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Volumn 33, Issue , 2015, Pages 57-66

Controlling the unfolded protein response-mediated life and death decisions in cancer

Author keywords

Apoptosis; Cancer; Cell death; ER stress; UPR

Indexed keywords

16F 16; ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; APY 29; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; GSK 2606414; GSK 2656157; GUANABENZ; IMATINIB; INITIATION FACTOR 2ALPHA; INTEGRATED STRESS RESPONSE INHIBITOR; ISOMERASE INHIBITOR; MESSENGER RNA; MKC 3946; P 1; PACMA 31; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN DISULFIDE ISOMERASE; PROTEIN IRE1; RB 11CA; RIBONUCLEASE INHIBITOR; SALUBRINAL; SERINE PROTEINASE INHIBITOR; STF 083010; SUNITINIB; TOYOCAMYCIN; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1; ADENOSINE TRIPHOSPHATE; ATF6 PROTEIN, HUMAN; ERN1 PROTEIN, HUMAN; PROTEIN SERINE THREONINE KINASE; RIBONUCLEASE;

EID: 84938207247     PISSN: 1044579X     EISSN: 10963650     Source Type: Journal    
DOI: 10.1016/j.semcancer.2015.03.003     Document Type: Review
Times cited : (87)

References (104)
  • 1
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007, 8:519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 3
    • 84859799949 scopus 로고    scopus 로고
    • Stress management at the ER: regulators of ER stress-induced apoptosis
    • Gorman A.M., Healy S.J., Jager R., Samali A. Stress management at the ER: regulators of ER stress-induced apoptosis. Pharmacol Ther 2012, 134:306-316.
    • (2012) Pharmacol Ther , vol.134 , pp. 306-316
    • Gorman, A.M.1    Healy, S.J.2    Jager, R.3    Samali, A.4
  • 4
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P., Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011, 334:1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 5
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2000, 2:326-332.
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 6
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E., Logue S.E., Gorman A.M., Samali A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 2006, 7:880-885.
    • (2006) EMBO Rep , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 8
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107:881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 9
    • 84926106643 scopus 로고    scopus 로고
    • A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB
    • Lu Y., Liang F.X., Wang X. A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB. Mol Cell 2014, 55:758-770.
    • (2014) Mol Cell , vol.55 , pp. 758-770
    • Lu, Y.1    Liang, F.X.2    Wang, X.3
  • 11
    • 68049110633 scopus 로고    scopus 로고
    • IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • Han D., Lerner A.G., Vande Walle L., Upton J.P., Xu W., Hagen A., et al. IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 2009, 138:562-575.
    • (2009) Cell , vol.138 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande Walle, L.3    Upton, J.P.4    Xu, W.5    Hagen, A.6
  • 12
    • 79958033194 scopus 로고    scopus 로고
    • Modulating stress responses by the UPRosome: a matter of life and death
    • Woehlbier U., Hetz C. Modulating stress responses by the UPRosome: a matter of life and death. Trends Biochem Sci 2011, 36:329-337.
    • (2011) Trends Biochem Sci , vol.36 , pp. 329-337
    • Woehlbier, U.1    Hetz, C.2
  • 13
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K., Yoshida H., Yanagi H., Yura T., Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 1999, 10:3787-3799.
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 14
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
    • Shen J., Chen X., Hendershot L., Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals. Dev Cell 2002, 3:99-111.
    • (2002) Dev Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 15
    • 84876991539 scopus 로고    scopus 로고
    • Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments
    • Shoulders M.D., Ryno L.M., Genereux J.C., Moresco J.J., Tu P.G., Wu C., et al. Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep 2013, 3:1279-1292.
    • (2013) Cell Rep , vol.3 , pp. 1279-1292
    • Shoulders, M.D.1    Ryno, L.M.2    Genereux, J.C.3    Moresco, J.J.4    Tu, P.G.5    Wu, C.6
  • 16
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P., Zhang Y., Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999, 397:271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 17
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu P.D., Harding H.P., Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol 2004, 167:27-33.
    • (2004) J Cell Biol , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 18
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • Harding H.P., Zhang Y., Zeng H., Novoa I., Lu P.D., Calfon M., et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 2003, 11:619-633.
    • (2003) Mol Cell , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3    Novoa, I.4    Lu, P.D.5    Calfon, M.6
  • 19
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y., Brewer J.W., Diehl J.A., Hendershot L.M. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol 2002, 318:1351-1365.
    • (2002) J Mol Biol , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 20
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D., Weinberg R.A. Hallmarks of cancer: the next generation. Cell 2011, 144:646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 21
    • 84862501186 scopus 로고    scopus 로고
    • Blockade of XBP1 splicing by inhibition of IRE1alpha is a promising therapeutic option in multiple myeloma
    • Mimura N., Fulciniti M., Gorgun G., Tai Y.T., Cirstea D., Santo L., et al. Blockade of XBP1 splicing by inhibition of IRE1alpha is a promising therapeutic option in multiple myeloma. Blood 2012, 119:5772-5781.
    • (2012) Blood , vol.119 , pp. 5772-5781
    • Mimura, N.1    Fulciniti, M.2    Gorgun, G.3    Tai, Y.T.4    Cirstea, D.5    Santo, L.6
  • 22
    • 79953319782 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the inositol-requiring enzyme 1 endoribonuclease
    • Volkmann K., Lucas J.L., Vuga D., Wang X., Brumm D., Stiles C., et al. Potent and selective inhibitors of the inositol-requiring enzyme 1 endoribonuclease. J Biol Chem 2011, 286:12743-12755.
    • (2011) J Biol Chem , vol.286 , pp. 12743-12755
    • Volkmann, K.1    Lucas, J.L.2    Vuga, D.3    Wang, X.4    Brumm, D.5    Stiles, C.6
  • 23
    • 84859587957 scopus 로고    scopus 로고
    • The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule
    • Cross B.C., Bond P.J., Sadowski P.G., Jha B.K., Zak J., Goodman J.M., et al. The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule. Proc Natl Acad Sci U S A 2012, 109:E869-E878.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. E869-E878
    • Cross, B.C.1    Bond, P.J.2    Sadowski, P.G.3    Jha, B.K.4    Zak, J.5    Goodman, J.M.6
  • 24
    • 79251589342 scopus 로고    scopus 로고
    • Identification of an Ire1alpha endonuclease specific inhibitor with cytotoxic activity against human multiple myeloma
    • Papandreou I., Denko N.C., Olson M., Van Melckebeke H., Lust S., Tam A., et al. Identification of an Ire1alpha endonuclease specific inhibitor with cytotoxic activity against human multiple myeloma. Blood 2011, 117:1311-1314.
    • (2011) Blood , vol.117 , pp. 1311-1314
    • Papandreou, I.1    Denko, N.C.2    Olson, M.3    Van Melckebeke, H.4    Lust, S.5    Tam, A.6
  • 25
    • 84866001506 scopus 로고    scopus 로고
    • Identification of toyocamycin, an agent cytotoxic for multiple myeloma cells, as a potent inhibitor of ER stress-induced XBP1 mRNA splicing
    • Ri M., Tashiro E., Oikawa D., Shinjo S., Tokuda M., Yokouchi Y., et al. Identification of toyocamycin, an agent cytotoxic for multiple myeloma cells, as a potent inhibitor of ER stress-induced XBP1 mRNA splicing. Blood Cancer J 2012, 2:e79.
    • (2012) Blood Cancer J , vol.2 , pp. e79
    • Ri, M.1    Tashiro, E.2    Oikawa, D.3    Shinjo, S.4    Tokuda, M.5    Yokouchi, Y.6
  • 26
    • 84883441798 scopus 로고    scopus 로고
    • Selective inhibition of the unfolded protein response: targeting catalytic sites for Schiff base modification
    • Tomasio S.M., Harding H.P., Ron D., Cross B.C., Bond P.J. Selective inhibition of the unfolded protein response: targeting catalytic sites for Schiff base modification. Mol Biosyst 2013, 9:2408-2416.
    • (2013) Mol Biosyst , vol.9 , pp. 2408-2416
    • Tomasio, S.M.1    Harding, H.P.2    Ron, D.3    Cross, B.C.4    Bond, P.J.5
  • 28
    • 79960658055 scopus 로고    scopus 로고
    • Inhibition of RNase L and RNA-dependent protein kinase (PKR) by sunitinib impairs antiviral innate immunity
    • Jha B.K., Polyakova I., Kessler P., Dong B., Dickerman B., Sen G.C., et al. Inhibition of RNase L and RNA-dependent protein kinase (PKR) by sunitinib impairs antiviral innate immunity. J Biol Chem 2011, 286:26319-26326.
    • (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
  • 29
    • 79952283168 scopus 로고    scopus 로고
    • Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response
    • Ali M.M., Bagratuni T., Davenport E.L., Nowak P.R., Silva-Santisteban M.C., Hardcastle A., et al. Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response. EMBO J 2011, 30:894-905.
    • (2011) EMBO J , vol.30 , pp. 894-905
    • Ali, M.M.1    Bagratuni, T.2    Davenport, E.L.3    Nowak, P.R.4    Silva-Santisteban, M.C.5    Hardcastle, A.6
  • 30
    • 80052668828 scopus 로고    scopus 로고
    • Peptides derived from the bifunctional kinase/RNase enzyme IRE1alpha modulate IRE1alpha activity and protect cells from endoplasmic reticulum stress
    • Bouchecareilh M., Higa A., Fribourg S., Moenner M., Chevet E. Peptides derived from the bifunctional kinase/RNase enzyme IRE1alpha modulate IRE1alpha activity and protect cells from endoplasmic reticulum stress. FASEB J 2011, 25:3115-3129.
    • (2011) FASEB J , vol.25 , pp. 3115-3129
    • Bouchecareilh, M.1    Higa, A.2    Fribourg, S.3    Moenner, M.4    Chevet, E.5
  • 31
    • 84905492694 scopus 로고    scopus 로고
    • Allosteric inhibition of the IRE1alpha RNase preserves cell viability and function during endoplasmic reticulum stress
    • Ghosh R., Wang L., Wang E.S., Perera B.G., Igbaria A., Morita S., et al. Allosteric inhibition of the IRE1alpha RNase preserves cell viability and function during endoplasmic reticulum stress. Cell 2014, 158:534-548.
    • (2014) Cell , vol.158 , pp. 534-548
    • Ghosh, R.1    Wang, L.2    Wang, E.S.3    Perera, B.G.4    Igbaria, A.5    Morita, S.6
  • 32
    • 84894236302 scopus 로고    scopus 로고
    • Protein disulfide isomerase A6 controls the decay of IRE1 alpha signaling via disulfide-dependent association
    • Eletto D., Eletto D., Dersh D., Gidalevitz T., Argon Y. Protein disulfide isomerase A6 controls the decay of IRE1 alpha signaling via disulfide-dependent association. Mol Cell 2014, 53:562-576.
    • (2014) Mol Cell , vol.53 , pp. 562-576
    • Eletto, D.1    Eletto, D.2    Dersh, D.3    Gidalevitz, T.4    Argon, Y.5
  • 33
    • 84902485658 scopus 로고    scopus 로고
    • Interplay between the oxidoreductase PDIA6 and microRNA-322 controls the response to disrupted endoplasmic reticulum calcium homeostasis
    • Groenendyk J., Peng Z., Dudek E., Fan X., Mizianty M.J., Dufey E., et al. Interplay between the oxidoreductase PDIA6 and microRNA-322 controls the response to disrupted endoplasmic reticulum calcium homeostasis. Sci Signal 2014, 7:ra54.
    • (2014) Sci Signal , vol.7 , pp. ra54
    • Groenendyk, J.1    Peng, Z.2    Dudek, E.3    Fan, X.4    Mizianty, M.J.5    Dufey, E.6
  • 34
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz C. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 2012, 13:89-102.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 89-102
    • Hetz, C.1
  • 35
    • 84866905708 scopus 로고    scopus 로고
    • Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-p yrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK)
    • Axten J.M., Medina J.R., Feng Y., Shu A., Romeril S.P., Grant S.W., et al. Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-p yrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK). J Med Chem 2012, 55:7193-7207.
    • (2012) J Med Chem , vol.55 , pp. 7193-7207
    • Axten, J.M.1    Medina, J.R.2    Feng, Y.3    Shu, A.4    Romeril, S.P.5    Grant, S.W.6
  • 36
    • 84885447174 scopus 로고    scopus 로고
    • Discovery of GSK2656157: an optimized PERK inhibitor selected for preclinical development
    • Axten J.M., Romeril S.P., Shu A., Ralph J., Medina J.R., Feng Y., et al. Discovery of GSK2656157: an optimized PERK inhibitor selected for preclinical development. ACS Med Chem Lett 2013, 4:964-968.
    • (2013) ACS Med Chem Lett , vol.4 , pp. 964-968
    • Axten, J.M.1    Romeril, S.P.2    Shu, A.3    Ralph, J.4    Medina, J.R.5    Feng, Y.6
  • 37
    • 84875235453 scopus 로고    scopus 로고
    • Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity
    • Atkins C., Liu Q., Minthorn E., Zhang S.Y., Figueroa D.J., 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
  • 39
    • 84899555002 scopus 로고    scopus 로고
    • Attenuation of malignant phenotypes of breast cancer cells through eIF2 alpha-mediated downregulation of Rac1 signaling
    • Hamamura K., Minami K., Tanjung N., Wan Q.Q., Koizumi M., Matsuura N., et al. Attenuation of malignant phenotypes of breast cancer cells through eIF2 alpha-mediated downregulation of Rac1 signaling. Int J Oncol 2014, 44:1980-1988.
    • (2014) Int J Oncol , vol.44 , pp. 1980-1988
    • Hamamura, K.1    Minami, K.2    Tanjung, N.3    Wan, Q.Q.4    Koizumi, M.5    Matsuura, N.6
  • 40
    • 84896740664 scopus 로고    scopus 로고
    • Inhibition of eIF2alpha dephosphorylation enhances TRAIL-induced apoptosis in hepatoma cells
    • Teng Y., Gao M., Wang J., Kong Q., Hua H., Luo T., et al. Inhibition of eIF2alpha dephosphorylation enhances TRAIL-induced apoptosis in hepatoma cells. Cell Death Dis 2014, 5:e1060.
    • (2014) Cell Death Dis , vol.5 , pp. e1060
    • Teng, Y.1    Gao, M.2    Wang, J.3    Kong, Q.4    Hua, H.5    Luo, T.6
  • 41
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
    • Nadanaka S., Okada T., Yoshida H., Mori K. Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Mol Cell Biol 2007, 27:1027-1043.
    • (2007) Mol Cell Biol , vol.27 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 42
    • 84867095394 scopus 로고    scopus 로고
    • Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment
    • Xu S., Butkevich A.N., Yamada R., Zhou Y., Debnath B., Duncan R., et al. Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment. Proc Natl Acad Sci U S A 2012, 109:16348-16353.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 16348-16353
    • Xu, S.1    Butkevich, A.N.2    Yamada, R.3    Zhou, Y.4    Debnath, B.5    Duncan, R.6
  • 43
    • 84874024997 scopus 로고    scopus 로고
    • 1,3,5-Triazine as a modular scaffold for covalent inhibitors with streamlined target identification
    • Banerjee R., Pace N.J., Brown D.R., Weerapana E. 1,3,5-Triazine as a modular scaffold for covalent inhibitors with streamlined target identification. J Am Chem Soc 2013, 135:2497-2500.
    • (2013) J Am Chem Soc , vol.135 , pp. 2497-2500
    • Banerjee, R.1    Pace, N.J.2    Brown, D.R.3    Weerapana, E.4
  • 44
    • 84887887254 scopus 로고    scopus 로고
    • Small molecule probe suitable for in situ profiling and inhibition of protein disulfide isomerase
    • Ge J., Zhang C.J., Li L., Chong L.M., Wu X., Hao P., et al. Small molecule probe suitable for in situ profiling and inhibition of protein disulfide isomerase. ACS Chem Biol 2013, 8:2577-2585.
    • (2013) ACS Chem Biol , vol.8 , pp. 2577-2585
    • Ge, J.1    Zhang, C.J.2    Li, L.3    Chong, L.M.4    Wu, X.5    Hao, P.6
  • 45
    • 84899139079 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-activated transcription factor ATF6alpha requires the disulfide isomerase PDIA5 to modulate chemoresistance
    • Higa A., Taouji S., Lhomond S., Jensen D., Fernandez-Zapico M.E., Simpson J.C., et al. Endoplasmic reticulum stress-activated transcription factor ATF6alpha requires the disulfide isomerase PDIA5 to modulate chemoresistance. Mol Cell Biol 2014, 34:1839-1849.
    • (2014) Mol Cell Biol , vol.34 , pp. 1839-1849
    • Higa, A.1    Taouji, S.2    Lhomond, S.3    Jensen, D.4    Fernandez-Zapico, M.E.5    Simpson, J.C.6
  • 46
    • 0041731803 scopus 로고    scopus 로고
    • A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6
    • Okada T., Haze K., Nadanaka S., Yoshida H., Seidah N.G., Hirano Y., et al. A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6. J Biol Chem 2003, 278:31024-31032.
    • (2003) J Biol Chem , vol.278 , pp. 31024-31032
    • Okada, T.1    Haze, K.2    Nadanaka, S.3    Yoshida, H.4    Seidah, N.G.5    Hirano, Y.6
  • 47
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz C., Chevet E., Harding H.P. Targeting the unfolded protein response in disease. Nat Rev Drug Discov 2013, 12:703-719.
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 703-719
    • Hetz, C.1    Chevet, E.2    Harding, H.P.3
  • 48
    • 80054969637 scopus 로고    scopus 로고
    • The expression of the endoplasmic reticulum stress sensor BiP/GRP78 predicts response to chemotherapy and determines the efficacy of proteasome inhibitors in diffuse large b-cell lymphoma
    • Mozos A., Roue G., Lopez-Guillermo A., Jares P., Campo E., Colomer D., et al. The expression of the endoplasmic reticulum stress sensor BiP/GRP78 predicts response to chemotherapy and determines the efficacy of proteasome inhibitors in diffuse large b-cell lymphoma. Am J Pathol 2011, 179:2601-2610.
    • (2011) Am J Pathol , vol.179 , pp. 2601-2610
    • Mozos, A.1    Roue, G.2    Lopez-Guillermo, A.3    Jares, P.4    Campo, E.5    Colomer, D.6
  • 49
    • 79251545172 scopus 로고    scopus 로고
    • The Hsp90 inhibitor IPI-504 overcomes bortezomib resistance in mantle cell lymphoma in vitro and in vivo by down-regulation of the prosurvival ER chaperone BiP/Grp78
    • Roue G., Perez-Galan P., Mozos A., Lopez-Guerra M., Xargay-Torrent S., Rosich L., et al. The Hsp90 inhibitor IPI-504 overcomes bortezomib resistance in mantle cell lymphoma in vitro and in vivo by down-regulation of the prosurvival ER chaperone BiP/Grp78. Blood 2011, 117:1270-1279.
    • (2011) Blood , vol.117 , pp. 1270-1279
    • Roue, G.1    Perez-Galan, P.2    Mozos, A.3    Lopez-Guerra, M.4    Xargay-Torrent, S.5    Rosich, L.6
  • 50
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M., Kaufman R.J. ER stress and the unfolded protein response. Mutat Res 2005, 569:29-63.
    • (2005) Mutat Res , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 53
    • 84868525253 scopus 로고    scopus 로고
    • IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic caspase-2
    • Upton J.P., Wang L., Han D., Wang E.S., Huskey N.E., Lim L., et al. IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic caspase-2. Science 2012, 338:818-822.
    • (2012) Science , vol.338 , pp. 818-822
    • Upton, J.P.1    Wang, L.2    Han, D.3    Wang, E.S.4    Huskey, N.E.5    Lim, L.6
  • 54
    • 84864682160 scopus 로고    scopus 로고
    • IRE1alpha induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress
    • Lerner A.G., Upton J.P., Praveen P.V., Ghosh R., Nakagawa Y., Igbaria A., et al. IRE1alpha induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress. Cell Metab 2012, 16:250-264.
    • (2012) Cell Metab , vol.16 , pp. 250-264
    • Lerner, A.G.1    Upton, J.P.2    Praveen, P.V.3    Ghosh, R.4    Nakagawa, Y.5    Igbaria, A.6
  • 55
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome
    • Hetz C., Glimcher L.H. Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome. Mol Cell 2009, 35:551-561.
    • (2009) Mol Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 56
    • 84861188701 scopus 로고    scopus 로고
    • BH3-only proteins are part of a regulatory network that control the sustained signalling of the unfolded protein response sensor IRE1alpha
    • Rodriguez D.A., Zamorano S., Lisbona F., Rojas-Rivera D., Urra H., Cubillos-Ruiz J.R., et al. BH3-only proteins are part of a regulatory network that control the sustained signalling of the unfolded protein response sensor IRE1alpha. EMBO J 2012, 31:2322-2335.
    • (2012) EMBO J , vol.31 , pp. 2322-2335
    • Rodriguez, D.A.1    Zamorano, S.2    Lisbona, F.3    Rojas-Rivera, D.4    Urra, H.5    Cubillos-Ruiz, J.R.6
  • 57
    • 67649547153 scopus 로고    scopus 로고
    • Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular Bak
    • Klee M., Pallauf K., Alcala S., Fleischer A., Pimentel-Muinos F.X. Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular Bak. EMBO J 2009, 28:1757-1768.
    • (2009) EMBO J , vol.28 , pp. 1757-1768
    • Klee, M.1    Pallauf, K.2    Alcala, S.3    Fleischer, A.4    Pimentel-Muinos, F.X.5
  • 58
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F., Wang X., Bertolotti A., Zhang Y., Chung P., Harding H.P., et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000, 287:664-666.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6
  • 59
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002, 16:1345-1355.
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6
  • 60
    • 85014221300 scopus 로고    scopus 로고
    • Estrogen regulation of X-box binding protein-1 and its role in estrogen induced growth of breast and endometrial cancer cells
    • Sengupta S., Sharma C.G.N., Jordan V.C. Estrogen regulation of X-box binding protein-1 and its role in estrogen induced growth of breast and endometrial cancer cells. Horm Mol Biol Clin Investig 2010, 2.
    • (2010) Horm Mol Biol Clin Investig , vol.2
    • Sengupta, S.1    Sharma, C.G.N.2    Jordan, V.C.3
  • 61
    • 84863158460 scopus 로고    scopus 로고
    • Cdc37/Hsp90 protein-mediated regulation of IRE1alpha protein activity in endoplasmic reticulum stress response and insulin synthesis in INS-1 cells
    • Ota A., Wang Y. Cdc37/Hsp90 protein-mediated regulation of IRE1alpha protein activity in endoplasmic reticulum stress response and insulin synthesis in INS-1 cells. J Biol Chem 2012, 287:6266-6274.
    • (2012) J Biol Chem , vol.287 , pp. 6266-6274
    • Ota, A.1    Wang, Y.2
  • 62
    • 84922211982 scopus 로고    scopus 로고
    • Phosphoregulation of Ire1 RNase splicing activity
    • Prischi F., Nowak P.R., Carrara M., Ali M.M. Phosphoregulation of Ire1 RNase splicing activity. Nat Commun 2014, 5:3554.
    • (2014) Nat Commun , vol.5 , pp. 3554
    • Prischi, F.1    Nowak, P.R.2    Carrara, M.3    Ali, M.M.4
  • 63
    • 84919708686 scopus 로고    scopus 로고
    • Ire1 has distinct catalytic mechanisms for XBP1/HAC1 splicing and RIDD
    • Tam Arvin B., Koong Albert C., Niwa M. Ire1 has distinct catalytic mechanisms for XBP1/HAC1 splicing and RIDD. Cell Rep 2014, 9:850-858.
    • (2014) Cell Rep , vol.9 , pp. 850-858
    • Tam Arvin, B.1    Koong Albert, C.2    Niwa, M.3
  • 64
    • 84869094697 scopus 로고    scopus 로고
    • PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1alpha-mediated unfolded protein response
    • Jwa M., Chang P. PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1alpha-mediated unfolded protein response. Nat Cell Biol 2012, 14:1223-1230.
    • (2012) Nat Cell Biol , vol.14 , pp. 1223-1230
    • Jwa, M.1    Chang, P.2
  • 65
    • 84908582767 scopus 로고    scopus 로고
    • Ubiquitination of inositol-requiring enzyme 1 (IRE1) by the E3 ligase CHIP mediates the IRE1/TRAF2/JNK pathway
    • Zhu X., Zhang J., Sun H., Jiang C., Dong Y., Shan Q., et al. Ubiquitination of inositol-requiring enzyme 1 (IRE1) by the E3 ligase CHIP mediates the IRE1/TRAF2/JNK pathway. J Biol Chem 2014, 289:30567-30577.
    • (2014) J Biol Chem , vol.289 , pp. 30567-30577
    • Zhu, X.1    Zhang, J.2    Sun, H.3    Jiang, C.4    Dong, Y.5    Shan, Q.6
  • 67
    • 84897541350 scopus 로고    scopus 로고
    • XBP1 promotes triple-negative breast cancer by controlling the HIF1alpha pathway
    • Chen X., Iliopoulos D., Zhang Q., Tang Q., Greenblatt M.B., Hatziapostolou M., et al. XBP1 promotes triple-negative breast cancer by controlling the HIF1alpha pathway. Nature 2014, 508:103-107.
    • (2014) Nature , vol.508 , pp. 103-107
    • Chen, X.1    Iliopoulos, D.2    Zhang, Q.3    Tang, Q.4    Greenblatt, M.B.5    Hatziapostolou, M.6
  • 68
    • 4344660747 scopus 로고    scopus 로고
    • XBP1 is essential for survival under hypoxic conditions and is required for tumor growth
    • Romero-Ramirez L., Cao H., Nelson D., Hammond E., Lee A.H., Yoshida H., et al. XBP1 is essential for survival under hypoxic conditions and is required for tumor growth. Cancer Res 2004, 64:5943-5947.
    • (2004) Cancer Res , vol.64 , pp. 5943-5947
    • Romero-Ramirez, L.1    Cao, H.2    Nelson, D.3    Hammond, E.4    Lee, A.H.5    Yoshida, H.6
  • 69
    • 84872173393 scopus 로고    scopus 로고
    • Autocrine control of glioma cells adhesion and migration through IRE1alpha-mediated cleavage of SPARC mRNA
    • Dejeans N., Pluquet O., Lhomond S., Grise F., Bouchecareilh M., Juin A., et al. Autocrine control of glioma cells adhesion and migration through IRE1alpha-mediated cleavage of SPARC mRNA. J Cell Sci 2012, 125:4278-4287.
    • (2012) J Cell Sci , vol.125 , pp. 4278-4287
    • Dejeans, N.1    Pluquet, O.2    Lhomond, S.3    Grise, F.4    Bouchecareilh, M.5    Juin, A.6
  • 70
    • 84881436099 scopus 로고    scopus 로고
    • Posttranscriptional regulation of PER1 underlies the oncogenic function of IREalpha
    • Pluquet O., Dejeans N., Bouchecareilh M., Lhomond S., Pineau R., Higa A., et al. Posttranscriptional regulation of PER1 underlies the oncogenic function of IREalpha. Cancer Res 2013, 73:4732-4743.
    • (2013) Cancer Res , vol.73 , pp. 4732-4743
    • Pluquet, O.1    Dejeans, N.2    Bouchecareilh, M.3    Lhomond, S.4    Pineau, R.5    Higa, A.6
  • 71
    • 84878047476 scopus 로고    scopus 로고
    • MicroRNA-1291-mediated silencing of IRE1 alpha enhances Glypican-3 expression
    • Maurel M., Dejeans N., Taouji S., Chevet E., Grosset C.F. MicroRNA-1291-mediated silencing of IRE1 alpha enhances Glypican-3 expression. RNA 2013, 19:778-788.
    • (2013) RNA , vol.19 , pp. 778-788
    • Maurel, M.1    Dejeans, N.2    Taouji, S.3    Chevet, E.4    Grosset, C.F.5
  • 72
    • 36049049392 scopus 로고    scopus 로고
    • IRE1 signaling affects cell fate during the unfolded protein response
    • Lin J.H., Li H., Yasumura D., Cohen H.R., Zhang C., Panning B., et al. IRE1 signaling affects cell fate during the unfolded protein response. Science 2007, 318:944-949.
    • (2007) Science , vol.318 , pp. 944-949
    • Lin, J.H.1    Li, H.2    Yasumura, D.3    Cohen, H.R.4    Zhang, C.5    Panning, B.6
  • 74
    • 84870984470 scopus 로고    scopus 로고
    • PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress
    • Verfaillie T., Rubio N., Garg A.D., Bultynck G., Rizzuto R., Decuypere J.P., et al. PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress. Cell Death differ 2012, 19:1880-1891.
    • (2012) Cell Death differ , vol.19 , pp. 1880-1891
    • Verfaillie, T.1    Rubio, N.2    Garg, A.D.3    Bultynck, G.4    Rizzuto, R.5    Decuypere, J.P.6
  • 75
    • 84903749341 scopus 로고    scopus 로고
    • Cell death. Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis
    • Lu M., Lawrence D.A., Marsters S., Acosta-Alvear D., Kimmig P., Mendez A.S., et al. Cell death. Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis. Science 2014, 345:98-101.
    • (2014) Science , vol.345 , pp. 98-101
    • Lu, M.1    Lawrence, D.A.2    Marsters, S.3    Acosta-Alvear, D.4    Kimmig, P.5    Mendez, A.S.6
  • 76
    • 84877578475 scopus 로고    scopus 로고
    • ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
    • Han J., Back S.H., Hur J., Lin Y.H., Gildersleeve R., Shan J., et al. ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death. Nat Cell Biol 2013, 15:481-490.
    • (2013) Nat Cell Biol , vol.15 , pp. 481-490
    • Han, J.1    Back, S.H.2    Hur, J.3    Lin, Y.H.4    Gildersleeve, R.5    Shan, J.6
  • 77
    • 84863484585 scopus 로고    scopus 로고
    • Perk-dependent repression of miR-106b-25 cluster is required for ER stress-induced apoptosis
    • Gupta S., Read D.E., Deepti A., Cawley K., Gupta A., Oommen D., et al. Perk-dependent repression of miR-106b-25 cluster is required for ER stress-induced apoptosis. Cell Death Dis 2012, 3.
    • (2012) Cell Death Dis , vol.3
    • Gupta, S.1    Read, D.E.2    Deepti, A.3    Cawley, K.4    Gupta, A.5    Oommen, D.6
  • 78
    • 84860297865 scopus 로고    scopus 로고
    • MicroRNA-30c-2* limits expression of proadaptive factor XBP1 in the unfolded protein response
    • Byrd A.E., Aragon I.V., Brewer J.W. MicroRNA-30c-2* limits expression of proadaptive factor XBP1 in the unfolded protein response. J Cell Biol 2012, 196:689-698.
    • (2012) J Cell Biol , vol.196 , pp. 689-698
    • Byrd, A.E.1    Aragon, I.V.2    Brewer, J.W.3
  • 79
    • 0033587675 scopus 로고    scopus 로고
    • Mammalian unfolded protein response inhibits cyclin D1 translation and cell-cycle progression
    • Brewer J.W., Hendershot L.M., Sherr C.J., Diehl J.A. Mammalian unfolded protein response inhibits cyclin D1 translation and cell-cycle progression. Proc Natl Acad Sci U S A 1999, 96:8505-8510.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 8505-8510
    • Brewer, J.W.1    Hendershot, L.M.2    Sherr, C.J.3    Diehl, J.A.4
  • 80
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding H.P., Zhang Y., Bertolotti A., Zeng H., Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 2000, 5:897-904.
    • (2000) Mol Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 81
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 2000, 6:1099-1108.
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6
  • 84
    • 84899672694 scopus 로고    scopus 로고
    • Translational and posttranslational regulation of XIAP by eIF2alpha and ATF4 promotes ER stress-induced cell death during the unfolded protein response
    • Hiramatsu N., Messah C., Han J., LaVail M.M., Kaufman R.J., Lin J.H. Translational and posttranslational regulation of XIAP by eIF2alpha and ATF4 promotes ER stress-induced cell death during the unfolded protein response. Mol Biol Cell 2014, 25:1411-1420.
    • (2014) Mol Biol Cell , vol.25 , pp. 1411-1420
    • Hiramatsu, N.1    Messah, C.2    Han, J.3    LaVail, M.M.4    Kaufman, R.J.5    Lin, J.H.6
  • 85
    • 84869087503 scopus 로고    scopus 로고
    • MiR-211 is a prosurvival microRNA that regulates chop expression in a PERK-dependent manner
    • Chitnis N.S., Pytel D., Bobrovnikova-Marjon E., Pant D., Zheng H., Maas N.L., et al. miR-211 is a prosurvival microRNA that regulates chop expression in a PERK-dependent manner. Mol Cell 2012, 48:353-364.
    • (2012) Mol Cell , vol.48 , pp. 353-364
    • Chitnis, N.S.1    Pytel, D.2    Bobrovnikova-Marjon, E.3    Pant, D.4    Zheng, H.5    Maas, N.L.6
  • 88
    • 84875235453 scopus 로고    scopus 로고
    • Characterization of a novel PERK kinase inhibitor with anti-tumor and anti-angiogenic activity
    • Atkins C., Liu Q., Minthorn E.A., Zhang S., Figueroa D.J., Moss K.G., et al. Characterization of a novel PERK kinase inhibitor with anti-tumor and anti-angiogenic activity. Cancer Res 2013, 73:1993-2002.
    • (2013) Cancer Res , vol.73 , pp. 1993-2002
    • Atkins, C.1    Liu, Q.2    Minthorn, E.A.3    Zhang, S.4    Figueroa, D.J.5    Moss, K.G.6
  • 89
    • 84901005666 scopus 로고    scopus 로고
    • VEGF Signals through ATF6 and PERK to promote endothelial cell survival and angiogenesis in the absence of ER stress
    • Karali E., Bellou S., Stellas D., Klinakis A., Murphy C., Fotsis T. VEGF Signals through ATF6 and PERK to promote endothelial cell survival and angiogenesis in the absence of ER stress. Mol Cell 2014, 54:559-572.
    • (2014) Mol Cell , vol.54 , pp. 559-572
    • Karali, E.1    Bellou, S.2    Stellas, D.3    Klinakis, A.4    Murphy, C.5    Fotsis, T.6
  • 90
    • 33845465578 scopus 로고    scopus 로고
    • Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress
    • Blais J.D., Addison C.L., Edge R., Falls T., Zhao H., Wary K., et al. Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress. Mol Cell Biol 2006, 26:9517-9532.
    • (2006) Mol Cell Biol , vol.26 , pp. 9517-9532
    • Blais, J.D.1    Addison, C.L.2    Edge, R.3    Falls, T.4    Zhao, H.5    Wary, K.6
  • 91
    • 84887024055 scopus 로고    scopus 로고
    • The PERK/ATF4/LAMP3-arm of the unfolded protein response affects radioresistance by interfering with the DNA damage response
    • Nagelkerke A., Bussink J., van der Kogel A.J., Sweep F.C., Span P.N. The PERK/ATF4/LAMP3-arm of the unfolded protein response affects radioresistance by interfering with the DNA damage response. Radiother Oncol 2013, 108:415-421.
    • (2013) Radiother Oncol , vol.108 , pp. 415-421
    • Nagelkerke, A.1    Bussink, J.2    van der Kogel, A.J.3    Sweep, F.C.4    Span, P.N.5
  • 92
    • 84887449676 scopus 로고    scopus 로고
    • Down-regulation of PERK enhances resistance to ionizing radiation
    • Oommen D., Prise K.M. Down-regulation of PERK enhances resistance to ionizing radiation. Biochem Biophys Res Commun 2013, 441:31-35.
    • (2013) Biochem Biophys Res Commun , vol.441 , pp. 31-35
    • Oommen, D.1    Prise, K.M.2
  • 93
    • 84880945595 scopus 로고    scopus 로고
    • Inhibition of vacuolar H+ ATPase enhances sensitivity to tamoxifen via up-regulation of CHOP in breast cancer cells
    • Jin H.O., Lee Y.H., Kim H.A., Kim E.K., Noh W.C., Kim Y.S., et al. Inhibition of vacuolar H+ ATPase enhances sensitivity to tamoxifen via up-regulation of CHOP in breast cancer cells. Biochem Biophys Res Commun 2013, 437:463-468.
    • (2013) Biochem Biophys Res Commun , vol.437 , pp. 463-468
    • Jin, H.O.1    Lee, Y.H.2    Kim, H.A.3    Kim, E.K.4    Noh, W.C.5    Kim, Y.S.6
  • 94
    • 84875985028 scopus 로고    scopus 로고
    • Macrolide antibiotics block autophagy flux and sensitize to bortezomib via endoplasmic reticulum stress-mediated CHOP induction in myeloma cells
    • Moriya S., Che X.F., Komatsu S., Abe A., Kawaguchi T., Gotoh A., et al. Macrolide antibiotics block autophagy flux and sensitize to bortezomib via endoplasmic reticulum stress-mediated CHOP induction in myeloma cells. Int J Oncol 2013, 42:1541-1550.
    • (2013) Int J Oncol , vol.42 , pp. 1541-1550
    • Moriya, S.1    Che, X.F.2    Komatsu, S.3    Abe, A.4    Kawaguchi, T.5    Gotoh, A.6
  • 96
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev 1999, 13:1211-1233.
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 97
    • 84906993311 scopus 로고    scopus 로고
    • Unfolded protein response activation reduces secretion and extracellular aggregation of amyloidogenic immunoglobulin light chain
    • Cooley C.B., Ryno L.M., Plate L., Morgan G.J., Hulleman J.D., Kelly J.W., et al. Unfolded protein response activation reduces secretion and extracellular aggregation of amyloidogenic immunoglobulin light chain. Proc Natl Acad Sci U S A 2014, 111:13046-13051.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 13046-13051
    • Cooley, C.B.1    Ryno, L.M.2    Plate, L.3    Morgan, G.J.4    Hulleman, J.D.5    Kelly, J.W.6
  • 98
    • 80053425920 scopus 로고    scopus 로고
    • Activating transcription factor-6 (ATF6) mediates apoptosis with reduction of myeloid cell leukemia sequence 1 (Mcl-1) protein via induction of WW domain binding protein 1
    • Morishima N., Nakanishi K., Nakano A. Activating transcription factor-6 (ATF6) mediates apoptosis with reduction of myeloid cell leukemia sequence 1 (Mcl-1) protein via induction of WW domain binding protein 1. J Biol Chem 2011, 286:35227-35235.
    • (2011) J Biol Chem , vol.286 , pp. 35227-35235
    • Morishima, N.1    Nakanishi, K.2    Nakano, A.3
  • 99
    • 48749105093 scopus 로고    scopus 로고
    • ATF6alpha-Rheb-mTOR signaling promotes survival of dormant tumor cells in vivo
    • Schewe D.M., Aguirre-Ghiso J.A. ATF6alpha-Rheb-mTOR signaling promotes survival of dormant tumor cells in vivo. Proc Natl Acad Sci U S A 2008, 105:10519-10524.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10519-10524
    • Schewe, D.M.1    Aguirre-Ghiso, J.A.2
  • 100
    • 0038216621 scopus 로고    scopus 로고
    • Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis
    • Shuda M., Kondoh N., Imazeki N., Tanaka K., Okada T., Mori K., et al. Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis. J Hepatol 2003, 38:605-614.
    • (2003) J Hepatol , vol.38 , pp. 605-614
    • Shuda, M.1    Kondoh, N.2    Imazeki, N.3    Tanaka, K.4    Okada, T.5    Mori, K.6
  • 101
    • 29344457845 scopus 로고    scopus 로고
    • Transformation-associated gene regulation by ATF6alpha during hepatocarcinogenesis
    • Arai M., Kondoh N., Imazeki N., Hada A., Hatsuse K., Kimura F., et al. Transformation-associated gene regulation by ATF6alpha during hepatocarcinogenesis. FEBS Lett 2006, 580:184-190.
    • (2006) FEBS Lett , vol.580 , pp. 184-190
    • Arai, M.1    Kondoh, N.2    Imazeki, N.3    Hada, A.4    Hatsuse, K.5    Kimura, F.6
  • 102
    • 84876416042 scopus 로고    scopus 로고
    • XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells
    • Zhao Y., Li X., Cai M.Y., Ma K., Yang J., Zhou J., et al. XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells. Cell Res 2013, 23:491-507.
    • (2013) Cell Res , vol.23 , pp. 491-507
    • Zhao, Y.1    Li, X.2    Cai, M.Y.3    Ma, K.4    Yang, J.5    Zhou, J.6
  • 103
    • 63649157914 scopus 로고    scopus 로고
    • PXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation
    • Yoshida H., Uemura A., Mori K. pXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation. Cell Struct Funct 2009, 34:1-10.
    • (2009) Cell Struct Funct , vol.34 , pp. 1-10
    • Yoshida, H.1    Uemura, A.2    Mori, K.3
  • 104
    • 1642442467 scopus 로고    scopus 로고
    • Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response
    • Hong M., Luo S., Baumeister P., Huang J.M., Gogia R.K., Li M., et al. Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response. J Biol Chem 2004, 279:11354-11363.
    • (2004) J Biol Chem , vol.279 , pp. 11354-11363
    • Hong, M.1    Luo, S.2    Baumeister, P.3    Huang, J.M.4    Gogia, R.K.5    Li, M.6


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