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Volumn 14, Issue 1, 2013, Pages 434-456

An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases

Author keywords

Disulfide bond formation; ER associated oxidative stress; ER stress; ER stress associated disease; ERO 1a; Mitochondria electron transport chain; PDI

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR; ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6A; ADENOSINE TRIPHOSPHATE; ALPHA TOCOPHEROL; ANTIOXIDANT; ASCORBIC ACID; AUTOPHAGY PROTEIN 5; BETA CAROTENE; CALCIUM; CALCIUM ION; CELL PROTEIN; CHAPERONE; DIBENZOYLMETHANE DERIVATIVE; ENDOPEPTIDASE LA; ENDOPLASMIC RETICULUM OXIDOREDUCTIN 1; GLUCOSE REGULATED PROTEIN 78; GLUTATHIONE; GLUTATHIONE DISULFIDE; LIPOFUSCIN; LYCOPENE; NITRIC OXIDE SYNTHASE; PARKIN; PROTEIN BCL 2; PROTEIN DISULFIDE ISOMERASE; RAS PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4; UNCLASSIFIED DRUG; UNINDEXED DRUG; ZINC;

EID: 84872192695     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14010434     Document Type: Review
Times cited : (325)

References (126)
  • 1
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith, M.H.; Ploegh, H.L.; Weissman, J.S. Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum. Science 2011, 334, 1086-1090.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 3
    • 70350692123 scopus 로고    scopus 로고
    • Acetylation of RTN-1C regulates the induction of ER stress by the inhibition of HDAC activity in neuroectodermal tumors
    • Fazi, B.; Melino, S.; De Rubeis, S.; Bagni, C.; Paci, M.; Piacentini, M.; Di Sano, F. Acetylation of RTN-1C regulates the induction of ER stress by the inhibition of HDAC activity in neuroectodermal tumors. Oncogene 2009, 28, 3814-3824.
    • (2009) Oncogene , vol.28 , pp. 3814-3824
    • Fazi, B.1    Melino, S.2    de Rubeis, S.3    Bagni, C.4    Paci, M.5    Piacentini, M.6    Di Sano, F.7
  • 4
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda, R.; Hoseki, J.; Araki, K.; Jansen, G.; Thomas, D.Y.; Nagata, K. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 2008, 321, 569-572.
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 5
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida, H. ER stress and diseases. FEBS J. 2007, 274, 630-658.
    • (2007) FEBS J. , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 6
    • 84861567265 scopus 로고    scopus 로고
    • Redox signaling loops in the unfolded protein response
    • Higa, A.; Chevet, E. Redox signaling loops in the unfolded protein response. Cell Signal 2012, 24, 1548-1555.
    • (2012) Cell Signal , vol.24 , pp. 1548-1555
    • Higa, A.1    Chevet, E.2
  • 7
    • 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
  • 8
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • Malhotra, J.D.; Kaufman, R.J. Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a 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
  • 10
    • 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
  • 11
    • 84888629624 scopus 로고    scopus 로고
    • Regulation of lifespan by the mitochondrial electron transport chain: ROS-dependent and ROS-independent mechanisms
    • in press
    • Sanz, A.; Scialo, F.; Mallikarjun, V.; Stefanatos, R. Regulation of lifespan by the mitochondrial electron transport chain: ROS-dependent and ROS-independent mechanisms. Antioxid. Redox Signal. 2012, in press.
    • (2012) Antioxid. Redox Signal.
    • Sanz, A.1    Scialo, F.2    Mallikarjun, V.3    Stefanatos, R.4
  • 12
    • 0029893791 scopus 로고    scopus 로고
    • Oxidative folding of cystine-rich peptides vs. regioselective cysteine pairing strategies
    • Moroder, L.; Besse, D.; Musiol, H.J.; RudolphBohner, S.; Siedler, F. Oxidative folding of cystine-rich peptides vs. regioselective cysteine pairing strategies. Biopolymers 1996, 40, 207-234.
    • (1996) Biopolymers , vol.40 , pp. 207-234
    • Moroder, L.1    Besse, D.2    Musiol, H.J.3    RudolphBohner, S.4    Siedler, F.5
  • 13
    • 84872175634 scopus 로고    scopus 로고
    • The mitochondrial intermembrane space: A hub for oxidative folding linked to protein biogenesis
    • in press
    • Chatzi, A.; Tokatlidis, K. The mitochondrial intermembrane space: A hub for oxidative folding linked to protein biogenesis. Antioxid. Redox Signal. 2012, in press.
    • (2012) Antioxid. Redox Signal.
    • Chatzi, A.1    Tokatlidis, K.2
  • 14
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C.; Sinskey, A.J.; Lodish, H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992, 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 15
    • 0041761700 scopus 로고    scopus 로고
    • Oxidation of ER resident proteins upon oxidative stress: Effects of altering cellular redox/antioxidant status and implications for protein maturation
    • Van der Vlies, D.; Makkinje, M.; Jansens, A.; Braakman, I.; Verkleij, A.J.; Wirtz, K.W.; Post, J.A. Oxidation of ER resident proteins upon oxidative stress: Effects of altering cellular redox/antioxidant status and implications for protein maturation. Antioxid. Redox Signal. 2003, 5, 381-387.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 381-387
    • Van der Vlies, D.1    Makkinje, M.2    Jansens, A.3    Braakman, I.4    Verkleij, A.J.5    Wirtz, K.W.6    Post, J.A.7
  • 16
    • 84868222562 scopus 로고    scopus 로고
    • Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms
    • Lisa, S.; Domingo, B.; Martinez, J.; Gilch, S.; Llopis, J.F.; Schatzl, H.M.; Gasset, M. Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms. J. Biol. Chem. 2012, 287, 36693-36702.
    • (2012) J. Biol. Chem. , vol.287 , pp. 36693-36702
    • Lisa, S.1    Domingo, B.2    Martinez, J.3    Gilch, S.4    Llopis, J.F.5    Schatzl, H.M.6    Gasset, M.7
  • 17
    • 0034620510 scopus 로고    scopus 로고
    • Mechanism of the antichaperone activity of protein disulfide isomerase: Facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDI
    • Sideraki, V.; Gilbert, H.F. Mechanism of the antichaperone activity of protein disulfide isomerase: Facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDI. Biochemistry 2000, 39, 1180-1188.
    • (2000) Biochemistry , vol.39 , pp. 1180-1188
    • Sideraki, V.1    Gilbert, H.F.2
  • 18
    • 2542475140 scopus 로고    scopus 로고
    • Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
    • Gross, E.; Kastner, D.B.; Kaiser, C.A.; Fass, D. Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 2004, 117, 601-610.
    • (2004) Cell , vol.117 , pp. 601-610
    • Gross, E.1    Kastner, D.B.2    Kaiser, C.A.3    Fass, D.4
  • 19
    • 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
  • 21
    • 0036862532 scopus 로고    scopus 로고
    • The FAD-and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu, B.P.; Weissman, J.S. The FAD-and O(2)-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
  • 23
    • 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
  • 24
    • 77954382142 scopus 로고    scopus 로고
    • 2 mediates endoplasmic reticulum signaling through local Ras activation
    • 2 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
  • 25
    • 79251512989 scopus 로고    scopus 로고
    • Proteasome inhibition represses unfolded protein response and Nox4, sensitizing vascular cells to endoplasmic reticulum stress-induced death
    • Amanso, A.M.; Debbas, V.; Laurindo, F.R. Proteasome inhibition represses unfolded protein response and Nox4, sensitizing vascular cells to endoplasmic reticulum stress-induced death. PLoS One 2011, 6, e14591.
    • (2011) PLoS One , vol.6
    • Amanso, A.M.1    Debbas, V.2    Laurindo, F.R.3
  • 26
    • 77956199539 scopus 로고    scopus 로고
    • Precursor of advanced glycation end products mediates ER-stress-induced caspase-3 activation of human dermal fibroblasts through NAD(P)H oxidase 4
    • Loughlin, D.T.; Artlett, C.M. Precursor of advanced glycation end products mediates ER-stress-induced caspase-3 activation of human dermal fibroblasts through NAD(P)H oxidase 4. PLoS One 2010, 5, e11093.
    • (2010) PLoS One , vol.5
    • Loughlin, D.T.1    Artlett, C.M.2
  • 27
    • 80155134262 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration and rapid depletion of mitochondrial glutathione by beta-phenethyl isothiocyanate: Mechanisms for anti-leukemia activity
    • Chen, G.; Chen, Z.; Hu, Y.; Huang, P. Inhibition of mitochondrial respiration and rapid depletion of mitochondrial glutathione by beta-phenethyl isothiocyanate: Mechanisms for anti-leukemia activity. Antioxid. Redox Signal. 2011, 15, 2911-2921.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 2911-2921
    • Chen, G.1    Chen, Z.2    Hu, Y.3    Huang, P.4
  • 29
    • 84861331187 scopus 로고    scopus 로고
    • Apoptosis induced by manganese on neuronal SK-N-MC cell line: Endoplasmic reticulum (ER) stress and mitochondria dysfunction
    • Yoon, H.; Kim, D.S.; Lee, G.H.; Kim, K.W.; Kim, H.R.; Chae, H.J. Apoptosis induced by manganese on neuronal SK-N-MC cell line: Endoplasmic reticulum (ER) stress and mitochondria dysfunction. Environ. Health Toxicol. 2011, 26, e2011017.
    • (2011) Environ. Health Toxicol. , vol.26
    • Yoon, H.1    Kim, D.S.2    Lee, G.H.3    Kim, K.W.4    Kim, H.R.5    Chae, H.J.6
  • 30
    • 77955359156 scopus 로고    scopus 로고
    • 2 produced during disulphide formation
    • 2 produced during disulphide formation. J. Cell Sci. 2010, 123, 2672-2679.
    • (2010) J. Cell Sci. , vol.123 , pp. 2672-2679
    • Tavender, T.J.1    Bulleid, N.J.2
  • 32
    • 29244462498 scopus 로고    scopus 로고
    • Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway
    • Cullinan, S.B.; Diehl, J.A. Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway. Int. J. Biochem. Cell Biol. 2006, 38, 317-332.
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 317-332
    • Cullinan, S.B.1    Diehl, J.A.2
  • 33
    • 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
  • 34
    • 57649221592 scopus 로고    scopus 로고
    • Hypoxic reactive oxygen species regulate the integrated stress response and cell survival
    • Liu, L.; Wise, D.R.; Diehl, J.A.; Simon, M.C. Hypoxic reactive oxygen species regulate the integrated stress response and cell survival. J. Biol. Chem. 2008, 283, 31153-31162.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31153-31162
    • Liu, L.1    Wise, D.R.2    Diehl, J.A.3    Simon, M.C.4
  • 35
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM)
    • Raturi, A.; Simmen, T. Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 2012, 1833, 213-224.
    • (2012) Biochim. Biophys. Acta , vol.1833 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 37
    • 77952683069 scopus 로고    scopus 로고
    • 2nd Dual autonomous mitochondrial cell death pathways are activated by Nix/BNip3L and induce cardiomyopathy
    • Chen, Y.; Lewis, W.; Diwan, A.; Cheng, E.H.; Matkovich, S.J.; Dorn, G.W. 2nd Dual autonomous mitochondrial cell death pathways are activated by Nix/BNip3L and induce cardiomyopathy. Proc. Natl. Acad. Sci. USA 2010, 107, 9035-9042.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 9035-9042
    • Chen, Y.1    Lewis, W.2    Diwan, A.3    Cheng, E.H.4    Matkovich, S.J.5    Dorn, G.W.6
  • 38
    • 84857767805 scopus 로고    scopus 로고
    • Role of ER stress response in photodynamic therapy: ROS generated in different subcellular compartments trigger diverse cell death pathways
    • Moserova, I.; Kralova, J. Role of ER stress response in photodynamic therapy: ROS generated in different subcellular compartments trigger diverse cell death pathways. PLoS One 2012, 7, e32972.
    • (2012) PLoS One , vol.7
    • Moserova, I.1    Kralova, J.2
  • 40
    • 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
  • 42
    • 84864296756 scopus 로고    scopus 로고
    • 2+ release via the IP3 receptor in cultured aortic endothelial cells
    • 2+ release via the IP3 receptor in cultured aortic endothelial cells. J. Phys. 2012, 590, 3431-3447.
    • (2012) J. Phys. , vol.590 , pp. 3431-3447
    • Lock, J.T.1    Sinkins, W.G.2    Schilling, W.P.3
  • 43
    • 0037087782 scopus 로고    scopus 로고
    • 2+ and sustained opening of the permeability transition pore
    • 2+ 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
  • 47
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation 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-alpha-mediated stimulation 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
  • 48
    • 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
  • 50
    • 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
  • 51
    • 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
  • 52
    • 80053252011 scopus 로고    scopus 로고
    • Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders
    • Doyle, K.M.; Kennedy, D.; Gorman, A.M.; Gupta, S.; Healy, S.J.; Samali, A. Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders. J. Cell. Mol. Med. 2011, 15, 2025-2039.
    • (2011) J. Cell. Mol. Med. , vol.15 , pp. 2025-2039
    • Doyle, K.M.1    Kennedy, D.2    Gorman, A.M.3    Gupta, S.4    Healy, S.J.5    Samali, A.6
  • 53
    • 84863740827 scopus 로고    scopus 로고
    • The impact of the unfolded protein response on human disease
    • Wang, S.; Kaufman, R.J. The impact of the unfolded protein response on human disease. J. Cell Biol. 2012, 197, 857-867.
    • (2012) J. Cell Biol. , vol.197 , pp. 857-867
    • Wang, S.1    Kaufman, R.J.2
  • 54
    • 84861473427 scopus 로고    scopus 로고
    • Endoplasmic reticulum: The unfolded protein response is tangled in neurodegeneration
    • Hoozemans, J.J.; Scheper, W. Endoplasmic reticulum: The unfolded protein response is tangled in neurodegeneration. Int. J. Biochem. Cell Biol. 2012, 44, 1295-1298.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1295-1298
    • Hoozemans, J.J.1    Scheper, W.2
  • 55
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: A glimpse into the ER
    • Matus, S.; Glimcher, L.H.; Hetz, C. Protein folding stress in neurodegenerative diseases: A glimpse into the ER. Curr. Opin. Cell Biol. 2011, 23, 239-252.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 239-252
    • Matus, S.1    Glimcher, L.H.2    Hetz, C.3
  • 56
    • 84858025731 scopus 로고    scopus 로고
    • C-terminal mutations destabilize SIL1/BAP and can cause Marinesco-Sjogren syndrome
    • Howes, J.; Shimizu, Y.; Feige, M.J.; Hendershot, L.M. C-terminal mutations destabilize SIL1/BAP and can cause Marinesco-Sjogren syndrome. J. Biol. Chem. 2012, 287, 8552-8560.
    • (2012) J. Biol. Chem. , vol.287 , pp. 8552-8560
    • Howes, J.1    Shimizu, Y.2    Feige, M.J.3    Hendershot, L.M.4
  • 58
    • 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
  • 62
    • 33745315287 scopus 로고    scopus 로고
    • S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara, T.; Nakamura, T.; Yao, D.; Shi, Z.Q.; Gu, Z.; Ma, Y.; Masliah, E.; Nomura, Y.; Lipton, S.A. S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 2006, 441, 513-517.
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4    Gu, Z.5    Ma, Y.6    Masliah, E.7    Nomura, Y.8    Lipton, S.A.9
  • 63
    • 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 , pp. 735206
    • 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
  • 65
    • 77956225923 scopus 로고    scopus 로고
    • Protective effects of galantamine against Abeta-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 Abeta-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
  • 69
    • 84861228335 scopus 로고    scopus 로고
    • α-Synuclein mRNA and soluble alpha-synuclein protein levels in post-mortem brain from patients with Parkinson's disease, dementia with Lewy bodies, and Alzheimer's disease
    • Quinn, J.G.; Coulson, D.T.; Brockbank, S.; Beyer, N.; Ravid, R.; Hellemans, J.; Irvine, G.B.; Johnston, J.A. α-Synuclein mRNA and soluble alpha-synuclein protein levels in post-mortem brain from patients with Parkinson's disease, dementia with Lewy bodies, and Alzheimer's disease. Brain Res. 2012, 1459, 71-80.
    • (2012) Brain Res. , vol.1459 , pp. 71-80
    • Quinn, J.G.1    Coulson, D.T.2    Brockbank, S.3    Beyer, N.4    Ravid, R.5    Hellemans, J.6    Irvine, G.B.7    Johnston, J.A.8
  • 70
    • 78649991684 scopus 로고    scopus 로고
    • The regulatory role of alpha-synuclein and parkin in neuronal cell apoptosis; possible implications for the pathogenesis of Parkinson's disease
    • Yasuda, T.; Mochizuki, H. The regulatory role of alpha-synuclein and parkin in neuronal cell apoptosis; possible implications for the pathogenesis of Parkinson's disease. Apoptosis 2010, 15, 1312-1321.
    • (2010) Apoptosis , vol.15 , pp. 1312-1321
    • Yasuda, T.1    Mochizuki, H.2
  • 72
    • 34247172998 scopus 로고    scopus 로고
    • Expanding insights on the involvement of endoplasmic reticulum stress in Parkinson's disease
    • Wang, H.Q.; Takahashi, R. Expanding insights on the involvement of endoplasmic reticulum stress in Parkinson's disease. Antioxid. Redox Signal. 2007, 9, 553-561.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 553-561
    • Wang, H.Q.1    Takahashi, R.2
  • 73
    • 79953148080 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress sensor, ATF6alpha, protects against neurotoxin-induced dopaminergic neuronal death
    • Egawa, N.; Yamamoto, K.; Inoue, H.; Hikawa, R.; Nishi, K.; Mori, K.; Takahashi, R. The endoplasmic reticulum stress sensor, ATF6alpha, protects against neurotoxin-induced dopaminergic neuronal death. J. Biol. Chem. 2011, 286, 7947-7957.
    • (2011) J. Biol. Chem. , vol.286 , pp. 7947-7957
    • Egawa, N.1    Yamamoto, K.2    Inoue, H.3    Hikawa, R.4    Nishi, K.5    Mori, K.6    Takahashi, R.7
  • 75
    • 84863845318 scopus 로고    scopus 로고
    • Mechanisms of age-related macular degeneration
    • Ambati, J.; Fowler, B.J. Mechanisms of age-related macular degeneration. Neuron 2012, 75, 26-39.
    • (2012) Neuron , vol.75 , pp. 26-39
    • Ambati, J.1    Fowler, B.J.2
  • 76
    • 78149272587 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress as a primary pathogenic mechanism leading to age-related macular degeneration
    • Libby, R.T.; Gould, D.B. Endoplasmic reticulum stress as a primary pathogenic mechanism leading to age-related macular degeneration. Adv. Exp. Med. Biol. 2010, 664, 403-409.
    • (2010) Adv. Exp. Med. Biol. , vol.664 , pp. 403-409
    • Libby, R.T.1    Gould, D.B.2
  • 77
    • 33645815074 scopus 로고    scopus 로고
    • Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression
    • Hu, P.; Han, Z.; Couvillon, A.D.; Kaufman, R.J.; Exton, J.H. Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression. Mol. Cell. Biol. 2006, 26, 3071-3084.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3071-3084
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3    Kaufman, R.J.4    Exton, J.H.5
  • 78
    • 8644282751 scopus 로고    scopus 로고
    • Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2
    • Deng, J.; Lu, P.D.; Zhang, Y.; Scheuner, D.; Kaufman, R.J.; Sonenberg, N.; Harding, H.P.; Ron, D. Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Mol. Cell. Biol. 2004, 24, 10161-10168.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10161-10168
    • Deng, J.1    Lu, P.D.2    Zhang, Y.3    Scheuner, D.4    Kaufman, R.J.5    Sonenberg, N.6    Harding, H.P.7    Ron, D.8
  • 80
    • 35348966298 scopus 로고    scopus 로고
    • Dietary antioxidants and primary prevention of age related macular degeneration: Systematic review and meta-analysis
    • Chong, E.W.; Wong, T.Y.; Kreis, A.J.; Simpson, J.A.; Guymer, R.H. Dietary antioxidants and primary prevention of age related macular degeneration: Systematic review and meta-analysis. BMJ 2007, 335, 755.
    • (2007) BMJ , vol.335 , pp. 755
    • Chong, E.W.1    Wong, T.Y.2    Kreis, A.J.3    Simpson, J.A.4    Guymer, R.H.5
  • 81
    • 0035879765 scopus 로고    scopus 로고
    • Lipofuscin-formation in retinal pigment epithelial cells is reduced by antioxidants
    • Sundelin, S.P.; Nilsson, S.E. Lipofuscin-formation in retinal pigment epithelial cells is reduced by antioxidants. Free Radic Biol. Med. 2001, 31, 217-225.
    • (2001) Free Radic Biol. Med. , vol.31 , pp. 217-225
    • Sundelin, S.P.1    Nilsson, S.E.2
  • 82
    • 4043076224 scopus 로고    scopus 로고
    • Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: Possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis
    • Okada, K.; Minamino, T.; Tsukamoto, Y.; Liao, Y.; Tsukamoto, O.; Takashima, S.; Hirata, A.; Fujita, M.; Nagamachi, Y.; Nakatani, T.; et al. Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: Possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis. Circulation 2004, 110, 705-712.
    • (2004) Circulation , vol.110 , pp. 705-712
    • Okada, K.1    Minamino, T.2    Tsukamoto, Y.3    Liao, Y.4    Tsukamoto, O.5    Takashima, S.6    Hirata, A.7    Fujita, M.8    Nagamachi, Y.9    Nakatani, T.10
  • 83
    • 84860693868 scopus 로고    scopus 로고
    • The chemical chaperone 4-phenylbutyric acid attenuates pressure-overload cardiac hypertrophy by alleviating endoplasmic reticulum stress
    • Park, C.S.; Cha, H.; Kwon, E.J.; Sreenivasaiah, P.K.; Kim do, H. The chemical chaperone 4-phenylbutyric acid attenuates pressure-overload cardiac hypertrophy by alleviating endoplasmic reticulum stress. Biochem. Biophys. Res. Commun. 2012, 421, 578-584.
    • (2012) Biochem. Biophys. Res. Commun. , vol.421 , pp. 578-584
    • Park, C.S.1    Cha, H.2    Kwon, E.J.3    Sreenivasaiah, P.K.4    do Kim, H.5
  • 84
    • 0016681491 scopus 로고
    • Ultrastructural features of degenerated cardiac muscle cells in patients with cardiac hypertrophy
    • Maron, B.J.; Ferrans, V.J.; Roberts, W.C. Ultrastructural features of degenerated cardiac muscle cells in patients with cardiac hypertrophy. Am. J. Pathol. 1975, 79, 387-434.
    • (1975) Am. J. Pathol. , vol.79 , pp. 387-434
    • Maron, B.J.1    Ferrans, V.J.2    Roberts, W.C.3
  • 86
    • 84856080791 scopus 로고    scopus 로고
    • Sarcalumenin plays a critical role in age-related cardiac dysfunction due to decreases in SERCA2a expression and activity
    • Jiao, Q.; Takeshima, H.; Ishikawa, Y.; Minamisawa, S. Sarcalumenin plays a critical role in age-related cardiac dysfunction due to decreases in SERCA2a expression and activity. Cell Calcium 2012, 51, 31-39.
    • (2012) Cell Calcium , vol.51 , pp. 31-39
    • Jiao, Q.1    Takeshima, H.2    Ishikawa, Y.3    Minamisawa, S.4
  • 87
    • 81855170043 scopus 로고    scopus 로고
    • Thapsigargin triggers cardiac contractile dysfunction via NADPH oxidase-mediated mitochondrial dysfunction: Role of Akt dephosphorylation
    • Zhang, Y.; Ren, J. Thapsigargin triggers cardiac contractile dysfunction via NADPH oxidase-mediated mitochondrial dysfunction: Role of Akt dephosphorylation. Free Radic Biol. Med. 2011, 51, 2172-2184.
    • (2011) Free Radic Biol. Med. , vol.51 , pp. 2172-2184
    • Zhang, Y.1    Ren, J.2
  • 88
    • 80355143466 scopus 로고    scopus 로고
    • Beta-AR blockers suppresses ER stress in cardiac hypertrophy and heart failure
    • Ni, L.; Zhou, C.; Duan, Q.; Lv, J.; Fu, X.; Xia, Y.; Wang, D.W. beta-AR blockers suppresses ER stress in cardiac hypertrophy and heart failure. PLoS One 2011, 6, e27294.
    • (2011) PLoS One , vol.6
    • Ni, L.1    Zhou, C.2    Duan, Q.3    Lv, J.4    Fu, X.5    Xia, Y.6    Wang, D.W.7
  • 89
    • 36048931354 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in the heart
    • Glembotski, C.C. Endoplasmic reticulum stress in the heart. Circ Res 2007, 101, 975-984.
    • (2007) Circ Res , vol.101 , pp. 975-984
    • Glembotski, C.C.1
  • 91
    • 20444461628 scopus 로고    scopus 로고
    • Free cholesterol-loaded macrophages are an abundant source of tumor necrosis factor-alpha and interleukin-6: Model of NF-kappaB-and map kinase-dependent inflammation in advanced atherosclerosis
    • Li, Y.; Schwabe, R.F.; DeVries-Seimon, T.; Yao, P.M.; Gerbod-Giannone, M.C.; Tall, A.R.; Davis, R.J.; Flavell, R.; Brenner, D.A.; Tabas, I. Free cholesterol-loaded macrophages are an abundant source of tumor necrosis factor-alpha and interleukin-6: Model of NF-kappaB-and map kinase-dependent inflammation in advanced atherosclerosis. J. Biol. Chem. 2005, 280, 21763-21772.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21763-21772
    • Li, Y.1    Schwabe, R.F.2    DeVries-Seimon, T.3    Yao, P.M.4    Gerbod-Giannone, M.C.5    Tall, A.R.6    Davis, R.J.7    Flavell, R.8    Brenner, D.A.9    Tabas, I.10
  • 92
    • 84859505076 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress controls M2 macrophage differentiation and foam cell formation
    • Oh, J.; Riek, A.E.; Weng, S.; Petty, M.; Kim, D.; Colonna, M.; Cella, M.; Bernal-Mizrachi, C. Endoplasmic reticulum stress controls M2 macrophage differentiation and foam cell formation. J. Biol. Chem. 2012, 287, 11629-11641.
    • (2012) J. Biol. Chem. , vol.287 , pp. 11629-11641
    • Oh, J.1    Riek, A.E.2    Weng, S.3    Petty, M.4    Kim, D.5    Colonna, M.6    Cella, M.7    Bernal-Mizrachi, C.8
  • 93
    • 35448946819 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum calcium disequilibria in the mechanism of homocysteine-induced ER stress
    • Dickhout, J.G.; Sood, S.K.; Austin, R.C. Role of endoplasmic reticulum calcium disequilibria in the mechanism of homocysteine-induced ER stress. Antioxid. Redox Signal. 2007, 9, 1863-1873.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 1863-1873
    • Dickhout, J.G.1    Sood, S.K.2    Austin, R.C.3
  • 94
    • 68949204491 scopus 로고    scopus 로고
    • Macrophage apoptosis in atherosclerosis: Consequences on plaque progression and the role of endoplasmic reticulum stress
    • Tabas, I. Macrophage apoptosis in atherosclerosis: Consequences on plaque progression and the role of endoplasmic reticulum stress. Antioxid. Redox Signal. 2009, 11, 2333-2339.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2333-2339
    • Tabas, I.1
  • 95
    • 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
  • 97
    • 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 , pp. 356487
    • Lenin, R.1    Maria, M.S.2    Agrawal, M.3    Balasubramanyam, J.4    Mohan, V.5    Balasubramanyam, M.6
  • 98
    • 33746788477 scopus 로고    scopus 로고
    • Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes
    • 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) Circ. 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
  • 99
    • 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
  • 100
    • 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
  • 101
    • 79952852144 scopus 로고    scopus 로고
    • Attenuation of endoplasmic reticulum stress-related myocardial apoptosis by SERCA2a gene delivery in ischemic heart disease
    • Xin, W.; Lu, X.; Li, X.; Niu, K.; Cai, J. Attenuation of endoplasmic reticulum stress-related myocardial apoptosis by SERCA2a gene delivery in ischemic heart disease. Mol. Med. 2011, 17, 201-210.
    • (2011) Mol. Med. , vol.17 , pp. 201-210
    • Xin, W.1    Lu, X.2    Li, X.3    Niu, K.4    Cai, J.5
  • 102
    • 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
  • 103
    • 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
  • 104
    • 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, S7-S9.
    • (2006) J. Gastroenterol. Hepatol. , vol.21
    • Kaplowitz, N.1    Ji, C.2
  • 108
    • 79952126737 scopus 로고    scopus 로고
    • Oncogenic potential of hepatitis C virus proteins
    • Banerjee, A.; Ray, R.B.; Ray, R. Oncogenic potential of hepatitis C virus proteins. Viruses 2010, 2, 2108-2133.
    • (2010) Viruses , vol.2 , pp. 2108-2133
    • Banerjee, A.1    Ray, R.B.2    Ray, R.3
  • 109
    • 80052899192 scopus 로고    scopus 로고
    • HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response
    • Merquiol, E.; Uzi, D.; Mueller, T.; Goldenberg, D.; Nahmias, Y.; Xavier, R.J.; Tirosh, B.; Shibolet, O. HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response. PLoS One 2011, 6, e24660.
    • (2011) PLoS One , vol.6
    • Merquiol, E.1    Uzi, D.2    Mueller, T.3    Goldenberg, D.4    Nahmias, Y.5    Xavier, R.J.6    Tirosh, B.7    Shibolet, O.8
  • 110
    • 79960951066 scopus 로고    scopus 로고
    • A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly
    • Boson, B.; Granio, O.; Bartenschlager, R.; Cosset, F.L. A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly. PLoS Pathog. 2011, 7, e1002144.
    • (2011) PLoS Pathog. , vol.7
    • Boson, B.1    Granio, O.2    Bartenschlager, R.3    Cosset, F.L.4
  • 112
    • 68549086862 scopus 로고    scopus 로고
    • Hepatitis C virus NS4B induces unfolded protein response and endoplasmic reticulum overload response-dependent NF-kappaB activation
    • Li, S.; Ye, L.; Yu, X.; Xu, B.; Li, K.; Zhu, X.; Liu, H.; Wu, X.; Kong, L. Hepatitis C virus NS4B induces unfolded protein response and endoplasmic reticulum overload response-dependent NF-kappaB activation. Virology 2009, 391, 257-264.
    • (2009) Virology , vol.391 , pp. 257-264
    • Li, S.1    Ye, L.2    Yu, X.3    Xu, B.4    Li, K.5    Zhu, X.6    Liu, H.7    Wu, X.8    Kong, L.9
  • 113
    • 0037111954 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) stress: Hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-kappaB and STAT-3
    • Waris, G.; Tardif, K.D.; Siddiqui, A. Endoplasmic reticulum (ER) stress: Hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-kappaB and STAT-3. Biochem. Pharmacol. 2002, 64, 1425-1430.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1425-1430
    • Waris, G.1    Tardif, K.D.2    Siddiqui, A.3
  • 114
    • 77954236285 scopus 로고    scopus 로고
    • Hepatocyte NAD(P)H oxidases as an endogenous source of reactive oxygen species during hepatitis C virus infection
    • de Mochel, N.S.; Seronello, S.; Wang, S.H.; Ito, C.; Zheng, J.X.; Liang, T.J.; Lambeth, J.D.; Choi, J. Hepatocyte NAD(P)H oxidases as an endogenous source of reactive oxygen species during hepatitis C virus infection. Hepatology 2010, 52, 47-59.
    • (2010) Hepatology , vol.52 , pp. 47-59
    • de Mochel, N.S.1    Seronello, S.2    Wang, S.H.3    Ito, C.4    Zheng, J.X.5    Liang, T.J.6    Lambeth, J.D.7    Choi, J.8
  • 115
    • 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 Harbor Perspect. Med. 2012, 2, a007666.
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2
    • Papa, F.R.1
  • 119
    • 84861905329 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and type 2 diabetes
    • Back, S.H.; Kaufman, R.J. Endoplasmic reticulum stress and type 2 diabetes. Ann. Rev. Biochem. 2012, 81, 767-793.
    • (2012) Ann. Rev. Biochem. , vol.81 , pp. 767-793
    • Back, S.H.1    Kaufman, R.J.2
  • 121
    • 83755207504 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect pancreatic beta-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 beta-cells against oxidative stress and improve insulin secretion in glucotoxicity and glucolipotoxicity. Cell. Phys. Biochem. 2011, 28, 873-886.
    • (2011) Cell. Phys. 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
  • 122
    • 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
  • 125
    • 78650105442 scopus 로고    scopus 로고
    • NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis
    • Li, G.; Scull, C.; Ozcan, L.; Tabas, I. NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis. J. Cell Biol. 2010, 191, 1113-1125.
    • (2010) J. Cell Biol. , vol.191 , pp. 1113-1125
    • Li, G.1    Scull, C.2    Ozcan, L.3    Tabas, I.4


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