer cells

Author keywords

Apoptosis; Cancer; DR4; DR5; TRAIL; TRAIL resistance

Indexed keywords

BEVACIZUMAB; CARBOPLATIN; CASPASE 10; CASPASE 3; CASPASE 8; CISPLATIN; DEATH RECEPTOR; GEMCITABINE; HEAT SHOCK PROTEIN; INITIATION FACTOR 4E; MAPATUMUMAB; MESSENGER RNA; PACLITAXEL; PROTEASOME; PROTEIN BAK; PROTEIN BAX; PROTEIN KINASE B; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UBIQUITIN;

EID: 84934278552     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2015.00069     Document Type: Review
Times cited : (191)

References (213)
  • 1
    • 0035001741 scopus 로고    scopus 로고
    • The potential of TRAIL for cancer chemotherapy
    • Nagane M, Huang HJ, Cavenee WK. The potential of TRAIL for cancer chemotherapy. Apoptosis (2001) 6(3):191-7. doi:10.1023/A:1011336726649
    • (2001) Apoptosis , vol.6 , Issue.3 , pp. 191-197
    • Nagane, M.1    Huang, H.J.2    Cavenee, W.K.3
  • 2
    • 34347272996 scopus 로고    scopus 로고
    • Clearing the TRAIL for cancer therapy
    • Hall MA, Cleveland JL. Clearing the TRAIL for cancer therapy. Cancer Cell (2007) 12(1):4-6. doi:10.1016/j.ccr.2007.06.011
    • (2007) Cancer Cell , vol.12 , Issue.1 , pp. 4-6
    • Hall, M.A.1    Cleveland, J.L.2
  • 3
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science (1998) 281(5381):1305-8. doi:10.1126/science.281.5381.1305
    • (1998) Science , vol.281 , Issue.5381 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 4
    • 34249663310 scopus 로고    scopus 로고
    • Targeting death-inducing receptors in cancer therapy
    • Takeda K, Stagg J, Yagita H, Okumura K, Smyth MJ. Targeting death-inducing receptors in cancer therapy. Oncogene (2007) 26(25):3745-57. doi:10.1038/sj.onc.1210374
    • (2007) Oncogene , vol.26 , Issue.25 , pp. 3745-3757
    • Takeda, K.1    Stagg, J.2    Yagita, H.3    Okumura, K.4    Smyth, M.J.5
  • 5
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
    • Pitti RM, Marsters SA, Ruppert S, Donahue CJ, Moore A, Ashkenazi A. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J Biol Chem (1996) 271(22):12687-90. doi:10.1074/jbc.271.22.12687
    • (1996) J Biol Chem , vol.271 , Issue.22 , pp. 12687-12690
    • Pitti, R.M.1    Marsters, S.A.2    Ruppert, S.3    Donahue, C.J.4    Moore, A.5    Ashkenazi, A.6
  • 6
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak H, Miller RE, Ariail K, Gliniak B, Griffith TS, Kubin M, et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med (1999) 5(2):157-63. doi:10.1038/5517
    • (1999) Nat Med , vol.5 , Issue.2 , pp. 157-163
    • Walczak, H.1    Miller, R.E.2    Ariail, K.3    Gliniak, B.4    Griffith, T.S.5    Kubin, M.6
  • 8
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley SR, Schooley K, Smolak PJ, Din WS, Huang CP, Nicholl JK, et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity (1995) 3(6):673-82. doi:10.1016/1074-7613(95)90057-8
    • (1995) Immunity , vol.3 , Issue.6 , pp. 673-682
    • Wiley, S.R.1    Schooley, K.2    Smolak, P.J.3    Din, W.S.4    Huang, C.P.5    Nicholl, J.K.6
  • 9
    • 84921673999 scopus 로고    scopus 로고
    • Tumor-necrosis-factor-related apoptosis-inducing ligand (TRAIL)
    • Fulda S. Tumor-necrosis-factor-related apoptosis-inducing ligand (TRAIL). Adv Exp Med Biol (2014) 818:167-80. doi:10.1007/978-1-4471-6458-6_8
    • (2014) Adv Exp Med Biol , vol.818 , pp. 167-180
    • Fulda, S.1
  • 11
    • 0032550366 scopus 로고    scopus 로고
    • Conversion of membrane-bound Fas(CD95) ligand to its soluble form is associated with downregulation of its proapoptotic activity and loss of liver toxicity
    • Schneider P, Holler N, Bodmer JL, Hahne M, Frei K, Fontana A, et al. Conversion of membrane-bound Fas(CD95) ligand to its soluble form is associated with downregulation of its proapoptotic activity and loss of liver toxicity. J Exp Med (1998) 187(8):1205-13. doi:10.1084/jem.187.8.1205
    • (1998) J Exp Med , vol.187 , Issue.8 , pp. 1205-1213
    • Schneider, P.1    Holler, N.2    Bodmer, J.L.3    Hahne, M.4    Frei, K.5    Fontana, A.6
  • 12
    • 9844225051 scopus 로고    scopus 로고
    • Activity of TNF-related apoptosis-inducing ligand (TRAIL) in haematological malignancies
    • Snell V, Clodi K, Zhao S, Goodwin R, Thomas EK, Morris SW, et al. Activity of TNF-related apoptosis-inducing ligand (TRAIL) in haematological malignancies. Br J Haematol (1997) 99(3):618-24. doi:10.1046/j.1365-2141.1997.4393250.x
    • (1997) Br J Haematol , vol.99 , Issue.3 , pp. 618-624
    • Snell, V.1    Clodi, K.2    Zhao, S.3    Goodwin, R.4    Thomas, E.K.5    Morris, S.W.6
  • 13
    • 0032941792 scopus 로고    scopus 로고
    • JNK/SAPK activity is not sufficient for anticancer therapy-induced apoptosis involving CD95-L, TRAIL and TNF-alpha
    • Herr I, Wilhelm D, Bohler T, Angel P, Debatin KM. JNK/SAPK activity is not sufficient for anticancer therapy-induced apoptosis involving CD95-L, TRAIL and TNF-alpha. Int J Cancer (1999) 80(3):417-24. doi:10.1002/(SICI)1097-0215(19990129)80:3%3C417::AID-IJC14%3E3.0.CO;2-B
    • (1999) Int J Cancer , vol.80 , Issue.3 , pp. 417-424
    • Herr, I.1    Wilhelm, D.2    Bohler, T.3    Angel, P.4    Debatin, K.M.5
  • 14
    • 0031974417 scopus 로고    scopus 로고
    • TRAIL/Apo-2-ligand-induced apoptosis in human T cells
    • Jeremias I, Herr I, Boehler T, Debatin KM. TRAIL/Apo-2-ligand-induced apoptosis in human T cells. Eur J Immunol (1998) 28(1):143-52. doi:10.1002/(SICI)1521-4141(199801)28:01%3C143::AID-IMMU143%3E3.0.CO;2-3
    • (1998) Eur J Immunol , vol.28 , Issue.1 , pp. 143-152
    • Jeremias, I.1    Herr, I.2    Boehler, T.3    Debatin, K.M.4
  • 15
    • 0347364696 scopus 로고    scopus 로고
    • NK cell TRAIL eliminates immature dendritic cells in vivo and limits dendritic cell vaccination efficacy
    • Hayakawa Y, Screpanti V, Yagita H, Grandien A, Ljunggren HG, Smyth MJ, et al. NK cell TRAIL eliminates immature dendritic cells in vivo and limits dendritic cell vaccination efficacy. J Immunol (2004) 172(1):123-9. doi:10.4049/jimmunol.172.1.123
    • (2004) J Immunol , vol.172 , Issue.1 , pp. 123-129
    • Hayakawa, Y.1    Screpanti, V.2    Yagita, H.3    Grandien, A.4    Ljunggren, H.G.5    Smyth, M.J.6
  • 16
    • 14544288632 scopus 로고    scopus 로고
    • CD4+ T-cell help controls CD8+ T-cell memory via TRAIL-mediated activation-induced cell death
    • Janssen EM, Droin NM, Lemmens EE, Pinkoski MJ, Bensinger SJ, Ehst BD, et al. CD4+ T-cell help controls CD8+ T-cell memory via TRAIL-mediated activation-induced cell death. Nature (2005) 434(7029):88-93. doi:10.1038/nature03337
    • (2005) Nature , vol.434 , Issue.7029 , pp. 88-93
    • Janssen, E.M.1    Droin, N.M.2    Lemmens, E.E.3    Pinkoski, M.J.4    Bensinger, S.J.5    Ehst, B.D.6
  • 17
    • 0031945015 scopus 로고    scopus 로고
    • Surface expression of TRAIL/Apo-2 ligand in activated mouse T and B cells
    • Mariani SM, Krammer PH. Surface expression of TRAIL/Apo-2 ligand in activated mouse T and B cells. Eur J Immunol (1998) 28(5):1492-8. doi:10.1002/(SICI)1521-4141(199805)28:05%3C1492::AID-IMMU1492%3E3.0.CO;2-X
    • (1998) Eur J Immunol , vol.28 , Issue.5 , pp. 1492-1498
    • Mariani, S.M.1    Krammer, P.H.2
  • 18
    • 0035892735 scopus 로고    scopus 로고
    • Differential secretion of Fas ligand- or APO2 ligand/TNF-related apoptosis-inducing ligand-carrying microvesicles during activation-induced death of human T cells
    • Monleon I, Martinez-Lorenzo MJ, Monteagudo L, Lasierra P, Taules M, Iturralde M, et al. Differential secretion of Fas ligand- or APO2 ligand/TNF-related apoptosis-inducing ligand-carrying microvesicles during activation-induced death of human T cells. J Immunol (2001) 167(12):6736-44. doi:10.4049/jimmunol.167.12.6736
    • (2001) J Immunol , vol.167 , Issue.12 , pp. 6736-6744
    • Monleon, I.1    Martinez-Lorenzo, M.J.2    Monteagudo, L.3    Lasierra, P.4    Taules, M.5    Iturralde, M.6
  • 19
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a death domain-containing receptor for TRAIL
    • Pan G, Ni J, Wei YF, Yu G, Gentz R, Dixit VM. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science (1997) 277(5327):815-8. doi:10.1126/science.277.5327.815
    • (1997) Science , vol.277 , Issue.5327 , pp. 815-818
    • Pan, G.1    Ni, J.2    Wei, Y.F.3    Yu, G.4    Gentz, R.5    Dixit, V.M.6
  • 20
    • 0030792712 scopus 로고    scopus 로고
    • Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors
    • Sheridan JP, Marsters SA, Pitti RM, Gurney A, Skubatch M, Baldwin D, et al. Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. Science (1997) 277(5327):818-21. doi:10.1126/science.277.5327.818
    • (1997) Science , vol.277 , Issue.5327 , pp. 818-821
    • Sheridan, J.P.1    Marsters, S.A.2    Pitti, R.M.3    Gurney, A.4    Skubatch, M.5    Baldwin, D.6
  • 22
    • 13144265771 scopus 로고    scopus 로고
    • A novel receptor for Apo2L/TRAIL contains a truncated death domain
    • Marsters SA, Sheridan JP, Pitti RM, Huang A, Skubatch M, Baldwin D, et al. A novel receptor for Apo2L/TRAIL contains a truncated death domain. Curr Biol (1997) 7(12):1003-6. doi:10.1016/S0960-9822(06)00422-2
    • (1997) Curr Biol , vol.7 , Issue.12 , pp. 1003-1006
    • Marsters, S.A.1    Sheridan, J.P.2    Pitti, R.M.3    Huang, A.4    Skubatch, M.5    Baldwin, D.6
  • 23
    • 0031414749 scopus 로고    scopus 로고
    • The novel receptor TRAIL-R4 induces NF-kappaB and protects against TRAIL-mediated apoptosis, yet retains an incomplete death domain
    • Degli-Esposti MA, Dougall WC, Smolak PJ, Waugh JY, Smith CA, Goodwin RG. The novel receptor TRAIL-R4 induces NF-kappaB and protects against TRAIL-mediated apoptosis, yet retains an incomplete death domain. Immunity (1997) 7(6):813-20. doi:10.1016/S1074-7613(00)80399-4
    • (1997) Immunity , vol.7 , Issue.6 , pp. 813-820
    • Degli-Esposti, M.A.1    Dougall, W.C.2    Smolak, P.J.3    Waugh, J.Y.4    Smith, C.A.5    Goodwin, R.G.6
  • 24
    • 7344233085 scopus 로고    scopus 로고
    • Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL
    • Emery JG, McDonnell P, Burke MB, Deen KC, Lyn S, Silverman C, et al. Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL. J Biol Chem (1998) 273(23):14363-7. doi:10.1074/jbc.273.23.14363
    • (1998) J Biol Chem , vol.273 , Issue.23 , pp. 14363-14367
    • Emery, J.G.1    McDonnell, P.2    Burke, M.B.3    Deen, K.C.4    Lyn, S.5    Silverman, C.6
  • 26
    • 69149092108 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis: between tumor therapy and immunopathology
    • Corazza N, Kassahn D, Jakob S, Badmann A, Brunner T. TRAIL-induced apoptosis: between tumor therapy and immunopathology. Ann N Y Acad Sci (2009) 1171:50-8. doi:10.1111/j.1749-6632.2009.04905.x
    • (2009) Ann N Y Acad Sci , vol.1171 , pp. 50-58
    • Corazza, N.1    Kassahn, D.2    Jakob, S.3    Badmann, A.4    Brunner, T.5
  • 27
    • 0034732258 scopus 로고    scopus 로고
    • Wild-type p53 transactivates the KILLER/DR5 gene through an intronic sequence-specific DNA-binding site
    • Takimoto R, El-Deiry WS. Wild-type p53 transactivates the KILLER/DR5 gene through an intronic sequence-specific DNA-binding site. Oncogene (2000) 19(14):1735-43. doi:10.1038/sj.onc.1203489
    • (2000) Oncogene , vol.19 , Issue.14 , pp. 1735-1743
    • Takimoto, R.1    El-Deiry, W.S.2
  • 28
    • 84880316942 scopus 로고    scopus 로고
    • The dark side of TRAIL signaling
    • Fulda S. The dark side of TRAIL signaling. Cell Death Differ (2013) 20(7):845-6. doi:10.1038/cdd.2013.36
    • (2013) Cell Death Differ , vol.20 , Issue.7 , pp. 845-846
    • Fulda, S.1
  • 29
    • 77956170550 scopus 로고    scopus 로고
    • New insights into apoptosis signaling by Apo2L/TRAIL
    • Gonzalvez F, Ashkenazi A. New insights into apoptosis signaling by Apo2L/TRAIL. Oncogene (2013) 29(34):4752-65. doi:10.1038/onc.2010.221
    • (2013) Oncogene , vol.29 , Issue.34 , pp. 4752-4765
    • Gonzalvez, F.1    Ashkenazi, A.2
  • 30
    • 84865308642 scopus 로고    scopus 로고
    • TRAIL receptor signaling and therapeutic option in bone tumors: the trap of the bone microenvironment
    • Picarda G, Trichet V, Teletchea S, Heymann D, Redini F. TRAIL receptor signaling and therapeutic option in bone tumors: the trap of the bone microenvironment. Am J Cancer Res (2012) 2(1):45-64.
    • (2012) Am J Cancer Res , vol.2 , Issue.1 , pp. 45-64
    • Picarda, G.1    Trichet, V.2    Teletchea, S.3    Heymann, D.4    Redini, F.5
  • 31
    • 34948894931 scopus 로고    scopus 로고
    • Death-receptor O-glycosylation controls tumor-cell sensitivity to the proapoptotic ligand Apo2L/TRAIL
    • Wagner KW, Punnoose EA, Januario T, Lawrence DA, Pitti RM, Lancaster K, et al. Death-receptor O-glycosylation controls tumor-cell sensitivity to the proapoptotic ligand Apo2L/TRAIL. Nat Med (2007) 13(9):1070-7. doi:10.1038/nm1627
    • (2007) Nat Med , vol.13 , Issue.9 , pp. 1070-1077
    • Wagner, K.W.1    Punnoose, E.A.2    Januario, T.3    Lawrence, D.A.4    Pitti, R.M.5    Lancaster, K.6
  • 32
    • 0035735753 scopus 로고    scopus 로고
    • Potential and caveats of TRAIL in cancer therapy
    • Held J, Schulze-Osthoff K. Potential and caveats of TRAIL in cancer therapy. Drug Resist Updat (2001) 4(4):243-52. doi:10.1054/drup.2001.0208
    • (2001) Drug Resist Updat , vol.4 , Issue.4 , pp. 243-252
    • Held, J.1    Schulze-Osthoff, K.2
  • 33
    • 54249107246 scopus 로고    scopus 로고
    • The promise of cancer therapeutics targeting the TNF-related apoptosis-inducing ligand and TRAIL receptor pathway
    • Wang S. The promise of cancer therapeutics targeting the TNF-related apoptosis-inducing ligand and TRAIL receptor pathway. Oncogene (2008) 27(48):6207-15. doi:10.1038/onc.2008.298
    • (2008) Oncogene , vol.27 , Issue.48 , pp. 6207-6215
    • Wang, S.1
  • 34
    • 0036547417 scopus 로고    scopus 로고
    • Death and anti-death: tumour resistance to apoptosis
    • Igney FH, Krammer PH. Death and anti-death: tumour resistance to apoptosis. Nat Rev Cancer (2002) 2(4):277-88. doi:10.1038/nrc776
    • (2002) Nat Rev Cancer , vol.2 , Issue.4 , pp. 277-288
    • Igney, F.H.1    Krammer, P.H.2
  • 35
    • 0033662433 scopus 로고    scopus 로고
    • Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5
    • Kischkel FC, Lawrence DA, Chuntharapai A, Schow P, Kim KJ, Ashkenazi A. Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity (2000) 12(6):611-20. doi:10.1016/S1074-7613(00)80212-5
    • (2000) Immunity , vol.12 , Issue.6 , pp. 611-620
    • Kischkel, F.C.1    Lawrence, D.A.2    Chuntharapai, A.3    Schow, P.4    Kim, K.J.5    Ashkenazi, A.6
  • 36
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell (1998) 94(4):491-501. doi:10.1016/S0092-8674(00)81590-1
    • (1998) Cell , vol.94 , Issue.4 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 37
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell (1998) 94(4):481-90. doi:10.1016/S0092-8674(00)81589-5
    • (1998) Cell , vol.94 , Issue.4 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 38
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell (2000) 102(1):33-42. doi:10.1016/S0092-8674(00)00008-8
    • (2000) Cell , vol.102 , Issue.1 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 39
    • 17644378775 scopus 로고    scopus 로고
    • c-FLIPR, a new regulator of death receptor-induced apoptosis
    • Golks A, Brenner D, Fritsch C, Krammer PH, Lavrik IN. c-FLIPR, a new regulator of death receptor-induced apoptosis. J Biol Chem (2005) 280(15):14507-13. doi:10.1074/jbc.M414425200
    • (2005) J Biol Chem , vol.280 , Issue.15 , pp. 14507-14513
    • Golks, A.1    Brenner, D.2    Fritsch, C.3    Krammer, P.H.4    Lavrik, I.N.5
  • 40
    • 71749102407 scopus 로고    scopus 로고
    • TNF-related apoptosis-inducing ligand (TRAIL): a new path to anti-cancer therapies
    • Holoch PA, Griffith TS. TNF-related apoptosis-inducing ligand (TRAIL): a new path to anti-cancer therapies. Eur J Pharmacol (2009) 625(1-3):63-72. doi:10.1016/j.ejphar.2009.06.066
    • (2009) Eur J Pharmacol , vol.625 , Issue.1-3 , pp. 63-72
    • Holoch, P.A.1    Griffith, T.S.2
  • 41
    • 84864318803 scopus 로고    scopus 로고
    • A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death
    • Dickens LS, Boyd RS, Jukes-Jones R, Hughes MA, Robinson GL, Fairall L, et al. A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death. Mol Cell (2012) 47(2):291-305. doi:10.1016/j.molcel.2012.05.004
    • (2012) Mol Cell , vol.47 , Issue.2 , pp. 291-305
    • Dickens, L.S.1    Boyd, R.S.2    Jukes-Jones, R.3    Hughes, M.A.4    Robinson, G.L.5    Fairall, L.6
  • 42
    • 79959736864 scopus 로고    scopus 로고
    • Targeting the anti-apoptotic protein c-FLIP for cancer therapy
    • Safa AR, Pollok KE. Targeting the anti-apoptotic protein c-FLIP for cancer therapy. Cancers (Basel) (2011) 3(2):1639-71. doi:10.3390/cancers3021639
    • (2011) Cancers (Basel) , vol.3 , Issue.2 , pp. 1639-1671
    • Safa, A.R.1    Pollok, K.E.2
  • 43
    • 73749083635 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein (c-FLIP) signalling: a key regulator of receptor-mediated apoptosis in physiologic context and in cancer
    • Bagnoli M, Canevari S, Mezzanzanica D. Cellular FLICE-inhibitory protein (c-FLIP) signalling: a key regulator of receptor-mediated apoptosis in physiologic context and in cancer. Int J Biochem Cell Biol (2010) 42(2):210-3. doi:10.1016/j.biocel.2009.11.015
    • (2010) Int J Biochem Cell Biol , vol.42 , Issue.2 , pp. 210-213
    • Bagnoli, M.1    Canevari, S.2    Mezzanzanica, D.3
  • 44
    • 84872480731 scopus 로고    scopus 로고
    • c-FLIP, a master anti-apoptotic regulator
    • Safa AR. c-FLIP, a master anti-apoptotic regulator. Exp Oncol (2012) 34(3):176-84.
    • (2012) Exp Oncol , vol.34 , Issue.3 , pp. 176-184
    • Safa, A.R.1
  • 45
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover
    • Chang L, Kamata H, Solinas G, Luo JL, Maeda S, Venuprasad K, et al. The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover. Cell (2006) 124(3):601-13. doi:10.1016/j.cell.2006.01.021
    • (2006) Cell , vol.124 , Issue.3 , pp. 601-613
    • Chang, L.1    Kamata, H.2    Solinas, G.3    Luo, J.L.4    Maeda, S.5    Venuprasad, K.6
  • 46
    • 45349102347 scopus 로고    scopus 로고
    • Calmodulin binding to cellular FLICE-like inhibitory protein modulates Fas-induced signalling
    • Pawar PS, Micoli KJ, Ding H, Cook WJ, Kappes JC, Chen Y, et al. Calmodulin binding to cellular FLICE-like inhibitory protein modulates Fas-induced signalling. Biochem J (2008) 412(3):459-68. doi:10.1042/BJ20071507
    • (2008) Biochem J , vol.412 , Issue.3 , pp. 459-468
    • Pawar, P.S.1    Micoli, K.J.2    Ding, H.3    Cook, W.J.4    Kappes, J.C.5    Chen, Y.6
  • 47
    • 84863938860 scopus 로고    scopus 로고
    • Elevation of c-FLIP in castrate-resistant prostate cancer antagonizes therapeutic response to androgen receptor-targeted therapy
    • McCourt C, Maxwell P, Mazzucchelli R, Montironi R, Scarpelli M, Salto-Tellez M, et al. Elevation of c-FLIP in castrate-resistant prostate cancer antagonizes therapeutic response to androgen receptor-targeted therapy. Clin Cancer Res (2012) 18(14):3822-33. doi:10.1158/1078-0432.CCR-11-3277
    • (2012) Clin Cancer Res , vol.18 , Issue.14 , pp. 3822-3833
    • McCourt, C.1    Maxwell, P.2    Mazzucchelli, R.3    Montironi, R.4    Scarpelli, M.5    Salto-Tellez, M.6
  • 48
    • 78349305676 scopus 로고    scopus 로고
    • c-FLIPL enhances anti-apoptotic Akt functions by modulation of Gsk3beta activity
    • Quintavalle C, Incoronato M, Puca L, Acunzo M, Zanca C, Romano G, et al. c-FLIPL enhances anti-apoptotic Akt functions by modulation of Gsk3beta activity. Cell Death Differ (2010) 17(12):1908-16. doi:10.1038/cdd.2010.65
    • (2010) Cell Death Differ , vol.17 , Issue.12 , pp. 1908-1916
    • Quintavalle, C.1    Incoronato, M.2    Puca, L.3    Acunzo, M.4    Zanca, C.5    Romano, G.6
  • 49
    • 66249136447 scopus 로고    scopus 로고
    • Non-genetic origins of cell-to-cell variability in TRAIL-induced apoptosis
    • Spencer SL, Gaudet S, Albeck JG, Burke JM, Sorger PK. Non-genetic origins of cell-to-cell variability in TRAIL-induced apoptosis. Nature (2009) 459(7245):428-32. doi:10.1038/nature08012
    • (2009) Nature , vol.459 , Issue.7245 , pp. 428-432
    • Spencer, S.L.1    Gaudet, S.2    Albeck, J.G.3    Burke, J.M.4    Sorger, P.K.5
  • 50
    • 34548052424 scopus 로고    scopus 로고
    • Translation matters: protein synthesis defects in inherited disease
    • Scheper GC, van der Knaap MS, Proud CG. Translation matters: protein synthesis defects in inherited disease. Nat Rev Genet (2007) 8(9):711-23. doi:10.1038/nrg2142
    • (2007) Nat Rev Genet , vol.8 , Issue.9 , pp. 711-723
    • Scheper, G.C.1    van der Knaap, M.S.2    Proud, C.G.3
  • 51
    • 0036021444 scopus 로고    scopus 로고
    • Emerging links between initiation of translation and human diseases
    • Kozak M. Emerging links between initiation of translation and human diseases. Mamm Genome (2002) 13(8):401-10. doi:10.1007/s00335-002-4002-5
    • (2002) Mamm Genome , vol.13 , Issue.8 , pp. 401-410
    • Kozak, M.1
  • 52
    • 34848916373 scopus 로고    scopus 로고
    • Taking aim at translation for tumor therapy
    • Barnhart BC, Simon MC. Taking aim at translation for tumor therapy. J Clin Invest (2007) 117(9):2385-8. doi:10.1172/JCI33107
    • (2007) J Clin Invest , vol.117 , Issue.9 , pp. 2385-2388
    • Barnhart, B.C.1    Simon, M.C.2
  • 53
    • 2542506326 scopus 로고    scopus 로고
    • The mRNA cap-binding protein eIF4E in post-transcriptional gene expression
    • von der Haar T, Gross JD, Wagner G, McCarthy JE. The mRNA cap-binding protein eIF4E in post-transcriptional gene expression. Nat Struct Mol Biol (2004) 11(6):503-11. doi:10.1038/nsmb779
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.6 , pp. 503-511
    • von der Haar, T.1    Gross, J.D.2    Wagner, G.3    McCarthy, J.E.4
  • 54
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter JD, Sonenberg N. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature (2005) 433(7025):477-80. doi:10.1038/nature03205
    • (2005) Nature , vol.433 , Issue.7025 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 55
    • 38849180436 scopus 로고    scopus 로고
    • Targeting the eukaryotic translation initiation factor 4E for cancer therapy
    • Graff JR, Konicek BW, Carter JH, Marcusson EG. Targeting the eukaryotic translation initiation factor 4E for cancer therapy. Cancer Res (2008) 68(3):631-4. doi:10.1158/0008-5472.CAN-07-5635
    • (2008) Cancer Res , vol.68 , Issue.3 , pp. 631-634
    • Graff, J.R.1    Konicek, B.W.2    Carter, J.H.3    Marcusson, E.G.4
  • 56
    • 77951671938 scopus 로고    scopus 로고
    • The eIF4E/eIF4G interaction inhibitor 4EGI-1 augments TRAIL-mediated apoptosis through c-FLIP Down-regulation and DR5 induction independent of inhibition of cap-dependent protein translation
    • Fan S, Li Y, Yue P, Khuri FR, Sun SY. The eIF4E/eIF4G interaction inhibitor 4EGI-1 augments TRAIL-mediated apoptosis through c-FLIP Down-regulation and DR5 induction independent of inhibition of cap-dependent protein translation. Neoplasia (2010) 12(4):346-56. doi:10.1593/neo.10144
    • (2010) Neoplasia , vol.12 , Issue.4 , pp. 346-356
    • Fan, S.1    Li, Y.2    Yue, P.3    Khuri, F.R.4    Sun, S.Y.5
  • 57
    • 0035525733 scopus 로고    scopus 로고
    • Cellular stress response and apoptosis in cancer therapy
    • Herr I, Debatin KM. Cellular stress response and apoptosis in cancer therapy. Blood (2001) 98(9):2603-14. doi:10.1182/blood.V98.9.2603
    • (2001) Blood , vol.98 , Issue.9 , pp. 2603-2614
    • Herr, I.1    Debatin, K.M.2
  • 58
    • 5644258322 scopus 로고    scopus 로고
    • c-Jun NH2-terminal kinase-mediated up-regulation of death receptor 5 contributes to induction of apoptosis by the novel synthetic triterpenoid methyl-2-cyano-3,12-dioxooleana-1, 9-dien-28-oate in human lung cancer cells
    • Zou W, Liu X, Yue P, Zhou Z, Sporn MB, Lotan R, et al. c-Jun NH2-terminal kinase-mediated up-regulation of death receptor 5 contributes to induction of apoptosis by the novel synthetic triterpenoid methyl-2-cyano-3,12-dioxooleana-1, 9-dien-28-oate in human lung cancer cells. Cancer Res (2004) 64(20):7570-8. doi:10.1158/0008-5472.CAN-04-1238
    • (2004) Cancer Res , vol.64 , Issue.20 , pp. 7570-7578
    • Zou, W.1    Liu, X.2    Yue, P.3    Zhou, Z.4    Sporn, M.B.5    Lotan, R.6
  • 59
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities
    • Kim I, Xu W, Reed JC. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat Rev Drug Discov (2008) 7(12):1013-30. doi:10.1038/nrd2755
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.12 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 60
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E, Logue SE, Gorman AM, Samali A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep (2006) 7(9):880-5. doi:10.1038/sj.embor.7400779
    • (2006) EMBO Rep , vol.7 , Issue.9 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 61
    • 0037133929 scopus 로고    scopus 로고
    • Sustained ER Ca2+ depletion suppresses protein synthesis and induces activation-enhanced cell d13eath in mast cells
    • Soboloff J, Berger SA. Sustained ER Ca2+ depletion suppresses protein synthesis and induces activation-enhanced cell death in mast cells. J Biol Chem (2002) 277(16):13812-20. doi:10.1074/jbc.M112129200
    • (2002) J Biol Chem , vol.277 , Issue.16 , pp. 13812-13820
    • Soboloff, J.1    Berger, S.A.2
  • 62
    • 79251525523 scopus 로고    scopus 로고
    • Measuring ER stress and the unfolded protein response using mammalian tissue culture system
    • Oslowski CM, Urano F. Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol (2011) 490:71-92. doi:10.1016/B978-0-12-385114-7.00004-0
    • (2011) Methods Enzymol , vol.490 , pp. 71-92
    • Oslowski, C.M.1    Urano, F.2
  • 63
    • 34347218245 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced death of mouse embryonic fibroblasts requires the intrinsic pathway of apoptosis
    • Masud A, Mohapatra A, Lakhani SA, Ferrandino A, Hakem R, Flavell RA. Endoplasmic reticulum stress-induced death of mouse embryonic fibroblasts requires the intrinsic pathway of apoptosis. J Biol Chem (2007) 282(19):14132-9. doi:10.1074/jbc.M700077200
    • (2007) J Biol Chem , vol.282 , Issue.19 , pp. 14132-14139
    • Masud, A.1    Mohapatra, A.2    Lakhani, S.A.3    Ferrandino, A.4    Hakem, R.5    Flavell, R.A.6
  • 64
    • 18344384228 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium pool depletion-induced apoptosis is coupled with activation of the death receptor 5 pathway
    • He Q, Lee DI, Rong R, Yu M, Luo X, Klein M, et al. Endoplasmic reticulum calcium pool depletion-induced apoptosis is coupled with activation of the death receptor 5 pathway. Oncogene (2002) 21(17):2623-33. doi:10.1038/sj.onc.1205345
    • (2002) Oncogene , vol.21 , Issue.17 , pp. 2623-2633
    • He, Q.1    Lee, D.I.2    Rong, R.3    Yu, M.4    Luo, X.5    Klein, M.6
  • 65
    • 22244472001 scopus 로고    scopus 로고
    • Tunicamycin enhances tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human prostate cancer cells
    • Shiraishi T, Yoshida T, Nakata S, Horinaka M, Wakada M, Mizutani Y, et al. Tunicamycin enhances tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human prostate cancer cells. Cancer Res (2005) 65(14):6364-70. doi:10.1158/0008-5472.CAN-05-0312
    • (2005) Cancer Res , vol.65 , Issue.14 , pp. 6364-6370
    • Shiraishi, T.1    Yoshida, T.2    Nakata, S.3    Horinaka, M.4    Wakada, M.5    Mizutani, Y.6
  • 66
    • 74049087498 scopus 로고    scopus 로고
    • 2-Deoxy-D-glucose enhances TRAIL-induced apoptosis in human melanoma cells through XBP-1-mediated up-regulation of TRAIL-R2
    • Liu H, Jiang CC, Lavis CJ, Croft A, Dong L, Tseng HY, et al. 2-Deoxy-D-glucose enhances TRAIL-induced apoptosis in human melanoma cells through XBP-1-mediated up-regulation of TRAIL-R2. Mol Cancer (2009) 8:122. doi:10.1186/1476-4598-8-122
    • (2009) Mol Cancer , vol.8 , pp. 122
    • Liu, H.1    Jiang, C.C.2    Lavis, C.J.3    Croft, A.4    Dong, L.5    Tseng, H.Y.6
  • 67
    • 84896740664 scopus 로고    scopus 로고
    • Inhibition of eIF2alpha dephosphorylation enhances TRAIL-induced apoptosis in hepatoma cells
    • Teng Y, Gao M, Wang J, Kong Q, Hua H, Luo T, et al. Inhibition of eIF2alpha dephosphorylation enhances TRAIL-induced apoptosis in hepatoma cells. Cell Death Dis (2014) 5:e1060. doi:10.1038/cddis.2014.24
    • (2014) Cell Death Dis , vol.5
    • Teng, Y.1    Gao, M.2    Wang, J.3    Kong, Q.4    Hua, H.5    Luo, T.6
  • 68
    • 67650632688 scopus 로고    scopus 로고
    • The tumor suppressor Par-4 activates an extrinsic pathway for apoptosis
    • Burikhanov R, Zhao Y, Goswami A, Qiu S, Schwarze SR, Rangnekar VM. The tumor suppressor Par-4 activates an extrinsic pathway for apoptosis. Cell (2009) 138(2):377-88. doi:10.1016/j.cell.2009.05.022
    • (2009) Cell , vol.138 , Issue.2 , pp. 377-388
    • Burikhanov, R.1    Zhao, Y.2    Goswami, A.3    Qiu, S.4    Schwarze, S.R.5    Rangnekar, V.M.6
  • 69
    • 33645294370 scopus 로고    scopus 로고
    • 3,3'-diindolylmethane (DIM) and its derivatives induce apoptosis in pancreatic cancer cells through endoplasmic reticulum stress-dependent upregulation of DR5
    • Abdelrahim M, Newman K, Vanderlaag K, Samudio I, Safe S. 3,3'-diindolylmethane (DIM) and its derivatives induce apoptosis in pancreatic cancer cells through endoplasmic reticulum stress-dependent upregulation of DR5. Carcinogenesis (2006) 27(4):717-28. doi:10.1093/carcin/bgi270
    • (2006) Carcinogenesis , vol.27 , Issue.4 , pp. 717-728
    • Abdelrahim, M.1    Newman, K.2    Vanderlaag, K.3    Samudio, I.4    Safe, S.5
  • 70
    • 84862502203 scopus 로고    scopus 로고
    • ER stress sensitizes cells to TRAIL through down-regulation of FLIP and Mcl-1 and PERK-dependent up-regulation of TRAIL-R2
    • Martin-Perez R, Niwa M, Lopez-Rivas A. ER stress sensitizes cells to TRAIL through down-regulation of FLIP and Mcl-1 and PERK-dependent up-regulation of TRAIL-R2. Apoptosis (2012) 17(4):349-63. doi:10.1007/s10495-011-0673-2
    • (2012) Apoptosis , vol.17 , Issue.4 , pp. 349-363
    • Martin-Perez, R.1    Niwa, M.2    Lopez-Rivas, A.3
  • 71
    • 77955643939 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress in alpha-TEA mediated TRAIL/DR5 death receptor dependent apoptosis
    • Tiwary R, Yu W, Li J, Park SK, Sanders BG, Kline K. Role of endoplasmic reticulum stress in alpha-TEA mediated TRAIL/DR5 death receptor dependent apoptosis. PLoS One (2010) 5(7):e11865. doi:10.1371/journal.pone.0011865
    • (2010) PLoS One , vol.5 , Issue.7
    • Tiwary, R.1    Yu, W.2    Li, J.3    Park, S.K.4    Sanders, B.G.5    Kline, K.6
  • 72
    • 84869799967 scopus 로고    scopus 로고
    • Diallyl trisulfide sensitizes human melanoma cells to TRAIL-induced cell death by promoting endoplasmic reticulum-mediated apoptosis
    • Murai M, Inoue T, Suzuki-Karasaki M, Ochiai T, Ra C, Nishida S, et al. Diallyl trisulfide sensitizes human melanoma cells to TRAIL-induced cell death by promoting endoplasmic reticulum-mediated apoptosis. Int J Oncol (2012) 41(6):2029-37. doi:10.3892/ijo.2012.1656
    • (2012) Int J Oncol , vol.41 , Issue.6 , pp. 2029-2037
    • Murai, M.1    Inoue, T.2    Suzuki-Karasaki, M.3    Ochiai, T.4    Ra, C.5    Nishida, S.6
  • 73
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • Zhang HG, Wang J, Yang X, Hsu HC, Mountz JD. Regulation of apoptosis proteins in cancer cells by ubiquitin. Oncogene (2004) 23(11):2009-15. doi:10.1038/sj.onc.1207373
    • (2004) Oncogene , vol.23 , Issue.11 , pp. 2009-2015
    • Zhang, H.G.1    Wang, J.2    Yang, X.3    Hsu, H.C.4    Mountz, J.D.5
  • 74
    • 0036483901 scopus 로고    scopus 로고
    • Deadly encounter: ubiquitin meets apoptosis
    • Jesenberger V, Jentsch S. Deadly encounter: ubiquitin meets apoptosis. Nat Rev Mol Cell Biol (2002) 3(2):112-21. doi:10.1038/nrm731
    • (2002) Nat Rev Mol Cell Biol , vol.3 , Issue.2 , pp. 112-121
    • Jesenberger, V.1    Jentsch, S.2
  • 75
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer (2004) 4(5):349-60. doi:10.1371/journal.pone.0084248
    • (2004) Nat Rev Cancer , vol.4 , Issue.5 , pp. 349-360
    • Adams, J.1
  • 76
    • 0037305877 scopus 로고    scopus 로고
    • Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation
    • Leverkus M, Sprick MR, Wachter T, Mengling T, Baumann B, Serfling E, et al. Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation. Mol Cell Biol (2003) 23(3):777-90. doi:10.1128/MCB.23.3.777-790.2003
    • (2003) Mol Cell Biol , vol.23 , Issue.3 , pp. 777-790
    • Leverkus, M.1    Sprick, M.R.2    Wachter, T.3    Mengling, T.4    Baumann, B.5    Serfling, E.6
  • 77
    • 0043287140 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 overcomes TRAIL resistance in Bax and caspase 9-negative or Bcl-xL overexpressing cells
    • Johnson TR, Stone K, Nikrad M, Yeh T, Zong WX, Thompson CB, et al. The proteasome inhibitor PS-341 overcomes TRAIL resistance in Bax and caspase 9-negative or Bcl-xL overexpressing cells. Oncogene (2003) 22(32):4953-63. doi:10.1038/sj.onc.1206656
    • (2003) Oncogene , vol.22 , Issue.32 , pp. 4953-4963
    • Johnson, T.R.1    Stone, K.2    Nikrad, M.3    Yeh, T.4    Zong, W.X.5    Thompson, C.B.6
  • 78
    • 1942436864 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 upregulates death receptor 5 and cooperates with Apo2L/TRAIL to induce apoptosis in Bax-proficient and -deficient cells
    • He Q, Huang Y, Sheikh MS. Proteasome inhibitor MG132 upregulates death receptor 5 and cooperates with Apo2L/TRAIL to induce apoptosis in Bax-proficient and -deficient cells. Oncogene (2004) 23(14):2554-8. doi:10.1038/sj.onc.1207351
    • (2004) Oncogene , vol.23 , Issue.14 , pp. 2554-2558
    • He, Q.1    Huang, Y.2    Sheikh, M.S.3
  • 79
    • 49849096091 scopus 로고    scopus 로고
    • Antitumor activity of bortezomib alone and in combination with TRAIL in human acute myeloid leukemia
    • Conticello C, Adamo L, Vicari L, Giuffrida R, Iannolo G, Anastasi G, et al. Antitumor activity of bortezomib alone and in combination with TRAIL in human acute myeloid leukemia. Acta Haematol (2008) 120(1):19-30. doi:10.1159/000151511
    • (2008) Acta Haematol , vol.120 , Issue.1 , pp. 19-30
    • Conticello, C.1    Adamo, L.2    Vicari, L.3    Giuffrida, R.4    Iannolo, G.5    Anastasi, G.6
  • 80
    • 34447294826 scopus 로고    scopus 로고
    • TRAIL therapy in non-small cell lung cancer cells: sensitization to death receptor-mediated apoptosis by proteasome inhibitor bortezomib
    • Voortman J, Resende TP, Abou El Hassan MA, Giaccone G, Kruyt FA. TRAIL therapy in non-small cell lung cancer cells: sensitization to death receptor-mediated apoptosis by proteasome inhibitor bortezomib. Mol Cancer Ther (2007) 6(7):2103-12. doi:10.1158/1535-7163.MCT-07-0167
    • (2007) Mol Cancer Ther , vol.6 , Issue.7 , pp. 2103-2112
    • Voortman, J.1    Resende, T.P.2    Abou El Hassan, M.A.3    Giaccone, G.4    Kruyt, F.A.5
  • 81
    • 84880910575 scopus 로고    scopus 로고
    • A novel inhibitor of proteasome deubiquitinating activity renders tumor cells sensitive to TRAIL-mediated apoptosis by natural killer cells and T cells
    • Sarhan D, Wennerberg E, D'Arcy P, Gurajada D, Linder S, Lundqvist A. A novel inhibitor of proteasome deubiquitinating activity renders tumor cells sensitive to TRAIL-mediated apoptosis by natural killer cells and T cells. Cancer Immunol Immunother (2013) 62(8):1359-68. doi:10.1007/s00262-013-1439-1
    • (2013) Cancer Immunol Immunother , vol.62 , Issue.8 , pp. 1359-1368
    • Sarhan, D.1    Wennerberg, E.2    D'Arcy, P.3    Gurajada, D.4    Linder, S.5    Lundqvist, A.6
  • 82
    • 44449107683 scopus 로고    scopus 로고
    • Inhibition of Yin Yang 1-dependent repressor activity of DR5 transcription and expression by the novel proteasome inhibitor NPI-0052 contributes to its TRAIL-enhanced apoptosis in cancer cells
    • Baritaki S, Suzuki E, Umezawa K, Spandidos DA, Berenson J, Daniels TR, et al. Inhibition of Yin Yang 1-dependent repressor activity of DR5 transcription and expression by the novel proteasome inhibitor NPI-0052 contributes to its TRAIL-enhanced apoptosis in cancer cells. J Immunol (2008) 180(9):6199-210. doi:10.4049/jimmunol.180.9.6199
    • (2008) J Immunol , vol.180 , Issue.9 , pp. 6199-6210
    • Baritaki, S.1    Suzuki, E.2    Umezawa, K.3    Spandidos, D.A.4    Berenson, J.5    Daniels, T.R.6
  • 83
    • 33646112384 scopus 로고    scopus 로고
    • Proteasome inhibition sensitizes hepatocellular carcinoma cells to TRAIL by suppressing caspase inhibitors and AKT pathway
    • Inoue T, Shiraki K, Fuke H, Yamanaka Y, Miyashita K, Yamaguchi Y, et al. Proteasome inhibition sensitizes hepatocellular carcinoma cells to TRAIL by suppressing caspase inhibitors and AKT pathway. Anticancer Drugs (2006) 17(3):261-8. doi:10.1097/00001813-200603000-00004
    • (2006) Anticancer Drugs , vol.17 , Issue.3 , pp. 261-268
    • Inoue, T.1    Shiraki, K.2    Fuke, H.3    Yamanaka, Y.4    Miyashita, K.5    Yamaguchi, Y.6
  • 84
  • 85
    • 13344278692 scopus 로고    scopus 로고
    • Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes
    • Liston P, Roy N, Tamai K, Lefebvre C, Baird S, Cherton-Horvat G, et al. Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes. Nature (1996) 379(6563):349-53. doi:10.1038/379349a0
    • (1996) Nature , vol.379 , Issue.6563 , pp. 349-353
    • Liston, P.1    Roy, N.2    Tamai, K.3    Lefebvre, C.4    Baird, S.5    Cherton-Horvat, G.6
  • 86
    • 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(3):169-77. doi:10.1038/sj.cr.7290046
    • (2000) Cell Res , vol.10 , Issue.3 , pp. 169-177
    • Yang, Y.L.1    Li, X.M.2
  • 87
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • Suzuki Y, Nakabayashi Y, Takahashi R. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. Proc Natl Acad Sci U S A (2001) 98(15):8662-7. doi:10.1073/pnas.161506698
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.15 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 88
    • 84875165367 scopus 로고    scopus 로고
    • TRAIL and proteasome inhibitors combination induces a robust apoptosis in human malignant pleural mesothelioma cells through Mcl-1 and Akt protein cleavages
    • Yuan BZ, Chapman J, Ding M, Wang J, Jiang B, Rojanasakul Y, et al. TRAIL and proteasome inhibitors combination induces a robust apoptosis in human malignant pleural mesothelioma cells through Mcl-1 and Akt protein cleavages. BMC Cancer (2013) 13:140. doi:10.1186/1471-2407-13-140
    • (2013) BMC Cancer , vol.13 , pp. 140
    • Yuan, B.Z.1    Chapman, J.2    Ding, M.3    Wang, J.4    Jiang, B.5    Rojanasakul, Y.6
  • 89
    • 84926212187 scopus 로고    scopus 로고
    • Bortezomib sensitises TRAIL-resistant HPV-positive head and neck cancer cells to TRAIL through a caspase-dependent, E6-independent mechanism
    • Bullenkamp J, Raulf N, Ayaz B, Walczak H, Kulms D, Odell E, et al. Bortezomib sensitises TRAIL-resistant HPV-positive head and neck cancer cells to TRAIL through a caspase-dependent, E6-independent mechanism. Cell Death Dis (2014) 5:e1489. doi:10.1038/cddis.2014.455
    • (2014) Cell Death Dis , vol.5
    • Bullenkamp, J.1    Raulf, N.2    Ayaz, B.3    Walczak, H.4    Kulms, D.5    Odell, E.6
  • 91
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science (2002) 295(5561):1852-8. doi:10.1126/science.1068408
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 92
    • 0031297298 scopus 로고    scopus 로고
    • The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones
    • Morimoto RI, Kline MP, Bimston DN, Cotto JJ. The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem (1997) 32:17-29.
    • (1997) Essays Biochem , vol.32 , pp. 17-29
    • Morimoto, R.I.1    Kline, M.P.2    Bimston, D.N.3    Cotto, J.J.4
  • 93
    • 35148854097 scopus 로고    scopus 로고
    • Heat shock protein 90alpha recruits FLIPS to the death-inducing signaling complex and contributes to TRAIL resistance in human glioma
    • Panner A, Murray JC, Berger MS, Pieper RO. Heat shock protein 90alpha recruits FLIPS to the death-inducing signaling complex and contributes to TRAIL resistance in human glioma. Cancer Res (2007) 67(19):9482-9. doi:10.1158/0008-5472.CAN-07-0569
    • (2007) Cancer Res , vol.67 , Issue.19 , pp. 9482-9489
    • Panner, A.1    Murray, J.C.2    Berger, M.S.3    Pieper, R.O.4
  • 94
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J. Protein folding in the cell. Nature (1992) 355(6355):33-45. doi:10.1038/355033a0
    • (1992) Nature , vol.355 , Issue.6355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 95
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • Hightower LE. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell (1991) 66(2):191-7. doi:10.1016/0092-8674(91)90611-2
    • (1991) Cell , vol.66 , Issue.2 , pp. 191-197
    • Hightower, L.E.1
  • 97
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood) (2003) 228(2):111-33.
    • (2003) Exp Biol Med (Maywood) , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 98
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny MV, Toretsky J, Bohen S, Neckers L. Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc Natl Acad Sci U S A (1996) 93(16):8379-83. doi:10.1073/pnas.93.16.8379
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.16 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 99
    • 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, Mosser DD, Mahboubi A, Kuwana T, et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol (2000) 2(8):469-75. doi:10.1038/35019501
    • (2000) Nat Cell Biol , vol.2 , Issue.8 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3    Mosser, D.D.4    Mahboubi, A.5    Kuwana, T.6
  • 100
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • Pandey P, Saleh A, Nakazawa A, Kumar S, Srinivasula SM, Kumar V, et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J (2000) 19(16):4310-22. doi:10.1093/emboj/19.16.4310
    • (2000) EMBO J , vol.19 , Issue.16 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3    Kumar, S.4    Srinivasula, S.M.5    Kumar, V.6
  • 101
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells
    • Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J (1999) 18(8):2040-8. doi:10.1093/emboj/18.8.2040
    • (1999) EMBO J , vol.18 , Issue.8 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 102
    • 84858008290 scopus 로고    scopus 로고
    • Hsp90 inhibitors and drug resistance in cancer: the potential benefits of combination therapies of Hsp90 inhibitors and other anti-cancer drugs
    • Lu X, Xiao L, Wang L, Ruden DM. Hsp90 inhibitors and drug resistance in cancer: the potential benefits of combination therapies of Hsp90 inhibitors and other anti-cancer drugs. Biochem Pharmacol (2012) 83(8):995-1004. doi:10.1016/j.bcp.2011.11.011
    • (2012) Biochem Pharmacol , vol.83 , Issue.8 , pp. 995-1004
    • Lu, X.1    Xiao, L.2    Wang, L.3    Ruden, D.M.4
  • 103
    • 34548490977 scopus 로고    scopus 로고
    • Intratumor injection of the Hsp90 inhibitor 17AAG decreases tumor growth and induces apoptosis in a prostate cancer xenograft model
    • Williams CR, Tabios R, Linehan WM, Neckers L. Intratumor injection of the Hsp90 inhibitor 17AAG decreases tumor growth and induces apoptosis in a prostate cancer xenograft model. J Urol (2007) 178(4 Pt 1):1528-32. doi:10.1016/j.juro.2007.05.120
    • (2007) J Urol , vol.178 , Issue.4 , pp. 1528-1532
    • Williams, C.R.1    Tabios, R.2    Linehan, W.M.3    Neckers, L.4
  • 104
    • 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 RW, Kumar MV. Sensitization of TRAIL-resistant cells by inhibition of heat shock protein 90 with low-dose geldanamycin. Mol Cancer Ther (2006) 5(1):170-8. doi:10.1158/1535-7163.MCT-05-0129
    • (2006) Mol Cancer Ther , vol.5 , Issue.1 , pp. 170-178
    • Ma, Y.1    Lakshmikanthan, V.2    Lewis, R.W.3    Kumar, M.V.4
  • 105
    • 22144462525 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin overcomes TRAIL resistance in colon cancer cell lines
    • Vasilevskaya IA, O'Dwyer PJ. 17-Allylamino-17-demethoxygeldanamycin overcomes TRAIL resistance in colon cancer cell lines. Biochem Pharmacol (2005) 70(4):580-9. doi:10.1016/j.bcp.2005.05.018
    • (2005) Biochem Pharmacol , vol.70 , Issue.4 , pp. 580-589
    • Vasilevskaya, I.A.1    O'Dwyer, P.J.2
  • 106
    • 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 GV, Li Y, Rassidakis GZ, Martinez-Valdez H, Medeiros LJ, Younes A. 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 (2006) 12(2):584-90. doi:10.1158/1078-0432.CCR-05-1194
    • (2006) Clin Cancer Res , vol.12 , Issue.2 , pp. 584-590
    • Georgakis, G.V.1    Li, Y.2    Rassidakis, G.Z.3    Martinez-Valdez, H.4    Medeiros, L.J.5    Younes, A.6
  • 107
    • 84887437596 scopus 로고    scopus 로고
    • Autophagy and chemotherapy resistance: a promising therapeutic target for cancer treatment
    • Sui X, Chen R, Wang Z, Huang Z, Kong N, Zhang M, et al. Autophagy and chemotherapy resistance: a promising therapeutic target for cancer treatment. Cell Death Dis (2013) 4:e838. doi:10.1038/cddis.2013.350
    • (2013) Cell Death Dis , vol.4
    • Sui, X.1    Chen, R.2    Wang, Z.3    Huang, Z.4    Kong, N.5    Zhang, M.6
  • 108
    • 80052697287 scopus 로고    scopus 로고
    • The role of autophagy in cancer: therapeutic implications
    • Yang ZJ, Chee CE, Huang S, Sinicrope FA. The role of autophagy in cancer: therapeutic implications. Mol Cancer Ther (2011) 10(9):1533-41. doi:10.1158/1535-7163.MCT-11-0047
    • (2011) Mol Cancer Ther , vol.10 , Issue.9 , pp. 1533-1541
    • Yang, Z.J.1    Chee, C.E.2    Huang, S.3    Sinicrope, F.A.4
  • 109
    • 75349083568 scopus 로고    scopus 로고
    • Immunogenic cell death, DAMPs and anticancer therapeutics: an emerging amalgamation
    • Garg AD, Nowis D, Golab J, Vandenabeele P, Krysko DV, Agostinis P. Immunogenic cell death, DAMPs and anticancer therapeutics: an emerging amalgamation. Biochim Biophys Acta (2009) 1805(1):53-71. doi:10.1016/j.bbcan.2009.08.003
    • (2009) Biochim Biophys Acta , vol.1805 , Issue.1 , pp. 53-71
    • Garg, A.D.1    Nowis, D.2    Golab, J.3    Vandenabeele, P.4    Krysko, D.V.5    Agostinis, P.6
  • 110
    • 53549092494 scopus 로고    scopus 로고
    • Enhancement of tumor-TRAIL susceptibility by modulation of autophagy
    • Hou W, Han J, Lu C, Goldstein LA, Rabinowich H. Enhancement of tumor-TRAIL susceptibility by modulation of autophagy. Autophagy (2008) 4(7):940-3. doi:10.4161/auto.6769
    • (2008) Autophagy , vol.4 , Issue.7 , pp. 940-943
    • Hou, W.1    Han, J.2    Lu, C.3    Goldstein, L.A.4    Rabinowich, H.5
  • 111
    • 67349128584 scopus 로고    scopus 로고
    • Reactivation of death receptor 4 (DR4) expression sensitizes medulloblastoma cell lines to TRAIL
    • Aguilera DG, Das CM, Sinnappah-Kang ND, Joyce C, Taylor PH, Wen S, et al. Reactivation of death receptor 4 (DR4) expression sensitizes medulloblastoma cell lines to TRAIL. J Neurooncol (2009) 93(3):303-18. doi:10.1007/s11060-008-9788-x
    • (2009) J Neurooncol , vol.93 , Issue.3 , pp. 303-318
    • Aguilera, D.G.1    Das, C.M.2    Sinnappah-Kang, N.D.3    Joyce, C.4    Taylor, P.H.5    Wen, S.6
  • 112
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden JE, Peart MJ, Johnstone RW. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov (2006) 5(9):769-84. doi:10.1038/nrd2133
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 113
    • 40849139208 scopus 로고    scopus 로고
    • Epigenetics in cancer
    • Esteller M. Epigenetics in cancer. N Engl J Med (2008) 358(11):1148-59. doi:10.1056/NEJMra072067
    • (2008) N Engl J Med , vol.358 , Issue.11 , pp. 1148-1159
    • Esteller, M.1
  • 114
    • 0346333258 scopus 로고    scopus 로고
    • Loss of caspase-8 protein expression correlates with unfavorable survival outcome in childhood medulloblastoma
    • Pingoud-Meier C, Lang D, Janss AJ, Rorke LB, Phillips PC, Shalaby T, et al. Loss of caspase-8 protein expression correlates with unfavorable survival outcome in childhood medulloblastoma. Clin Cancer Res (2003) 9(17):6401-9.
    • (2003) Clin Cancer Res , vol.9 , Issue.17 , pp. 6401-6409
    • Pingoud-Meier, C.1    Lang, D.2    Janss, A.J.3    Rorke, L.B.4    Phillips, P.C.5    Shalaby, T.6
  • 115
    • 0036139396 scopus 로고    scopus 로고
    • Loss of caspase-8 mRNA expression is common in childhood primitive neuroectodermal brain tumour/medulloblastoma
    • Zuzak TJ, Steinhoff DF, Sutton LN, Phillips PC, Eggert A, Grotzer MA. Loss of caspase-8 mRNA expression is common in childhood primitive neuroectodermal brain tumour/medulloblastoma. Eur J Cancer (2002) 38(1):83-91. doi:10.1016/S0959-8049(01)00355-0
    • (2002) Eur J Cancer , vol.38 , Issue.1 , pp. 83-91
    • Zuzak, T.J.1    Steinhoff, D.F.2    Sutton, L.N.3    Phillips, P.C.4    Eggert, A.5    Grotzer, M.A.6
  • 116
    • 0035490840 scopus 로고    scopus 로고
    • Ex vivo pediatric brain tumors express Fas (CD95) and FasL (CD95L) and are resistant to apoptosis induction
    • Riffkin CD, Gray AZ, Hawkins CJ, Chow CW, Ashley DM. Ex vivo pediatric brain tumors express Fas (CD95) and FasL (CD95L) and are resistant to apoptosis induction. Neuro Oncol (2001) 3(4):229-40. doi:10.1215/15228517-3-4-229
    • (2001) Neuro Oncol , vol.3 , Issue.4 , pp. 229-240
    • Riffkin, C.D.1    Gray, A.Z.2    Hawkins, C.J.3    Chow, C.W.4    Ashley, D.M.5
  • 117
    • 25144489068 scopus 로고    scopus 로고
    • Overview of cell death signaling pathways
    • Jin Z, El-Deiry WS. Overview of cell death signaling pathways. Cancer Biol Ther (2005) 4(2):139-63. doi:10.4161/cbt.4.2.1508
    • (2005) Cancer Biol Ther , vol.4 , Issue.2 , pp. 139-163
    • Jin, Z.1    El-Deiry, W.S.2
  • 118
    • 85027932431 scopus 로고    scopus 로고
    • Verrucarin A sensitizes TRAIL-induced apoptosis via the upregulation of DR5 in an eIF2alpha/CHOP-dependent manner
    • Moon DO, Asami Y, Long H, Jang JH, Bae EY, Kim BY, et al. Verrucarin A sensitizes TRAIL-induced apoptosis via the upregulation of DR5 in an eIF2alpha/CHOP-dependent manner. Toxicol In vitro (2013) 27(1):257-63. doi:10.1016/j.tiv.2012.09.001
    • (2013) Toxicol In vitro , vol.27 , Issue.1 , pp. 257-263
    • Moon, D.O.1    Asami, Y.2    Long, H.3    Jang, J.H.4    Bae, E.Y.5    Kim, B.Y.6
  • 119
    • 84881531214 scopus 로고    scopus 로고
    • Monensin, a polyether ionophore antibiotic, overcomes TRAIL resistance in glioma cells via endoplasmic reticulum stress, DR5 upregulation and c-FLIP downregulation
    • Yoon MJ, Kang YJ, Kim IY, Kim EH, Lee JA, Lim JH, et al. Monensin, a polyether ionophore antibiotic, overcomes TRAIL resistance in glioma cells via endoplasmic reticulum stress, DR5 upregulation and c-FLIP downregulation. Carcinogenesis (2013) 34(8):1918-28. doi:10.1093/carcin/bgt137
    • (2013) Carcinogenesis , vol.34 , Issue.8 , pp. 1918-1928
    • Yoon, M.J.1    Kang, Y.J.2    Kim, I.Y.3    Kim, E.H.4    Lee, J.A.5    Lim, J.H.6
  • 120
    • 84928037433 scopus 로고    scopus 로고
    • Medicarpin, a legume phytoalexin sensitizes myeloid leukemia cells to TRAIL-induced apoptosis through the induction of DR5 and activation of the ROS-JNK-CHOP pathway
    • Trivedi R, Maurya R, Mishra DP. Medicarpin, a legume phytoalexin sensitizes myeloid leukemia cells to TRAIL-induced apoptosis through the induction of DR5 and activation of the ROS-JNK-CHOP pathway. Cell Death Dis (2014) 5:e1465. doi:10.1038/cddis.2014.429
    • (2014) Cell Death Dis , vol.5
    • Trivedi, R.1    Maurya, R.2    Mishra, D.P.3
  • 121
    • 84872602964 scopus 로고    scopus 로고
    • Oligomycin A enhances apoptotic effect of TRAIL through CHOP-mediated death receptor 5 expression
    • He L, Jang JH, Choi HG, Lee SM, Nan MH, Jeong SJ, et al. Oligomycin A enhances apoptotic effect of TRAIL through CHOP-mediated death receptor 5 expression. Mol Carcinog (2013) 52(2):85-93. doi:10.1002/mc.21831
    • (2013) Mol Carcinog , vol.52 , Issue.2 , pp. 85-93
    • He, L.1    Jang, J.H.2    Choi, H.G.3    Lee, S.M.4    Nan, M.H.5    Jeong, S.J.6
  • 122
    • 34250888209 scopus 로고    scopus 로고
    • Tunicamycin sensitizes human melanoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by up-regulation of TRAIL-R2 via the unfolded protein response
    • Jiang CC, Chen LH, Gillespie S, Kiejda KA, Mhaidat N, Wang YF, et al. Tunicamycin sensitizes human melanoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by up-regulation of TRAIL-R2 via the unfolded protein response. Cancer Res (2007) 67(12):5880-8. doi:10.1158/0008-5472.CAN-07-0213
    • (2007) Cancer Res , vol.67 , Issue.12 , pp. 5880-5888
    • Jiang, C.C.1    Chen, L.H.2    Gillespie, S.3    Kiejda, K.A.4    Mhaidat, N.5    Wang, Y.F.6
  • 123
    • 55749086991 scopus 로고    scopus 로고
    • 15-deoxy-Delta12,14-prostaglandin J2 up-regulates death receptor 5 gene expression in HCT116 cells: involvement of reactive oxygen species and C/EBP homologous transcription factor gene transcription
    • Su RY, Chi KH, Huang DY, Tai MH, Lin WW. 15-deoxy-Delta12,14-prostaglandin J2 up-regulates death receptor 5 gene expression in HCT116 cells: involvement of reactive oxygen species and C/EBP homologous transcription factor gene transcription. Mol Cancer Ther (2008) 7(10):3429-40. doi:10.1158/1535-7163.MCT-08-0498
    • (2008) Mol Cancer Ther , vol.7 , Issue.10 , pp. 3429-3440
    • Su, R.Y.1    Chi, K.H.2    Huang, D.Y.3    Tai, M.H.4    Lin, W.W.5
  • 124
    • 78751522712 scopus 로고    scopus 로고
    • ROS and CHOP are critical for dibenzylideneacetone to sensitize tumor cells to TRAIL through induction of death receptors and downregulation of cell survival proteins
    • Prasad S, Yadav VR, Ravindran J, Aggarwal BB. ROS and CHOP are critical for dibenzylideneacetone to sensitize tumor cells to TRAIL through induction of death receptors and downregulation of cell survival proteins. Cancer Res (2011) 71(2):538-49. doi:10.1158/0008-5472.CAN-10-3121
    • (2011) Cancer Res , vol.71 , Issue.2 , pp. 538-549
    • Prasad, S.1    Yadav, V.R.2    Ravindran, J.3    Aggarwal, B.B.4
  • 125
    • 84856753924 scopus 로고    scopus 로고
    • 5, 7-Dimethoxyflavone sensitizes TRAIL-induced apoptosis through DR5 upregulation in hepatocellular carcinoma cells
    • Yang JF, Cao JG, Tian L, Liu F. 5, 7-Dimethoxyflavone sensitizes TRAIL-induced apoptosis through DR5 upregulation in hepatocellular carcinoma cells. Cancer Chemother Pharmacol (2012) 69(1):195-206. doi:10.1007/s00280-011-1686-9
    • (2012) Cancer Chemother Pharmacol , vol.69 , Issue.1 , pp. 195-206
    • Yang, J.F.1    Cao, J.G.2    Tian, L.3    Liu, F.4
  • 126
    • 84892818305 scopus 로고    scopus 로고
    • Neobavaisoflavone sensitizes apoptosis via the inhibition of metastasis in TRAIL-resistant human glioma U373MG cells
    • Kim YJ, Choi WI, Ko H, So Y, Kang KS, Kim I, et al. Neobavaisoflavone sensitizes apoptosis via the inhibition of metastasis in TRAIL-resistant human glioma U373MG cells. Life Sci (2014) 95(2):101-7. doi:10.1016/j.lfs.2013.10.035
    • (2014) Life Sci , vol.95 , Issue.2 , pp. 101-107
    • Kim, Y.J.1    Choi, W.I.2    Ko, H.3    So, Y.4    Kang, K.S.5    Kim, I.6
  • 127
    • 79955017535 scopus 로고    scopus 로고
    • High susceptibility of metastatic cells derived from human prostate and colon cancer cells to TRAIL and sensitization of TRAIL-insensitive primary cells to TRAIL by 4,5-dimethoxy-2-nitrobenzaldehyde
    • Kim HB, Kim MJ, Kim DY, Lee JW, Bae JH, Kim DW, et al. High susceptibility of metastatic cells derived from human prostate and colon cancer cells to TRAIL and sensitization of TRAIL-insensitive primary cells to TRAIL by 4,5-dimethoxy-2-nitrobenzaldehyde. Mol Cancer (2011) 10:46. doi:10.1186/1476-4598-10-46
    • (2011) Mol Cancer , vol.10 , pp. 46
    • Kim, H.B.1    Kim, M.J.2    Kim, D.Y.3    Lee, J.W.4    Bae, J.H.5    Kim, D.W.6
  • 128
    • 84862025394 scopus 로고    scopus 로고
    • The proteasome inhibitor MG132 potentiates TRAIL receptor agonist-induced apoptosis by stabilizing tBid and Bik in human head and neck squamous cell carcinoma cells
    • Sung ES, Park KJ, Choi HJ, Kim CH, Kim YS. The proteasome inhibitor MG132 potentiates TRAIL receptor agonist-induced apoptosis by stabilizing tBid and Bik in human head and neck squamous cell carcinoma cells. Exp Cell Res (2012) 318(13):1564-76. doi:10.1016/j.yexcr.2012.04.003
    • (2012) Exp Cell Res , vol.318 , Issue.13 , pp. 1564-1576
    • Sung, E.S.1    Park, K.J.2    Choi, H.J.3    Kim, C.H.4    Kim, Y.S.5
  • 129
    • 84916226044 scopus 로고    scopus 로고
    • Bortezomib sensitizes primary meningioma cells to TRAIL-induced apoptosis by enhancing formation of the death-inducing signaling complex
    • Koschny R, Boehm C, Sprick MR, Haas TL, Holland H, Xu LX, et al. Bortezomib sensitizes primary meningioma cells to TRAIL-induced apoptosis by enhancing formation of the death-inducing signaling complex. J Neuropathol Exp Neurol (2014) 73(11):1034-46. doi:10.1097/NEN.0000000000000129
    • (2014) J Neuropathol Exp Neurol , vol.73 , Issue.11 , pp. 1034-1046
    • Koschny, R.1    Boehm, C.2    Sprick, M.R.3    Haas, T.L.4    Holland, H.5    Xu, L.X.6
  • 130
    • 77952944929 scopus 로고    scopus 로고
    • Bortezomib sensitizes human renal cell carcinomas to TRAIL apoptosis through increased activation of caspase-8 in the death-inducing signaling complex
    • Brooks AD, Jacobsen KM, Li W, Shanker A, Sayers TJ. Bortezomib sensitizes human renal cell carcinomas to TRAIL apoptosis through increased activation of caspase-8 in the death-inducing signaling complex. Mol Cancer Res (2010) 8(5):729-38. doi:10.1158/1541-7786.MCR-10-0022
    • (2010) Mol Cancer Res , vol.8 , Issue.5 , pp. 729-738
    • Brooks, A.D.1    Jacobsen, K.M.2    Li, W.3    Shanker, A.4    Sayers, T.J.5
  • 131
    • 83055179401 scopus 로고    scopus 로고
    • p53-Independent up-regulation of a TRAIL receptor DR5 by proteasome inhibitors: a mechanism for proteasome inhibitor-enhanced TRAIL-induced apoptosis
    • Seol DW. p53-Independent up-regulation of a TRAIL receptor DR5 by proteasome inhibitors: a mechanism for proteasome inhibitor-enhanced TRAIL-induced apoptosis. Biochem Biophys Res Commun (2011) 416(1-2):222-5. doi:10.1016/j.bbrc.2011.11.053
    • (2011) Biochem Biophys Res Commun , vol.416 , Issue.1-2 , pp. 222-225
    • Seol, D.W.1
  • 132
    • 79955843451 scopus 로고    scopus 로고
    • Proteasome inhibitors sensitize glioma cells and glioma stem cells to TRAIL-induced apoptosis by PKCepsilon-dependent downregulation of AKT and XIAP expressions
    • Kahana S, Finniss S, Cazacu S, Xiang C, Lee HK, Brodie S, et al. Proteasome inhibitors sensitize glioma cells and glioma stem cells to TRAIL-induced apoptosis by PKCepsilon-dependent downregulation of AKT and XIAP expressions. Cell Signal (2011) 23(8):1348-57. doi:10.1016/j.cellsig.2011.03.017
    • (2011) Cell Signal , vol.23 , Issue.8 , pp. 1348-1357
    • Kahana, S.1    Finniss, S.2    Cazacu, S.3    Xiang, C.4    Lee, H.K.5    Brodie, S.6
  • 133
    • 78751483373 scopus 로고    scopus 로고
    • Bortezomib sensitizes malignant human glioma cells to TRAIL, mediated by inhibition of the NF-{kappa}B signaling pathway
    • Jane EP, Premkumar DR, Pollack IF. Bortezomib sensitizes malignant human glioma cells to TRAIL, mediated by inhibition of the NF-{kappa}B signaling pathway. Mol Cancer Ther (2011) 10(1):198-208. doi:10.1158/1535-7163.MCT-10-0725
    • (2011) Mol Cancer Ther , vol.10 , Issue.1 , pp. 198-208
    • Jane, E.P.1    Premkumar, D.R.2    Pollack, I.F.3
  • 134
    • 77953474730 scopus 로고    scopus 로고
    • Bortezomib sensitizes human esophageal squamous cell carcinoma cells to TRAIL-mediated apoptosis via activation of both extrinsic and intrinsic apoptosis pathways
    • Seki N, Toh U, Sayers TJ, Fujii T, Miyagi M, Akagi Y, et al. Bortezomib sensitizes human esophageal squamous cell carcinoma cells to TRAIL-mediated apoptosis via activation of both extrinsic and intrinsic apoptosis pathways. Mol Cancer Ther (2010) 9(6):1842-51. doi:10.1158/1535-7163.MCT-09-0918
    • (2010) Mol Cancer Ther , vol.9 , Issue.6 , pp. 1842-1851
    • Seki, N.1    Toh, U.2    Sayers, T.J.3    Fujii, T.4    Miyagi, M.5    Akagi, Y.6
  • 135
    • 49849089793 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 (VELCADE) induces stabilization of the TRAIL receptor DR5 mRNA through the 3'-untranslated region
    • Kandasamy K, Kraft AS. Proteasome inhibitor PS-341 (VELCADE) induces stabilization of the TRAIL receptor DR5 mRNA through the 3'-untranslated region. Mol Cancer Ther (2008) 7(5):1091-100. doi:10.1158/1535-7163.MCT-07-2368
    • (2008) Mol Cancer Ther , vol.7 , Issue.5 , pp. 1091-1100
    • Kandasamy, K.1    Kraft, A.S.2
  • 136
    • 41949136647 scopus 로고    scopus 로고
    • Bortezomib blocks Bax degradation in malignant B cells during treatment with TRAIL
    • Liu FT, Agrawal SG, Gribben JG, Ye H, Du MQ, Newland AC, et al. Bortezomib blocks Bax degradation in malignant B cells during treatment with TRAIL. Blood (2008) 111(5):2797-805. doi:10.1182/blood-2007-08-110445
    • (2008) Blood , vol.111 , Issue.5 , pp. 2797-2805
    • Liu, F.T.1    Agrawal, S.G.2    Gribben, J.G.3    Ye, H.4    Du, M.Q.5    Newland, A.C.6
  • 137
    • 34249851194 scopus 로고    scopus 로고
    • Proteasome inhibitors synergize with tumor necrosis factor-related apoptosis-induced ligand to induce anaplastic thyroid carcinoma cell death
    • Conticello C, Adamo L, Giuffrida R, Vicari L, Zeuner A, Eramo A, et al. Proteasome inhibitors synergize with tumor necrosis factor-related apoptosis-induced ligand to induce anaplastic thyroid carcinoma cell death. J Clin Endocrinol Metab (2007) 92(5):1938-42. doi:10.1210/jc.2006-2157
    • (2007) J Clin Endocrinol Metab , vol.92 , Issue.5 , pp. 1938-1942
    • Conticello, C.1    Adamo, L.2    Giuffrida, R.3    Vicari, L.4    Zeuner, A.5    Eramo, A.6
  • 138
    • 58249137998 scopus 로고    scopus 로고
    • 17-AAG sensitized malignant glioma cells to death-receptor mediated apoptosis
    • Siegelin MD, Habel A, Gaiser T. 17-AAG sensitized malignant glioma cells to death-receptor mediated apoptosis. Neurobiol Dis (2009) 33(2):243-9. doi:10.1016/j.nbd.2008.10.005
    • (2009) Neurobiol Dis , vol.33 , Issue.2 , pp. 243-249
    • Siegelin, M.D.1    Habel, A.2    Gaiser, T.3
  • 139
    • 84887417311 scopus 로고    scopus 로고
    • Small molecule sensitization to TRAIL is mediated via nuclear localization, phosphorylation and inhibition of chaperone activity of Hsp27
    • Mellier G, Liu D, Bellot G, Holme AL, Pervaiz S. Small molecule sensitization to TRAIL is mediated via nuclear localization, phosphorylation and inhibition of chaperone activity of Hsp27. Cell Death Dis (2013) 4:e890. doi:10.1038/cddis.2013.413
    • (2013) Cell Death Dis , vol.4
    • Mellier, G.1    Liu, D.2    Bellot, G.3    Holme, A.L.4    Pervaiz, S.5
  • 140
    • 84876477696 scopus 로고    scopus 로고
    • The HSP70 and autophagy inhibitor pifithrin-mu enhances the antitumor effects of TRAIL on human pancreatic cancer
    • Monma H, Harashima N, Inao T, Okano S, Tajima Y, Harada M. The HSP70 and autophagy inhibitor pifithrin-mu enhances the antitumor effects of TRAIL on human pancreatic cancer. Mol Cancer Ther (2013) 12(4):341-51. doi:10.1158/1535-7163.MCT-12-0954
    • (2013) Mol Cancer Ther , vol.12 , Issue.4 , pp. 341-351
    • Monma, H.1    Harashima, N.2    Inao, T.3    Okano, S.4    Tajima, Y.5    Harada, M.6
  • 141
    • 22744437647 scopus 로고    scopus 로고
    • HDAC inhibitors enhance the apoptosis-inducing potential of TRAIL in breast carcinoma
    • Singh TR, Shankar S, Srivastava RK. HDAC inhibitors enhance the apoptosis-inducing potential of TRAIL in breast carcinoma. Oncogene (2005) 24(29):4609-23. doi:10.1038/sj.onc.1208585
    • (2005) Oncogene , vol.24 , Issue.29 , pp. 4609-4623
    • Singh, T.R.1    Shankar, S.2    Srivastava, R.K.3
  • 142
    • 12744261484 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors potentiate TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in lymphoid malignancies
    • Inoue S, MacFarlane M, Harper N, Wheat LM, Dyer MJ, Cohen GM. Histone deacetylase inhibitors potentiate TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in lymphoid malignancies. Cell Death Differ (2004) 11(Suppl 2):S193-206. doi:10.1038/sj.cdd.4401535
    • (2004) Cell Death Differ , vol.11 , pp. S193-S206
    • Inoue, S.1    MacFarlane, M.2    Harper, N.3    Wheat, L.M.4    Dyer, M.J.5    Cohen, G.M.6
  • 143
    • 33748887599 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors strongly sensitise neuroblastoma cells to TRAIL-induced apoptosis by a caspases-dependent increase of the pro- to anti-apoptotic proteins ratio
    • Muhlethaler-Mottet A, Flahaut M, Bourloud KB, Auderset K, Meier R, Joseph JM, et al. Histone deacetylase inhibitors strongly sensitise neuroblastoma cells to TRAIL-induced apoptosis by a caspases-dependent increase of the pro- to anti-apoptotic proteins ratio. BMC Cancer (2006) 6:214. doi:10.1186/1471-2407-6-214
    • (2006) BMC Cancer , vol.6 , pp. 214
    • Muhlethaler-Mottet, A.1    Flahaut, M.2    Bourloud, K.B.3    Auderset, K.4    Meier, R.5    Joseph, J.M.6
  • 144
    • 4344666663 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells
    • Nakata S, Yoshida T, Horinaka M, Shiraishi T, Wakada M, Sakai T. Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells. Oncogene (2004) 23(37):6261-71. doi:10.1038/sj.onc.1207830
    • (2004) Oncogene , vol.23 , Issue.37 , pp. 6261-6271
    • Nakata, S.1    Yoshida, T.2    Horinaka, M.3    Shiraishi, T.4    Wakada, M.5    Sakai, T.6
  • 145
    • 77951034685 scopus 로고    scopus 로고
    • LGP1, A histone deacetylase inhibitor analogue of FR235222, sensitizes promyelocytic leukaemia U937 cells to TRAIL-mediated apoptosis
    • D'Acunto CW, Carratu A, Rodriquez M, Taddei M, Parente L, Petrella A. LGP1, A histone deacetylase inhibitor analogue of FR235222, sensitizes promyelocytic leukaemia U937 cells to TRAIL-mediated apoptosis. Anticancer Res (2010) 30(3):887-94.
    • (2010) Anticancer Res , vol.30 , Issue.3 , pp. 887-894
    • D'Acunto, C.W.1    Carratu, A.2    Rodriquez, M.3    Taddei, M.4    Parente, L.5    Petrella, A.6
  • 146
    • 84861992922 scopus 로고    scopus 로고
    • Amurensin G, a novel SIRT1 inhibitor, sensitizes TRAIL-resistant human leukemic K562 cells to TRAIL-induced apoptosis
    • Kim HB, Kim MJ, Lee SH, Lee JW, Bae JH, Kim DW, et al. Amurensin G, a novel SIRT1 inhibitor, sensitizes TRAIL-resistant human leukemic K562 cells to TRAIL-induced apoptosis. Biochem Pharmacol (2012) 84(3):402-10. doi:10.1016/j.bcp.2012.03.014
    • (2012) Biochem Pharmacol , vol.84 , Issue.3 , pp. 402-410
    • Kim, H.B.1    Kim, M.J.2    Lee, S.H.3    Lee, J.W.4    Bae, J.H.5    Kim, D.W.6
  • 147
    • 80053161379 scopus 로고    scopus 로고
    • Combined inhibition of DNA methyltransferase and histone deacetylase restores caspase-8 expression and sensitizes SCLC cells to TRAIL
    • Kaminskyy VO, Surova OV, Vaculova A, Zhivotovsky B. Combined inhibition of DNA methyltransferase and histone deacetylase restores caspase-8 expression and sensitizes SCLC cells to TRAIL. Carcinogenesis (2011) 32(10):1450-8. doi:10.1093/carcin/bgr135
    • (2011) Carcinogenesis , vol.32 , Issue.10 , pp. 1450-1458
    • Kaminskyy, V.O.1    Surova, O.V.2    Vaculova, A.3    Zhivotovsky, B.4
  • 148
    • 29244477848 scopus 로고    scopus 로고
    • Inhibition of DNA methylation sensitizes glioblastoma for tumor necrosis factor-related apoptosis-inducing ligand-mediated destruction
    • Eramo A, Pallini R, Lotti F, Sette G, Patti M, Bartucci M, et al. Inhibition of DNA methylation sensitizes glioblastoma for tumor necrosis factor-related apoptosis-inducing ligand-mediated destruction. Cancer Res (2005) 65(24):11469-77. doi:10.1158/0008-5472.CAN-05-1724
    • (2005) Cancer Res , vol.65 , Issue.24 , pp. 11469-11477
    • Eramo, A.1    Pallini, R.2    Lotti, F.3    Sette, G.4    Patti, M.5    Bartucci, M.6
  • 149
    • 33747841204 scopus 로고    scopus 로고
    • 5-Aza-2'-deoxycytidine and IFN-gamma cooperate to sensitize for TRAIL-induced apoptosis by upregulating caspase-8
    • Fulda S, Debatin KM. 5-Aza-2'-deoxycytidine and IFN-gamma cooperate to sensitize for TRAIL-induced apoptosis by upregulating caspase-8. Oncogene (2006) 25(37):5125-33. doi:10.1038/sj.onc.1209518
    • (2006) Oncogene , vol.25 , Issue.37 , pp. 5125-5133
    • Fulda, S.1    Debatin, K.M.2
  • 150
    • 0035855626 scopus 로고    scopus 로고
    • Sensitization for death receptor- or drug-induced apoptosis by re-expression of caspase-8 through demethylation or gene transfer
    • Fulda S, Kufer MU, Meyer E, van Valen F, Dockhorn-Dworniczak B, Debatin KM. Sensitization for death receptor- or drug-induced apoptosis by re-expression of caspase-8 through demethylation or gene transfer. Oncogene (2001) 20(41):5865-77. doi:10.1038/sj.onc.1204750
    • (2001) Oncogene , vol.20 , Issue.41 , pp. 5865-5877
    • Fulda, S.1    Kufer, M.U.2    Meyer, E.3    van Valen, F.4    Dockhorn-Dworniczak, B.5    Debatin, K.M.6
  • 151
    • 77949653043 scopus 로고    scopus 로고
    • Glycolysis inhibition sensitizes tumor cells to death receptors-induced apoptosis by AMP kinase activation leading to Mcl-1 block in translation
    • Pradelli LA, Beneteau M, Chauvin C, Jacquin MA, Marchetti S, Munoz-Pinedo C, et al. Glycolysis inhibition sensitizes tumor cells to death receptors-induced apoptosis by AMP kinase activation leading to Mcl-1 block in translation. Oncogene (2010) 29(11):1641-52. doi:10.1038/onc.2009.448
    • (2010) Oncogene , vol.29 , Issue.11 , pp. 1641-1652
    • Pradelli, L.A.1    Beneteau, M.2    Chauvin, C.3    Jacquin, M.A.4    Marchetti, S.5    Munoz-Pinedo, C.6
  • 152
    • 84867421065 scopus 로고    scopus 로고
    • Targeting the glyoxalase pathway enhances TRAIL efficacy in cancer cells by downregulating the expression of antiapoptotic molecules
    • Taniguchi H, Horinaka M, Yoshida T, Yano K, Goda AE, Yasuda S, et al. Targeting the glyoxalase pathway enhances TRAIL efficacy in cancer cells by downregulating the expression of antiapoptotic molecules. Mol Cancer Ther (2012) 11(10):2294-300. doi:10.1158/1535-7163.MCT-12-0031
    • (2012) Mol Cancer Ther , vol.11 , Issue.10 , pp. 2294-2300
    • Taniguchi, H.1    Horinaka, M.2    Yoshida, T.3    Yano, K.4    Goda, A.E.5    Yasuda, S.6
  • 153
    • 44449102684 scopus 로고    scopus 로고
    • Mechanisms of enhancement of TRAIL tumoricidal activity against human cancer cells of different origin by dipyridamole
    • Goda AE, Yoshida T, Horinaka M, Yasuda T, Shiraishi T, Wakada M, et al. Mechanisms of enhancement of TRAIL tumoricidal activity against human cancer cells of different origin by dipyridamole. Oncogene (2008) 27(24):3435-45. doi:10.1038/sj.onc.1211008
    • (2008) Oncogene , vol.27 , Issue.24 , pp. 3435-3445
    • Goda, A.E.1    Yoshida, T.2    Horinaka, M.3    Yasuda, T.4    Shiraishi, T.5    Wakada, M.6
  • 154
    • 84903820636 scopus 로고    scopus 로고
    • The novel thymidylate synthase inhibitor trifluorothymidine (TFT) and TRAIL synergistically eradicate non-small cell lung cancer cells
    • Azijli K, van Roosmalen IA, Smit J, Pillai S, Fukushima M, de Jong S, et al. The novel thymidylate synthase inhibitor trifluorothymidine (TFT) and TRAIL synergistically eradicate non-small cell lung cancer cells. Cancer Chemother Pharmacol (2014) 73(6):1273-83. doi:10.1007/s00280-014-2465-1
    • (2014) Cancer Chemother Pharmacol , vol.73 , Issue.6 , pp. 1273-1283
    • Azijli, K.1    van Roosmalen, I.A.2    Smit, J.3    Pillai, S.4    Fukushima, M.5    de Jong, S.6
  • 155
    • 84903887727 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial pyrimidine biosynthesis enzyme dihydroorotate dehydrogenase by doxorubicin and brequinar sensitizes cancer cells to TRAIL-induced apoptosis
    • He T, Haapa-Paananen S, Kaminskyy VO, Kohonen P, Fey V, Zhivotovsky B, et al. Inhibition of the mitochondrial pyrimidine biosynthesis enzyme dihydroorotate dehydrogenase by doxorubicin and brequinar sensitizes cancer cells to TRAIL-induced apoptosis. Oncogene (2014) 33(27):3538-49. doi:10.1038/onc.2013.313
    • (2014) Oncogene , vol.33 , Issue.27 , pp. 3538-3549
    • He, T.1    Haapa-Paananen, S.2    Kaminskyy, V.O.3    Kohonen, P.4    Fey, V.5    Zhivotovsky, B.6
  • 156
    • 0037743569 scopus 로고    scopus 로고
    • Translation inhibitors sensitize prostate cancer cells to apoptosis induced by tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) by activating c-Jun N-terminal kinase
    • Sah NK, Munshi A, Kurland JF, McDonnell TJ, Su B, Meyn RE. Translation inhibitors sensitize prostate cancer cells to apoptosis induced by tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) by activating c-Jun N-terminal kinase. J Biol Chem (2003) 278(23):20593-602. doi:10.1074/jbc.M211010200
    • (2003) J Biol Chem , vol.278 , Issue.23 , pp. 20593-20602
    • Sah, N.K.1    Munshi, A.2    Kurland, J.F.3    McDonnell, T.J.4    Su, B.5    Meyn, R.E.6
  • 157
    • 0035228470 scopus 로고    scopus 로고
    • Sensitization of human colon cancer cells to TRAIL-mediated apoptosis
    • Hernandez A, Wang QD, Schwartz SA, Evers BM. Sensitization of human colon cancer cells to TRAIL-mediated apoptosis. J Gastrointest Surg (2001) 5(1):56-65. doi:10.1016/S1091-255X(01)80014-7
    • (2001) J Gastrointest Surg , vol.5 , Issue.1 , pp. 56-65
    • Hernandez, A.1    Wang, Q.D.2    Schwartz, S.A.3    Evers, B.M.4
  • 158
    • 0037631325 scopus 로고    scopus 로고
    • Inhibition of glucose metabolism sensitizes tumor cells to death receptor-triggered apoptosis through enhancement of death-inducing signaling complex formation and apical procaspase-8 processing
    • Munoz-Pinedo C, Ruiz-Ruiz C, Ruiz de Almodovar C, Palacios C, Lopez-Rivas A. Inhibition of glucose metabolism sensitizes tumor cells to death receptor-triggered apoptosis through enhancement of death-inducing signaling complex formation and apical procaspase-8 processing. J Biol Chem (2003) 278(15):12759-68. doi:10.1074/jbc.M212392200
    • (2003) J Biol Chem , vol.278 , Issue.15 , pp. 12759-12768
    • Munoz-Pinedo, C.1    Ruiz-Ruiz, C.2    Ruiz de Almodovar, C.3    Palacios, C.4    Lopez-Rivas, A.5
  • 159
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation
    • Vander Heiden MG, Cantley LC, Thompson CB. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science (2009) 324(5930):1029-33. doi:10.1126/science.1160809
    • (2009) Science , vol.324 , Issue.5930 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 160
    • 84860512005 scopus 로고    scopus 로고
    • Links between metabolism and cancer
    • Dang CV. Links between metabolism and cancer. Genes Dev (2012) 26(9):877-90. doi:10.1101/gad.189365.112
    • (2012) Genes Dev , vol.26 , Issue.9 , pp. 877-890
    • Dang, C.V.1
  • 161
    • 12544256565 scopus 로고    scopus 로고
    • Inhibition of glycolysis in cancer cells: a novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia
    • Xu RH, Pelicano H, Zhou Y, Carew JS, Feng L, Bhalla KN, et al. Inhibition of glycolysis in cancer cells: a novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia. Cancer Res (2005) 65(2):613-21.
    • (2005) Cancer Res , vol.65 , Issue.2 , pp. 613-621
    • Xu, R.H.1    Pelicano, H.2    Zhou, Y.3    Carew, J.S.4    Feng, L.5    Bhalla, K.N.6
  • 162
    • 58149236959 scopus 로고    scopus 로고
    • Cell-cycle restriction limits DNA damage and maintains self-renewal of leukaemia stem cells
    • Viale A, De Franco F, Orleth A, Cambiaghi V, Giuliani V, Bossi D, et al. Cell-cycle restriction limits DNA damage and maintains self-renewal of leukaemia stem cells. Nature (2009) 457(7225):51-6. doi:10.1038/nature07618
    • (2009) Nature , vol.457 , Issue.7225 , pp. 51-56
    • Viale, A.1    De Franco, F.2    Orleth, A.3    Cambiaghi, V.4    Giuliani, V.5    Bossi, D.6
  • 163
    • 0034282419 scopus 로고    scopus 로고
    • Cells overexpressing fructose-2,6-bisphosphatase showed enhanced pentose phosphate pathway flux and resistance to oxidative stress
    • Boada J, Roig T, Perez X, Gamez A, Bartrons R, Cascante M, et al. Cells overexpressing fructose-2,6-bisphosphatase showed enhanced pentose phosphate pathway flux and resistance to oxidative stress. FEBS Lett (2000) 480(2-3):261-4. doi:10.1016/S0014-5793(00)01950-5
    • (2000) FEBS Lett , vol.480 , Issue.2-3 , pp. 261-264
    • Boada, J.1    Roig, T.2    Perez, X.3    Gamez, A.4    Bartrons, R.5    Cascante, M.6
  • 164
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • Gatenby RA, Gillies RJ. Why do cancers have high aerobic glycolysis? Nat Rev Cancer (2004) 4(11):891-9. doi:10.1038/nrc1478
    • (2004) Nat Rev Cancer , vol.4 , Issue.11 , pp. 891-899
    • Gatenby, R.A.1    Gillies, R.J.2
  • 165
    • 42249111525 scopus 로고    scopus 로고
    • 2-Deoxyglucose induces Akt phosphorylation via a mechanism independent of LKB1/AMP-activated protein kinase signaling activation or glycolysis inhibition
    • Zhong D, Liu X, Schafer-Hales K, Marcus AI, Khuri FR, Sun SY, et al. 2-Deoxyglucose induces Akt phosphorylation via a mechanism independent of LKB1/AMP-activated protein kinase signaling activation or glycolysis inhibition. Mol Cancer Ther (2008) 7(4):809-17. doi:10.1158/1535-7163.MCT-07-0559
    • (2008) Mol Cancer Ther , vol.7 , Issue.4 , pp. 809-817
    • Zhong, D.1    Liu, X.2    Schafer-Hales, K.3    Marcus, A.I.4    Khuri, F.R.5    Sun, S.Y.6
  • 166
    • 0442313668 scopus 로고    scopus 로고
    • Greater cell cycle inhibition and cytotoxicity induced by 2-deoxy-D-glucose in tumor cells treated under hypoxic vs aerobic conditions
    • Maher JC, Krishan A, Lampidis TJ. Greater cell cycle inhibition and cytotoxicity induced by 2-deoxy-D-glucose in tumor cells treated under hypoxic vs aerobic conditions. Cancer Chemother Pharmacol (2004) 53(2):116-22. doi:10.1007/s00280-003-0724-7
    • (2004) Cancer Chemother Pharmacol , vol.53 , Issue.2 , pp. 116-122
    • Maher, J.C.1    Krishan, A.2    Lampidis, T.J.3
  • 167
    • 33846002728 scopus 로고    scopus 로고
    • A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth
    • Bonnet S, Archer SL, Allalunis-Turner J, Haromy A, Beaulieu C, Thompson R, et al. A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth. Cancer Cell (2007) 11(1):37-51. doi:10.1016/j.ccr.2006.10.020
    • (2007) Cancer Cell , vol.11 , Issue.1 , pp. 37-51
    • Bonnet, S.1    Archer, S.L.2    Allalunis-Turner, J.3    Haromy, A.4    Beaulieu, C.5    Thompson, R.6
  • 168
    • 74849137483 scopus 로고    scopus 로고
    • Reversal of the glycolytic phenotype by dichloroacetate inhibits metastatic breast cancer cell growth in vitro and in vivo
    • Sun RC, Fadia M, Dahlstrom JE, Parish CR, Board PG, Blackburn AC. Reversal of the glycolytic phenotype by dichloroacetate inhibits metastatic breast cancer cell growth in vitro and in vivo. Breast Cancer Res Treat (2010) 120(1):253-60. doi:10.1007/s10549-009-0435-9
    • (2010) Breast Cancer Res Treat , vol.120 , Issue.1 , pp. 253-260
    • Sun, R.C.1    Fadia, M.2    Dahlstrom, J.E.3    Parish, C.R.4    Board, P.G.5    Blackburn, A.C.6
  • 169
    • 84875890762 scopus 로고    scopus 로고
    • Targeting cellular metabolism to improve cancer therapeutics
    • Zhao Y, Butler EB, Tan M. Targeting cellular metabolism to improve cancer therapeutics. Cell Death Dis (2013) 4:e532. doi:10.1038/cddis.2013.60
    • (2013) Cell Death Dis , vol.4
    • Zhao, Y.1    Butler, E.B.2    Tan, M.3
  • 170
    • 77954164403 scopus 로고    scopus 로고
    • Silencing of pkm2 increases the efficacy of docetaxel in human lung cancer xenografts in mice
    • Shi HS, Li D, Zhang J, Wang YS, Yang L, Zhang HL, et al. Silencing of pkm2 increases the efficacy of docetaxel in human lung cancer xenografts in mice. Cancer Sci (2010) 101(6):1447-53. doi:10.1111/j.1349-7006.2010.01562.x
    • (2010) Cancer Sci , vol.101 , Issue.6 , pp. 1447-1453
    • Shi, H.S.1    Li, D.2    Zhang, J.3    Wang, Y.S.4    Yang, L.5    Zhang, H.L.6
  • 171
    • 0037122892 scopus 로고    scopus 로고
    • Low glucose-enhanced TRAIL cytotoxicity is mediated through the ceramide-Akt-FLIP pathway
    • Nam SY, Amoscato AA, Lee YJ. Low glucose-enhanced TRAIL cytotoxicity is mediated through the ceramide-Akt-FLIP pathway. Oncogene (2002) 21(3):337-46. doi:10.1038/sj.onc.1205068
    • (2002) Oncogene , vol.21 , Issue.3 , pp. 337-346
    • Nam, S.Y.1    Amoscato, A.A.2    Lee, Y.J.3
  • 172
    • 77953209898 scopus 로고    scopus 로고
    • Q&A: cancer: clues from cell metabolism
    • Kaelin WG Jr, Thompson CB. Q&A: cancer: clues from cell metabolism. Nature (2010) 465(7298):562-4. doi:10.1038/465562a
    • (2010) Nature , vol.465 , Issue.7298 , pp. 562-564
    • Kaelin, W.G.1    Thompson, C.B.2
  • 173
    • 79957991472 scopus 로고    scopus 로고
    • Glutaminase: a hot spot for regulation of cancer cell metabolism?
    • Erickson JW, Cerione RA. Glutaminase: a hot spot for regulation of cancer cell metabolism? Oncotarget (2010) 1(8):734-40.
    • (2010) Oncotarget , vol.1 , Issue.8 , pp. 734-740
    • Erickson, J.W.1    Cerione, R.A.2
  • 174
    • 1842685083 scopus 로고    scopus 로고
    • Thymidylate synthase as an oncogene: a novel role for an essential DNA synthesis enzyme
    • Rahman L, Voeller D, Rahman M, Lipkowitz S, Allegra C, Barrett JC, et al. Thymidylate synthase as an oncogene: a novel role for an essential DNA synthesis enzyme. Cancer Cell (2004) 5(4):341-51. doi:10.1016/S1535-6108(04)00080-7
    • (2004) Cancer Cell , vol.5 , Issue.4 , pp. 341-351
    • Rahman, L.1    Voeller, D.2    Rahman, M.3    Lipkowitz, S.4    Allegra, C.5    Barrett, J.C.6
  • 176
    • 33746851956 scopus 로고    scopus 로고
    • Tumor metastasis: mechanistic insights and clinical challenges
    • Steeg PS. Tumor metastasis: mechanistic insights and clinical challenges. Nat Med (2006) 12(8):895-904. doi:10.1038/nm1469
    • (2006) Nat Med , vol.12 , Issue.8 , pp. 895-904
    • Steeg, P.S.1
  • 177
    • 41849150003 scopus 로고    scopus 로고
    • Metastasis: a therapeutic target for cancer
    • Steeg PS, Theodorescu D. Metastasis: a therapeutic target for cancer. Nat Clin Pract Oncol (2008) 5(4):206-19. doi:10.1038/ncponc1066
    • (2008) Nat Clin Pract Oncol , vol.5 , Issue.4 , pp. 206-219
    • Steeg, P.S.1    Theodorescu, D.2
  • 178
    • 78650443648 scopus 로고    scopus 로고
    • MS-275 sensitizes TRAIL-resistant breast cancer cells, inhibits angiogenesis and metastasis, and reverses epithelial-mesenchymal transition in vivo
    • Srivastava RK, Kurzrock R, Shankar S. MS-275 sensitizes TRAIL-resistant breast cancer cells, inhibits angiogenesis and metastasis, and reverses epithelial-mesenchymal transition in vivo. Mol Cancer Ther (2010) 9(12):3254-66. doi:10.1158/1535-7163.MCT-10-0582
    • (2010) Mol Cancer Ther , vol.9 , Issue.12 , pp. 3254-3266
    • Srivastava, R.K.1    Kurzrock, R.2    Shankar, S.3
  • 179
    • 84885915873 scopus 로고    scopus 로고
    • Epithelial-mesenchymal plasticity in carcinoma metastasis
    • Tsai JH, Yang J. Epithelial-mesenchymal plasticity in carcinoma metastasis. Genes Dev (2013) 27(20):2192-206. doi:10.1101/gad.225334.113
    • (2013) Genes Dev , vol.27 , Issue.20 , pp. 2192-2206
    • Tsai, J.H.1    Yang, J.2
  • 180
    • 36348994426 scopus 로고    scopus 로고
    • Pre-EMTing metastasis? Recapitulation of morphogenetic processes in cancer
    • Berx G, Raspe E, Christofori G, Thiery JP, Sleeman JP. Pre-EMTing metastasis? Recapitulation of morphogenetic processes in cancer. Clin Exp Metastasis (2007) 24(8):587-97. doi:10.1007/s10585-007-9114-6
    • (2007) Clin Exp Metastasis , vol.24 , Issue.8 , pp. 587-597
    • Berx, G.1    Raspe, E.2    Christofori, G.3    Thiery, J.P.4    Sleeman, J.P.5
  • 181
    • 0242720727 scopus 로고    scopus 로고
    • Expression profiling of epithelial plasticity in tumor progression
    • Jechlinger M, Grunert S, Tamir IH, Janda E, Ludemann S, Waerner T, et al. Expression profiling of epithelial plasticity in tumor progression. Oncogene (2003) 22(46):7155-69. doi:10.1038/sj.onc.1206887
    • (2003) Oncogene , vol.22 , Issue.46 , pp. 7155-7169
    • Jechlinger, M.1    Grunert, S.2    Tamir, I.H.3    Janda, E.4    Ludemann, S.5    Waerner, T.6
  • 182
    • 54949147234 scopus 로고    scopus 로고
    • Expression of the ZEB1 (deltaEF1) transcription factor in human: additional insights
    • Hurt EM, Saykally JN, Anose BM, Kalli KR, Sanders MM. Expression of the ZEB1 (deltaEF1) transcription factor in human: additional insights. Mol Cell Biochem (2008) 318(1-2):89-99. doi:10.1007/s11010-008-9860-z
    • (2008) Mol Cell Biochem , vol.318 , Issue.1-2 , pp. 89-99
    • Hurt, E.M.1    Saykally, J.N.2    Anose, B.M.3    Kalli, K.R.4    Sanders, M.M.5
  • 183
    • 39049160267 scopus 로고    scopus 로고
    • The transcriptional repressor ZEB1 promotes metastasis and loss of cell polarity in cancer
    • Spaderna S, Schmalhofer O, Wahlbuhl M, Dimmler A, Bauer K, Sultan A, et al. The transcriptional repressor ZEB1 promotes metastasis and loss of cell polarity in cancer. Cancer Res (2008) 68(2):537-44. doi:10.1158/0008-5472.CAN-07-5682
    • (2008) Cancer Res , vol.68 , Issue.2 , pp. 537-544
    • Spaderna, S.1    Schmalhofer, O.2    Wahlbuhl, M.3    Dimmler, A.4    Bauer, K.5    Sultan, A.6
  • 184
    • 84902603060 scopus 로고    scopus 로고
    • Trail resistance induces epithelial-mesenchymal transition and enhances invasiveness by suppressing PTEN via miR-221 in breast cancer
    • Wang H, Xu C, Kong X, Li X, Wang Y, Ding X, et al. Trail resistance induces epithelial-mesenchymal transition and enhances invasiveness by suppressing PTEN via miR-221 in breast cancer. PLoS One (2014) 9(6):e99067. doi:10.1371/journal.pone.0099067
    • (2014) PLoS One , vol.9 , Issue.6
    • Wang, H.1    Xu, C.2    Kong, X.3    Li, X.4    Wang, Y.5    Ding, X.6
  • 185
    • 84928017461 scopus 로고    scopus 로고
    • Synergistic anti-tumor activity and inhibition of angiogenesis by cotargeting of oncogenic and death receptor pathways in human melanoma
    • Grazia G, Vegetti C, Benigni F, Penna I, Perotti V, Tassi E, et al. Synergistic anti-tumor activity and inhibition of angiogenesis by cotargeting of oncogenic and death receptor pathways in human melanoma. Cell Death Dis (2014) 5:e1434. doi:10.1038/cddis.2014.410
    • (2014) Cell Death Dis , vol.5
    • Grazia, G.1    Vegetti, C.2    Benigni, F.3    Penna, I.4    Perotti, V.5    Tassi, E.6
  • 186
    • 0344441904 scopus 로고    scopus 로고
    • Role of the TRAIL/APO2-L death receptors in chlorambucil- and fludarabine-induced apoptosis in chronic lymphocytic leukemia
    • Johnston JB, Kabore AF, Strutinsky J, Hu X, Paul JT, Kropp DM, et al. Role of the TRAIL/APO2-L death receptors in chlorambucil- and fludarabine-induced apoptosis in chronic lymphocytic leukemia. Oncogene (2003) 22(51):8356-69. doi:10.1038/sj.onc.1207004
    • (2003) Oncogene , vol.22 , Issue.51 , pp. 8356-8369
    • Johnston, J.B.1    Kabore, A.F.2    Strutinsky, J.3    Hu, X.4    Paul, J.T.5    Kropp, D.M.6
  • 187
    • 0038007343 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Burkitt's lymphoma cell lines
    • Mouzakiti A, Packham G. Regulation of tumour necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Burkitt's lymphoma cell lines. Br J Haematol (2003) 122(1):61-9. doi:10.1046/j.1365-2141.2003.04424.x
    • (2003) Br J Haematol , vol.122 , Issue.1 , pp. 61-69
    • Mouzakiti, A.1    Packham, G.2
  • 188
    • 62449168519 scopus 로고    scopus 로고
    • TRAIL agonists on clinical trials for cancer therapy: the promises and the challenges
    • Bellail AC, Qi L, Mulligan P, Chhabra V, Hao C. TRAIL agonists on clinical trials for cancer therapy: the promises and the challenges. Rev Recent Clin Trials (2009) 4(1):34-41. doi:10.2174/157488709787047530
    • (2009) Rev Recent Clin Trials , vol.4 , Issue.1 , pp. 34-41
    • Bellail, A.C.1    Qi, L.2    Mulligan, P.3    Chhabra, V.4    Hao, C.5
  • 189
    • 77956414973 scopus 로고    scopus 로고
    • Phase I dose-escalation study of recombinant human Apo2L/TRAIL, a dual proapoptotic receptor agonist, in patients with advanced cancer
    • Herbst RS, Eckhardt SG, Kurzrock R, Ebbinghaus S, O'Dwyer PJ, Gordon MS, et al. Phase I dose-escalation study of recombinant human Apo2L/TRAIL, a dual proapoptotic receptor agonist, in patients with advanced cancer. J Clin Oncol (2010) 28(17):2839-46. doi:10.1200/JCO.2009.25.1991
    • (2010) J Clin Oncol , vol.28 , Issue.17 , pp. 2839-2846
    • Herbst, R.S.1    Eckhardt, S.G.2    Kurzrock, R.3    Ebbinghaus, S.4    O'Dwyer, P.J.5    Gordon, M.S.6
  • 190
    • 0038320035 scopus 로고    scopus 로고
    • Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy
    • Almasan A, Ashkenazi A. Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy. Cytokine Growth Factor Rev (2003) 14(3-4):337-48. doi:10.1016/S1359-6101(03)00029-7
    • (2003) Cytokine Growth Factor Rev , vol.14 , Issue.3-4 , pp. 337-348
    • Almasan, A.1    Ashkenazi, A.2
  • 191
    • 9244237679 scopus 로고    scopus 로고
    • TRAIL inhibits tumor growth but is nontoxic to human hepatocytes in chimeric mice
    • Hao C, Song JH, Hsi B, Lewis J, Song DK, Petruk KC, et al. TRAIL inhibits tumor growth but is nontoxic to human hepatocytes in chimeric mice. Cancer Res (2004) 64(23):8502-6. doi:10.1158/0008-5472.CAN-04-2599
    • (2004) Cancer Res , vol.64 , Issue.23 , pp. 8502-8506
    • Hao, C.1    Song, J.H.2    Hsi, B.3    Lewis, J.4    Song, D.K.5    Petruk, K.C.6
  • 192
    • 44849120686 scopus 로고    scopus 로고
    • A novel humanized anti-human death receptor 5 antibody CS-1008 induces apoptosis in tumor cells without toxicity in hepatocytes
    • Yada A, Yazawa M, Ishida S, Yoshida H, Ichikawa K, Kurakata S, et al. A novel humanized anti-human death receptor 5 antibody CS-1008 induces apoptosis in tumor cells without toxicity in hepatocytes. Ann Oncol (2008) 19(6):1060-7. doi:10.1093/annonc/mdn015
    • (2008) Ann Oncol , vol.19 , Issue.6 , pp. 1060-1067
    • Yada, A.1    Yazawa, M.2    Ishida, S.3    Yoshida, H.4    Ichikawa, K.5    Kurakata, S.6
  • 193
    • 33748120956 scopus 로고    scopus 로고
    • TRAIL receptor-targeted therapy
    • Buchsbaum DJ, Zhou T, Lobuglio AF. TRAIL receptor-targeted therapy. Future Oncol (2006) 2(4):493-508. doi:10.2217/14796694.2.4.493
    • (2006) Future Oncol , vol.2 , Issue.4 , pp. 493-508
    • Buchsbaum, D.J.1    Zhou, T.2    Lobuglio, A.F.3
  • 195
    • 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, Esplen JE, Dorko K, Billiar TR, et al. Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand. Nat Med (2000) 6(5):564-7. doi:10.1038/75045
    • (2000) Nat Med , vol.6 , Issue.5 , pp. 564-567
    • Jo, M.1    Kim, T.H.2    Seol, D.W.3    Esplen, J.E.4    Dorko, K.5    Billiar, T.R.6
  • 196
    • 0035044296 scopus 로고    scopus 로고
    • Avoiding premature apoptosis of normal epidermal cells
    • Qin J, Chaturvedi V, Bonish B, Nickoloff BJ. Avoiding premature apoptosis of normal epidermal cells. Nat Med (2001) 7(4):385-6. doi:10.1038/86401
    • (2001) Nat Med , vol.7 , Issue.4 , pp. 385-386
    • Qin, J.1    Chaturvedi, V.2    Bonish, B.3    Nickoloff, B.J.4
  • 197
    • 0035050960 scopus 로고    scopus 로고
    • Differential hepatocyte toxicity of recombinant Apo2L/TRAIL versions
    • Lawrence D, Shahrokh Z, Marsters S, Achilles K, Shih D, Mounho B, et al. Differential hepatocyte toxicity of recombinant Apo2L/TRAIL versions. Nat Med (2001) 7(4):383-5. doi:10.1038/nm1201-1291
    • (2001) Nat Med , vol.7 , Issue.4 , pp. 383-385
    • Lawrence, D.1    Shahrokh, Z.2    Marsters, S.3    Achilles, K.4    Shih, D.5    Mounho, B.6
  • 198
    • 49049086338 scopus 로고    scopus 로고
    • Ligand-based targeting of apoptosis in cancer: the potential of recombinant human apoptosis ligand 2/tumor necrosis factor-related apoptosis-inducing ligand (rhApo2L/TRAIL)
    • Ashkenazi A, Holland P, Eckhardt SG. Ligand-based targeting of apoptosis in cancer: the potential of recombinant human apoptosis ligand 2/tumor necrosis factor-related apoptosis-inducing ligand (rhApo2L/TRAIL). J Clin Oncol (2008) 26(21):3621-30. doi:10.1200/JCO.2007.15.7198
    • (2008) J Clin Oncol , vol.26 , Issue.21 , pp. 3621-3630
    • Ashkenazi, A.1    Holland, P.2    Eckhardt, S.G.3
  • 199
    • 36348971707 scopus 로고    scopus 로고
    • Selective induction of apoptosis in leukemic B-lymphoid cells by a CD19-specific TRAIL fusion protein
    • Stieglmaier J, Bremer E, Kellner C, Liebig TM, Ten Cate B, Peipp M, et al. Selective induction of apoptosis in leukemic B-lymphoid cells by a CD19-specific TRAIL fusion protein. Cancer Immunol Immunother (2008) 57(2):233-46. doi:10.1007/s00262-007-0370-8
    • (2008) Cancer Immunol Immunother , vol.57 , Issue.2 , pp. 233-246
    • Stieglmaier, J.1    Bremer, E.2    Kellner, C.3    Liebig, T.M.4    Ten Cate, B.5    Peipp, M.6
  • 200
    • 56749164942 scopus 로고    scopus 로고
    • Potent systemic anticancer activity of adenovirally expressed EGFR-selective TRAIL fusion protein
    • Bremer E, van Dam GM, de Bruyn M, van Riezen M, Dijkstra M, Kamps G, et al. Potent systemic anticancer activity of adenovirally expressed EGFR-selective TRAIL fusion protein. Mol Ther (2008) 16(12):1919-26. doi:10.1038/mt.2008.203
    • (2008) Mol Ther , vol.16 , Issue.12 , pp. 1919-1926
    • Bremer, E.1    van Dam, G.M.2    de Bruyn, M.3    van Riezen, M.4    Dijkstra, M.5    Kamps, G.6
  • 201
    • 12544255082 scopus 로고    scopus 로고
    • Receptor-selective mutants of apoptosis-inducing ligand 2/tumor necrosis factor-related apoptosis-inducing ligand reveal a greater contribution of death receptor (DR) 5 than DR4 to apoptosis signaling
    • Kelley RF, Totpal K, Lindstrom SH, Mathieu M, Billeci K, Deforge L, et al. Receptor-selective mutants of apoptosis-inducing ligand 2/tumor necrosis factor-related apoptosis-inducing ligand reveal a greater contribution of death receptor (DR) 5 than DR4 to apoptosis signaling. J Biol Chem (2005) 280(3):2205-12. doi:10.1074/jbc.M410660200
    • (2005) J Biol Chem , vol.280 , Issue.3 , pp. 2205-2212
    • Kelley, R.F.1    Totpal, K.2    Lindstrom, S.H.3    Mathieu, M.4    Billeci, K.5    Deforge, L.6
  • 202
    • 33745056174 scopus 로고    scopus 로고
    • Designed tumor necrosis factor-related apoptosis-inducing ligand variants initiating apoptosis exclusively via the DR5 receptor
    • van der Sloot AM, Tur V, Szegezdi E, Mullally MM, Cool RH, Samali A, et al. Designed tumor necrosis factor-related apoptosis-inducing ligand variants initiating apoptosis exclusively via the DR5 receptor. Proc Natl Acad Sci U S A (2006) 103(23):8634-9. doi:10.1073/pnas.0510187103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.23 , pp. 8634-8639
    • van der Sloot, A.M.1    Tur, V.2    Szegezdi, E.3    Mullally, M.M.4    Cool, R.H.5    Samali, A.6
  • 204
    • 17944376030 scopus 로고    scopus 로고
    • Tumoricidal activity of a novel anti-human DR5 monoclonal antibody without hepatocyte cytotoxicity
    • Ichikawa K, Liu W, Zhao L, Wang Z, Liu D, Ohtsuka T, et al. Tumoricidal activity of a novel anti-human DR5 monoclonal antibody without hepatocyte cytotoxicity. Nat Med (2001) 7(8):954-60. doi:10.1038/91000
    • (2001) Nat Med , vol.7 , Issue.8 , pp. 954-960
    • Ichikawa, K.1    Liu, W.2    Zhao, L.3    Wang, Z.4    Liu, D.5    Ohtsuka, T.6
  • 205
    • 35948952826 scopus 로고    scopus 로고
    • Phase 1 and pharmacokinetic study of lexatumumab in patients with advanced cancers
    • Plummer R, Attard G, Pacey S, Li L, Razak A, Perrett R, et al. Phase 1 and pharmacokinetic study of lexatumumab in patients with advanced cancers. Clin Cancer Res (2007) 13(20):6187-94. doi:10.1158/1078-0432.CCR-07-0950
    • (2007) Clin Cancer Res , vol.13 , Issue.20 , pp. 6187-6194
    • Plummer, R.1    Attard, G.2    Pacey, S.3    Li, L.4    Razak, A.5    Perrett, R.6
  • 206
    • 44749085513 scopus 로고    scopus 로고
    • Targeting the extrinsic apoptosis pathway in cancer
    • Ashkenazi A. Targeting the extrinsic apoptosis pathway in cancer. Cytokine Growth Factor Rev (2008) 19(3-4):325-31. doi:10.1016/j.cytogfr.2008.04.001
    • (2008) Cytokine Growth Factor Rev , vol.19 , Issue.3-4 , pp. 325-331
    • Ashkenazi, A.1
  • 207
    • 29244483111 scopus 로고    scopus 로고
    • TRAIL receptor-selective mutants signal to apoptosis via TRAIL-R1 in primary lymphoid malignancies
    • MacFarlane M, Kohlhaas SL, Sutcliffe MJ, Dyer MJ, Cohen GM. TRAIL receptor-selective mutants signal to apoptosis via TRAIL-R1 in primary lymphoid malignancies. Cancer Res (2005) 65(24):11265-70. doi:10.1158/0008-5472.CAN-05-2801
    • (2005) Cancer Res , vol.65 , Issue.24 , pp. 11265-11270
    • MacFarlane, M.1    Kohlhaas, S.L.2    Sutcliffe, M.J.3    Dyer, M.J.4    Cohen, G.M.5
  • 208
    • 0035871757 scopus 로고    scopus 로고
    • Isotype-dependent inhibition of tumor growth in vivo by monoclonal antibodies to death receptor 4
    • Chuntharapai A, Dodge K, Grimmer K, Schroeder K, Marsters SA, Koeppen H, et al. Isotype-dependent inhibition of tumor growth in vivo by monoclonal antibodies to death receptor 4. J Immunol (2001) 166(8):4891-8. doi:10.4049/jimmunol.166.8.4891
    • (2001) J Immunol , vol.166 , Issue.8 , pp. 4891-4898
    • Chuntharapai, A.1    Dodge, K.2    Grimmer, K.3    Schroeder, K.4    Marsters, S.A.5    Koeppen, H.6
  • 209
    • 69949110775 scopus 로고    scopus 로고
    • Mapatumumab, a fully human agonistic monoclonal antibody that targets TRAIL-R1, in combination with gemcitabine and cisplatin: a phase I study
    • Mom CH, Verweij J, Oldenhuis CN, Gietema JA, Fox NL, Miceli R, et al. Mapatumumab, a fully human agonistic monoclonal antibody that targets TRAIL-R1, in combination with gemcitabine and cisplatin: a phase I study. Clin Cancer Res (2009) 15(17):5584-90. doi:10.1158/1078-0432.CCR-09-0996
    • (2009) Clin Cancer Res , vol.15 , Issue.17 , pp. 5584-5590
    • Mom, C.H.1    Verweij, J.2    Oldenhuis, C.N.3    Gietema, J.A.4    Fox, N.L.5    Miceli, R.6
  • 210
    • 0035476255 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis of human melanoma is regulated by smac/DIABLO release from mitochondria
    • Zhang XD, Zhang XY, Gray CP, Nguyen T, Hersey P. Tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis of human melanoma is regulated by smac/DIABLO release from mitochondria. Cancer Res (2001) 61(19):7339-48.
    • (2001) Cancer Res , vol.61 , Issue.19 , pp. 7339-7348
    • Zhang, X.D.1    Zhang, X.Y.2    Gray, C.P.3    Nguyen, T.4    Hersey, P.5
  • 211
    • 37249013515 scopus 로고    scopus 로고
    • Human agonistic TRAIL receptor antibodies mapatumumab and lexatumumab induce apoptosis in malignant mesothelioma and act synergistically with cisplatin
    • Belyanskaya LL, Marti TM, Hopkins-Donaldson S, Kurtz S, Felley-Bosco E, Stahel RA. Human agonistic TRAIL receptor antibodies mapatumumab and lexatumumab induce apoptosis in malignant mesothelioma and act synergistically with cisplatin. Mol Cancer (2007) 6:66. doi:10.1186/1476-4598-6-66
    • (2007) Mol Cancer , vol.6 , pp. 66
    • Belyanskaya, L.L.1    Marti, T.M.2    Hopkins-Donaldson, S.3    Kurtz, S.4    Felley-Bosco, E.5    Stahel, R.A.6
  • 212
    • 84896775029 scopus 로고    scopus 로고
    • DRUGSURV: a resource for repositioning of approved and experimental drugs in oncology based on patient survival information
    • Amelio I, Gostev M, Knight RA, Willis AE, Melino G, Antonov AV. DRUGSURV: a resource for repositioning of approved and experimental drugs in oncology based on patient survival information. Cell Death Dis (2014) 5:e1051. doi:10.1038/cddis.2014.9
    • (2014) Cell Death Dis , vol.5
    • Amelio, I.1    Gostev, M.2    Knight, R.A.3    Willis, A.E.4    Melino, G.5    Antonov, A.V.6


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