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Volumn 17, Issue 3, 2016, Pages

Endoplasmic reticulum stress and associated ROS

Author keywords

Calcium; ER stress; Glutathione; NADPH dependent p450 reductase; Nox4; Reactive oxygen species

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; ACTIVATING TRANSCRIPTION FACTOR 6; BRCA1 PROTEIN; CLOMETHIAZOLE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; ENDOPLASMIC RETICULUM OXIDOREDUCTIN 1; GLUTATHIONE; HEAT SHOCK PROTEIN 70; MESSENGER RNA; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; CALCIUM; NOX4 PROTEIN, HUMAN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 84959451604     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms17030327     Document Type: Review
Times cited : (671)

References (173)
  • 1
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M.; Kaufman, R.J. The mammalian unfolded protein response. Annu. Rev. Biochem. 2005, 74, 739–789
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 3
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton, R.Y. ER-associated degradation in protein quality control and cellular regulation. Curr. Opin. Cell Biol. 2002, 14, 476–482
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 4
    • 84880424838 scopus 로고    scopus 로고
    • Acute caffeine ingestion enhances strength performance and reduces perceived exertion and muscle pain perception during resistance exercise
    • Duncan, M.J.; Stanley, M.; Parkhouse, N.; Cook, K.; Smith, M. Acute caffeine ingestion enhances strength performance and reduces perceived exertion and muscle pain perception during resistance exercise. Eur. J. Sport Sci. 2013, 13, 392–399
    • (2013) Eur. J. Sport Sci , vol.13 , pp. 392-399
    • Duncan, M.J.1    Stanley, M.2    Parkhouse, N.3    Cook, K.4    Smith, M.5
  • 5
    • 80052698007 scopus 로고    scopus 로고
    • Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway
    • Araki, K.; Nagata, K. Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway. J. Biol. Chem. 2011, 286, 32705–32712.
    • (2011) J. Biol. Chem , vol.286 , pp. 32705-32712
    • Araki, K.1    Nagata, K.2
  • 6
    • 33947402280 scopus 로고    scopus 로고
    • The unfolded protein response and cancer: A brighter future unfolding
    • Scriven, P.; Brown, N.J.; Pockley, A.G.; Wyld, L. The unfolded protein response and cancer: A brighter future unfolding? J. Mol. Med. 2007, 85, 331–341
    • (2007) J. Mol. Med , vol.85 , pp. 331-341
    • Scriven, P.1    Brown, N.J.2    Pockley, A.G.3    Wyld, L.4
  • 7
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are IRE1-activating ligands that directly induce the unfolded protein response
    • Gardner, B.M.; Walter, P. Unfolded proteins are IRE1-activating ligands that directly induce the unfolded protein response. Science 2011, 333, 1891–1894.
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 8
    • 84979527743 scopus 로고    scopus 로고
    • When supply does not meet demand-ER stress and plant programmed cell death
    • Williams, B.; Verchot, J.; Dickman, M.B. When supply does not meet demand-ER stress and plant programmed cell death. Front. Plant Sci. 2014, 5
    • (2014) Front. Plant Sci , vol.5
    • Williams, B.1    Verchot, J.2    Dickman, M.B.3
  • 9
    • 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
  • 10
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the IRE1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C.E.; Walter, P. Oligomerization and phosphorylation of the IRE1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 1996, 15, 3028–3039.
    • (1996) EMBO J , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 11
    • 84869049922 scopus 로고    scopus 로고
    • IRE1, a double-edged sword in pre-miRNA slicing and cell death
    • Hassler, J.; Cao, S.S.; Kaufman, R.J. IRE1, a double-edged sword in pre-miRNA slicing and cell death. Dev. Cell 2012, 23, 921–923.
    • (2012) Dev. Cell , vol.23 , pp. 921-923
    • Hassler, J.1    Cao, S.S.2    Kaufman, R.J.3
  • 13
    • 68549092781 scopus 로고    scopus 로고
    • Regulated IRE1-dependent decay of messenger RNAs in mammalian cells
    • Hollien, J.; Lin, J.H.; Li, H.; Stevens, N.; Walter, P.; Weissman, J.S. Regulated IRE1-dependent decay of messenger RNAs in mammalian cells. J. Cell Biol. 2009, 186, 323–331
    • (2009) J. Cell Biol , vol.186 , pp. 323-331
    • Hollien, J.1    Lin, J.H.2    Li, H.3    Stevens, N.4    Walter, P.5    Weissman, J.S.6
  • 15
    • 0037418238 scopus 로고    scopus 로고
    • JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
    • Lei, K.; Davis, R.J. JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. Proc. Natl. Acad. Sci. USA 2003, 100, 2432–2437.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2432-2437
    • Lei, K.1    Davis, R.J.2
  • 16
    • 0035968287 scopus 로고    scopus 로고
    • Novel role for JNK as a stress-activated Bcl2 kinase
    • Deng, X.; Xiao, L.; Lang, W.; Gao, F.; Ruvolo, P.; May, W.S., Jr. Novel role for JNK as a stress-activated Bcl2 kinase. J. Biol. Chem. 2001, 276, 23681–23688.
    • (2001) J. Biol. Chem , vol.276 , pp. 23681-23688
    • Deng, X.1    Xiao, L.2    Lang, W.3    Gao, F.4    Ruvolo, P.5    May, W.S.6
  • 17
    • 84887620237 scopus 로고    scopus 로고
    • ER stress-induced cell death mechanisms
    • Sano, R.; Reed, J.C. ER stress-induced cell death mechanisms. Biochim. Biophys. Acta 2013, 1833, 3460–3470.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 3460-3470
    • Sano, R.1    Reed, J.C.2
  • 18
    • 73349106233 scopus 로고    scopus 로고
    • Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response
    • Schuck, S.; Prinz, W.A.; Thorn, K.S.; Voss, C.; Walter, P. Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J. Cell Biol. 2009, 187, 525–536.
    • (2009) J. Cell Biol , vol.187 , pp. 525-536
    • Schuck, S.1    Prinz, W.A.2    Thorn, K.S.3    Voss, C.4    Walter, P.5
  • 19
    • 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
  • 20
    • 35848940511 scopus 로고    scopus 로고
    • Transmembrane bZIP transcription factors in ER stress signaling and the unfolded protein response
    • Bailey, D.; O’Hare, P. Transmembrane bZIP transcription factors in ER stress signaling and the unfolded protein response. Antioxid. Redox Signal. 2007, 9, 2305–2321.
    • (2007) Antioxid. Redox Signal , vol.9 , pp. 2305-2321
    • Bailey, D.1    O’Hare, P.2
  • 21
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • Cullinan, S.B.; Diehl, J.A. PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J. Biol. Chem. 2004, 279, 20108–20117.
    • (2004) J. Biol. Chem , vol.279 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 22
    • 84934278085 scopus 로고    scopus 로고
    • Polypeptide from Chlamys farreri suppresses ultraviolet-B irradiation-induced apoptosis through restoring ER redox homeostasis, scavenging ROS generation, and suppressing the PERK-eIF2α-CHOP pathway in HaCaT cells
    • Zhong, F.; Xie, J.; Zhang, D.; Han, Y.; Wang, C. Polypeptide from Chlamys farreri suppresses ultraviolet-B irradiation-induced apoptosis through restoring ER redox homeostasis, scavenging ROS generation, and suppressing the PERK-eIF2α-CHOP pathway in HaCaT cells. J. Photochem. Photobiol. B 2015, 151, 10–16.
    • (2015) J. Photochem. Photobiol. B , vol.151 , pp. 10-16
    • Zhong, F.1    Xie, J.2    Zhang, D.3    Han, Y.4    Wang, C.5
  • 23
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • Ellgaard, L.; Ruddock, L.W. The human protein disulphide isomerase family: Substrate interactions and functional properties. EMBO Rep. 2005, 6, 28–32
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 24
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman, I.; Bulleid, N.J. Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 2011, 80, 71–99.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 25
    • 0035396642 scopus 로고    scopus 로고
    • Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding
    • Kramer, B.; Ferrari, D.M.; Klappa, P.; Pohlmann, N.; Soling, H.D. Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding. Biochem. J. 2001, 357, 83–95.
    • (2001) Biochem. J , vol.357 , pp. 83-95
    • Kramer, B.1    Ferrari, D.M.2    Klappa, P.3    Pohlmann, N.4    Soling, H.D.5
  • 26
    • 0030765707 scopus 로고    scopus 로고
    • Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER
    • Carelli, S.; Ceriotti, A.; Cabibbo, A.; Fassina, G.; Ruvo, M.; Sitia, R. Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER. Science 1997, 277, 1681–1684.
    • (1997) Science , vol.277 , pp. 1681-1684
    • Carelli, S.1    Ceriotti, A.2    Cabibbo, A.3    Fassina, G.4    Ruvo, M.5    Sitia, R.6
  • 27
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand, A.R.; Kaiser, C.A. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell 1998, 1, 161–170.
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 28
    • 0031610364 scopus 로고    scopus 로고
    • ERO1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard, M.G.; Travers, K.J.; Weissman, J.S. ERO1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell 1998, 1, 171–182.
    • (1998) Mol. Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 29
    • 34848927255 scopus 로고    scopus 로고
    • Substrate recognition by the protein disulfide isomerases
    • Hatahet, F.; Ruddock, L.W. Substrate recognition by the protein disulfide isomerases. FEBS J. 2007, 274, 5223–5234.
    • (2007) FEBS J , vol.274 , pp. 5223-5234
    • Hatahet, F.1    Ruddock, L.W.2
  • 30
    • 84878866786 scopus 로고    scopus 로고
    • Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase
    • Wang, C.; Li, W.; Ren, J.; Fang, J.; Ke, H.; Gong, W.; Feng, W.; Wang, C.C. Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase. Antioxid. Redox Signal. 2013, 19, 36–45.
    • (2013) Antioxid. Redox Signal , vol.19 , pp. 36-45
    • Wang, C.1    Li, W.2    Ren, J.3    Fang, J.4    Ke, H.5    Gong, W.6    Feng, W.7    Wang, C.C.8
  • 31
    • 84862907646 scopus 로고    scopus 로고
    • Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a’
    • Wang, C.; Yu, J.; Huo, L.; Wang, L.; Feng, W.; Wang, C.C. Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a’. J. Biol. Chem. 2012, 287, 1139–1149.
    • (2012) J. Biol. Chem , vol.287 , pp. 1139-1149
    • Wang, C.1    Yu, J.2    Huo, L.3    Wang, L.4    Feng, W.5    Wang, C.C.6
  • 32
    • 9644279595 scopus 로고    scopus 로고
    • The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum
    • Xiao, R.; Wilkinson, B.; Solovyov, A.; Winther, J.R.; Holmgren, A.; Lundstrom-Ljung, J.; Gilbert, H.F. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J. Biol. Chem. 2004, 279, 49780–49786.
    • (2004) J. Biol. Chem , vol.279 , pp. 49780-49786
    • Xiao, R.1    Wilkinson, B.2    Solovyov, A.3    Winther, J.R.4    Holmgren, A.5    Lundstrom-Ljung, J.6    Gilbert, H.F.7
  • 33
    • 84859480323 scopus 로고    scopus 로고
    • Protein disulfide isomerase in redox cell signaling and homeostasis
    • Laurindo, F.R.; Pescatore, L.A.; Fernandes Dde, C. Protein disulfide isomerase in redox cell signaling and homeostasis. Free Radic. Biol. Med. 2012, 52, 1954–1969.
    • (2012) Free Radic. Biol. Med , vol.52 , pp. 1954-1969
    • Laurindo, F.R.1    Pescatore, L.A.2    Fernandes Dde, C.3
  • 34
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu, B.P.; Weissman, J.S. Oxidative protein folding in eukaryotes: Mechanisms and consequences. J. Cell Biol. 2004, 164, 341–346.
    • (2004) J. Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 37
    • 34547852400 scopus 로고    scopus 로고
    • Nox family NADPH oxidases: Not just in mammals
    • Bedard, K.; Lardy, B.; Krause, K.H. Nox family NADPH oxidases: Not just in mammals. Biochimie 2007, 89,1107–1112.
    • (2007) Biochimie , vol.89 , pp. 1107-1112
    • Bedard, K.1    Lardy, B.2    Krause, K.H.3
  • 38
    • 77949522116 scopus 로고    scopus 로고
    • Constitutive NADPH-dependent electron transferase activity of the Nox4 dehydrogenase domain
    • Nisimoto, Y.; Jackson, H.M.; Ogawa, H.; Kawahara, T.; Lambeth, J.D. Constitutive NADPH-dependent electron transferase activity of the Nox4 dehydrogenase domain. Biochemistry 2010, 49, 2433–2442.
    • (2010) Biochemistry , vol.49 , pp. 2433-2442
    • Nisimoto, Y.1    Jackson, H.M.2    Ogawa, H.3    Kawahara, T.4    Lambeth, J.D.5
  • 39
    • 28844477782 scopus 로고    scopus 로고
    • Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells
    • Janiszewski, M.; Lopes, L.R.; Carmo, A.O.; Pedro, M.A.; Brandes, R.P.; Santos, C.X.; Laurindo, F.R. Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J. Biol. Chem. 2005, 280, 40813–40819
    • (2005) J. Biol. Chem , vol.280 , pp. 40813-40819
    • Janiszewski, M.1    Lopes, L.R.2    Carmo, A.O.3    Pedro, M.A.4    Brandes, R.P.5    Santos, C.X.6    Laurindo, F.R.7
  • 40
    • 70349643912 scopus 로고    scopus 로고
    • Protein disulfide isomerase (PDI) associates with NADPH oxidase and is required for phagocytosis of leishmania chagasi promastigotes by macrophages
    • Santos, C.X.; Stolf, B.S.; Takemoto, P.V.; Amanso, A.M.; Lopes, L.R.; Souza, E.B.; Goto, H.; Laurindo, F.R. Protein disulfide isomerase (PDI) associates with NADPH oxidase and is required for phagocytosis of leishmania chagasi promastigotes by macrophages. J. Leukoc. Biol. 2009, 86, 989–998.
    • (2009) J. Leukoc. Biol , vol.86 , pp. 989-998
    • Santos, C.X.1    Stolf, B.S.2    Takemoto, P.V.3    Amanso, A.M.4    Lopes, L.R.5    Souza, E.B.6    Goto, H.7    Laurindo, F.R.8
  • 41
    • 70349352744 scopus 로고    scopus 로고
    • Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: Roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase
    • Santos, C.X.; Tanaka, L.Y.; Wosniak, J.; Laurindo, F.R. Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: Roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase. Antioxid. Redox Signal. 2009, 11, 2409–2427.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 2409-2427
    • Santos, C.X.1    Tanaka, L.Y.2    Wosniak, J.3    Laurindo, F.R.4
  • 42
    • 84891790166 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and Nox-mediated reactive oxygen species signaling in the peripheral vasculature: Potential role in hypertension
    • Santos, C.X.; Nabeebaccus, A.A.; Shah, A.M.; Camargo, L.L.; Filho, S.V.; Lopes, L.R. Endoplasmic reticulum stress and Nox-mediated reactive oxygen species signaling in the peripheral vasculature: Potential role in hypertension. Antioxid. Redox Signal. 2014, 20, 121–134.
    • (2014) Antioxid. Redox Signal , vol.20 , pp. 121-134
    • Santos, C.X.1    Nabeebaccus, A.A.2    Shah, A.M.3    Camargo, L.L.4    Filho, S.V.5    Lopes, L.R.6
  • 43
    • 56349087407 scopus 로고    scopus 로고
    • Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions
    • Merksamer, P.I.; Trusina, A.; Papa, F.R. Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 2008, 135, 933–947
    • (2008) Cell , vol.135 , pp. 933-947
    • Merksamer, P.I.1    Trusina, A.2    Papa, F.R.3
  • 44
    • 10044220931 scopus 로고    scopus 로고
    • NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells
    • Pedruzzi, E.; Guichard, C.; Ollivier, V.; Driss, F.; Fay, M.; Prunet, C.; Marie, J.C.; Pouzet, C.; Samadi, M.; Elbim, C.; et al. NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells. Mol. Cell. Biol. 2004, 24, 10703–10717.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 10703-10717
    • Pedruzzi, E.1    Guichard, C.2    Ollivier, V.3    Driss, F.4    Fay, M.5    Prunet, C.6    Marie, J.C.7    Pouzet, C.8    Samadi, M.9    Elbim, C.10
  • 45
    • 77954382142 scopus 로고    scopus 로고
    • Nox4-derived H2O2 mediates endoplasmic reticulum signaling through local Ras activation
    • Wu, R.F.; Ma, Z.; Liu, Z.; Terada, L.S. Nox4-derived H2O2 mediates endoplasmic reticulum signaling through local Ras activation. Mol. Cell. Biol. 2010, 30, 3553–3568.
    • (2010) Mol. Cell. Biol , vol.30 , pp. 3553-3568
    • Wu, R.F.1    Ma, Z.2    Liu, Z.3    Terada, L.S.4
  • 46
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death
    • Haynes, C.M.; Titus, E.A.; Cooper, A.A. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol. Cell 2004, 15, 767–776.
    • (2004) Mol. Cell , vol.15 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 48
    • 0036960604 scopus 로고    scopus 로고
    • Glutathione in defense and signaling: Lessons from a small thiol
    • Dickinson, D.A.; Forman, H.J. Glutathione in defense and signaling: Lessons from a small thiol. Ann. N. Y. Acad. Sci. 2002, 973, 488–504.
    • (2002) Ann. N. Y. Acad. Sci , vol.973 , pp. 488-504
    • Dickinson, D.A.1    Forman, H.J.2
  • 49
    • 0036862532 scopus 로고    scopus 로고
    • The FAD- and O2-dependent reaction cycle of ERO1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu, B.P.; Weissman, J.S. The FAD- and O2-dependent reaction cycle of ERO1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell 2002, 10, 983–994
    • (2002) Mol. Cell , vol.10 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 50
    • 4544249202 scopus 로고    scopus 로고
    • Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway
    • Chakravarthi, S.; Bulleid, N.J. Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. J. Biol. Chem. 2004, 279, 39872–39879
    • (2004) J. Biol. Chem , vol.279 , pp. 39872-39879
    • Chakravarthi, S.1    Bulleid, N.J.2
  • 51
    • 19244365393 scopus 로고    scopus 로고
    • Stress, protein (Mis)folding, and signaling: The redox connection
    • Sitia, R.; Molteni, S.N. Stress, protein (mis)folding, and signaling: The redox connection. Sci. STKE 2004, 2004
    • (2004) Sci. STKE
    • Sitia, R.1    Molteni, S.N.2
  • 52
    • 4444366815 scopus 로고    scopus 로고
    • Amino acid-based peritoneal dialysis solution stimulates mesothelial nitric oxide production
    • Reimann, D.; Dachs, D.; Meye, C.; Gross, P. Amino acid-based peritoneal dialysis solution stimulates mesothelial nitric oxide production. Perit. Dial. Int. 2004, 24, 378–384.
    • (2004) Perit. Dial. Int , vol.24 , pp. 378-384
    • Reimann, D.1    Dachs, D.2    Meye, C.3    Gross, P.4
  • 53
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • Zhang, K.; Kaufman, R.J. Signaling the unfolded protein response from the endoplasmic reticulum. J. Biol. Chem. 2004, 279, 25935–25938.
    • (2004) J. Biol. Chem , vol.279 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2
  • 56
    • 0018801347 scopus 로고
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase
    • Enoch, H.G.; Strittmatter, P. Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase. J. Biol. Chem. 1979, 254, 8976–8981.
    • (1979) J. Biol. Chem , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 58
    • 0035281995 scopus 로고    scopus 로고
    • Microsomal monooxygenase in apoptosis: Another target for cytochrome c signaling?
    • Davydov, D.R. Microsomal monooxygenase in apoptosis: Another target for cytochrome c signaling? Trends Biochem. Sci. 2001, 26, 155–160.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 155-160
    • Davydov, D.R.1
  • 59
    • 0036139102 scopus 로고    scopus 로고
    • Stimulation and proliferation of primary rat hepatic stellate cells by cytochrome p450 2E1-derived reactive oxygen species
    • Nieto, N.; Friedman, S.L.; Cederbaum, A.I. Stimulation and proliferation of primary rat hepatic stellate cells by cytochrome p450 2E1-derived reactive oxygen species. Hepatology 2002, 35, 62–73.
    • (2002) Hepatology , vol.35 , pp. 62-73
    • Nieto, N.1    Friedman, S.L.2    Cederbaum, A.I.3
  • 61
    • 53849124696 scopus 로고    scopus 로고
    • Nox family NADPH oxidases in liver and in pancreatic islets: A role in the metabolic syndrome and diabetes?
    • Guichard, C.; Moreau, R.; Pessayre, D.; Epperson, T.K.; Krause, K.H. Nox family NADPH oxidases in liver and in pancreatic islets: A role in the metabolic syndrome and diabetes? Biochem. Soc. Trans. 2008, 36, 920–929.
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 920-929
    • Guichard, C.1    Moreau, R.2    Pessayre, D.3    Epperson, T.K.4    Krause, K.H.5
  • 63
    • 34447306293 scopus 로고    scopus 로고
    • Expression and activity of the cytochrome p450 2E1 in patients with nonalcoholic steatosis and steatohepatitis
    • Chtioui, H.; Semela, D.; Ledermann, M.; Zimmermann, A.; Dufour, J.F. Expression and activity of the cytochrome p450 2E1 in patients with nonalcoholic steatosis and steatohepatitis. Liver Int. 2007, 27, 764–771.
    • (2007) Liver Int , vol.27 , pp. 764-771
    • Chtioui, H.1    Semela, D.2    Ledermann, M.3    Zimmermann, A.4    Dufour, J.F.5
  • 64
    • 33644790212 scopus 로고    scopus 로고
    • Nrf2 is increased by CYP2E1 in rodent liver and HepG2 cells and protects against oxidative stress caused by CYP2E1
    • Gong, P.; Cederbaum, A.I. Nrf2 is increased by CYP2E1 in rodent liver and HepG2 cells and protects against oxidative stress caused by CYP2E1. Hepatology 2006, 43, 144–153
    • (2006) Hepatology , vol.43 , pp. 144-153
    • Gong, P.1    Cederbaum, A.I.2
  • 65
    • 66849138212 scopus 로고    scopus 로고
    • Bax inhibitor 1 regulates ER-stress-induced ROS accumulation through the regulation of cytochrome p450 2E1
    • Kim, H.R.; Lee, G.H.; Cho, E.Y.; Chae, S.W.; Ahn, T.; Chae, H.J. Bax inhibitor 1 regulates ER-stress-induced ROS accumulation through the regulation of cytochrome p450 2E1. J. Cell Sci. 2009, 122, 1126–1133
    • (2009) J. Cell Sci , vol.122 , pp. 1126-1133
    • Kim, H.R.1    Lee, G.H.2    Cho, E.Y.3    Chae, S.W.4    Ahn, T.5    Chae, H.J.6
  • 67
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-α-mediatedstimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li, G.; Mongillo, M.; Chin, K.T.; Harding, H.; Ron, D.; Marks, A.R.; Tabas, I. Role of ERO1-α-mediatedstimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J. Cell Biol. 2009, 186, 783–792
    • (2009) J. Cell Biol , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 68
    • 79961188130 scopus 로고    scopus 로고
    • Redox regulation of endothelial canonical transient receptor potential channels
    • Cioffi, D.L. Redox regulation of endothelial canonical transient receptor potential channels. Antioxid. Redox Signal. 2011, 15, 1567–1582
    • (2011) Antioxid. Redox Signal , vol.15 , pp. 1567-1582
    • Cioffi, D.L.1
  • 70
    • 84864296756 scopus 로고    scopus 로고
    • Protein S-glutathionylation enhances Ca2+-induced Ca2+ release via the IP3 receptor in cultured aortic endothelial cells
    • + release via the IP3 receptor in cultured aortic endothelial cells. J. Physiol. 2012, 590, 3431–3447.
    • (2012) J. Physiol , vol.590 , pp. 3431-3447
    • Lock, J.T.1    Sinkins, W.G.2    Schilling, W.P.3
  • 71
    • 77955299902 scopus 로고    scopus 로고
    • Modulation of endoplasmic reticulum Ca2+ store filling by cyclic ADP-ribose promotes inositol trisphosphate (IP3)-evoked Ca2+ signals
    • + signals. J. Biol. Chem. 2010, 285, 25053–25061.
    • (2010) J. Biol. Chem , vol.285 , pp. 25053-25061
    • Yamasaki-Mann, M.1    Demuro, A.2    Parker, I.3
  • 72
    • 0037087782 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and cell death in astrocytes—Requirement for stored Ca2+ and sustained opening of the permeability transition pore
    • + and sustained opening of the permeability transition pore. J. Cell Sci. 2002, 115, 1175–1188.
    • (2002) J. Cell Sci , vol.115 , pp. 1175-1188
    • Jacobson, J.1    Duchen, M.R.2
  • 73
    • 0033626637 scopus 로고    scopus 로고
    • Calmodulin and cyclic ADP-ribose interaction in Ca2+ signaling related to cardiac sarcoplasmic reticulum: Superoxide anion radical-triggered Ca2+ release
    • + release. Antioxid. Redox Signal. 2000, 2, 47–54
    • (2000) Antioxid. Redox Signal , vol.2 , pp. 47-54
    • Okabe, E.1    Tsujimoto, Y.2    Kobayashi, Y.3
  • 74
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle ora double-edged sword?
    • Malhotra, J.D.; Kaufman, R.J. Endoplasmic reticulum stress and oxidative stress: A vicious cycle ora double-edged sword? Antioxid. Redox Signal. 2007, 9, 2277–2293.
    • (2007) Antioxid. Redox Signal , vol.9 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 75
    • 84903795970 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease
    • Cao, S.S.; Kaufman, R.J. Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease. Antioxid. Redox Signal. 2014, 21, 396–413.
    • (2014) Antioxid. Redox Signal , vol.21 , pp. 396-413
    • Cao, S.S.1    Kaufman, R.J.2
  • 76
    • 33750902737 scopus 로고    scopus 로고
    • The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control
    • Gorlach, A.; Klappa, P.; Kietzmann, T. The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control. Antioxid. Redox Signal. 2006, 8, 1391–1418
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1391-1418
    • Gorlach, A.1    Klappa, P.2    Kietzmann, T.3
  • 78
    • 7944232052 scopus 로고    scopus 로고
    • Nitric oxide induces coupling of mitochondrial signalling with the endoplasmic reticulum stress response
    • Xu, W.; Liu, L.; Charles, I.G.; Moncada, S. Nitric oxide induces coupling of mitochondrial signalling with the endoplasmic reticulum stress response. Nat. Cell Biol. 2004, 6, 1129–1134.
    • (2004) Nat. Cell Biol , vol.6 , pp. 1129-1134
    • Xu, W.1    Liu, L.2    Charles, I.G.3    Moncada, S.4
  • 79
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417, 1–13
    • (2009) Biochem. J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 80
    • 0038462137 scopus 로고    scopus 로고
    • Nitric oxide and calcium together inactivate mitochondrial complex I and induce cytochrome c release
    • Jekabsone, A.; Ivanoviene, L.; Brown, G.C.; Borutaite, V. Nitric oxide and calcium together inactivate mitochondrial complex I and induce cytochrome c release. J. Mol. Cell. Cardiol. 2003, 35, 803–809
    • (2003) J. Mol. Cell. Cardiol , vol.35 , pp. 803-809
    • Jekabsone, A.1    Ivanoviene, L.2    Brown, G.C.3    Borutaite, V.4
  • 81
    • 84872192695 scopus 로고    scopus 로고
    • An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases
    • Bhandary, B.; Marahatta, A.; Kim, H.R.; Chae, H.J. An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases. Int. J. Mol. Sci. 2012, 14, 434–456
    • (2012) Int. J. Mol. Sci , vol.14 , pp. 434-456
    • Bhandary, B.1    Marahatta, A.2    Kim, H.R.3    Chae, H.J.4
  • 82
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F.; Sampat, R.M.; Kopito, R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292, 1552–1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 84
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000, 10, 524–530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 86
    • 84900794136 scopus 로고    scopus 로고
    • BRCA1 and estrogen/estrogen receptor in breast cancer: Where they interact
    • Wang, L.; Di, L.J. BRCA1 and estrogen/estrogen receptor in breast cancer: Where they interact? Int. J. Biol. Sci. 2014, 10, 566–575
    • (2014) Int. J. Biol. Sci , vol.10 , pp. 566-575
    • Wang, L.1    Di, L.J.2
  • 87
    • 84923871028 scopus 로고    scopus 로고
    • α-synuclein-mediated inhibition of ATF6 processing into COPII vesicles disrupts UPR signaling in Parkinson’s disease
    • Credle, J.J.; Forcelli, P.A.; Delannoy, M.; Oaks, A.W.; Permaul, E.; Berry, D.L.; Duka, V.; Wills, J.; Sidhu, A. α-synuclein-mediated inhibition of ATF6 processing into COPII vesicles disrupts UPR signaling in Parkinson’s disease. Neurobiol. Dis. 2015, 76, 112–125
    • (2015) Neurobiol. Dis , vol.76 , pp. 112-125
    • Credle, J.J.1    Forcelli, P.A.2    Delannoy, M.3    Oaks, A.W.4    Permaul, E.5    Berry, D.L.6    Duka, V.7    Wills, J.8    Sidhu, A.9
  • 88
    • 84949115685 scopus 로고    scopus 로고
    • Nutrient deprivation induces α-synuclein aggregation through endoplasmic reticulum stress response and SREBP2 pathway
    • Jiang, P.; Gan, M.; Lin, W.L.; Yen, S.H. Nutrient deprivation induces α-synuclein aggregation through endoplasmic reticulum stress response and SREBP2 pathway. Front. Aging Neurosci. 2014, 6
    • (2014) Front. Aging Neurosci , vol.6
    • Jiang, P.1    Gan, M.2    Lin, W.L.3    Yen, S.H.4
  • 90
    • 84864606531 scopus 로고    scopus 로고
    • Generation of superoxide anions by a glycation reaction in conventional laboratory media
    • Nakashima, T.; Omura, S.; Takahashi, Y. Generation of superoxide anions by a glycation reaction in conventional laboratory media. J. Biosci. Bioeng. 2012, 114, 275–280
    • (2012) J. Biosci. Bioeng , vol.114 , pp. 275-280
    • Nakashima, T.1    Omura, S.2    Takahashi, Y.3
  • 91
    • 84868135034 scopus 로고    scopus 로고
    • ATF6α promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson’s disease
    • Hashida, K.; Kitao, Y.; Sudo, H.; Awa, Y.; Maeda, S.; Mori, K.; Takahashi, R.; Iinuma, M.; Hori, O. ATF6α promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson’s disease. PLoS ONE 2012, 7, e47950
    • (2012) Plos ONE , vol.7
    • Hashida, K.1    Kitao, Y.2    Sudo, H.3    Awa, Y.4    Maeda, S.5    Mori, K.6    Takahashi, R.7    Iinuma, M.8    Hori, O.9
  • 92
    • 84922687031 scopus 로고    scopus 로고
    • Molecular pharmacological studies on the protection mechanism against endoplasmic reticulum stress-induced neurodegenerative disease
    • Kaneko, M. Molecular pharmacological studies on the protection mechanism against endoplasmic reticulum stress-induced neurodegenerative disease. Yakugaku Zasshi 2012, 132, 1437–1442.
    • (2012) Yakugaku Zasshi , vol.132 , pp. 1437-1442
    • Kaneko, M.1
  • 93
    • 84897520145 scopus 로고    scopus 로고
    • Pharmacological studies on neurodegenerative diseases focusing on refolding and degradation of unfolded proteins in the endoplasmic reticulum
    • Nomura, Y. Pharmacological studies on neurodegenerative diseases focusing on refolding and degradation of unfolded proteins in the endoplasmic reticulum. Yakugaku Zasshi 2014, 134, 537–543.
    • (2014) Yakugaku Zasshi , vol.134 , pp. 537-543
    • Nomura, Y.1
  • 95
    • 84864432337 scopus 로고    scopus 로고
    • Alzheimer’s disease: A protective mutation
    • De Strooper, B.; Voet, T. Alzheimer’s disease: A protective mutation. Nature 2012, 488, 38–39.
    • (2012) Nature , vol.488 , pp. 38-39
    • De Strooper, B.1    Voet, T.2
  • 96
    • 33748473579 scopus 로고    scopus 로고
    • Molecular insights into mechanisms of the cell death program: Role in the progression of neurodegenerative disorders
    • Culmsee, C.; Landshamer, S. Molecular insights into mechanisms of the cell death program: Role in the progression of neurodegenerative disorders. Curr. Alzheimer Res. 2006, 3, 269–283.
    • (2006) Curr. Alzheimer Res , vol.3 , pp. 269-283
    • Culmsee, C.1    Landshamer, S.2
  • 98
    • 77956494238 scopus 로고    scopus 로고
    • The oxysterol 27-hydroxycholesterol increases βamyloid and oxidative stress in retinal pigment epithelial cells
    • Dasari, B.; Prasanthi, J.R.; Marwarha, G.; Singh, B.B.; Ghribi, O. The oxysterol 27-hydroxycholesterol increases βamyloid and oxidative stress in retinal pigment epithelial cells. BMC Ophthalmol. 2010, 10.
    • (2010) BMC Ophthalmol
    • Dasari, B.1    Prasanthi, J.R.2    Marwarha, G.3    Singh, B.B.4    Ghribi, O.5
  • 99
    • 84863688106 scopus 로고    scopus 로고
    • Mitochondrial- and endoplasmic reticulum-associated oxidative stress in Alzheimer’s disease: From pathogenesis to biomarkers
    • Ferreiro, E.; Baldeiras, I.; Ferreira, I.L.; Costa, R.O.; Rego, A.C.; Pereira, C.F.; Oliveira, C.R. Mitochondrial- and endoplasmic reticulum-associated oxidative stress in Alzheimer’s disease: From pathogenesis to biomarkers. Int. J. Cell Biol. 2012, 2012, 735206.
    • (2012) Int. J. Cell Biol , vol.2012
    • Ferreiro, E.1    Baldeiras, I.2    Ferreira, I.L.3    Costa, R.O.4    Rego, A.C.5    Pereira, C.F.6    Oliveira, C.R.7
  • 101
    • 77956225923 scopus 로고    scopus 로고
    • Protective effects of galantamine against Aβ-induced PC12 cell apoptosis by preventing mitochondrial dysfunction and endoplasmic reticulum stress
    • Liu, X.; Xu, K.; Yan, M.; Wang, Y.; Zheng, X. Protective effects of galantamine against Aβ-induced PC12 cell apoptosis by preventing mitochondrial dysfunction and endoplasmic reticulum stress. Neurochem. Int. 2010, 57, 588–599
    • (2010) Neurochem. Int , vol.57 , pp. 588-599
    • Liu, X.1    Xu, K.2    Yan, M.3    Wang, Y.4    Zheng, X.5
  • 102
    • 0030967165 scopus 로고    scopus 로고
    • A controlled trial of selegiline, α-tocopherol, or both as treatment for Alzheimer’s disease. The Alzheimer’s disease cooperative study
    • Sano, M.; Ernesto, C.; Thomas, R.G.; Klauber, M.R.; Schafer, K.; Grundman, M.; Woodbury, P.; Growdon, J.; Cotman, C. W.; Pfeiffer, E.; et al. A controlled trial of selegiline, α-tocopherol, or both as treatment for Alzheimer’s disease. The Alzheimer’s disease cooperative study. N. Engl. J. Med. 1997, 336, 1216–1222.
    • (1997) N. Engl. J. Med , vol.336 , pp. 1216-1222
    • Sano, M.1    Ernesto, C.2    Thomas, R.G.3    Klauber, M.R.4    Schafer, K.5    Grundman, M.6    Woodbury, P.7    Growdon, J.8    Cotman, C.W.9    Pfeiffer, E.10
  • 107
    • 84883352804 scopus 로고    scopus 로고
    • Stress-inducible phosphoprotein 1 has unique cochaperone activity during development and regulates cellular response to ischemia via the prion protein
    • Beraldo, F.H.; Soares, I.N.; Goncalves, D.F.; Fan, J.; Thomas, A.A.; Santos, T.G.; Mohammad, A.H.; Roffe, M.; Calder, M.D.; Nikolova, S.; et al. Stress-inducible phosphoprotein 1 has unique cochaperone activity during development and regulates cellular response to ischemia via the prion protein. FASEB J. 2013, 27, 3594–3607.
    • (2013) FASEB J , vol.27 , pp. 3594-3607
    • Beraldo, F.H.1    Soares, I.N.2    Goncalves, D.F.3    Fan, J.4    Thomas, A.A.5    Santos, T.G.6    Mohammad, A.H.7    Roffe, M.8    Calder, M.D.9    Nikolova, S.10
  • 108
    • 84856415637 scopus 로고    scopus 로고
    • PrpC displays an essential protective role from oxidative stress in an astrocyte cell line derived from PrpC knockout mice
    • Bertuchi, F.R.; Bourgeon, D.M.; Landemberger, M.C.; Martins, V.R.; Cerchiaro, G. PrpC displays an essential protective role from oxidative stress in an astrocyte cell line derived from PrpC knockout mice. Biochem. Biophys. Res. Commun. 2012, 418, 27–32
    • (2012) Biochem. Biophys. Res. Commun , vol.418 , pp. 27-32
    • Bertuchi, F.R.1    Bourgeon, D.M.2    Landemberger, M.C.3    Martins, V.R.4    Cerchiaro, G.5
  • 110
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz, C.; Russelakis-Carneiro, M.; Maundrell, K.; Castilla, J.; Soto, C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J. 2003, 22, 5435–5445.
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 111
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H.Y.; Orr, H.T. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 2000, 23, 217–247.
    • (2000) Annu. Rev. Neurosci , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 112
    • 0742323776 scopus 로고    scopus 로고
    • Mechanisms of cell death in polyglutamine expansion diseases
    • Lipinski, M.M.; Yuan, J. Mechanisms of cell death in polyglutamine expansion diseases. Curr. Opin. Pharmacol. 2004, 4, 85–90
    • (2004) Curr. Opin. Pharmacol , vol.4 , pp. 85-90
    • Lipinski, M.M.1    Yuan, J.2
  • 113
    • 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.; Hori, S.; Kakizuka, A.; Ichijo, H. 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    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 115
    • 20444378891 scopus 로고    scopus 로고
    • The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor
    • Thomas, M.; Yu, Z.; Dadgar, N.; Varambally, S.; Yu, J.; Chinnaiyan, A.M.; Lieberman, A.P. The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor. J. Biol. Chem. 2005, 280, 21264–21271
    • (2005) J. Biol. Chem , vol.280 , pp. 21264-21271
    • Thomas, M.1    Yu, Z.2    Dadgar, N.3    Varambally, S.4    Yu, J.5    Chinnaiyan, A.M.6    Lieberman, A.P.7
  • 116
    • 0347298790 scopus 로고    scopus 로고
    • Functional atpase activity of p97/valosin-containingprotein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells
    • Kobayashi, T.; Tanaka, K.; Inoue, K.; Kakizuka, A. Functional atpase activity of p97/valosin-containingprotein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells. J. Biol. Chem. 2002, 277, 47358–47365.
    • (2002) J. Biol. Chem , vol.277 , pp. 47358-47365
    • Kobayashi, T.1    Tanaka, K.2    Inoue, K.3    Kakizuka, A.4
  • 117
    • 59249087087 scopus 로고    scopus 로고
    • Valproate, a mood stabilizer, induces WFS1 expression and modulates its interaction with ER stress protein GRP94
    • Kakiuchi, C.; Ishigaki, S.; Oslowski, C.M.; Fonseca, S.G.; Kato, T.; Urano, F. Valproate, a mood stabilizer, induces WFS1 expression and modulates its interaction with ER stress protein GRP94. PLoS ONE 2009, 4, e4134.
    • (2009) Plos ONE , vol.4
    • Kakiuchi, C.1    Ishigaki, S.2    Oslowski, C.M.3    Fonseca, S.G.4    Kato, T.5    Urano, F.6
  • 118
    • 0036105204 scopus 로고    scopus 로고
    • Regulation of ER stress proteins by valproate: Therapeutic implications.
    • Bown, C.D.; Wang, J.F.; Chen, B.; Young, L.T. Regulation of ER stress proteins by valproate: Therapeutic implications. Bipolar Disord. 2002, 4, 145–151.
    • (2002) Bipolar Disord , vol.4 , pp. 145-151
    • Bown, C.D.1    Wang, J.F.2    Chen, B.3    Young, L.T.4
  • 124
    • 3543015566 scopus 로고    scopus 로고
    • Lack of support for a genetic association of the XBP1 promoter polymorphism with bipolar disorder in probands of european origin
    • Cichon, S.; Buervenich, S.; Kirov, G.; Akula, N.; Dimitrova, A.; Green, E.; Schumacher, J.; Klopp, N.; Becker, T.; Ohlraun, S.; et al. Lack of support for a genetic association of the XBP1 promoter polymorphism with bipolar disorder in probands of european origin. Nat. Genet. 2004, 36, 783–784
    • (2004) Nat. Genet , vol.36 , pp. 783-784
    • Cichon, S.1    Buervenich, S.2    Kirov, G.3    Akula, N.4    Dimitrova, A.5    Green, E.6    Schumacher, J.7    Klopp, N.8    Becker, T.9    Ohlraun, S.10
  • 126
    • 32044462724 scopus 로고    scopus 로고
    • Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells
    • Shao, L.; Sun, X.; Xu, L.; Young, L.T.; Wang, J.F. Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells. Life Sci. 2006, 78, 1317–1323.
    • (2006) Life Sci , vol.78 , pp. 1317-1323
    • Shao, L.1    Sun, X.2    Xu, L.3    Young, L.T.4    Wang, J.F.5
  • 128
    • 84872194492 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress, pancreatic β-cell degeneration, and diabetes
    • Papa, F.R. Endoplasmic reticulum stress, pancreatic β-cell degeneration, and diabetes. Cold Spring Harb. Perspect. Med. 2012, 2.
    • (2012) Cold Spring Harb. Perspect. Med , vol.2
    • Papa, F.R.1
  • 129
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in PERK˗{˗ mice reveals a role for translational control in secretory cell survival
    • Harding, H.P.; Zeng, H.; Zhang, Y.; Jungries, R.; Chung, P.; Plesken, H.; Sabatini, D.D.; Ron, D. Diabetes mellitus and exocrine pancreatic dysfunction in PERK˗{˗ mice reveals a role for translational control in secretory cell survival. Mol. Cell 2001, 7, 1153–1163
    • (2001) Mol. Cell , vol.7 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 132
    • 83755207504 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect pancreatic β-cells against oxidative stress and improve insulin secretion in glucotoxicity and glucolipotoxicity
    • Lim, S.; Rashid, M.A.; Jang, M.; Kim, Y.; Won, H.; Lee, J.; Woo, J.T.; Kim, Y.S.; Murphy, M.P.; Ali, L.; et al. Mitochondria-targeted antioxidants protect pancreatic β-cells against oxidative stress and improve insulin secretion in glucotoxicity and glucolipotoxicity. Cell. Physiol. Biochem. 2011, 28, 873–886.
    • (2011) Cell. Physiol. Biochem , vol.28 , pp. 873-886
    • Lim, S.1    Rashid, M.A.2    Jang, M.3    Kim, Y.4    Won, H.5    Lee, J.6    Woo, J.T.7    Kim, Y.S.8    Murphy, M.P.9    Ali, L.10
  • 133
    • 84959567309 scopus 로고    scopus 로고
    • β cell ER stress and the implications for immunogenicity in type 1 diabetes
    • Marre, M.L.; James, E.A.; Piganelli, J.D. β cell ER stress and the implications for immunogenicity in type 1 diabetes. Front. Cell Dev. Biol. 2015, 3
    • (2015) Front. Cell Dev. Biol , vol.3
    • Marre, M.L.1    James, E.A.2    Piganelli, J.D.3
  • 134
    • 0041989674 scopus 로고    scopus 로고
    • TDAG51 is induced by homocysteine, promotes detachment-mediated programmed cell death, and contributes to the cevelopment of atherosclerosis in hyperhomocysteinemia
    • Hossain, G.S.; van Thienen, J.V.; Werstuck, G.H.; Zhou, J.; Sood, S.K.; Dickhout, J.G.; de Koning, A.B.; Tang, D.; Wu, D.; Falk, E.; et al. TDAG51 is induced by homocysteine, promotes detachment-mediated programmed cell death, and contributes to the cevelopment of atherosclerosis in hyperhomocysteinemia. J. Biol. Chem. 2003, 278, 30317–30327
    • (2003) J. Biol. Chem , vol.278 , pp. 30317-30327
    • Hossain, G.S.1    Van Thienen, J.V.2    Werstuck, G.H.3    Zhou, J.4    Sood, S.K.5    Dickhout, J.G.6    De Koning, A.B.7    Tang, D.8    Wu, D.9    Falk, E.10
  • 138
    • 26444524411 scopus 로고    scopus 로고
    • Cholesterol-induced macrophage apoptosis requires ER stress pathways and engagement of the type A scavenger receptor
    • Devries-Seimon, T.; Li, Y.; Yao, P.M.; Stone, E.; Wang, Y.; Davis, R.J.; Flavell, R.; Tabas, I. Cholesterol-induced macrophage apoptosis requires ER stress pathways and engagement of the type A scavenger receptor. J. Cell Biol. 2005, 171, 61–73
    • (2005) J. Cell Biol , vol.171 , pp. 61-73
    • Devries-Seimon, T.1    Li, Y.2    Yao, P.M.3    Stone, E.4    Wang, Y.5    Davis, R.J.6    Flavell, R.7    Tabas, I.8
  • 140
    • 33645567816 scopus 로고    scopus 로고
    • Macrophage insulin receptor deficiency increases ER stress-induced apoptosis and necrotic core formation in advanced atherosclerotic lesions
    • Han, S.; Liang, C.P.; DeVries-Seimon, T.; Ranalletta, M.; Welch, C.L.; Collins-Fletcher, K.; Accili, D.; Tabas, I.; Tall, A.R. Macrophage insulin receptor deficiency increases ER stress-induced apoptosis and necrotic core formation in advanced atherosclerotic lesions. Cell Metab. 2006, 3, 257–266
    • (2006) Cell Metab , vol.3 , pp. 257-266
    • Han, S.1    Liang, C.P.2    Devries-Seimon, T.3    Ranalletta, M.4    Welch, C.L.5    Collins-Fletcher, K.6    Accili, D.7    Tabas, I.8    Tall, A.R.9
  • 142
    • 34247213490 scopus 로고    scopus 로고
    • Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation
    • Horke, S.; Witte, I.; Wilgenbus, P.; Kruger, M.; Strand, D.; Forstermann, U. Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation. Circulation 2007, 115, 2055–2064
    • (2007) Circulation , vol.115 , pp. 2055-2064
    • Horke, S.1    Witte, I.2    Wilgenbus, P.3    Kruger, M.4    Strand, D.5    Forstermann, U.6
  • 144
    • 84861078292 scopus 로고    scopus 로고
    • Amelioration of glucolipotoxicity-induced endoplasmic reticulum stress by a “chemical chaperone” in human THP-1 monocytes
    • Lenin, R.; Maria, M.S.; Agrawal, M.; Balasubramanyam, J.; Mohan, V.; Balasubramanyam, M. Amelioration of glucolipotoxicity-induced endoplasmic reticulum stress by a “chemical chaperone” in human THP-1 monocytes. Exp. Diabetes Res. 2012, 2012, 356487.
    • (2012) Exp. Diabetes Res , vol.2012
    • Lenin, R.1    Maria, M.S.2    Agrawal, M.3    Balasubramanyam, J.4    Mohan, V.5    Balasubramanyam, M.6
  • 145
    • 33646491144 scopus 로고    scopus 로고
    • C/EBP homologous protein (CHOP) is crucial for the induction of caspase-11 and the pathogenesis of lipopolysaccharide-induced inflammation
    • Endo, M.; Mori, M.; Akira, S.; Gotoh, T. C/EBP homologous protein (CHOP) is crucial for the induction of caspase-11 and the pathogenesis of lipopolysaccharide-induced inflammation. J. Immunol. 2006, 176, 6245–6253.
    • (2006) J. Immunol , vol.176 , pp. 6245-6253
    • Endo, M.1    Mori, M.2    Akira, S.3    Gotoh, T.4
  • 146
    • 84929454653 scopus 로고    scopus 로고
    • Fucosylated chondroitin sulphate from Cusumaria frondosa mitigates hepatic endoplasmic reticulum stress and inflammation in insulin resistant mice
    • Li, S.; Jiang, W.; Hu, S.; Song, W.; Ji, L.; Wang, Y.; Cai, L. Fucosylated chondroitin sulphate from Cusumaria frondosa mitigates hepatic endoplasmic reticulum stress and inflammation in insulin resistant mice. Food Funct. 2015, 6, 1547–1556.
    • (2015) Food Funct , vol.6 , pp. 1547-1556
    • Li, S.1    Jiang, W.2    Hu, S.3    Song, W.4    Ji, L.5    Wang, Y.6    Cai, L.7
  • 147
    • 33645216351 scopus 로고    scopus 로고
    • Diclofenac, a non-steroidal anti-inflammatory drug, suppresses apoptosis induced by endoplasmic reticulum stresses by inhibiting caspase signaling
    • Yamazaki, T.; Muramoto, M.; Oe, T.; Morikawa, N.; Okitsu, O.; Nagashima, T.; Nishimura, S.; Katayama, Y.; Kita, Y. Diclofenac, a non-steroidal anti-inflammatory drug, suppresses apoptosis induced by endoplasmic reticulum stresses by inhibiting caspase signaling. Neuropharmacology 2006, 50, 558–567
    • (2006) Neuropharmacology , vol.50 , pp. 558-567
    • Yamazaki, T.1    Muramoto, M.2    Oe, T.3    Morikawa, N.4    Okitsu, O.5    Nagashima, T.6    Nishimura, S.7    Katayama, Y.8    Kita, Y.9
  • 148
  • 150
    • 80053994563 scopus 로고    scopus 로고
    • Transgenic expression of entire hepatitis B virus in mice induces hepatocarcinogenesis independent of chronic liver injury
    • Na, B.; Huang, Z.; Wang, Q.; Qi, Z.; Tian, Y.; Lu, C.C.; Yu, J.; Hanes, M.A.; Kakar, S.; Huang, E.J.; et al. Transgenic expression of entire hepatitis B virus in mice induces hepatocarcinogenesis independent of chronic liver injury. PLoS ONE 2011, 6, e26240
    • (2011) Plos ONE , vol.6
    • Na, B.1    Huang, Z.2    Wang, Q.3    Qi, Z.4    Tian, Y.5    Lu, C.C.6    Yu, J.7    Hanes, M.A.8    Kakar, S.9    Huang, E.J.10
  • 151
    • 33747615232 scopus 로고    scopus 로고
    • Unfolding new mechanisms of alcoholic liver disease in the endoplasmic reticulum
    • Kaplowitz, N.; Ji, C. Unfolding new mechanisms of alcoholic liver disease in the endoplasmic reticulum. J. Gastroenterol. Hepatol. 2006, 21 (Suppl. S3), S7–S9
    • (2006) J. Gastroenterol. Hepatol , vol.21 , pp. S7-S9
    • Kaplowitz, N.1    Ji, C.2
  • 154
    • 4043064391 scopus 로고    scopus 로고
    • Role of TNF-_ in ethanol-induced hyperhomocysteinemia and murine alcoholic liver injury
    • Ji, C.; Deng, Q.; Kaplowitz, N. Role of TNF-_ in ethanol-induced hyperhomocysteinemia and murine alcoholic liver injury. Hepatology 2004, 40, 442–451.
    • (2004) Hepatology , vol.40 , pp. 442-451
    • Ji, C.1    Deng, Q.2    Kaplowitz, N.3
  • 155
    • 0037960128 scopus 로고    scopus 로고
    • Betaine decreases hyperhomocysteinemia, endoplasmic reticulum stress, and liver injury in alcohol-fed mice
    • Ji, C.; Kaplowitz, N. Betaine decreases hyperhomocysteinemia, endoplasmic reticulum stress, and liver injury in alcohol-fed mice. Gastroenterology 2003, 124, 1488–1499
    • (2003) Gastroenterology , vol.124 , pp. 1488-1499
    • Ji, C.1    Kaplowitz, N.2
  • 157
    • 24344433558 scopus 로고    scopus 로고
    • Induction of endoplasmic reticulum stress and apoptosis by a marine prostanoid in human hepatocellular carcinoma
    • Chiang, P.C.; Chien, C.L.; Pan, S.L.; Chen, W.P.; Teng, C.M.; Shen, Y.C.; Guh, J.H. Induction of endoplasmic reticulum stress and apoptosis by a marine prostanoid in human hepatocellular carcinoma. J. Hepatol. 2005, 43, 679–686.
    • (2005) J. Hepatol , vol.43 , pp. 679-686
    • Chiang, P.C.1    Chien, C.L.2    Pan, S.L.3    Chen, W.P.4    Teng, C.M.5    Shen, Y.C.6    Guh, J.H.7
  • 158
    • 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.; Hada, A.; Arai, M.; Wakatsuki, T.; Matsubara, O.; 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    Hada, A.7    Arai, M.8    Wakatsuki, T.9    Matsubara, O.10
  • 160
    • 33646860572 scopus 로고    scopus 로고
    • Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke
    • Rissanen, A.; Sivenius, J.; Jolkkonen, J. Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke. Brain Res. 2006, 1087, 60–66.
    • (2006) Brain Res , vol.1087 , pp. 60-66
    • Rissanen, A.1    Sivenius, J.2    Jolkkonen, J.3
  • 161
    • 1842854719 scopus 로고    scopus 로고
    • Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP
    • Tajiri, S.; Oyadomari, S.; Yano, S.; Morioka, M.; Gotoh, T.; Hamada, J.I.; Ushio, Y.; Mori, M. Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP. Cell Death Differ. 2004, 11, 403–415.
    • (2004) Cell Death Differ , vol.11 , pp. 403-415
    • Tajiri, S.1    Oyadomari, S.2    Yano, S.3    Morioka, M.4    Gotoh, T.5    Hamada, J.I.6    Ushio, Y.7    Mori, M.8
  • 162
    • 33748423869 scopus 로고    scopus 로고
    • Activation of endoplasmic reticulum stress response during the development of ischemic heart disease
    • Azfer, A.; Niu, J.; Rogers, L.M.; Adamski, F.M.; Kolattukudy, P.E. Activation of endoplasmic reticulum stress response during the development of ischemic heart disease. Am. J. Physiol. Heart Circ. Physiol. 2006, 291, H1411–H1420.
    • (2006) Am. J. Physiol. Heart Circ. Physiol , vol.291 , pp. H1411-H1420
    • Azfer, A.1    Niu, J.2    Rogers, L.M.3    Adamski, F.M.4    Kolattukudy, P.E.5
  • 163
    • 33746788477 scopus 로고    scopus 로고
    • Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes. Circ
    • Thuerauf, D.J.; Marcinko, M.; Gude, N.; Rubio, M.; Sussman, M.A.; Glembotski, C.C. Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes. Circ. Res. 2006, 99, 275–282.
    • (2006) Res , vol.99 , pp. 275-282
    • Thuerauf, D.J.1    Marcinko, M.2    Gude, N.3    Rubio, M.4    Sussman, M.A.5    Glembotski, C.C.6
  • 164
    • 33745962325 scopus 로고    scopus 로고
    • Nitric oxide and endoplasmic reticulum stress
    • Gotoh, T.; Mori, M. Nitric oxide and endoplasmic reticulum stress. Arterioscler. Thromb. Vasc. Biol. 2006, 26, 1439–1446.
    • (2006) Arterioscler. Thromb. Vasc. Biol , vol.26 , pp. 1439-1446
    • Gotoh, T.1    Mori, M.2
  • 165
    • 33744504827 scopus 로고    scopus 로고
    • Ischemic preconditioning protects cardiomyocytes against ischemic injury by inducing grp78
    • Shintani-Ishida, K.; Nakajima, M.; Uemura, K.; Yoshida, K. Ischemic preconditioning protects cardiomyocytes against ischemic injury by inducing grp78. Biochem. Biophys. Res. Commun. 2006, 345, 1600–1605
    • (2006) Biochem. Biophys. Res. Commun , vol.345 , pp. 1600-1605
    • Shintani-Ishida, K.1    Nakajima, M.2    Uemura, K.3    Yoshida, K.4
  • 166
    • 84953398172 scopus 로고    scopus 로고
    • TGF-β improves myocardial function and prevents apoptosis induced by anoxia-reoxygenation, through the reduction of endoplasmic reticulum stress. Can
    • Wang, Y.; Zong, L.; Wang, X. TGF-β improves myocardial function and prevents apoptosis induced by anoxia-reoxygenation, through the reduction of endoplasmic reticulum stress. Can. J. Physiol. Pharmacol. 2015, 94, 9–17.
    • (2015) J. Physiol. Pharmacol , vol.94 , pp. 9-17
    • Wang, Y.1    Zong, L.2    Wang, X.3
  • 167
    • 84942846115 scopus 로고    scopus 로고
    • Lycopene protects against hypoxia/reoxygenation injury by alleviating ER stress induced apoptosis in neonatal mouse cardiomyocytes
    • Xu, J.; Hu, H.; Chen, B.; Yue, R.; Zhou, Z.; Liu, Y.; Zhang, S.; Xu, L.; Wang, H.; Yu, Z. Lycopene protects against hypoxia/reoxygenation injury by alleviating ER stress induced apoptosis in neonatal mouse cardiomyocytes. PLoS ONE 2015, 10, e0136443.
    • (2015) Plos ONE , vol.10
    • Xu, J.1    Hu, H.2    Chen, B.3    Yue, R.4    Zhou, Z.5    Liu, Y.6    Zhang, S.7    Xu, L.8    Wang, H.9    Yu, Z.10
  • 168
    • 4644274936 scopus 로고    scopus 로고
    • Edaravone protects against hypoxia/ischemia-induced endoplasmic reticulum dysfunction
    • Qi, X.; Okuma, Y.; Hosoi, T.; Nomura, Y. Edaravone protects against hypoxia/ischemia-induced endoplasmic reticulum dysfunction. J. Pharmacol. Exp. Ther. 2004, 311, 388–393
    • (2004) J. Pharmacol. Exp. Ther , vol.311 , pp. 388-393
    • Qi, X.1    Okuma, Y.2    Hosoi, T.3    Nomura, Y.4
  • 169
    • 0032850199 scopus 로고    scopus 로고
    • Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins. Mol. Cell
    • Adler, H.T.; Chinery, R.; Wu, D.Y.; Kussick, S.J.; Payne, J.M.; Fornace, A.J., Jr.; Tkachuk, D.C. Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins. Mol. Cell. Biol. 1999, 19, 7050–7060.
    • (1999) Biol , vol.19 , pp. 7050-7060
    • Adler, H.T.1    Chinery, R.2    Wu, D.Y.3    Kussick, S.J.4    Payne, J.M.5    Fornace, A.J.6    Tkachuk, D.C.7
  • 172
    • 67049172152 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response and aging
    • Naidoo, N. The endoplasmic reticulum stress response and aging. Rev. Neurosci. 2009, 20, 23–37.
    • (2009) Rev. Neurosci , vol.20 , pp. 23-37
    • Naidoo, N.1


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