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Volumn 4 APR, Issue , 2014, Pages

Oncolytic immunotherapy: Dying the right way is a key to eliciting potent antitumor immunity

Author keywords

Antitumor immunity; Autophagy; Cross presentation; DAMPs; Immune tolerance; Immunogenic cancer cell death; PAMP; Tumor associated antigen

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADVANCED GLYCATION END PRODUCT RECEPTOR; CALRETICULIN; CYTOKINE; HEAT SHOCK PROTEIN; HEPARIN; HIGH MOBILITY GROUP B1 PROTEIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; RETINOIC ACID INDUCIBLE PROTEIN I; T LYMPHOCYTE RECEPTOR; TOLL LIKE RECEPTOR; TUMOR ANTIGEN; TUMOR NECROSIS FACTOR; URIC ACID; VIRUS VECTOR;

EID: 84901044424     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2014.00074     Document Type: Review
Times cited : (233)

References (136)
  • 1
    • 84863653214 scopus 로고    scopus 로고
    • Oncolytic virotherapy
    • doi: 10.1038/nbt.2287
    • Russell SJ, Peng KW, Bell JC. Oncolytic virotherapy. Nat Biotechnol (2012) 30:658-70. doi: 10.1038/nbt.2287.
    • (2012) Nat Biotechnol , vol.30 , pp. 658-670
    • Russell, S.J.1    Peng, K.W.2    Bell, J.C.3
  • 2
    • 84875182214 scopus 로고    scopus 로고
    • Oncolytic virus therapy for cancer: the first wave of translational clinical trials
    • doi:10.1016/j.trsl.2012.12.010
    • Patel MR, Kratzke RA. Oncolytic virus therapy for cancer: the first wave of translational clinical trials. Transl Res (2013) 161:355-64. doi:10.1016/j.trsl.2012.12.010.
    • (2013) Transl Res , vol.161 , pp. 355-364
    • Patel, M.R.1    Kratzke, R.A.2
  • 3
    • 41949096891 scopus 로고    scopus 로고
    • Oncolytic virotherapy: molecular targets in tumor-selective replication and carrier cell-mediated delivery of oncolytic viruses
    • doi:10.1016/j.bbcan.2008.02.001
    • Guo ZS, Thorne SH, Bartlett DL. Oncolytic virotherapy: molecular targets in tumor-selective replication and carrier cell-mediated delivery of oncolytic viruses. Biochim Biophys Acta (2008) 1785:217-31. doi:10.1016/j.bbcan.2008.02.001.
    • (2008) Biochim Biophys Acta , vol.1785 , pp. 217-231
    • Guo, Z.S.1    Thorne, S.H.2    Bartlett, D.L.3
  • 4
    • 34548062828 scopus 로고    scopus 로고
    • Targeted inflammation during oncolytic virus therapy severely compromises tumor blood flow
    • doi:10.1038/sj.mt.6300215
    • Breitbach CJ, Paterson JM, Lemay CG, Falls TJ, McGuire A, Parato KA, et al. Targeted inflammation during oncolytic virus therapy severely compromises tumor blood flow. Mol Ther (2007) 15:1686-93. doi:10.1038/sj.mt.6300215.
    • (2007) Mol Ther , vol.15 , pp. 1686-1693
    • Breitbach, C.J.1    Paterson, J.M.2    Lemay, C.G.3    Falls, T.J.4    McGuire, A.5    Parato, K.A.6
  • 5
    • 50549091297 scopus 로고    scopus 로고
    • The targeted oncolytic poxvirus JX-594 demonstrates antitumoral, antivascular, and anti-HBV activities in patients with hepatocellular carcinoma
    • doi:10.1038/mt.2008.143
    • Liu TC, Hwang T, Park BH, Bell J, Kirn DH. The targeted oncolytic poxvirus JX-594 demonstrates antitumoral, antivascular, and anti-HBV activities in patients with hepatocellular carcinoma. Mol Ther (2008) 16:1637-42. doi:10.1038/mt.2008.143.
    • (2008) Mol Ther , vol.16 , pp. 1637-1642
    • Liu, T.C.1    Hwang, T.2    Park, B.H.3    Bell, J.4    Kirn, D.H.5
  • 6
    • 84874309252 scopus 로고    scopus 로고
    • Oncolytic vaccinia virus disrupts tumor-associated vasculature in humans
    • doi:10.1158/0008-5472.CAN-12-2687
    • Breitbach CJ, Arulanandam R, De Silva N, Thorne SH, Patt R, Daneshmand M, et al. Oncolytic vaccinia virus disrupts tumor-associated vasculature in humans. Cancer Res (2013) 73:1265-75. doi:10.1158/0008-5472.CAN-12-2687.
    • (2013) Cancer Res , vol.73 , pp. 1265-1275
    • Breitbach, C.J.1    Arulanandam, R.2    De Silva, N.3    Thorne, S.H.4    Patt, R.5    Daneshmand, M.6
  • 7
    • 34047262198 scopus 로고    scopus 로고
    • Oncolytic immunovirotherapy for melanoma using vesicular stomatitis virus
    • doi:10.1158/0008-5472.CAN-06-3974
    • Diaz RM, Galivo F, Kottke T, Wongthida P, Qiao J, Thompson J, et al. Oncolytic immunovirotherapy for melanoma using vesicular stomatitis virus. Cancer Res (2007) 67:2840-8. doi:10.1158/0008-5472.CAN-06-3974.
    • (2007) Cancer Res , vol.67 , pp. 2840-2848
    • Diaz, R.M.1    Galivo, F.2    Kottke, T.3    Wongthida, P.4    Qiao, J.5    Thompson, J.6
  • 8
    • 58149359320 scopus 로고    scopus 로고
    • Tumor infection by oncolytic reovirus primes adaptive antitumor immunity
    • doi:10.1158/1078-0432.CCR-08-0831
    • Prestwich RJ, Errington F, Ilett EJ, Morgan RS, Scott KJ, Kottke T, et al. Tumor infection by oncolytic reovirus primes adaptive antitumor immunity. Clin Cancer Res (2008) 14:7358-66. doi:10.1158/1078-0432.CCR-08-0831.
    • (2008) Clin Cancer Res , vol.14 , pp. 7358-7366
    • Prestwich, R.J.1    Errington, F.2    Ilett, E.J.3    Morgan, R.S.4    Scott, K.J.5    Kottke, T.6
  • 9
    • 67650375869 scopus 로고    scopus 로고
    • Immune-mediated antitumor activity of reovirus is required for therapy and is independent of direct viral oncolysis and replication
    • doi:10.1158/1078-0432.CCR-09-0334
    • Prestwich RJ, Ilett EJ, Errington F, Diaz RM, Steele LP, Kottke T, et al. Immune-mediated antitumor activity of reovirus is required for therapy and is independent of direct viral oncolysis and replication. Clin Cancer Res (2009) 15:4374-81. doi:10.1158/1078-0432.CCR-09-0334.
    • (2009) Clin Cancer Res , vol.15 , pp. 4374-4381
    • Prestwich, R.J.1    Ilett, E.J.2    Errington, F.3    Diaz, R.M.4    Steele, L.P.5    Kottke, T.6
  • 10
    • 77953172635 scopus 로고    scopus 로고
    • Type III IFN interleukin-28 mediates the antitumor efficacy of oncolytic virus VSV in immune-competent mouse models of cancer
    • doi:10.1158/0008-5472.CAN-09-4658
    • Wongthida P, Diaz RM, Galivo F, Kottke T, Thompson J, Pulido J, et al. Type III IFN interleukin-28 mediates the antitumor efficacy of oncolytic virus VSV in immune-competent mouse models of cancer. Cancer Res (2010) 70:4539-49. doi:10.1158/0008-5472.CAN-09-4658.
    • (2010) Cancer Res , vol.70 , pp. 4539-4549
    • Wongthida, P.1    Diaz, R.M.2    Galivo, F.3    Kottke, T.4    Thompson, J.5    Pulido, J.6
  • 11
    • 79551614963 scopus 로고    scopus 로고
    • Adaptive antiviral immunity is a determinant of the therapeutic success of oncolytic virotherapy
    • doi:10.1038/mt.2010.264
    • Sobol PT, Boudreau JE, Stephenson K, Wan Y, Lichty BD, Mossman KL. Adaptive antiviral immunity is a determinant of the therapeutic success of oncolytic virotherapy. Mol Ther (2011) 19:335-44. doi:10.1038/mt.2010.264.
    • (2011) Mol Ther , vol.19 , pp. 335-344
    • Sobol, P.T.1    Boudreau, J.E.2    Stephenson, K.3    Wan, Y.4    Lichty, B.D.5    Mossman, K.L.6
  • 12
    • 84860520650 scopus 로고    scopus 로고
    • Immune response is an important aspect of the antitumor effect produced by a CD40L-encoding oncolytic adenovirus
    • doi:10.1158/0008-5472.CAN-11-2975
    • Diaconu I, Cerullo V, Hirvinen ML, Escutenaire S, Ugolini M, Pesonen SK, et al. Immune response is an important aspect of the antitumor effect produced by a CD40L-encoding oncolytic adenovirus. Cancer Res (2012) 72:2327-38. doi:10.1158/0008-5472.CAN-11-2975.
    • (2012) Cancer Res , vol.72 , pp. 2327-2338
    • Diaconu, I.1    Cerullo, V.2    Hirvinen, M.L.3    Escutenaire, S.4    Ugolini, M.5    Pesonen, S.K.6
  • 13
    • 84856554267 scopus 로고    scopus 로고
    • Oncolytic Sindbis virus targets tumors defective in the interferon response and induces significant bystander antitumor immunity in vivo
    • doi:10.1038/mt.2011.245
    • Huang PY, Guo JH, Hwang LH. Oncolytic Sindbis virus targets tumors defective in the interferon response and induces significant bystander antitumor immunity in vivo. Mol Ther (2012) 20:298-305. doi:10.1038/mt.2011.245.
    • (2012) Mol Ther , vol.20 , pp. 298-305
    • Huang, P.Y.1    Guo, J.H.2    Hwang, L.H.3
  • 14
    • 84891825541 scopus 로고    scopus 로고
    • Immunogenic HSV-mediated oncolysis shapes the antitumor immune response and contributes to therapeutic efficacy
    • doi:10.1038/mt.2013.238
    • Workenhe ST, Simmons G, Pol JG, Lichty BD, Halford WP, Mossman KL. Immunogenic HSV-mediated oncolysis shapes the antitumor immune response and contributes to therapeutic efficacy. Mol Ther (2014) 22:123-31. doi:10.1038/mt.2013.238.
    • (2014) Mol Ther , vol.22 , pp. 123-131
    • Workenhe, S.T.1    Simmons, G.2    Pol, J.G.3    Lichty, B.D.4    Halford, W.P.5    Mossman, K.L.6
  • 15
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: a renewed sense of self
    • doi:10.1126/science.1071059
    • Matzinger P. The danger model: a renewed sense of self. Science (2002) 296:301-5. doi:10.1126/science.1071059.
    • (2002) Science , vol.296 , pp. 301-305
    • Matzinger, P.1
  • 16
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • doi:10.1126/science.1068883
    • Medzhitov R, Janeway CA Jr. Decoding the patterns of self and nonself by the innate immune system. Science (2002) 296:298-300. doi:10.1126/science.1068883.
    • (2002) Science , vol.296 , pp. 298-300
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 17
    • 84865299726 scopus 로고    scopus 로고
    • PAMPs and DAMPs: signal 0s that spur autophagy and immunity
    • doi:10.1111/j.1600-065X.2012.01146.x
    • Tang D, Kang R, Coyne CB, Zeh HJ, Lotze MT. PAMPs and DAMPs: signal 0s that spur autophagy and immunity. Immunol Rev (2012) 249:158-75. doi:10.1111/j.1600-065X.2012.01146.x.
    • (2012) Immunol Rev , vol.249 , pp. 158-175
    • Tang, D.1    Kang, R.2    Coyne, C.B.3    Zeh, H.J.4    Lotze, M.T.5
  • 18
    • 16844379997 scopus 로고    scopus 로고
    • Immunosuppressive networks in the tumour environment and their therapeutic relevance
    • doi:10.1038/nrc1586
    • Zou W. Immunosuppressive networks in the tumour environment and their therapeutic relevance. Nat Rev Cancer (2005) 5:263-74. doi:10.1038/nrc1586.
    • (2005) Nat Rev Cancer , vol.5 , pp. 263-274
    • Zou, W.1
  • 19
    • 68949155451 scopus 로고    scopus 로고
    • Engineering oncolytic viruses to exploit tumor specific defects in innate immune signaling pathways
    • doi:10.1517/14712590903170653
    • Naik S, Russell SJ. Engineering oncolytic viruses to exploit tumor specific defects in innate immune signaling pathways. Expert Opin Biol Ther (2009) 9:1163-76. doi:10.1517/14712590903170653.
    • (2009) Expert Opin Biol Ther , vol.9 , pp. 1163-1176
    • Naik, S.1    Russell, S.J.2
  • 20
    • 77954541596 scopus 로고    scopus 로고
    • The viral tropism of two distinct oncolytic viruses, reovirus and myxoma virus, is modulated by cellular tumor suppressor gene status
    • doi:10.1038/onc.2010.137
    • Kim M, Williamson CT, Prudhomme J, Bebb DG, Riabowol K, Lee PW, et al. The viral tropism of two distinct oncolytic viruses, reovirus and myxoma virus, is modulated by cellular tumor suppressor gene status. Oncogene (2010) 29:3990-6. doi:10.1038/onc.2010.137.
    • (2010) Oncogene , vol.29 , pp. 3990-3996
    • Kim, M.1    Williamson, C.T.2    Prudhomme, J.3    Bebb, D.G.4    Riabowol, K.5    Lee, P.W.6
  • 21
    • 84867055900 scopus 로고    scopus 로고
    • Failure of translation of human adenovirus mRNA in murine cancer cells can be partially overcome by L4-100K expression in vitro and in vivo
    • doi:10.1038/mt.2012.116
    • Young AM, Archibald KM, Tookman LA, Pool A, Dudek K, Jones C, et al. Failure of translation of human adenovirus mRNA in murine cancer cells can be partially overcome by L4-100K expression in vitro and in vivo. Mol Ther (2012) 20:1676-88. doi:10.1038/mt.2012.116.
    • (2012) Mol Ther , vol.20 , pp. 1676-1688
    • Young, A.M.1    Archibald, K.M.2    Tookman, L.A.3    Pool, A.4    Dudek, K.5    Jones, C.6
  • 22
    • 0024721339 scopus 로고
    • Immunogenicity signals 1,2,3 ... and 0
    • doi:10.1016/0167-5699(89)90081-9
    • Janeway C. Immunogenicity signals 1,2,3 ... and 0. Immunol Today (1989) 10:283-6. doi:10.1016/0167-5699(89)90081-9.
    • (1989) Immunol Today , vol.10 , pp. 283-286
    • Janeway, C.1
  • 23
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • doi:10.1101/SQB.1989.054.01.003
    • Janeway CA Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol (1989) 54(Pt 1):1-13. doi:10.1101/SQB.1989.054.01.003.
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PART 1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 24
    • 0036212849 scopus 로고    scopus 로고
    • Innate immune recognition
    • doi:10.1146/annurev.immunol.20.083001.084359
    • Janeway CA Jr, Medzhitov R. Innate immune recognition. Annu Rev Immunol (2002) 20:197-216. doi:10.1146/annurev.immunol.20.083001.084359.
    • (2002) Annu Rev Immunol , vol.20 , pp. 197-216
    • Janeway Jr., C.A.1    Medzhitov, R.2
  • 25
    • 33845951211 scopus 로고    scopus 로고
    • DAMPs, PAMPs and alarmins: all we need to know about danger
    • doi:10.1189/jlb.0306164
    • Bianchi ME. DAMPs, PAMPs and alarmins: all we need to know about danger. J Leukoc Biol (2007) 81:1-5. doi:10.1189/jlb.0306164.
    • (2007) J Leukoc Biol , vol.81 , pp. 1-5
    • Bianchi, M.E.1
  • 26
    • 84887308873 scopus 로고    scopus 로고
    • Defective viral genomes arising in vivo provide critical danger signals for the triggering of lung antiviral immunity
    • doi:10.1371/journal.ppat.1003703
    • Tapia K, Kim WK, Sun Y, Mercado-López X, Dunay E, Wise M, et al. Defective viral genomes arising in vivo provide critical danger signals for the triggering of lung antiviral immunity. PLoS Pathog (2013) 9:e1003703. doi:10.1371/journal.ppat.1003703.
    • (2013) PLoS Pathog , vol.9
    • Tapia, K.1    Kim, W.K.2    Sun, Y.3    Mercado-López, X.4    Dunay, E.5    Wise, M.6
  • 27
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • doi:10.1016/j.cell.2010.01.022
    • Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell (2010) 140:805-20. doi:10.1016/j.cell.2010.01.022.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 28
    • 58049209834 scopus 로고    scopus 로고
    • Inflammatory signals in dendritic cell activation and the induction of adaptive immunity
    • doi:10.1111/j.1600-065X.2008.00718.x
    • Joffre O, Nolte MA, Sporri R, Reis e Sousa C. Inflammatory signals in dendritic cell activation and the induction of adaptive immunity. Immunol Rev (2009) 227:234-47. doi:10.1111/j.1600-065X.2008.00718.x.
    • (2009) Immunol Rev , vol.227 , pp. 234-247
    • Joffre, O.1    Nolte, M.A.2    Sporri, R.3    Reis Sousa, C.4
  • 29
    • 77956409179 scopus 로고    scopus 로고
    • Regulation of antigen uptake, migration, and lifespan of dendritic cell by toll-like receptors
    • doi:10.1007/s00109-010-0638-x
    • Zanoni I, Granucci F. Regulation of antigen uptake, migration, and lifespan of dendritic cell by toll-like receptors. J Mol Med (Berl) (2010) 88:873-80. doi:10.1007/s00109-010-0638-x.
    • (2010) J Mol Med (Berl) , vol.88 , pp. 873-880
    • Zanoni, I.1    Granucci, F.2
  • 30
    • 0028201732 scopus 로고
    • Tolerance, danger, and the extended family
    • doi:10.1146/annurev.immunol.12.1.991
    • Matzinger P. Tolerance, danger, and the extended family. Annu Rev Immunol (1994) 12:991-1045. doi:10.1146/annurev.immunol.12.1.991.
    • (1994) Annu Rev Immunol , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 31
    • 41149118513 scopus 로고    scopus 로고
    • How dying cells alert the immune system to danger
    • doi:10.1038/nri2215
    • Kono H, Rock KL. How dying cells alert the immune system to danger. Nat Rev Immunol (2008) 8:279-89. doi:10.1038/nri2215.
    • (2008) Nat Rev Immunol , vol.8 , pp. 279-289
    • Kono, H.1    Rock, K.L.2
  • 32
    • 0141998606 scopus 로고    scopus 로고
    • Molecular identification of a danger signal that alerts the immune system to dying cells
    • doi:10.1038/nature01991
    • Shi Y, Evans JE, Rock KL. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature (2003) 425:516-21. doi:10.1038/nature01991.
    • (2003) Nature , vol.425 , pp. 516-521
    • Shi, Y.1    Evans, J.E.2    Rock, K.L.3
  • 34
    • 48149096398 scopus 로고    scopus 로고
    • HMGB1: endogenous danger signaling
    • doi:10.2119/2008-00034.Klune
    • Klune JR, Dhupar R, Cardinal J, Billiar TR, Tsung A. HMGB1: endogenous danger signaling. Mol Med (2008) 14:476-84. doi:10.2119/2008-00034.Klune.
    • (2008) Mol Med , vol.14 , pp. 476-484
    • Klune, J.R.1    Dhupar, R.2    Cardinal, J.3    Billiar, T.R.4    Tsung, A.5
  • 35
    • 84879651810 scopus 로고    scopus 로고
    • Life after death: targeting high mobility group box 1 in emergent cancer therapies
    • Guo ZS, Liu Z, Bartlett DL, Tang D, Lotze MT. Life after death: targeting high mobility group box 1 in emergent cancer therapies. Am J Cancer Res (2013) 3:1-20.
    • (2013) Am J Cancer Res , vol.3 , pp. 1-20
    • Guo, Z.S.1    Liu, Z.2    Bartlett, D.L.3    Tang, D.4    Lotze, M.T.5
  • 36
    • 79953068336 scopus 로고    scopus 로고
    • Emerging role of damage-associated molecular patterns derived from mitochondria in inflammation
    • doi:10.1016/j.it.2011.01.005
    • Krysko DV, Agostinis P, Krysko O, Garg AD, Bachert C, Lambrecht BN, et al. Emerging role of damage-associated molecular patterns derived from mitochondria in inflammation. Trends Immunol (2011) 32:157-64. doi:10.1016/j.it.2011.01.005.
    • (2011) Trends Immunol , vol.32 , pp. 157-164
    • Krysko, D.V.1    Agostinis, P.2    Krysko, O.3    Garg, A.D.4    Bachert, C.5    Lambrecht, B.N.6
  • 38
    • 29144530630 scopus 로고    scopus 로고
    • Caspase-dependent immunogenicity of doxorubicin-induced tumor cell death
    • doi:10.1084/jem.20050915
    • Casares N, Pequignot MO, Tesniere A, Ghiringhelli F, Roux S, Chaput N, et al. Caspase-dependent immunogenicity of doxorubicin-induced tumor cell death. J Exp Med (2005) 202:1691-701. doi:10.1084/jem.20050915.
    • (2005) J Exp Med , vol.202 , pp. 1691-1701
    • Casares, N.1    Pequignot, M.O.2    Tesniere, A.3    Ghiringhelli, F.4    Roux, S.5    Chaput, N.6
  • 39
    • 0014106471 scopus 로고
    • Viral oncolysis: increased immunogenicity of host cell antigen associated with influenza virus
    • doi:10.1084/jem.126.1.93
    • Lindenmann J, Klein PA. Viral oncolysis: increased immunogenicity of host cell antigen associated with influenza virus. J Exp Med (1967) 126:93-108. doi:10.1084/jem.126.1.93.
    • (1967) J Exp Med , vol.126 , pp. 93-108
    • Lindenmann, J.1    Klein, P.A.2
  • 40
    • 0031836938 scopus 로고    scopus 로고
    • Tumor immunogenicity is determined by the mechanism of cell death via induction of heat shock protein expression
    • doi:10.1038/nm0598-581
    • Melcher A, Todryk S, Hardwick N, Ford M, Jacobson M, Vile RG. Tumor immunogenicity is determined by the mechanism of cell death via induction of heat shock protein expression. Nat Med (1998) 4:581-7. doi:10.1038/nm0598-581.
    • (1998) Nat Med , vol.4 , pp. 581-587
    • Melcher, A.1    Todryk, S.2    Hardwick, N.3    Ford, M.4    Jacobson, M.5    Vile, R.G.6
  • 41
    • 33846057130 scopus 로고    scopus 로고
    • Calreticulin exposure dictates the immunogenicity of cancer cell death
    • doi:10.1038/nm1523
    • Obeid M, Tesniere A, Ghiringhelli F, Fimia GM, Apetoh L, Perfettini JL, et al. Calreticulin exposure dictates the immunogenicity of cancer cell death. Nat Med (2007) 13:54-61. doi:10.1038/nm1523.
    • (2007) Nat Med , vol.13 , pp. 54-61
    • Obeid, M.1    Tesniere, A.2    Ghiringhelli, F.3    Fimia, G.M.4    Apetoh, L.5    Perfettini, J.L.6
  • 44
    • 84883642231 scopus 로고    scopus 로고
    • Oncolytic viruses as therapeutic cancer vaccines
    • doi:10.1186/1476-4598-12-103
    • Bartlett DL, Liu Z, Sathaiah M, Ravindranathan R, Guo Z, He Y, et al. Oncolytic viruses as therapeutic cancer vaccines. Mol Cancer (2013) 12:103. doi:10.1186/1476-4598-12-103.
    • (2013) Mol Cancer , vol.12 , pp. 103
    • Bartlett, D.L.1    Liu, Z.2    Sathaiah, M.3    Ravindranathan, R.4    Guo, Z.5    He, Y.6
  • 45
    • 84890086459 scopus 로고    scopus 로고
    • Multimodal immunogenic cancer cell death as a consequence of anticancer cytotoxic treatments
    • doi:10.1038/cdd.2013.84
    • Inoue H, Tani K. Multimodal immunogenic cancer cell death as a consequence of anticancer cytotoxic treatments. Cell Death Differ (2014) 21:39-49. doi:10.1038/cdd.2013.84.
    • (2014) Cell Death Differ , vol.21 , pp. 39-49
    • Inoue, H.1    Tani, K.2
  • 47
    • 77958184901 scopus 로고    scopus 로고
    • Manipulation of host cell death pathways during microbial infections
    • doi:10.1016/j.chom.2010.06.007
    • Lamkanfi M, Dixit VM. Manipulation of host cell death pathways during microbial infections. Cell Host Microbe (2010) 8:44-54. doi:10.1016/j.chom.2010.06.007.
    • (2010) Cell Host Microbe , vol.8 , pp. 44-54
    • Lamkanfi, M.1    Dixit, V.M.2
  • 48
    • 33646462468 scopus 로고    scopus 로고
    • Autophagic cell death of malignant glioma cells induced by a conditionally replicating adenovirus
    • doi:10.1093/jnci/djj161
    • Ito H, Aoki H, Kühnel F, Kondo Y, Kubicka S, Wirth T, et al. Autophagic cell death of malignant glioma cells induced by a conditionally replicating adenovirus. J Natl Cancer Inst (2006) 98:625-36. doi:10.1093/jnci/djj161.
    • (2006) J Natl Cancer Inst , vol.98 , pp. 625-636
    • Ito, H.1    Aoki, H.2    Kühnel, F.3    Kondo, Y.4    Kubicka, S.5    Wirth, T.6
  • 49
    • 39849083763 scopus 로고    scopus 로고
    • Delta-24-RGD in combination with RAD001 induces enhanced anti-glioma effect via autophagic cell death
    • doi:10.1038/sj.mt.6300400
    • Alonso MM, Jiang H, Yokoyama T, Xu J, Bekele NB, Lang FF, et al. Delta-24-RGD in combination with RAD001 induces enhanced anti-glioma effect via autophagic cell death. Mol Ther (2008) 16:487-93. doi:10.1038/sj.mt.6300400.
    • (2008) Mol Ther , vol.16 , pp. 487-493
    • Alonso, M.M.1    Jiang, H.2    Yokoyama, T.3    Xu, J.4    Bekele, N.B.5    Lang, F.F.6
  • 50
    • 43749104658 scopus 로고    scopus 로고
    • Oncolytic adenoviral mutants induce a novel mode of programmed cell death in ovarian cancer
    • doi:10.1038/sj.onc.1210977
    • Baird SK, Aerts JL, Eddaoudi A, Lockley M, Lemoine NR, McNeish IA. Oncolytic adenoviral mutants induce a novel mode of programmed cell death in ovarian cancer. Oncogene (2008) 27:3081-90. doi:10.1038/sj.onc.1210977.
    • (2008) Oncogene , vol.27 , pp. 3081-3090
    • Baird, S.K.1    Aerts, J.L.2    Eddaoudi, A.3    Lockley, M.4    Lemoine, N.R.5    McNeish, I.A.6
  • 52
    • 84861112821 scopus 로고    scopus 로고
    • Coxsackievirus B3 is an oncolytic virus with immunostimulatory properties that is active against lung adenocarcinoma
    • doi:10.1158/0008-5472.CAN-11-3185
    • Miyamoto S, Inoue H, Nakamura T, Yamada M, Sakamoto C, Urata Y, et al. Coxsackievirus B3 is an oncolytic virus with immunostimulatory properties that is active against lung adenocarcinoma. Cancer Res (2012) 72:2609-21. doi:10.1158/0008-5472.CAN-11-3185.
    • (2012) Cancer Res , vol.72 , pp. 2609-2621
    • Miyamoto, S.1    Inoue, H.2    Nakamura, T.3    Yamada, M.4    Sakamoto, C.5    Urata, Y.6
  • 53
  • 54
    • 27544491235 scopus 로고    scopus 로고
    • The enhanced tumor selectivity of an oncolytic vaccinia lacking the host range and antiapoptosis genes SPI-1 and SPI-2
    • doi:10.1158/0008-5472.CAN-05-1630
    • Guo ZS, Naik A, O'Malley ME, Popovic P, Demarco R, Hu Y, et al. The enhanced tumor selectivity of an oncolytic vaccinia lacking the host range and antiapoptosis genes SPI-1 and SPI-2. Cancer Res (2005) 65:9991-8. doi:10.1158/0008-5472.CAN-05-1630.
    • (2005) Cancer Res , vol.65 , pp. 9991-9998
    • Guo, Z.S.1    Naik, A.2    O'Malley, M.E.3    Popovic, P.4    Demarco, R.5    Hu, Y.6
  • 55
    • 79951508366 scopus 로고    scopus 로고
    • Synergistic anti-tumor effects between oncolytic vaccinia virus and paclitaxel are mediated by the IFN response and HMGB1
    • doi:10.1038/gt.2010.121
    • Huang B, Sikorski R, Kirn DH, Thorne SH. Synergistic anti-tumor effects between oncolytic vaccinia virus and paclitaxel are mediated by the IFN response and HMGB1. Gene Ther (2011) 18:164-72. doi:10.1038/gt.2010.121.
    • (2011) Gene Ther , vol.18 , pp. 164-172
    • Huang, B.1    Sikorski, R.2    Kirn, D.H.3    Thorne, S.H.4
  • 56
    • 84858762241 scopus 로고    scopus 로고
    • Oncolytic virus and anti-4-1BB combination therapy elicits strong anti-tumor immunity against established cancer
    • doi:10.1158/0008-5472.CAN-11-2788
    • John LB, Howland LJ, Flynn JK, West AC, Devaud C, Duong CP, et al. Oncolytic virus and anti-4-1BB combination therapy elicits strong anti-tumor immunity against established cancer. Cancer Res (2012) 72:1651-60. doi:10.1158/0008-5472.CAN-11-2788.
    • (2012) Cancer Res , vol.72 , pp. 1651-1660
    • John, L.B.1    Howland, L.J.2    Flynn, J.K.3    West, A.C.4    Devaud, C.5    Duong, C.P.6
  • 57
    • 84887431193 scopus 로고    scopus 로고
    • Vaccinia virus induces programmed necrosis in ovarian cancer cells
    • doi:10.1038/mt.2013.195
    • Whilding LM, Archibald KM, Kulbe H, Balkwill FR, Öberg D, McNeish IA. Vaccinia virus induces programmed necrosis in ovarian cancer cells. Mol Ther (2013) 21:2074-86. doi:10.1038/mt.2013.195.
    • (2013) Mol Ther , vol.21 , pp. 2074-2086
    • Whilding, L.M.1    Archibald, K.M.2    Kulbe, H.3    Balkwill, F.R.4    Öberg, D.5    McNeish, I.A.6
  • 58
    • 79251628505 scopus 로고    scopus 로고
    • Stepwise release of biologically active HMGB1 during HSV-2 infection
    • doi:10.1371/journal.pone.0016145
    • Borde C, Barnay-Verdier S, Gaillard C, Hocini H, Maréchal V, Gozlan J. Stepwise release of biologically active HMGB1 during HSV-2 infection. PLoS One (2011) 6:e16145. doi:10.1371/journal.pone.0016145.
    • (2011) PLoS One , vol.6
    • Borde, C.1    Barnay-Verdier, S.2    Gaillard, C.3    Hocini, H.4    Maréchal, V.5    Gozlan, J.6
  • 59
    • 84899085760 scopus 로고    scopus 로고
    • Complementary induction of immunogenic cell death by oncolytic parvovirus H-1PV and gemcitabine in pancreatic cancer
    • doi:10.1128/JVI.03688-13.
    • Angelova AL, Grekova SP, Heller A, Kuhlmann O, Soyka E, Giese T, et al. Complementary induction of immunogenic cell death by oncolytic parvovirus H-1PV and gemcitabine in pancreatic cancer. J Virol (2014). doi:10.1128/JVI.03688-13.
    • (2014) J Virol
    • Angelova, A.L.1    Grekova, S.P.2    Heller, A.3    Kuhlmann, O.4    Soyka, E.5    Giese, T.6
  • 60
    • 84878530852 scopus 로고    scopus 로고
    • Oncolytic adenovirus with temozolomide induces autophagy and antitumor immune responses in cancer patients
    • doi:10.1038/mt.2013.51
    • Liikanen I, Ahtiainen L, Hirvinen ML, Bramante S, Cerullo V, Nokisalmi P, et al. Oncolytic adenovirus with temozolomide induces autophagy and antitumor immune responses in cancer patients. Mol Ther (2013) 21:1212-23. doi:10.1038/mt.2013.51.
    • (2013) Mol Ther , vol.21 , pp. 1212-1223
    • Liikanen, I.1    Ahtiainen, L.2    Hirvinen, M.L.3    Bramante, S.4    Cerullo, V.5    Nokisalmi, P.6
  • 61
    • 42049104455 scopus 로고    scopus 로고
    • Virus-mediated oncolysis induces danger signal and stimulates cytotoxic T-lymphocyte activity via proteasome activator upregulation
    • doi:10.1038/sj.onc.1210884
    • Endo Y, Sakai R, Ouchi M, Onimatsu H, Hioki M, Kagawa S, et al. Virus-mediated oncolysis induces danger signal and stimulates cytotoxic T-lymphocyte activity via proteasome activator upregulation. Oncogene (2008) 27:2375-81. doi:10.1038/sj.onc.1210884.
    • (2008) Oncogene , vol.27 , pp. 2375-2381
    • Endo, Y.1    Sakai, R.2    Ouchi, M.3    Onimatsu, H.4    Hioki, M.5    Kagawa, S.6
  • 62
    • 77949423196 scopus 로고    scopus 로고
    • The HSV-2 mutant DeltaPK induces melanoma oncolysis through nonredundant death programs and associated with autophagy and pyroptosis proteins
    • doi:10.1038/gt.2009.126
    • Colunga AG, Laing JM, Aurelian L. The HSV-2 mutant DeltaPK induces melanoma oncolysis through nonredundant death programs and associated with autophagy and pyroptosis proteins. Gene Ther (2010) 17:315-27. doi:10.1038/gt.2009.126.
    • (2010) Gene Ther , vol.17 , pp. 315-327
    • Colunga, A.G.1    Laing, J.M.2    Aurelian, L.3
  • 63
    • 84878434348 scopus 로고    scopus 로고
    • Pyroptotic cells externalize eat-me and release find-me signals and are efficiently engulfed by macrophages
    • doi:10.1093/intimm/dxs161
    • Wang Q, Imamura R, Motani K, Kushiyama H, Nagata S, Suda T. Pyroptotic cells externalize eat-me and release find-me signals and are efficiently engulfed by macrophages. Int Immunol (2013) 25:363-72. doi:10.1093/intimm/dxs161.
    • (2013) Int Immunol , vol.25 , pp. 363-372
    • Wang, Q.1    Imamura, R.2    Motani, K.3    Kushiyama, H.4    Nagata, S.5    Suda, T.6
  • 64
  • 65
    • 0038277131 scopus 로고    scopus 로고
    • Oncolytic parvovirus H1 induces release of heat-shock protein HSP72 in susceptible human tumor cells but may not affect primary immune cells
    • doi:10.1038/sj.cgt.7700591
    • Moehler M, Zeidler M, Schede J, Rommelaere J, Galle PR, Cornelis JJ, et al. Oncolytic parvovirus H1 induces release of heat-shock protein HSP72 in susceptible human tumor cells but may not affect primary immune cells. Cancer Gene Ther (2003) 10:477-80. doi:10.1038/sj.cgt.7700591.
    • (2003) Cancer Gene Ther , vol.10 , pp. 477-480
    • Moehler, M.1    Zeidler, M.2    Schede, J.3    Rommelaere, J.4    Galle, P.R.5    Cornelis, J.J.6
  • 66
    • 78650312207 scopus 로고    scopus 로고
    • Immune cells participate in the oncosuppressive activity of parvovirus H-1PV and are activated as a result of their abortive infection with this agent
    • doi:10.4161/cbt.10.12.13455
    • Grekova S, Aprahamian M, Giese N, Schmitt S, Giese T, Falk CS, et al. Immune cells participate in the oncosuppressive activity of parvovirus H-1PV and are activated as a result of their abortive infection with this agent. Cancer Biol Ther (2010) 10:1280-9. doi:10.4161/cbt.10.12.13455.
    • (2010) Cancer Biol Ther , vol.10 , pp. 1280-1289
    • Grekova, S.1    Aprahamian, M.2    Giese, N.3    Schmitt, S.4    Giese, T.5    Falk, C.S.6
  • 67
    • 84863717012 scopus 로고    scopus 로고
    • Activation of a glioma-specific immune response by oncolytic parvovirus minute virus of mice infection
    • doi:10.1038/cgt.2012.20
    • Grekova SP, Raykov Z, Zawatzky R, Rommelaere J, Koch U. Activation of a glioma-specific immune response by oncolytic parvovirus minute virus of mice infection. Cancer Gene Ther (2012) 19:468-75. doi:10.1038/cgt.2012.20.
    • (2012) Cancer Gene Ther , vol.19 , pp. 468-475
    • Grekova, S.P.1    Raykov, Z.2    Zawatzky, R.3    Rommelaere, J.4    Koch, U.5
  • 68
    • 2442707797 scopus 로고    scopus 로고
    • Nucleosomes are exposed at the cell surface in apoptosis
    • Radic M, Marion T, Monestier M. Nucleosomes are exposed at the cell surface in apoptosis. J Immunol (2004) 172:6692-700.
    • (2004) J Immunol , vol.172 , pp. 6692-6700
    • Radic, M.1    Marion, T.2    Monestier, M.3
  • 69
    • 84855399703 scopus 로고    scopus 로고
    • P2Y6 receptor signaling pathway mediates inflammatory responses induced by monosodium urate crystals
    • doi:10.4049/jimmunol.1003746
    • Uratsuji H, Tada Y, Kawashima T, Kamata M, Hau CS, Asano Y, et al. P2Y6 receptor signaling pathway mediates inflammatory responses induced by monosodium urate crystals. J Immunol (2012) 188:436-44. doi:10.4049/jimmunol.1003746.
    • (2012) J Immunol , vol.188 , pp. 436-444
    • Uratsuji, H.1    Tada, Y.2    Kawashima, T.3    Kamata, M.4    Hau, C.S.5    Asano, Y.6
  • 70
    • 33746210139 scopus 로고    scopus 로고
    • Newcastle disease virus exerts oncolysis by both intrinsic and extrinsic caspase-dependent pathways of cell death
    • doi:10.1128/JVI.00241-06
    • Elankumaran S, Rockemann D, Samal SK. Newcastle disease virus exerts oncolysis by both intrinsic and extrinsic caspase-dependent pathways of cell death. J Virol (2006) 80:7522-34. doi:10.1128/JVI.00241-06.
    • (2006) J Virol , vol.80 , pp. 7522-7534
    • Elankumaran, S.1    Rockemann, D.2    Samal, S.K.3
  • 71
    • 84862813177 scopus 로고    scopus 로고
    • Newcastle disease virus triggers autophagy in U251 glioma cells to enhance virus replication
    • doi:10.1007/s00705-012-1270-6
    • Meng C, Zhou Z, Jiang K, Yu S, Jia L, Wu Y, et al. Newcastle disease virus triggers autophagy in U251 glioma cells to enhance virus replication. Arch Virol (2012) 157:1011-8. doi:10.1007/s00705-012-1270-6.
    • (2012) Arch Virol , vol.157 , pp. 1011-1018
    • Meng, C.1    Zhou, Z.2    Jiang, K.3    Yu, S.4    Jia, L.5    Wu, Y.6
  • 72
    • 0036654058 scopus 로고    scopus 로고
    • Human tumor cell infection by Newcastle disease virus leads to upregulation of HLA and cell adhesion molecules and to induction of interferons, chemokines and finally apoptosis
    • doi:10.3892/ijo.21.1.85
    • Washburn B, Schirrmacher V. Human tumor cell infection by Newcastle disease virus leads to upregulation of HLA and cell adhesion molecules and to induction of interferons, chemokines and finally apoptosis. Int J Oncol (2002) 21:85-93. doi:10.3892/ijo.21.1.85.
    • (2002) Int J Oncol , vol.21 , pp. 85-93
    • Washburn, B.1    Schirrmacher, V.2
  • 73
    • 84857185580 scopus 로고    scopus 로고
    • Newcastle disease virus induces pro-inflammatory conditions and type I interferon for counter-acting Treg activity
    • doi:10.3892/ijo.2011.1265
    • Fournier P, Arnold A, Wilden H, Schirrmacher V. Newcastle disease virus induces pro-inflammatory conditions and type I interferon for counter-acting Treg activity. Int J Oncol (2012) 40:840-50. doi:10.3892/ijo.2011.1265.
    • (2012) Int J Oncol , vol.40 , pp. 840-850
    • Fournier, P.1    Arnold, A.2    Wilden, H.3    Schirrmacher, V.4
  • 74
    • 84897476768 scopus 로고    scopus 로고
    • Localized oncolytic virotherapy overcomes systemic tumor resistance to immune checkpoint blockade immunotherapy
    • doi:10.1126/scitranslmed.3008095
    • Zamarin D, Holmgaard RB, Subudhi SK, Park JS, Mansour M, Palese P, et al. Localized oncolytic virotherapy overcomes systemic tumor resistance to immune checkpoint blockade immunotherapy. Sci Transl Med (2014) 6:226-32. doi:10.1126/scitranslmed.3008095.
    • (2014) Sci Transl Med , vol.6 , pp. 226-232
    • Zamarin, D.1    Holmgaard, R.B.2    Subudhi, S.K.3    Park, J.S.4    Mansour, M.5    Palese, P.6
  • 76
    • 84901068466 scopus 로고    scopus 로고
    • Oncolytic Newcastle disease virus as cutting edge between tumor and host
    • doi:10.3390/biology2030936
    • Fournier P, Schirrmacher V. Oncolytic Newcastle disease virus as cutting edge between tumor and host. Biology (2013) 2:936-75. doi:10.3390/biology2030936.
    • (2013) Biology , vol.2 , pp. 936-975
    • Fournier, P.1    Schirrmacher, V.2
  • 77
    • 0033881830 scopus 로고    scopus 로고
    • Reovirus-induced apoptosis is mediated by TRAIL
    • doi:10.1128/JVI.74.17.8135-8139.2000
    • Clarke P, Meintzer SM, Gibson S, Widmann C, Garrington TP, Johnson GL, et al. Reovirus-induced apoptosis is mediated by TRAIL. J Virol (2000) 74:8135-9. doi:10.1128/JVI.74.17.8135-8139.2000.
    • (2000) J Virol , vol.74 , pp. 8135-8139
    • Clarke, P.1    Meintzer, S.M.2    Gibson, S.3    Widmann, C.4    Garrington, T.P.5    Johnson, G.L.6
  • 78
    • 84879590236 scopus 로고    scopus 로고
    • Reovirus activates a caspase-independent cell death pathway
    • doi:10.1128/mBio.00178-13
    • Berger AK, Danthi P. Reovirus activates a caspase-independent cell death pathway. MBio (2013) 4:e178-113. doi:10.1128/mBio.00178-13.
    • (2013) MBio , vol.4
    • Berger, A.K.1    Danthi, P.2
  • 79
    • 84873280040 scopus 로고    scopus 로고
    • The p17 nonstructural protein of avian reovirus triggers autophagy enhancing virus replication via activation of phosphatase and tensin deleted on chromosome 10 (PTEN) and AMP-activated protein kinase (AMPK), as well as dsRNA-dependent protein kinase (PKR)/eIF2alpha signaling pathways
    • doi:10.1074/jbc.M112.390245
    • Chi PI, Huang WR, Lai IH, Cheng CY, Liu HJ. The p17 nonstructural protein of avian reovirus triggers autophagy enhancing virus replication via activation of phosphatase and tensin deleted on chromosome 10 (PTEN) and AMP-activated protein kinase (AMPK), as well as dsRNA-dependent protein kinase (PKR)/eIF2alpha signaling pathways. J Biol Chem (2012) 288:3571-84. doi:10.1074/jbc.M112.390245.
    • (2012) J Biol Chem , vol.288 , pp. 3571-3584
    • Chi, P.I.1    Huang, W.R.2    Lai, I.H.3    Cheng, C.Y.4    Liu, H.J.5
  • 80
    • 84862807921 scopus 로고    scopus 로고
    • Avian reovirus triggers autophagy in primary chicken fibroblast cells and Vero cells to promote virus production
    • doi:10.1007/s00705-012-1226-x
    • Meng S, Jiang K, Zhang X, Zhang M, Zhou Z, Hu M, et al. Avian reovirus triggers autophagy in primary chicken fibroblast cells and Vero cells to promote virus production. Arch Virol (2012) 157:661-8. doi:10.1007/s00705-012-1226-x.
    • (2012) Arch Virol , vol.157 , pp. 661-668
    • Meng, S.1    Jiang, K.2    Zhang, X.3    Zhang, M.4    Zhou, Z.5    Hu, M.6
  • 81
    • 84877342608 scopus 로고    scopus 로고
    • Reovirus modulates autophagy during oncolysis of multiple myeloma
    • doi:10.4161/auto.22867
    • Thirukkumaran CM, Shi ZQ, Luider J, Kopciuk K, Gao H, Bahlis N, et al. Reovirus modulates autophagy during oncolysis of multiple myeloma. Autophagy (2013) 9:413-4. doi:10.4161/auto.22867.
    • (2013) Autophagy , vol.9 , pp. 413-414
    • Thirukkumaran, C.M.1    Shi, Z.Q.2    Luider, J.3    Kopciuk, K.4    Gao, H.5    Bahlis, N.6
  • 82
    • 51049090205 scopus 로고    scopus 로고
    • Inflammatory tumour cell killing by oncolytic reovirus for the treatment of melanoma
    • doi:10.1038/gt.2008.58
    • Errington F, White CL, Twigger KR, Rose A, Scott K, Steele L, et al. Inflammatory tumour cell killing by oncolytic reovirus for the treatment of melanoma. Gene Ther (2008) 15:1257-70. doi:10.1038/gt.2008.58.
    • (2008) Gene Ther , vol.15 , pp. 1257-1270
    • Errington, F.1    White, C.L.2    Twigger, K.R.3    Rose, A.4    Scott, K.5    Steele, L.6
  • 83
    • 34548700796 scopus 로고    scopus 로고
    • Unveiling the roles of autophagy in innate and adaptive immunity
    • doi:10.1038/nri2161
    • Levine B, Deretic V. Unveiling the roles of autophagy in innate and adaptive immunity. Nat Rev Immunol (2007) 7:767-77. doi:10.1038/nri2161.
    • (2007) Nat Rev Immunol , vol.7 , pp. 767-777
    • Levine, B.1    Deretic, V.2
  • 84
    • 84869057548 scopus 로고    scopus 로고
    • RNase L triggers autophagy in response to viral infections
    • doi:10.1128/JVI.00270-12
    • Chakrabarti A, Ghosh PK, Banerjee S, Gaughan C, Silverman RH. RNase L triggers autophagy in response to viral infections. J Virol (2012) 86:11311-21. doi:10.1128/JVI.00270-12.
    • (2012) J Virol , vol.86 , pp. 11311-11321
    • Chakrabarti, A.1    Ghosh, P.K.2    Banerjee, S.3    Gaughan, C.4    Silverman, R.H.5
  • 85
    • 67349269904 scopus 로고    scopus 로고
    • Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection
    • doi:10.1038/ni.1720
    • English L, Chemali M, Duron J, Rondeau C, Laplante A, Gingras D, et al. Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection. Nat Immunol (2009) 10:480-7. doi:10.1038/ni.1720.
    • (2009) Nat Immunol , vol.10 , pp. 480-487
    • English, L.1    Chemali, M.2    Duron, J.3    Rondeau, C.4    Laplante, A.5    Gingras, D.6
  • 86
    • 36048964024 scopus 로고    scopus 로고
    • Analysis of the role of autophagy in replication of herpes simplex virus in cell culture
    • doi:10.1128/JVI.01356-07
    • Alexander DE, Ward SL, Mizushima N, Levine B, Leib DA. Analysis of the role of autophagy in replication of herpes simplex virus in cell culture. J Virol (2007) 81:12128-34. doi:10.1128/JVI.01356-07.
    • (2007) J Virol , vol.81 , pp. 12128-12134
    • Alexander, D.E.1    Ward, S.L.2    Mizushima, N.3    Levine, B.4    Leib, D.A.5
  • 87
    • 79960793780 scopus 로고    scopus 로고
    • Functional macroautophagy induction by influenza A virus without a contribution to major histocompatibility complex class II-restricted presentation
    • doi:10.1128/JVI.02122-10
    • Comber JD, Robinson TM, Siciliano NA, Snook AE, Eisenlohr LC. Functional macroautophagy induction by influenza A virus without a contribution to major histocompatibility complex class II-restricted presentation. J Virol (2010) 85:6453-63. doi:10.1128/JVI.02122-10.
    • (2010) J Virol , vol.85 , pp. 6453-6463
    • Comber, J.D.1    Robinson, T.M.2    Siciliano, N.A.3    Snook, A.E.4    Eisenlohr, L.C.5
  • 88
    • 83755181759 scopus 로고    scopus 로고
    • Autophagy-dependent anticancer immune responses induced by chemotherapeutic agents in mice
    • doi:10.1126/science.1208347
    • Michaud M, Martins I, Sukkurwala AQ, Adjemian S, Ma Y, Pellegatti P, et al. Autophagy-dependent anticancer immune responses induced by chemotherapeutic agents in mice. Science (2011) 334:1573-7. doi:10.1126/science.1208347.
    • (2011) Science , vol.334 , pp. 1573-1577
    • Michaud, M.1    Martins, I.2    Sukkurwala, A.Q.3    Adjemian, S.4    Ma, Y.5    Pellegatti, P.6
  • 89
    • 84863103053 scopus 로고    scopus 로고
    • ATP release from dying autophagic cells and their phagocytosis are crucial for inflammasome activation in macrophages
    • doi:10.1371/journal.pone.0040069
    • Ayna G, Krysko DV, Kaczmarek A, Petrovski G, Vandenabeele P, Fésüs L. ATP release from dying autophagic cells and their phagocytosis are crucial for inflammasome activation in macrophages. PLoS One (2012) 7:e40069. doi:10.1371/journal.pone.0040069.
    • (2012) PLoS One , vol.7
    • Ayna, G.1    Krysko, D.V.2    Kaczmarek, A.3    Petrovski, G.4    Vandenabeele, P.5    Fésüs, L.6
  • 90
    • 57649217868 scopus 로고    scopus 로고
    • Autophagy regulates selective HMGB1 release in tumor cells that are destined to die
    • doi:10.1038/cdd.2008.143
    • Thorburn J, Horita H, Redzic J, Hansen K, Frankel AE, Thorburn A. Autophagy regulates selective HMGB1 release in tumor cells that are destined to die. Cell Death Differ (2009) 16:175-83. doi:10.1038/cdd.2008.143.
    • (2009) Cell Death Differ , vol.16 , pp. 175-183
    • Thorburn, J.1    Horita, H.2    Redzic, J.3    Hansen, K.4    Frankel, A.E.5    Thorburn, A.6
  • 91
    • 20344361954 scopus 로고    scopus 로고
    • Autophagy promotes MHC class II presentation of peptides from intracellular source proteins
    • doi:10.1073/pnas.0501190102
    • Dengjel J, Schoor O, Fischer R, Reich M, Kraus M, Müller M, et al. Autophagy promotes MHC class II presentation of peptides from intracellular source proteins. Proc Natl Acad Sci U S A (2005) 102:7922-7. doi:10.1073/pnas.0501190102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 7922-7927
    • Dengjel, J.1    Schoor, O.2    Fischer, R.3    Reich, M.4    Kraus, M.5    Müller, M.6
  • 92
    • 52049102433 scopus 로고    scopus 로고
    • Efficient cross-presentation depends on autophagy in tumor cells
    • doi:10.1158/0008-5472.CAN-08-0161
    • Li Y, Wang LX, Yang G, Hao F, Urba WJ, Hu HM. Efficient cross-presentation depends on autophagy in tumor cells. Cancer Res (2008) 68:6889-95. doi:10.1158/0008-5472.CAN-08-0161.
    • (2008) Cancer Res , vol.68 , pp. 6889-6895
    • Li, Y.1    Wang, L.X.2    Yang, G.3    Hao, F.4    Urba, W.J.5    Hu, H.M.6
  • 93
    • 78650642085 scopus 로고    scopus 로고
    • Influenza A infection enhances cross-priming of CD8+ T cells to cell-associated antigens in a TLR7- and type I IFN-dependent fashion
    • doi:10.4049/jimmunol.1002129
    • Wei J, Waithman J, Lata R, Mifsud NA, Cebon J, Kay T, et al. Influenza A infection enhances cross-priming of CD8+ T cells to cell-associated antigens in a TLR7- and type I IFN-dependent fashion. J Immunol (2010) 185:6013-22. doi:10.4049/jimmunol.1002129.
    • (2010) J Immunol , vol.185 , pp. 6013-6022
    • Wei, J.1    Waithman, J.2    Lata, R.3    Mifsud, N.A.4    Cebon, J.5    Kay, T.6
  • 94
    • 49649111732 scopus 로고    scopus 로고
    • Measles virus induces oncolysis of mesothelioma cells and allows dendritic cells to cross-prime tumor-specific CD8 response
    • doi:10.1158/0008-5472.CAN-07-6265
    • Gauvrit A, Brandler S, Sapede-Peroz C, Boisgerault N, Tangy F, Gregoire M. Measles virus induces oncolysis of mesothelioma cells and allows dendritic cells to cross-prime tumor-specific CD8 response. Cancer Res (2008) 68:4882-92. doi:10.1158/0008-5472.CAN-07-6265.
    • (2008) Cancer Res , vol.68 , pp. 4882-4892
    • Gauvrit, A.1    Brandler, S.2    Sapede-Peroz, C.3    Boisgerault, N.4    Tangy, F.5    Gregoire, M.6
  • 95
    • 67549117101 scopus 로고    scopus 로고
    • Autophagy within the antigen donor cell facilitates efficient antigen cross-priming of virus-specific CD8+ T cells
    • doi:10.1038/cdd.2009.8
    • Uhl M, Kepp O, Jusforgues-Saklani H, Vicencio JM, Kroemer G, Albert ML. Autophagy within the antigen donor cell facilitates efficient antigen cross-priming of virus-specific CD8+ T cells. Cell Death Differ (2009) 16:991-1005. doi:10.1038/cdd.2009.8.
    • (2009) Cell Death Differ , vol.16 , pp. 991-1005
    • Uhl, M.1    Kepp, O.2    Jusforgues-Saklani, H.3    Vicencio, J.M.4    Kroemer, G.5    Albert, M.L.6
  • 96
    • 81255138298 scopus 로고    scopus 로고
    • Tumor-derived autophagosome vaccine: mechanism of cross-presentation and therapeutic efficacy
    • doi:10.1158/1078-0432.CCR-11-0951
    • Li Y, Wang LX, Pang P, Cui Z, Aung S, Haley D, et al. Tumor-derived autophagosome vaccine: mechanism of cross-presentation and therapeutic efficacy. Clin Cancer Res (2011) 17:7047-57. doi:10.1158/1078-0432.CCR-11-0951.
    • (2011) Clin Cancer Res , vol.17 , pp. 7047-7057
    • Li, Y.1    Wang, L.X.2    Pang, P.3    Cui, Z.4    Aung, S.5    Haley, D.6
  • 97
    • 84877918290 scopus 로고    scopus 로고
    • Targeting autophagy to enhance oncolytic virus-based cancer therapy
    • doi:10.1517/14712598.2013.774365
    • Meng S, Xu J, Wu Y, Ding C. Targeting autophagy to enhance oncolytic virus-based cancer therapy. Expert Opin Biol Ther (2013) 13:863-73. doi:10.1517/14712598.2013.774365.
    • (2013) Expert Opin Biol Ther , vol.13 , pp. 863-873
    • Meng, S.1    Xu, J.2    Wu, Y.3    Ding, C.4
  • 98
    • 0027262606 scopus 로고
    • Stabilization of the p53 tumor suppressor is induced by adenovirus 5 E1A and accompanies apoptosis
    • doi:10.1101/gad.7.4.535
    • Lowe SW, Ruley HE. Stabilization of the p53 tumor suppressor is induced by adenovirus 5 E1A and accompanies apoptosis. Genes Dev (1993) 7:535-45. doi:10.1101/gad.7.4.535.
    • (1993) Genes Dev , vol.7 , pp. 535-545
    • Lowe, S.W.1    Ruley, H.E.2
  • 99
    • 0027251720 scopus 로고
    • Wild-type p53 mediates apoptosis by E1A, which is inhibited by E1B
    • doi:10.1101/gad.7.4.546
    • Debbas M, White E. Wild-type p53 mediates apoptosis by E1A, which is inhibited by E1B. Genes Dev (1993) 7:546-54. doi:10.1101/gad.7.4.546.
    • (1993) Genes Dev , vol.7 , pp. 546-554
    • Debbas, M.1    White, E.2
  • 100
    • 0033634781 scopus 로고    scopus 로고
    • TNF-alpha signals apoptosis through a bid-dependent conformational change in Bax that is inhibited by E1B 19K
    • doi:10.1016/S1097-2765(00)00007-1
    • Perez D, White E. TNF-alpha signals apoptosis through a bid-dependent conformational change in Bax that is inhibited by E1B 19K. Mol Cell (2000) 6:53-63. doi:10.1016/S1097-2765(00)00007-1.
    • (2000) Mol Cell , vol.6 , pp. 53-63
    • Perez, D.1    White, E.2
  • 101
    • 0026773471 scopus 로고
    • The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor alpha
    • White E, Sabbatini P, Debbas M, Wold WS, Kusher DI, Gooding LR. The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor alpha. Mol Cell Biol (1992) 12:2570-80.
    • (1992) Mol Cell Biol , vol.12 , pp. 2570-2580
    • White, E.1    Sabbatini, P.2    Debbas, M.3    Wold, W.S.4    Kusher, D.I.5    Gooding, L.R.6
  • 102
    • 0029847416 scopus 로고    scopus 로고
    • Expression of p53 in Saos-2 osteosarcoma cells induces apoptosis which can be inhibited by Bcl-2 or the adenovirus E1B-55 kDa protein
    • Marcellus RC, Teodoro JG, Charbonneau R, Shore GC, Branton PE. Expression of p53 in Saos-2 osteosarcoma cells induces apoptosis which can be inhibited by Bcl-2 or the adenovirus E1B-55 kDa protein. Cell Growth Differ (1996) 7:1643-50.
    • (1996) Cell Growth Differ , vol.7 , pp. 1643-1650
    • Marcellus, R.C.1    Teodoro, J.G.2    Charbonneau, R.3    Shore, G.C.4    Branton, P.E.5
  • 103
    • 0035793551 scopus 로고    scopus 로고
    • Three adenovirus E3 proteins cooperate to evade apoptosis by tumor necrosis factor-related apoptosis-inducing ligand receptor-1 and -2
    • doi:10.1074/jbc.M008218200
    • Benedict CA, Norris PS, Prigozy TI, Bodmer JL, Mahr JA, Garnett CT, et al. Three adenovirus E3 proteins cooperate to evade apoptosis by tumor necrosis factor-related apoptosis-inducing ligand receptor-1 and -2. J Biol Chem (2001) 276:3270-8. doi:10.1074/jbc.M008218200.
    • (2001) J Biol Chem , vol.276 , pp. 3270-3278
    • Benedict, C.A.1    Norris, P.S.2    Prigozy, T.I.3    Bodmer, J.L.4    Mahr, J.A.5    Garnett, C.T.6
  • 104
    • 33947715151 scopus 로고    scopus 로고
    • HSV-1 ICP34.5 confers neurovirulence by targeting the beclin 1 autophagy protein
    • doi:10.1016/j.chom.2006.12.001
    • Orvedahl A, Alexander D, Tallóczy Z, Sun Q, Wei Y, Zhang W, et al. HSV-1 ICP34.5 confers neurovirulence by targeting the beclin 1 autophagy protein. Cell Host Microbe (2007) 1:23-35. doi:10.1016/j.chom.2006.12.001.
    • (2007) Cell Host Microbe , vol.1 , pp. 23-35
    • Orvedahl, A.1    Alexander, D.2    Tallóczy, Z.3    Sun, Q.4    Wei, Y.5    Zhang, W.6
  • 105
    • 0031868959 scopus 로고    scopus 로고
    • The second-site mutation in the herpes simplex virus recombinants lacking the gamma134.5 genes precludes shutoff of protein synthesis by blocking the phosphorylation of eIF-2alpha
    • Cassady KA, Gross M, Roizman B. The second-site mutation in the herpes simplex virus recombinants lacking the gamma134.5 genes precludes shutoff of protein synthesis by blocking the phosphorylation of eIF-2alpha. J Virol (1998) 72:7005-11.
    • (1998) J Virol , vol.72 , pp. 7005-7011
    • Cassady, K.A.1    Gross, M.2    Roizman, B.3
  • 106
    • 0030727823 scopus 로고    scopus 로고
    • Herpes simplex virus 1716, an ICP 34.5 null mutant, is unable to replicate in CV-1 cells due to a translational block that can be overcome by coinfection with SV40
    • Randazzo BP, Tal-Singer R, Zabolotny JM, Kesari S, Fraser NW. Herpes simplex virus 1716, an ICP 34.5 null mutant, is unable to replicate in CV-1 cells due to a translational block that can be overcome by coinfection with SV40. J Gen Virol (1997) 78(Pt 12):3333-9.
    • (1997) J Gen Virol , vol.78 , Issue.PART 12 , pp. 3333-3339
    • Randazzo, B.P.1    Tal-Singer, R.2    Zabolotny, J.M.3    Kesari, S.4    Fraser, N.W.5
  • 107
    • 0026539149 scopus 로고
    • The gamma 1(34.5) gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programed cell death in neuronal cells
    • doi:10.1073/pnas.89.8.3266
    • Chou J, Roizman B. The gamma 1(34.5) gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programed cell death in neuronal cells. Proc Natl Acad Sci U S A (1992) 89:3266-70. doi:10.1073/pnas.89.8.3266.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 3266-3270
    • Chou, J.1    Roizman, B.2
  • 108
    • 0032830315 scopus 로고    scopus 로고
    • Herpes simplex virus inhibits apoptosis through the action of two genes, Us5 and Us3
    • Jerome KR, Fox R, Chen Z, Sears AE, Lee Hy, Corey L. Herpes simplex virus inhibits apoptosis through the action of two genes, Us5 and Us3. J Virol (1999) 73:8950-7.
    • (1999) J Virol , vol.73 , pp. 8950-8957
    • Jerome, K.R.1    Fox, R.2    Chen, Z.3    Sears, A.E.4    Lee, H.5    Corey, L.6
  • 109
    • 0026736421 scopus 로고
    • The vaccinia virus K2L gene encodes a serine protease inhibitor which inhibits cell-cell fusion
    • doi:10.1016/0042-6822(92)90591-C
    • Zhou J, Sun XY, Fernando GJ, Frazer IH. The vaccinia virus K2L gene encodes a serine protease inhibitor which inhibits cell-cell fusion. Virology (1992) 189:678-86. doi:10.1016/0042-6822(92)90591-C.
    • (1992) Virology , vol.189 , pp. 678-686
    • Zhou, J.1    Sun, X.Y.2    Fernando, G.J.3    Frazer, I.H.4
  • 110
    • 0029813306 scopus 로고    scopus 로고
    • Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product
    • Dobbelstein M, Shenk T. Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product. J Virol (1996) 70:6479-85.
    • (1996) J Virol , vol.70 , pp. 6479-6485
    • Dobbelstein, M.1    Shenk, T.2
  • 111
    • 27644535708 scopus 로고    scopus 로고
    • The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation
    • doi:10.1128/JVI.79.22.14031-14043.2005
    • Wasilenko ST, Banadyga L, Bond D, Barry M. The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation. J Virol (2005) 79:14031-43. doi:10.1128/JVI.79.22.14031-14043.2005.
    • (2005) J Virol , vol.79 , pp. 14031-14043
    • Wasilenko, S.T.1    Banadyga, L.2    Bond, D.3    Barry, M.4
  • 112
    • 34249787896 scopus 로고    scopus 로고
    • Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein
    • doi:10.1099/vir.0.82772-0
    • Cooray S, Bahar MW, Abrescia NG, McVey CE, Bartlett NW, Chen RA, et al. Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein. J Gen Virol (2007) 88:1656-66. doi:10.1099/vir.0.82772-0.
    • (2007) J Gen Virol , vol.88 , pp. 1656-1666
    • Cooray, S.1    Bahar, M.W.2    Abrescia, N.G.3    McVey, C.E.4    Bartlett, N.W.5    Chen, R.A.6
  • 113
    • 0034192298 scopus 로고    scopus 로고
    • M11L: a novel mitochondria-localized protein of myxoma virus that blocks apoptosis of infected leukocytes
    • doi:10.1084/jem.191.9.1487
    • Everett H, Barry M, Lee SF, Sun X, Graham K, Stone J, et al. M11L: a novel mitochondria-localized protein of myxoma virus that blocks apoptosis of infected leukocytes. J Exp Med (2000) 191:1487-98. doi:10.1084/jem.191.9.1487.
    • (2000) J Exp Med , vol.191 , pp. 1487-1498
    • Everett, H.1    Barry, M.2    Lee, S.F.3    Sun, X.4    Graham, K.5    Stone, J.6
  • 114
    • 0029971614 scopus 로고    scopus 로고
    • Expression of the myxoma virus tumor necrosis factor receptor homologue and M11L genes is required to prevent virus-induced apoptosis in infected rabbit T lymphocytes
    • doi:10.1006/viro.1996.0183
    • Macen JL, Graham KA, Lee SF, Schreiber M, Boshkov LK, McFadden G. Expression of the myxoma virus tumor necrosis factor receptor homologue and M11L genes is required to prevent virus-induced apoptosis in infected rabbit T lymphocytes. Virology (1996) 218:232-7. doi:10.1006/viro.1996.0183.
    • (1996) Virology , vol.218 , pp. 232-237
    • Macen, J.L.1    Graham, K.A.2    Lee, S.F.3    Schreiber, M.4    Boshkov, L.K.5    McFadden, G.6
  • 115
    • 77954593965 scopus 로고    scopus 로고
    • Virus inhibition of RIP3-dependent necrosis
    • doi:10.1016/j.chom.2010.03.006
    • Upton JW, Kaiser WJ, Mocarski ES. Virus inhibition of RIP3-dependent necrosis. Cell Host Microbe (2010) 7:302-13. doi:10.1016/j.chom.2010.03.006.
    • (2010) Cell Host Microbe , vol.7 , pp. 302-313
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 116
    • 72649105081 scopus 로고    scopus 로고
    • Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes
    • doi:10.1016/j.chom.2009.09.005
    • Gannagé M, Dormann D, Albrecht R, Dengjel J, Torossi T, Rämer PC, et al. Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes. Cell Host Microbe (2009) 6:367-80. doi:10.1016/j.chom.2009.09.005.
    • (2009) Cell Host Microbe , vol.6 , pp. 367-380
    • Gannagé, M.1    Dormann, D.2    Albrecht, R.3    Dengjel, J.4    Torossi, T.5    Rämer, P.C.6
  • 117
    • 84888029430 scopus 로고    scopus 로고
    • Influenza A virus proteins NS1 and hemagglutinin along with M2 are involved in stimulation of autophagy in infected cells
    • doi:10.1128/JVI.02148-13
    • Zhirnov OP, Klenk HD. Influenza A virus proteins NS1 and hemagglutinin along with M2 are involved in stimulation of autophagy in infected cells. J Virol (2013) 87:13107-14. doi:10.1128/JVI.02148-13.
    • (2013) J Virol , vol.87 , pp. 13107-13114
    • Zhirnov, O.P.1    Klenk, H.D.2
  • 118
    • 84890023653 scopus 로고    scopus 로고
    • Hemagglutinin protein of measles virus induces apoptosis of HeLa cells via both extrinsic and intrinsic pathways
    • doi:10.1139/cjm-2013-0544
    • Yi C, Liu X, Liu Y, Lu S, Qi Y. Hemagglutinin protein of measles virus induces apoptosis of HeLa cells via both extrinsic and intrinsic pathways. Can J Microbiol (2013) 59:814-24. doi:10.1139/cjm-2013-0544.
    • (2013) Can J Microbiol , vol.59 , pp. 814-824
    • Yi, C.1    Liu, X.2    Liu, Y.3    Lu, S.4    Qi, Y.5
  • 119
    • 77953483387 scopus 로고    scopus 로고
    • Pathogen recognition by the cell surface receptor CD46 induces autophagy
    • doi:10.4161/auto.6.2.11132
    • Meiffren G, Joubert PE, Grégoire IP, Codogno P, Rabourdin-Combe C, Faure M. Pathogen recognition by the cell surface receptor CD46 induces autophagy. Autophagy (2010) 6:299-300. doi:10.4161/auto.6.2.11132.
    • (2010) Autophagy , vol.6 , pp. 299-300
    • Meiffren, G.1    Joubert, P.E.2    Grégoire, I.P.3    Codogno, P.4    Rabourdin-Combe, C.5    Faure, M.6
  • 120
    • 0041387412 scopus 로고    scopus 로고
    • Newcastle disease virus V protein is a determinant of host range restriction
    • doi:10.1128/JVI.77.17.9522-9532.2003
    • Park MS, García-Sastre A, Cros JF, Basler CF, Palese P. Newcastle disease virus V protein is a determinant of host range restriction. J Virol (2003) 77:9522-32. doi:10.1128/JVI.77.17.9522-9532.2003.
    • (2003) J Virol , vol.77 , pp. 9522-9532
    • Park, M.S.1    García-Sastre, A.2    Cros, J.F.3    Basler, C.F.4    Palese, P.5
  • 121
    • 0036547417 scopus 로고    scopus 로고
    • Death and anti-death: tumour resistance to apoptosis
    • doi:10.1038/nrc776
    • Igney FH, Krammer PH. Death and anti-death: tumour resistance to apoptosis. Nat Rev Cancer (2002) 2:277-88. doi:10.1038/nrc776.
    • (2002) Nat Rev Cancer , vol.2 , pp. 277-288
    • Igney, F.H.1    Krammer, P.H.2
  • 122
    • 84862006553 scopus 로고    scopus 로고
    • Dysregulation of TNFalpha-induced necroptotic signaling in chronic lymphocytic leukemia: suppression of CYLD gene by LEF1
    • doi:10.1038/leu.2011.357
    • Liu P, Xu B, Shen W, Zhu H, Wu W, Fu Y, et al. Dysregulation of TNFalpha-induced necroptotic signaling in chronic lymphocytic leukemia: suppression of CYLD gene by LEF1. Leukemia (2012) 26:1293-300. doi:10.1038/leu.2011.357.
    • (2012) Leukemia , vol.26 , pp. 1293-1300
    • Liu, P.1    Xu, B.2    Shen, W.3    Zhu, H.4    Wu, W.5    Fu, Y.6
  • 123
    • 78650305124 scopus 로고    scopus 로고
    • An inactivating CYLD mutation promotes skin tumor progression by conferring enhanced proliferative, survival and angiogenic properties to epidermal cancer cells
    • doi:10.1038/onc.2010.378
    • Alameda JP, Moreno-Maldonado R, Navarro M, Bravo A, Ramírez A, Page A, et al. An inactivating CYLD mutation promotes skin tumor progression by conferring enhanced proliferative, survival and angiogenic properties to epidermal cancer cells. Oncogene (2010) 29:6522-32. doi:10.1038/onc.2010.378.
    • (2010) Oncogene , vol.29 , pp. 6522-6532
    • Alameda, J.P.1    Moreno-Maldonado, R.2    Navarro, M.3    Bravo, A.4    Ramírez, A.5    Page, A.6
  • 124
    • 34250748014 scopus 로고    scopus 로고
    • Shikonin circumvents cancer drug resistance by induction of a necroptotic death
    • doi:10.1158/1535-7163.MCT-06-0511
    • Han W, Li L, Qiu S, Lu Q, Pan Q, Gu Y, et al. Shikonin circumvents cancer drug resistance by induction of a necroptotic death. Mol Cancer Ther (2007) 6:1641-9. doi:10.1158/1535-7163.MCT-06-0511.
    • (2007) Mol Cancer Ther , vol.6 , pp. 1641-1649
    • Han, W.1    Li, L.2    Qiu, S.3    Lu, Q.4    Pan, Q.5    Gu, Y.6
  • 125
    • 77957253429 scopus 로고    scopus 로고
    • OPTIM trial: a phase III trial of an oncolytic herpes virus encoding GM-CSF for unresectable stage III or IV melanoma
    • doi:10.2217/fon.10.66
    • Kaufman HL, Bines SD. OPTIM trial: a phase III trial of an oncolytic herpes virus encoding GM-CSF for unresectable stage III or IV melanoma. Future Oncol (2010) 6:941-9. doi:10.2217/fon.10.66.
    • (2010) Future Oncol , vol.6 , pp. 941-949
    • Kaufman, H.L.1    Bines, S.D.2
  • 126
    • 3042735443 scopus 로고    scopus 로고
    • An E1B-19 kDa gene deletion mutant adenovirus demonstrates tumor necrosis factor-enhanced cancer selectivity and enhanced oncolytic potency
    • doi:10.1016/j.ymthe.2004.03.017
    • Liu TC, Hallden G, Wang Y, Brooks G, Francis J, Lemoine N, et al. An E1B-19 kDa gene deletion mutant adenovirus demonstrates tumor necrosis factor-enhanced cancer selectivity and enhanced oncolytic potency. Mol Ther (2004) 9:786-803. doi:10.1016/j.ymthe.2004.03.017.
    • (2004) Mol Ther , vol.9 , pp. 786-803
    • Liu, T.C.1    Hallden, G.2    Wang, Y.3    Brooks, G.4    Francis, J.5    Lemoine, N.6
  • 127
    • 84891828604 scopus 로고    scopus 로고
    • Combining oncolytic HSV-1 with immunogenic cell death-inducing drug mitoxantrone breaks cancer immune tolerance and improves therapeutic efficacy
    • doi:10.1158/2326-6066.CIR-13-0059-T
    • Workenhe ST, Pol JG, Lichty BD, Cummings DT, Mossman KL. Combining oncolytic HSV-1 with immunogenic cell death-inducing drug mitoxantrone breaks cancer immune tolerance and improves therapeutic efficacy. Cancer Immunol Res (2013) 1:309-19. doi:10.1158/2326-6066.CIR-13-0059-T.
    • (2013) Cancer Immunol Res , vol.1 , pp. 309-319
    • Workenhe, S.T.1    Pol, J.G.2    Lichty, B.D.3    Cummings, D.T.4    Mossman, K.L.5
  • 128
    • 84884365359 scopus 로고    scopus 로고
    • Combination of autophagy inducer rapamycin and oncolytic adenovirus improves antitumor effect in cancer cells
    • doi:10.1186/1743-422X-10-293
    • Cheng PH, Lian S, Zhao R, Rao XM, McMasters KM, Zhou HS. Combination of autophagy inducer rapamycin and oncolytic adenovirus improves antitumor effect in cancer cells. Virol J (2013) 10:293. doi:10.1186/1743-422X-10-293.
    • (2013) Virol J , vol.10 , pp. 293
    • Cheng, P.H.1    Lian, S.2    Zhao, R.3    Rao, X.M.4    McMasters, K.M.5    Zhou, H.S.6
  • 129
    • 84875225339 scopus 로고    scopus 로고
    • Randomized dose-finding clinical trial of oncolytic immunotherapeutic vaccinia JX-594 in liver cancer
    • doi:10.1038/nm.3089
    • Heo J, Reid T, Ruo L, Breitbach CJ, Rose S, Bloomston M, et al. Randomized dose-finding clinical trial of oncolytic immunotherapeutic vaccinia JX-594 in liver cancer. Nat Med (2013) 19:329-36. doi:10.1038/nm.3089.
    • (2013) Nat Med , vol.19 , pp. 329-336
    • Heo, J.1    Reid, T.2    Ruo, L.3    Breitbach, C.J.4    Rose, S.5    Bloomston, M.6
  • 130
    • 70350536582 scopus 로고    scopus 로고
    • Host lymphodepletion enhances the therapeutic activity of an oncolytic vaccinia virus expressing 4-1BB ligand
    • doi:10.1158/0008-5472.CAN-09-2522
    • Kim HS, Kim-Schulze S, Kim DW, Kaufman HL. Host lymphodepletion enhances the therapeutic activity of an oncolytic vaccinia virus expressing 4-1BB ligand. Cancer Res (2009) 69:8516-25. doi:10.1158/0008-5472.CAN-09-2522.
    • (2009) Cancer Res , vol.69 , pp. 8516-8525
    • Kim, H.S.1    Kim-Schulze, S.2    Kim, D.W.3    Kaufman, H.L.4
  • 131
    • 79953327283 scopus 로고    scopus 로고
    • Chemokine expression from oncolytic vaccinia virus enhances vaccine therapies of cancer
    • doi:10.1038/mt.2010.312
    • Li J, O'Malley M, Urban J, Sampath P, Guo ZS, Kalinski P, et al. Chemokine expression from oncolytic vaccinia virus enhances vaccine therapies of cancer. Mol Ther (2011) 19:650-7. doi:10.1038/mt.2010.312.
    • (2011) Mol Ther , vol.19 , pp. 650-657
    • Li, J.1    O'Malley, M.2    Urban, J.3    Sampath, P.4    Guo, Z.S.5    Kalinski, P.6
  • 132
    • 84891817178 scopus 로고    scopus 로고
    • T-cell engager-armed oncolytic vaccinia virus significantly enhances antitumor therapy
    • doi:10.1038/mt.2013.240
    • Yu F, Wang X, Guo ZS, Bartlett DL, Gottschalk SM, Song XT. T-cell engager-armed oncolytic vaccinia virus significantly enhances antitumor therapy. Mol Ther (2014) 22:102-11. doi:10.1038/mt.2013.240.
    • (2014) Mol Ther , vol.22 , pp. 102-111
    • Yu, F.1    Wang, X.2    Guo, Z.S.3    Bartlett, D.L.4    Gottschalk, S.M.5    Song, X.T.6
  • 133
    • 41949109932 scopus 로고    scopus 로고
    • Redirecting adaptive immunity against foreign antigens to tumors for cancer therapy
    • doi:10.4161/cbt.6.11.4855
    • Hu W, Davis JJ, Zhu H, Dong F, Guo W, Ang J, et al. Redirecting adaptive immunity against foreign antigens to tumors for cancer therapy. Cancer Biol Ther (2007) 6:1773-9. doi:10.4161/cbt.6.11.4855.
    • (2007) Cancer Biol Ther , vol.6 , pp. 1773-1779
    • Hu, W.1    Davis, J.J.2    Zhu, H.3    Dong, F.4    Guo, W.5    Ang, J.6
  • 134
    • 84878074018 scopus 로고    scopus 로고
    • Antiviral and antitumor T-cell immunity in patients treated with GM-CSF-coding oncolytic adenovirus
    • doi:10.1158/1078-0432.CCR-12-2546
    • Kanerva A, Nokisalmi P, Diaconu I, Koski A, Cerullo V, Liikanen I, et al. Antiviral and antitumor T-cell immunity in patients treated with GM-CSF-coding oncolytic adenovirus. Clin Cancer Res (2013) 19:2734-44. doi:10.1158/1078-0432.CCR-12-2546.
    • (2013) Clin Cancer Res , vol.19 , pp. 2734-2744
    • Kanerva, A.1    Nokisalmi, P.2    Diaconu, I.3    Koski, A.4    Cerullo, V.5    Liikanen, I.6
  • 135
    • 84895907145 scopus 로고    scopus 로고
    • Oncolytic virotherapy and immunogenic cancer cell death: sharpening the sword for improved cancer treatment strategies
    • doi:10.1038/mt.2013.220
    • Workenhe ST, Mossman KL. Oncolytic virotherapy and immunogenic cancer cell death: sharpening the sword for improved cancer treatment strategies. Mol Ther (2014) 22:251-6. doi:10.1038/mt.2013.220.
    • (2014) Mol Ther , vol.22 , pp. 251-256
    • Workenhe, S.T.1    Mossman, K.L.2
  • 136
    • 84902145394 scopus 로고    scopus 로고
    • The strength of the T cell response against a surrogate tumor antigen induced by oncolytic VSV therapy does not correlate with tumor control
    • doi:10.1038/mt.2014.34.
    • Janelle V, Langlois MP, Lapierre P, Charpentier T, Poliquin L, Lamarre A. The strength of the T cell response against a surrogate tumor antigen induced by oncolytic VSV therapy does not correlate with tumor control. Mol Ther (2014). doi:10.1038/mt.2014.34.
    • (2014) Mol Ther
    • Janelle, V.1    Langlois, M.P.2    Lapierre, P.3    Charpentier, T.4    Poliquin, L.5    Lamarre, A.6


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