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Volumn 35, Issue 7, 2014, Pages 6255-6264

Translational regulator eIF2α in tumor

Author keywords

EIF2 ; Stress response; Translation initiation; Tumor; Tumor therapy

Indexed keywords

2 AMINO N [4 [5 (2 PHENANTHRENYL) 3 TRIFLUOROMETHYL 1H PYRAZOL 1 YL]PHENYL]ACETAMIDE; ARSENIC TRIOXIDE; INITIATION FACTOR 2ALPHA; LAPATINIB; SALUBRINAL; SORAFENIB; SULFORAPHANE; SUNITINIB; VORINOSTAT;

EID: 84905060749     PISSN: 10104283     EISSN: 14230380     Source Type: Journal    
DOI: 10.1007/s13277-014-1789-0     Document Type: Article
Times cited : (30)

References (95)
  • 2
    • 84874750871 scopus 로고    scopus 로고
    • Corrigendum: Global quantification of mammalian gene expression control
    • Schwanhausser B, Busse D, Li N, Dittmar G, Schuchhardt J, Wolf J, et al. Corrigendum: global quantification of mammalian gene expression control. Nature. 2013;495:126-7.
    • (2013) Nature , vol.495 , pp. 126-127
    • Schwanhausser, B.1    Busse, D.2    Li, N.3    Dittmar, G.4    Schuchhardt, J.5    Wolf, J.6
  • 3
    • 84866782195 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism
    • Baird TD, Wek RC. Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism. Adv Nutr. 2012;3:307-21.
    • (2012) Adv Nutr , vol.3 , pp. 307-321
    • Baird, T.D.1    Wek, R.C.2
  • 4
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - A key regulatory factor in tumour growth
    • Harris AL. Hypoxia - a key regulatory factor in tumour growth. Nat Rev Cancer. 2002;2:38-47. (Pubitemid 37328806)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.1 , pp. 38-47
    • Harris, A.L.1
  • 5
    • 11844254414 scopus 로고    scopus 로고
    • Normalization of tumor vasculature: An emerging concept in antiangiogenic therapy
    • DOI 10.1126/science.1104819
    • Jain RK. Normalization of tumor vasculature: an emerging concept in antiangiogenic therapy. Science. 2005;307:58-62. (Pubitemid 40093472)
    • (2005) Science , vol.307 , Issue.5706 , pp. 58-62
    • Jain, R.K.1
  • 6
    • 79954437206 scopus 로고    scopus 로고
    • Eukaryotic type translation initiation factor 2: Structure-functional aspects
    • Stolboushkina EA, Garber MB. Eukaryotic type translation initiation factor 2: structure-functional aspects. Biochemistry (Mosc). 2011;76:283-94.
    • (2011) Biochemistry (Mosc) , vol.76 , pp. 283-294
    • Stolboushkina, E.A.1    Garber, M.B.2
  • 8
    • 80052742721 scopus 로고    scopus 로고
    • Molecular mechanism of scanning and start codon selection in eukaryotes
    • Hinnebusch AG. Molecular mechanism of scanning and start codon selection in eukaryotes. Microbiol Mol Biol Rev. 2011;75:434-67.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 434-467
    • Hinnebusch, A.G.1
  • 9
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol. 2010;11:113-27.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 10
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell. 2009;136:731-45.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 12
    • 0035886531 scopus 로고    scopus 로고
    • Expression of eukaryotic translation initiation factors 4E and 2alpha is increased frequently in bronchioloalveolar but not in squamous cell carcinomas of the lung
    • DOI 10.1002/1097-0142(20011015)92:8<2164::AID-CNCR1
    • Rosenwald IB, Hutzler MJ, Wang S, Savas L, Fraire AE. Expression of eukaryotic translation initiation factors 4E and 2alpha is increased frequently in bronchioloalveolar but not in squamous cell carcinomas of the lung. Cancer. 2001;92:2164-71. (Pubitemid 32973328)
    • (2001) Cancer , vol.92 , Issue.8 , pp. 2164-2171
    • Rosenwald, I.B.1    Hutzler, M.J.2    Wang, S.3    Savas, L.4    Fraire, A.E.5
  • 13
    • 44649178786 scopus 로고    scopus 로고
    • Expression of the translation initiation factors eIF-4E and eIF-2α is frequently increased in neoplastic cells of Hodgkin lymphoma
    • Rosenwald IB, Koifman L, Savas L, Chen JJ, Woda BA, Kadin ME. Expression of the translation initiation factors eIF-4E and eIF-2α is frequently increased in neoplastic cells of Hodgkin lymphoma. Hum Pathol. 2008;39:910-6.
    • (2008) Hum Pathol , vol.39 , pp. 910-916
    • Rosenwald, I.B.1    Koifman, L.2    Savas, L.3    Chen, J.J.4    Woda, B.A.5    Kadin, M.E.6
  • 14
    • 0034075460 scopus 로고    scopus 로고
    • Levels, phosphorylation status and cellular localization of translational factor eIF2 in gastrointestinal carcinomas
    • DOI 10.1023/A:1004091122351
    • Lobo MV, Martin ME, Perez MI, Alonso FJ, Redondo C, Alvarez MI, et al. Levels, phosphorylation status and cellular localization of translational factor eIF2 in gastrointestinal carcinomas. Histochem J. 2000;32:139-50. (Pubitemid 30312790)
    • (2000) Histochemical Journal , vol.32 , Issue.3 , pp. 139-150
    • Lobo, M.V.T.1    Martin, M.E.2    Perez, M.I.3    Alonso, F.J.M.4    Redondo, C.5    Alvarez, M.I.6    Salinas, M.7
  • 15
    • 0041386193 scopus 로고    scopus 로고
    • Expression of translation initiation factor eIF-2alpha is increased in benign and malignant melanocytic and colonic epithelial neoplasms
    • DOI 10.1002/cncr.11619
    • Rosenwald IB, Wang S, Savas L, Woda B, Pullman J. Expression of translation initiation factor eIF-2alpha is increased in benign and malignant melanocytic and colonic epithelial neoplasms. Cancer. 2003;98:1080-8. (Pubitemid 37022111)
    • (2003) Cancer , vol.98 , Issue.5 , pp. 1080-1088
    • Rosenwald, I.B.1    Wang, S.2    Savas, L.3    Woda, B.4    Pullman, J.5
  • 17
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas AE, Roy S, Barber GN, Katze MG, Sonenberg N. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science. 1992;257:1685-9.
    • (1992) Science , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonenberg, N.5
  • 18
    • 0029118217 scopus 로고
    • Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3 T3 cells
    • Donze O, Jagus R, Koromilas AE, Hershey JW, Sonenberg N. Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3 T3 cells. EMBO J. 1995;14:3828-34.
    • (1995) EMBO J , vol.14 , pp. 3828-3834
    • Donze, O.1    Jagus, R.2    Koromilas, A.E.3    Hershey, J.W.4    Sonenberg, N.5
  • 21
    • 0033230617 scopus 로고    scopus 로고
    • PKR: A sentinel kinase for cellular stress
    • Williams BR. PKR: a sentinel kinase for cellular stress. Oncogene. 1999;18:6112-20.
    • (1999) Oncogene , vol.18 , pp. 6112-6120
    • Williams, B.R.1
  • 22
    • 77952509193 scopus 로고    scopus 로고
    • Uncovering the PKR pathway's potential for treatment of tumors
    • Mounir Z, Koromilas AE. Uncovering the PKR pathway's potential for treatment of tumors. Future Oncol. 2010;6:643-5.
    • (2010) Future Oncol , vol.6 , pp. 643-645
    • Mounir, Z.1    Koromilas, A.E.2
  • 23
    • 84858312636 scopus 로고    scopus 로고
    • Regulation of interferon pathway in 2-methoxyestradiol-treated osteosarcoma cells
    • Wimbauer F, Yang C, Shogren KL, Zhang M, Goyal R, Riester SM, et al. Regulation of interferon pathway in 2-methoxyestradiol-treated osteosarcoma cells. BMC Cancer. 2012;12:93.
    • (2012) BMC Cancer , vol.12 , pp. 93
    • Wimbauer, F.1    Yang, C.2    Shogren, K.L.3    Zhang, M.4    Goyal, R.5    Riester, S.M.6
  • 24
    • 80755143201 scopus 로고    scopus 로고
    • The role of PKR/eIF2alpha signaling pathway in prognosis of non-small cell lung cancer
    • He Y, Correa AM, Raso MG, Hofstetter WL, Fang B, Behrens C, et al. The role of PKR/eIF2alpha signaling pathway in prognosis of non-small cell lung cancer. PLoS One. 2011;6:e24855.
    • (2011) PLoS One , vol.6
    • He, Y.1    Correa, A.M.2    Raso, M.G.3    Hofstetter, W.L.4    Fang, B.5    Behrens, C.6
  • 26
    • 32544458522 scopus 로고    scopus 로고
    • Hypoxia selects for high-metastatic Lewis lung carcinoma cells overexpressing Mcl-1 and exhibiting reduced apoptotic potential in solid tumors
    • DOI 10.1038/sj.onc.1209128, PII 1209128
    • Koshikawa N, Maejima C, Miyazaki K, Nakagawara A, Takenaga K. Hypoxia selects for high-metastatic Lewis lung carcinoma cells overexpressing Mcl-1 and exhibiting reduced apoptotic potential in solid tumors. Oncogene. 2006;25:917-28. (Pubitemid 43237710)
    • (2006) Oncogene , vol.25 , Issue.6 , pp. 917-928
    • Koshikawa, N.1    Maejima, C.2    Miyazaki, K.3    Nakagawara, A.4    Takenaga, K.5
  • 27
    • 54549089738 scopus 로고    scopus 로고
    • Hypoxia signalling through mTOR and the unfolded protein response in cancer
    • Wouters BG, Koritzinsky M. Hypoxia signalling through mTOR and the unfolded protein response in cancer. Nat Rev Cancer. 2008;8:851-64.
    • (2008) Nat Rev Cancer , vol.8 , pp. 851-864
    • Wouters, B.G.1    Koritzinsky, M.2
  • 28
    • 0036837864 scopus 로고    scopus 로고
    • Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha
    • Koumenis C, Naczki C, Koritzinsky M, Rastani S, Diehl A, Sonenberg N, et al. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha. Mol Cell Biol. 2002;22:7405-16.
    • (2002) Mol Cell Biol , vol.22 , pp. 7405-7416
    • Koumenis, C.1    Naczki, C.2    Koritzinsky, M.3    Rastani, S.4    Diehl, A.5    Sonenberg, N.6
  • 30
    • 4344650113 scopus 로고    scopus 로고
    • Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2
    • DOI 10.1074/jbc.M404559200
    • Anthony TG, McDaniel BJ, Byerley RL, McGrath BC, Cavener DR, McNurlan MA, et al. Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2. J Biol Chem. 2004;279:36553-61. (Pubitemid 39128998)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36553-36561
    • Anthony, T.G.1    McDaniel, B.J.2    Byerley, R.L.3    McGrath, B.C.4    Cavener, D.B.5    McNurlan, M.A.6    Wek, R.C.7
  • 31
    • 77953565102 scopus 로고    scopus 로고
    • The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation
    • Ye J, Kumanova M, Hart LS, Sloane K, Zhang H, De Panis DN, et al. The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation. EMBO J. 2010;29:2082-96.
    • (2010) EMBO J , vol.29 , pp. 2082-2096
    • Ye, J.1    Kumanova, M.2    Hart, L.S.3    Sloane, K.4    Zhang, H.5    De Panis, D.N.6
  • 33
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • DOI 10.1083/jcb.200408003
    • Lu PD, Harding HP, Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol. 2004;167:27-33. (Pubitemid 39363411)
    • (2004) Journal of Cell Biology , vol.167 , Issue.1 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 34
  • 35
    • 0036729656 scopus 로고    scopus 로고
    • Mouse Atf5: Molecular cloning of two novel mRNAs, genomic organization, and odorant sensory neuron localization
    • DOI 10.1006/geno.2002.6838
    • Hansen MB, Mitchelmore C, Kjaerulff KM, Rasmussen TE, Pedersen KM, Jensen NA. Mouse Atf5: molecular cloning of two novel mRNAs, genomic organization, and odorant sensory neuron localization. Genomics. 2002;80:344-50. (Pubitemid 34985025)
    • (2002) Genomics , vol.80 , Issue.3 , pp. 344-350
    • Hansen, M.B.1    Mitchelmore, C.2    Kjarulff, K.M.3    Rasmussen, T.E.4    Pedersen, K.M.5    Jensen, N.A.6
  • 36
    • 72049124015 scopus 로고    scopus 로고
    • ATF4-dependent transcription mediates signaling of amino acid limitation
    • Kilberg MS, Shan J, Su N. ATF4-dependent transcription mediates signaling of amino acid limitation. Trends Endocrinol Metab. 2009;20:436-43.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 436-443
    • Kilberg, M.S.1    Shan, J.2    Su, N.3
  • 37
    • 23944431858 scopus 로고    scopus 로고
    • Nutritional control of gene expression: How mammalian cells respond to amino acid limitation
    • DOI 10.1146/annurev.nutr.24.012003.132145
    • Kilberg MS, Pan YX, Chen H, Leung-Pineda V. Nutritional control of gene expression: how mammalian cells respond to amino acid limitation. Annu Rev Nutr. 2005;25:59-85. (Pubitemid 41208994)
    • (2005) Annual Review of Nutrition , vol.25 , pp. 59-85
    • Kilberg, M.S.1    Pan, Y.-X.2    Chen, H.3    Leung-Pineda, V.4
  • 38
    • 10944269132 scopus 로고    scopus 로고
    • Amino acid deprivation induces the transcription rate of the human asparagine synthetase gene through a timed program of expression and promoter binding of nutrient-responsive basic region/leucine zipper transcription factors as well as localized histone acetylation
    • DOI 10.1074/jbc.M409173200
    • Chen H, Pan YX, Dudenhausen EE, Kilberg MS. Amino acid deprivation induces the transcription rate of the human asparagine synthetase gene through a timed program of expression and promoter binding of nutrient-responsive basic region/leucine zipper transcription factors as well as localized histone acetylation. J Biol Chem. 2004;279:50829-39. (Pubitemid 40017821)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50829-50839
    • Chen, H.1    Pan, Y.-X.2    Dudenhausen, E.E.3    Kilberg, M.S.4
  • 39
    • 69949124669 scopus 로고    scopus 로고
    • Hypoxia-induced expression of carbonic anhydrase 9 is dependent on the unfolded protein response
    • van den Beucken T, Koritzinsky M, Niessen H, Dubois L, Savelkouls K, Mujcic H, et al. Hypoxia-induced expression of carbonic anhydrase 9 is dependent on the unfolded protein response. J Biol Chem. 2009;284:24204-12.
    • (2009) J Biol Chem , vol.284 , pp. 24204-24212
    • Van Den Beucken, T.1    Koritzinsky, M.2    Niessen, H.3    Dubois, L.4    Savelkouls, K.5    Mujcic, H.6
  • 42
    • 33748079158 scopus 로고    scopus 로고
    • Tumor-associated Carbonic Anhydrases and Their Clinical Significance
    • DOI 10.1016/S0065-2423(06)42005-9, PII S0065242306420059
    • Pastorekova S, Parkkila S, Zavada J. Tumor-associated carbonic anhydrases and their clinical significance. Adv Clin Chem. 2006;42:167-216. (Pubitemid 44302109)
    • (2006) Advances in Clinical Chemistry , vol.42 , pp. 167-216
    • Pastorekova, S.1    Parkkila, S.2    Zavada, J.3
  • 44
    • 0025868208 scopus 로고
    • The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells
    • Murphy BJ, Laderoute KR, Short SM, Sutherland RM. The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells. Br J Cancer. 1991;64:69-73.
    • (1991) Br J Cancer , vol.64 , pp. 69-73
    • Murphy, B.J.1    Laderoute, K.R.2    Short, S.M.3    Sutherland, R.M.4
  • 47
    • 0037517089 scopus 로고    scopus 로고
    • The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha
    • DOI 10.1046/j.1432-1033.2003.03590.x
    • Gess B, Hofbauer KH, Wenger RH, Lohaus C, Meyer HE, Kurtz A. The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. Eur J Biochem. 2003;270:2228-35. (Pubitemid 36605572)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.10 , pp. 2228-2235
    • Gess, B.1    Hofbauer, K.-H.2    Wenger, R.H.3    Lohaus, C.4    Meyer, H.E.5    Kurtz, A.6
  • 48
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev. 2002;82:373-428. (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 51
    • 84875981508 scopus 로고    scopus 로고
    • Role of ubiquitin ligases and the proteasome in oncogenesis: Novel targets for anticancer therapies
    • Micel LN, Tentler JJ, Smith PG, Eckhardt GS. Role of ubiquitin ligases and the proteasome in oncogenesis: novel targets for anticancer therapies. J Clin Oncol. 2013;31:1231-8.
    • (2013) J Clin Oncol , vol.31 , pp. 1231-1238
    • Micel, L.N.1    Tentler, J.J.2    Smith, P.G.3    Eckhardt, G.S.4
  • 53
    • 0033118409 scopus 로고    scopus 로고
    • Complexes containing activating transcription factor (ATF)/cAMP- responsive-element-binding protein (CREB) interact with the CCAAT/enhancer- binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response
    • DOI 10.1042/0264-6021:3390135
    • Fawcett TW, Martindale JL, Guyton KZ, Hai T, Holbrook NJ. Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAA T/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response. Biochem J. 1999;339(Pt 1):135-41. (Pubitemid 29179300)
    • (1999) Biochemical Journal , vol.339 , Issue.1 , pp. 135-141
    • Fawcett, T.W.1    Martindale, J.L.2    Guyton, K.Z.3    Hai, T.4    Holbrook, N.J.5
  • 54
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • DOI 10.1016/S0022-2836(02)00234-6
    • Ma Y, Brewer JW, Diehl JA, Hendershot LM. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol. 2002;318:1351-65. (Pubitemid 34754003)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.5 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Alan, D.J.3    Hendershot, L.M.4
  • 55
    • 1242272070 scopus 로고    scopus 로고
    • Induction of CHOP Expression by Amino Acid Limitation Requires Both ATF4 Expression and ATF2 Phosphorylation
    • DOI 10.1074/jbc.M311862200
    • Averous J, Bruhat A, Jousse C, Carraro V, Thiel G, Fafournoux P. Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation. J Biol Chem. 2004;279:5288-97. (Pubitemid 38220549)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5288-5297
    • Averous, J.1    Bruhat, A.2    Jousse, C.3    Carraro, V.4    Thiel, G.5    Fafournoux, P.6
  • 56
    • 0042411985 scopus 로고    scopus 로고
    • Tumour hypoxia, chemotherapeutic resistance and hypoxia-related therapies
    • DOI 10.1016/S0305-7372(03)00003-3
    • Shannon AM, Bouchier-Hayes DJ, Condron CM, Toomey D. Tumour hypoxia, chemotherapeutic resistance and hypoxia-related therapies. Cancer Treat Rev. 2003;29:297-307. (Pubitemid 37069660)
    • (2003) Cancer Treatment Reviews , vol.29 , Issue.4 , pp. 297-307
    • Shannon, A.M.1    Bouchier-Hayes, D.J.2    Condron, C.M.3    Toomey, D.4
  • 57
    • 0035925098 scopus 로고    scopus 로고
    • Tumor hypoxia: Definitions and current clinical, biologic, and molecular aspects
    • Hockel M, Vaupel P. Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects. J Natl Cancer Inst. 2001;93:266-76. (Pubitemid 32219813)
    • (2001) Journal of the National Cancer Institute , vol.93 , Issue.4 , pp. 266-276
    • Hockel, M.1    Vaupel, P.2
  • 58
    • 2942590732 scopus 로고    scopus 로고
    • Exploiting tumour hypoxia in cancer treatment
    • Brown JM, Wilson WR. Exploiting tumour hypoxia in cancer treatment. Nat Rev Cancer. 2004;4:437-47. (Pubitemid 38745529)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.6 , pp. 437-447
    • Brown, J.M.1    Wilson, W.R.2
  • 59
    • 0022453226 scopus 로고
    • Influence of growth phase, nutrition and hypoxia on heterogeneity of cellular buoyant densities in in vitro tumor model systems
    • Luk CK, Sutherland RM. Influence of growth phase, nutrition and hypoxia on heterogeneity of cellular buoyant densities in in vitro tumor model systems. Int J Cancer. 1986;37:883-90. (Pubitemid 16018595)
    • (1986) International Journal of Cancer , vol.37 , Issue.6 , pp. 883-890
    • Luk, C.K.1    Sutherland, R.M.2
  • 60
    • 84875234688 scopus 로고    scopus 로고
    • PERK/eIF2alpha signaling protects therapy resistant hypoxic cells through induction of glutathione synthesis and protection against ROS
    • Rouschop KM, Dubois LJ, Keulers TG, van den Beucken T, Lambin P, Bussink J, et al. PERK/eIF2alpha signaling protects therapy resistant hypoxic cells through induction of glutathione synthesis and protection against ROS. Proc Natl Acad Sci U S A. 2013;110:4622-7.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 4622-4627
    • Rouschop, K.M.1    Dubois, L.J.2    Keulers, T.G.3    Van Den Beucken, T.4    Lambin, P.5    Bussink, J.6
  • 62
    • 34548550698 scopus 로고    scopus 로고
    • Genetic alterations determine chemotherapy resistance in childhood T-ALL: Modelling in stage-specific cell lines and correlation with diagnostic patient samples
    • DOI 10.1111/j.1365-2141.2007.06763.x
    • Estes DA, Lovato DM, Khawaja HM, Winter SS, Larson RS. Genetic alterations determine chemotherapy resistance in childhood T-ALL: modelling in stage-specific cell lines and correlation with diagnostic patient samples. Br J Haematol. 2007;139:20-30. (Pubitemid 47389934)
    • (2007) British Journal of Haematology , vol.139 , Issue.1 , pp. 20-30
    • Estes, D.A.1    Lovato, D.M.2    Khawaja, H.M.3    Winter, S.S.4    Larson, R.S.5
  • 64
    • 32944478891 scopus 로고    scopus 로고
    • Functional coupling of p38-induced up-regulation of BiP and activation of RNA-dependent protein kinase-like endoplasmic reticulum kinase to drug resistance of dormant carcinoma cells
    • DOI 10.1158/0008-5472.CAN-05-3092
    • Ranganathan AC, Zhang L, Adam AP, Aguirre-Ghiso JA. Functional coupling of p38-induced up-regulation of BiP and activation of RNA-dependent protein kinase-like endoplasmic reticulum kinase to drug resistance of dormant carcinoma cells. Cancer Res. 2006;66:1702-11. (Pubitemid 43259955)
    • (2006) Cancer Research , vol.66 , Issue.3 , pp. 1702-1711
    • Ranganathan, A.C.1    Zhang, L.2    Adam, A.P.3    Aguirre-Ghiso, J.A.4
  • 66
    • 77950605203 scopus 로고    scopus 로고
    • Are tumoral factors responsible for host tissue wasting in cancer cachexia?
    • Tisdale MJ. Are tumoral factors responsible for host tissue wasting in cancer cachexia? Future Oncol. 2010;6:503-13.
    • (2010) Future Oncol , vol.6 , pp. 503-513
    • Tisdale, M.J.1
  • 67
    • 67649982995 scopus 로고    scopus 로고
    • Mechanisms of cancer cachexia
    • Tisdale MJ. Mechanisms of cancer cachexia. Physiol Rev. 2009;89:381-410.
    • (2009) Physiol Rev , vol.89 , pp. 381-410
    • Tisdale, M.J.1
  • 69
    • 78649738532 scopus 로고    scopus 로고
    • Suppression of hypoxia-inducible factor 1alpha (HIF-1alpha) by tirapazamine is dependent on eIF2alpha phosphorylation rather than the mTORC1/4E-BP1 pathway
    • Zhang J, Cao J, Weng Q, Wu R, Yan Y, Jing H, et al. Suppression of hypoxia-inducible factor 1alpha (HIF-1alpha) by tirapazamine is dependent on eIF2alpha phosphorylation rather than the mTORC1/4E-BP1 pathway. PLoS One. 2010;5:e13910.
    • (2010) PLoS One , vol.5
    • Zhang, J.1    Cao, J.2    Weng, Q.3    Wu, R.4    Yan, Y.5    Jing, H.6
  • 70
    • 84863091501 scopus 로고    scopus 로고
    • 6-Shogaol induces apoptosis in human hepatocellular carcinoma cells and exhibits antitumor activity in vivo through endoplasmic reticulum stress
    • Hu R, Zhou P, Peng YB, Xu X, Ma J, Liu Q, et al. 6-Shogaol induces apoptosis in human hepatocellular carcinoma cells and exhibits antitumor activity in vivo through endoplasmic reticulum stress. PLoS One. 2012;7:e39664.
    • (2012) PLoS One , vol.7
    • Hu, R.1    Zhou, P.2    Peng, Y.B.3    Xu, X.4    Ma, J.5    Liu, Q.6
  • 71
    • 84869391588 scopus 로고    scopus 로고
    • The PERK-eIF2alpha phosphorylation arm is a pro-survival pathway of BCRABL signaling and confers resistance to imatinib treatment in chronic myeloid leukemia cells
    • Kusio-Kobialka M, Podszywalow-Bartnicka P, Peidis P, Glodkowska-Mrowka E, Wolanin K, Leszak G, et al. The PERK-eIF2alpha phosphorylation arm is a pro-survival pathway of BCRABL signaling and confers resistance to imatinib treatment in chronic myeloid leukemia cells. Cell Cycle. 2012;11:4069-78.
    • (2012) Cell Cycle , vol.11 , pp. 4069-4078
    • Kusio-Kobialka, M.1    Podszywalow-Bartnicka, P.2    Peidis, P.3    Glodkowska-Mrowka, E.4    Wolanin, K.5    Leszak, G.6
  • 72
    • 84875235453 scopus 로고    scopus 로고
    • Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity
    • Atkins C, Liu Q, Minthorn E, Zhang SY, Figueroa DJ, Moss K, et al. Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity. Cancer Res. 2013;73:1993-2002.
    • (2013) Cancer Res , vol.73 , pp. 1993-2002
    • Atkins, C.1    Liu, Q.2    Minthorn, E.3    Zhang, S.Y.4    Figueroa, D.J.5    Moss, K.6
  • 73
    • 33751285479 scopus 로고    scopus 로고
    • The PERK/eIF2alpha/ATF4 module of the UPR in hypoxia resistance and tumor growth
    • Fels DR, Koumenis C. The PERK/eIF2alpha/ATF4 module of the UPR in hypoxia resistance and tumor growth. Cancer Biol Ther. 2006;5:723-8. (Pubitemid 44794028)
    • (2006) Cancer Biology and Therapy , vol.5 , Issue.7 , pp. 723-728
    • Fels, D.R.1    Koumenis, C.2
  • 74
    • 84855320818 scopus 로고    scopus 로고
    • Protein quality control in the ER: Balancing the ubiquitin checkbook
    • Claessen JH, Kundrat L, Ploegh HL. Protein quality control in the ER: balancing the ubiquitin checkbook. Trends Cell Biol. 2012;22:22-32.
    • (2012) Trends Cell Biol , vol.22 , pp. 22-32
    • Claessen, J.H.1    Kundrat, L.2    Ploegh, H.L.3
  • 75
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • DOI 10.1182/blood-2005-08-3531
    • Obeng EA, Carlson LM, Gutman DM, Harrington Jr WJ, Lee KP, Boise LH. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood. 2006;107:4907-16. (Pubitemid 43882644)
    • (2006) Blood , vol.107 , Issue.12 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, L.H.6
  • 76
    • 60549106248 scopus 로고    scopus 로고
    • Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy
    • Schewe DM, Aguirre-Ghiso JA. Inhibition of eIF2alpha dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy. Cancer Res. 2009;69:1545-52.
    • (2009) Cancer Res , vol.69 , pp. 1545-1552
    • Schewe, D.M.1    Aguirre-Ghiso, J.A.2
  • 77
    • 84866455708 scopus 로고    scopus 로고
    • Sulforaphane synergistically enhances the cytotoxicity of arsenic trioxide in multiple myeloma cells via stress-mediated pathways
    • Doudican NA, Wen SY, Mazumder A, Orlow SJ. Sulforaphane synergistically enhances the cytotoxicity of arsenic trioxide in multiple myeloma cells via stress-mediated pathways. Oncol Rep. 2012;28:1851-8.
    • (2012) Oncol Rep , vol.28 , pp. 1851-1858
    • Doudican, N.A.1    Wen, S.Y.2    Mazumder, A.3    Orlow, S.J.4
  • 78
    • 80051691845 scopus 로고    scopus 로고
    • In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells
    • Chauhan D, Tian Z, Zhou B, Kuhn D, Orlowski R, Raje N, et al. In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells. Clin Cancer Res. 2011;17:5311-21.
    • (2011) Clin Cancer Res , vol.17 , pp. 5311-5321
    • Chauhan, D.1    Tian, Z.2    Zhou, B.3    Kuhn, D.4    Orlowski, R.5    Raje, N.6
  • 79
    • 78649704325 scopus 로고    scopus 로고
    • Autophagy and metabolism
    • Rabinowitz JD, White E. Autophagy and metabolism. Science. 2010;330:1344-8.
    • (2010) Science , vol.330 , pp. 1344-1348
    • Rabinowitz, J.D.1    White, E.2
  • 80
    • 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;10:1533-41.
    • (2011) Mol Cancer Ther , vol.10 , pp. 1533-1541
    • Yang, Z.J.1    Chee, C.E.2    Huang, S.3    Sinicrope, F.A.4
  • 82
    • 84861434652 scopus 로고    scopus 로고
    • Autophagy inhibitor Lys05 has single-agent antitumor activity and reproduces the phenotype of a genetic autophagy deficiency
    • McAfee Q, Zhang Z, Samanta A, Levi SM, Ma XH, Piao S, et al. Autophagy inhibitor Lys05 has single-agent antitumor activity and reproduces the phenotype of a genetic autophagy deficiency. Proc Natl Acad Sci U S A. 2012;109:8253-8.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 8253-8258
    • McAfee, Q.1    Zhang, Z.2    Samanta, A.3    Levi, S.M.4    Ma, X.H.5    Piao, S.6
  • 83
    • 84875220307 scopus 로고    scopus 로고
    • Anti-leukemic mechanisms of pegylated arginase I in acute lymphoblastic T-cell leukemia
    • Morrow K, Hernandez CP, Raber P, Del Valle L, Wilk AM, Majumdar S, et al. Anti-leukemic mechanisms of pegylated arginase I in acute lymphoblastic T-cell leukemia. Leukemia. 2013;27:569-77.
    • (2013) Leukemia , vol.27 , pp. 569-577
    • Morrow, K.1    Hernandez, C.P.2    Raber, P.3    Del Valle, L.4    Wilk, A.M.5    Majumdar, S.6
  • 84
    • 84861220296 scopus 로고    scopus 로고
    • Antitumor alkyl-lysophospholipid analog edelfosine induces apoptosis in pancreatic cancer by targeting endoplasmic reticulum
    • Gajate C, Matos-da-Silva M, el Dakir H, Fonteriz RI, Alvarez J, Mollinedo F. Antitumor alkyl-lysophospholipid analog edelfosine induces apoptosis in pancreatic cancer by targeting endoplasmic reticulum. Oncogene. 2012;31:2627-39.
    • (2012) Oncogene , vol.31 , pp. 2627-2639
    • Gajate, C.1    Matos-da-Silva, M.2    El Dakir, H.3    Fonteriz, R.I.4    Alvarez, J.5    Mollinedo, F.6
  • 85
    • 80054869356 scopus 로고    scopus 로고
    • Tetradecylthioacetic acid inhibits proliferation of human SW620 colon cancer cells-gene expression profiling implies endoplasmic reticulum stress
    • Lundemo AG, Pettersen CH, Berge K, Berge RK, Schonberg SA. Tetradecylthioacetic acid inhibits proliferation of human SW620 colon cancer cells-gene expression profiling implies endoplasmic reticulum stress. Lipids Health Dis. 2011;10:190.
    • (2011) Lipids Health Dis , vol.10 , pp. 190
    • Lundemo, A.G.1    Pettersen, C.H.2    Berge, K.3    Berge, R.K.4    Schonberg, S.A.5
  • 86
    • 84875319418 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress in isoliquiritigenin-induced SKOV-3 cell apoptosis
    • Yuan X, Yu B, Wang Y, Jiang J, Liu L, Zhao H, et al. Involvement of endoplasmic reticulum stress in isoliquiritigenin-induced SKOV-3 cell apoptosis. Recent Pat Anticancer Drug Discov. 2013;8:191-9.
    • (2013) Recent Pat Anticancer Drug Discov , vol.8 , pp. 191-199
    • Yuan, X.1    Yu, B.2    Wang, Y.3    Jiang, J.4    Liu, L.5    Zhao, H.6
  • 87
    • 84879313068 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress in capsaicin-induced apoptosis of human pancreatic cancer cells
    • Lin S, Zhang J, Chen H, Chen K, Lai F, Luo J, et al. Involvement of endoplasmic reticulum stress in capsaicin-induced apoptosis of human pancreatic cancer cells. Evid Based Complement Alternat Med. 2013;2013:629750.
    • (2013) Evid Based Complement Alternat Med , vol.2013 , pp. 629750
    • Lin, S.1    Zhang, J.2    Chen, H.3    Chen, K.4    Lai, F.5    Luo, J.6
  • 88
    • 84874775471 scopus 로고    scopus 로고
    • Induction of endoplasmic reticulum stress-mediated apoptosis and non-canonical autophagy by luteolin in NCI-H460 lung carcinoma cells
    • Park SH, Park HS, Lee JH, Chi GY, Kim GY, Moon SK, et al. Induction of endoplasmic reticulum stress-mediated apoptosis and non-canonical autophagy by luteolin in NCI-H460 lung carcinoma cells. Food Chem Toxicol. 2013;56:100-9.
    • (2013) Food Chem Toxicol , vol.56 , pp. 100-109
    • Park, S.H.1    Park, H.S.2    Lee, J.H.3    Chi, G.Y.4    Kim, G.Y.5    Moon, S.K.6
  • 89
    • 84864587755 scopus 로고    scopus 로고
    • Platycodin D induces reactive oxygen speciesmediated apoptosis signal-regulating kinase 1 activation and endoplasmic reticulum stress response in human breast cancer cells
    • Yu JS, Kim AK. Platycodin D induces reactive oxygen speciesmediated apoptosis signal-regulating kinase 1 activation and endoplasmic reticulum stress response in human breast cancer cells. J Med Food. 2012;15:691-9.
    • (2012) J Med Food , vol.15 , pp. 691-699
    • Yu, J.S.1    Kim, A.K.2
  • 90
    • 84855767695 scopus 로고    scopus 로고
    • Mechanism-based screen for G1/S checkpoint activators identifies a selective activator of EIF2AK3/PERK signalling
    • Stockwell SR, Platt G, Barrie SE, Zoumpoulidou G, Te Poele RH, Aherne GW, et al. Mechanism-based screen for G1/S checkpoint activators identifies a selective activator of EIF2AK3/PERK signalling. PLoS One. 2012;7:e28568.
    • (2012) PLoS One , vol.7
    • Stockwell, S.R.1    Platt, G.2    Barrie, S.E.3    Zoumpoulidou, G.4    Te Poele, R.H.5    Aherne, G.W.6
  • 91
    • 84881480185 scopus 로고    scopus 로고
    • Cell death/proliferation roles for nc886, a non-coding RNA, in the protein kinase R pathway in cholangiocarcinoma
    • Kunkeaw N, Jeon SH, Lee K, Johnson BH, Tanasanvimon S, Javle M, et al. Cell death/proliferation roles for nc886, a non-coding RNA, in the protein kinase R pathway in cholangiocarcinoma. Oncogene. 2012;32:3722-31.
    • (2012) Oncogene , vol.32 , pp. 3722-3731
    • Kunkeaw, N.1    Jeon, S.H.2    Lee, K.3    Johnson, B.H.4    Tanasanvimon, S.5    Javle, M.6
  • 92
    • 79960658055 scopus 로고    scopus 로고
    • Inhibition of RNase L and RNA-dependent protein kinase (PKR) by sunitinib impairs antiviral innate immunity
    • Jha BK, Polyakova I, Kessler P, Dong B, Dickerman B, Sen GC, et al. Inhibition of RNase L and RNA-dependent protein kinase (PKR) by sunitinib impairs antiviral innate immunity. J Biol Chem. 2011;286:26319-26.
    • (2011) J Biol Chem , vol.286 , pp. 26319-26326
    • Jha, B.K.1    Polyakova, I.2    Kessler, P.3    Dong, B.4    Dickerman, B.5    Sen, G.C.6
  • 93
    • 84883741789 scopus 로고    scopus 로고
    • Suppression of antiviral innate immunity by sunitinib enhances oncolytic virotherapy
    • Jha BK, Dong B, Nguyen CT, Polyakova I, Silverman RH. Suppression of antiviral innate immunity by sunitinib enhances oncolytic virotherapy. Mol Ther. 2013;21:1749-57.
    • (2013) Mol Ther , vol.21 , pp. 1749-1757
    • Jha, B.K.1    Dong, B.2    Nguyen, C.T.3    Polyakova, I.4    Silverman, R.H.5
  • 94
    • 53549119055 scopus 로고    scopus 로고
    • Vorinostat and sorafenib increase ER stress, autophagy and apoptosis via ceramide-dependent CD95 and PERK activation
    • Park MA, Zhang G, Martin AP, Hamed H, Mitchell C, Hylemon PB, et al. Vorinostat and sorafenib increase ER stress, autophagy and apoptosis via ceramide-dependent CD95 and PERK activation. Cancer Biol Ther. 2008;7:1648-62.
    • (2008) Cancer Biol Ther , vol.7 , pp. 1648-1662
    • Park, M.A.1    Zhang, G.2    Martin, A.P.3    Hamed, H.4    Mitchell, C.5    Hylemon, P.B.6
  • 95
    • 84878006006 scopus 로고    scopus 로고
    • OSU-03012 sensitizes breast cancers to lapatinib-induced cell killing: A role for Nck1 but not Nck2
    • West NW, Garcia-Vargas A, Chalfant CE, Park MA. OSU-03012 sensitizes breast cancers to lapatinib-induced cell killing: a role for Nck1 but not Nck2. BMC Cancer. 2013;13:256.
    • (2013) BMC Cancer , vol.13 , pp. 256
    • West, N.W.1    Garcia-Vargas, A.2    Chalfant, C.E.3    Park, M.A.4


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