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Volumn 14, Issue 4, 2015, Pages 518-533

Modulation of endoplasmic reticulum stress: An opportunity to prevent neurodegeneration?

Author keywords

Endoplasmic reticulum; Neurodegeneration; Therapeutic targets; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; AMYLOID PRECURSOR PROTEIN; CASPASE 12; CASPASE 3; CASPASE 7; CASPASE 8; CASPASE 9; GLUCOSE REGULATED PROTEIN 78; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INITIATION FACTOR 2; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR NRF2; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 84929628537     PISSN: 18715273     EISSN: 19963181     Source Type: Journal    
DOI: 10.2174/1871527314666150429112353     Document Type: Article
Times cited : (24)

References (236)
  • 1
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz C, Mollereau B. Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat Rev Neurosci 2014; 15(4): 233-49.
    • (2014) Nat Rev Neurosci , vol.15 , Issue.4 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 3
    • 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(6059): 1081-6.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 4
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1
    • Sevier CS, Qu H, Heldman N, Gross E, Fass D, Kaiser CA. Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 2007; 129(2): 333-44.
    • (2007) Cell , vol.129 , Issue.2 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 5
    • 84903458925 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum in amyloid precursor protein processing and trafficking: Implication's for Alzheimer's disease
    • 201
    • Placido AI, Pereira CM, Duarte AI, et al. The role of endoplasmic reticulum in amyloid precursor protein processing and trafficking: Implication's for Alzheimer's disease. Biochim Biophys Acta 201; 1842(9): 1444-53.
    • Biochim Biophys Acta , vol.1842 , Issue.9 , pp. 1444-1453
    • Placido, A.I.1    Pereira, C.M.2    Duarte, A.I.3
  • 6
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • Xu C, Bailly-Maitre B, Reed JC. Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest 2005; 115(10): 2656-64.
    • (2005) J Clin Invest , vol.115 , Issue.10 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 7
    • 84864484497 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress stimulates p53 expression through NF-kappaB activation
    • Lin WC, Chuang YC, Chang YS, et al. Endoplasmic reticulum stress stimulates p53 expression through NF-kappaB activation. PLoS One 2012; 7(7): e39120.
    • (2012) PLoS One , vol.7 , Issue.7
    • Lin, W.C.1    Chuang, Y.C.2    Chang, Y.S.3
  • 8
    • 84878646405 scopus 로고    scopus 로고
    • ER-stress-associated functional link between Parkin and DJ-1 via a transcriptional cascade involving the tumor suppressor p53 and the spliced X-box binding protein XBP-1
    • Duplan E, Giaime E, Viotti J, et al. ER-stress-associated functional link between Parkin and DJ-1 via a transcriptional cascade involving the tumor suppressor p53 and the spliced X-box binding protein XBP-1. J Cell Sci 2013; 126(Pt 9): 2124-33.
    • (2013) J Cell Sci , vol.126 , pp. 2124-2133
    • Duplan, E.1    Giaime, E.2    Viotti, J.3
  • 9
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2000; 2(6): 326-32.
    • (2000) Nat Cell Biol , vol.2 , Issue.6 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 10
    • 58149109602 scopus 로고    scopus 로고
    • GRP78: A chaperone with diverse roles beyond the endoplasmic reticulum
    • Quinones QJ, de Ridder GG, Pizzo SV. GRP78: a chaperone with diverse roles beyond the endoplasmic reticulum. Histol Histopathol 2008; 23(11): 1409-16.
    • (2008) Histol Histopathol , vol.23 , Issue.11 , pp. 1409-1416
    • Quinones, Q.J.1    de Ridder, G.G.2    Pizzo, S.V.3
  • 11
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J, Chen X, Hendershot L, Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 2002; 3(1): 99- 111.
    • (2002) Dev Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 12
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 2000; 5(5): 897-904.
    • (2000) Mol Cell , vol.5 , Issue.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 13
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 2000; 6(5): 1099-108.
    • (2000) Mol Cell , vol.6 , Issue.5 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3
  • 14
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu PD, Harding HP, Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol 2004; 167(1): 27-33.
    • (2004) J Cell Biol , vol.167 , Issue.1 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 15
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem KM, Wek RC. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc Natl Acad Sci USA 2004; 101(31): 11269-74.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.31 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 16
    • 0034973982 scopus 로고    scopus 로고
    • Translational control is required for the unfolded protein response and in vivo glucose homeostasis
    • Scheuner D, Song B, McEwen E, et al. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol Cell 2001; 7(6): 1165-76.
    • (2001) Mol Cell , vol.7 , Issue.6 , pp. 1165-1176
    • Scheuner, D.1    Song, B.2    McEwen, E.3
  • 17
    • 84886749523 scopus 로고    scopus 로고
    • IRE1: ER stress sensor and cell fate executor
    • Chen Y, Brandizzi F. IRE1: ER stress sensor and cell fate executor. Trends Cell Biol 2013; 23(11): 547-55.
    • (2013) Trends Cell Biol , vol.23 , Issue.11 , pp. 547-555
    • Chen, Y.1    Brandizzi, F.2
  • 18
    • 70349756962 scopus 로고    scopus 로고
    • Function of IRE1 alpha in the placenta is essential for placental development and embryonic viability
    • Iwawaki T, Akai R, Yamanaka S, Kohno K. Function of IRE1 alpha in the placenta is essential for placental development and embryonic viability. Proc Natl Acad Sci USA 2009; 106(39): 16657-62.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.39 , pp. 16657-16662
    • Iwawaki, T.1    Akai, R.2    Yamanaka, S.3    Kohno, K.4
  • 19
    • 84874251933 scopus 로고    scopus 로고
    • Negative feedback by IRE1beta optimizes mucin production in goblet cells
    • Tsuru A, Fujimoto N, Takahashi S, et al. Negative feedback by IRE1beta optimizes mucin production in goblet cells. Proc Natl Acad Sci USA 2013; 110(8): 2864-9.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.8 , pp. 2864-2869
    • Tsuru, A.1    Fujimoto, N.2    Takahashi, S.3
  • 20
    • 37649004940 scopus 로고    scopus 로고
    • Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
    • Lee KP, Dey M, Neculai D, Cao C, Dever TE, Sicheri F. Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing. Cell 2008; 132(1): 89-100.
    • (2008) Cell , vol.132 , Issue.1 , pp. 89-100
    • Lee, K.P.1    Dey, M.2    Neculai, D.3    Cao, C.4    Dever, T.E.5    Sicheri, F.6
  • 21
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001; 107(7): 881-91.
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 22
    • 84890965447 scopus 로고    scopus 로고
    • Interregulation of the unfolded protein response and auxin signaling
    • Chen Y, Aung K, Rolcik J, Walicki K, Friml J, Brandizzi F. Interregulation of the unfolded protein response and auxin signaling. Plant J 2014; 77(1): 97-107.
    • (2014) Plant J , vol.77 , Issue.1 , pp. 97-107
    • Chen, Y.1    Aung, K.2    Rolcik, J.3    Walicki, K.4    Friml, J.5    Brandizzi, F.6
  • 23
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee AH, Iwakoshi NN, Glimcher LH. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 2003; 23(21): 7448-59.
    • (2003) Mol Cell Biol , vol.23 , Issue.21 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 24
    • 68549092781 scopus 로고    scopus 로고
    • Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
    • Hollien J, Lin JH, Li H, Stevens N, Walter P, Weissman JS. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J Cell Biol 2009; 186(3): 323-31.
    • (2009) J Cell Biol , vol.186 , Issue.3 , pp. 323-331
    • Hollien, J.1    Lin, J.H.2    Li, H.3    Stevens, N.4    Walter, P.5    Weissman, J.S.6
  • 25
  • 26
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K, Tirasophon W, Shen X, et al. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 2002; 16(4): 452-66.
    • (2002) Genes Dev , vol.16 , Issue.4 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3
  • 27
    • 44449101173 scopus 로고    scopus 로고
    • ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum
    • Adachi Y, Yamamoto K, Okada T, Yoshida H, Harada A, Mori K. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct 2008; 33(1): 75-89.
    • (2008) Cell Struct Funct , vol.33 , Issue.1 , pp. 75-89
    • Adachi, Y.1    Yamamoto, K.2    Okada, T.3    Yoshida, H.4    Harada, A.5    Mori, K.6
  • 28
    • 1542380581 scopus 로고    scopus 로고
    • Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB
    • Habelhah H, Takahashi S, Cho SG, Kadoya T, Watanabe T, Ronai Z. Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB. EMBO J 2004; 23(2): 322-32.
    • (2004) EMBO J , vol.23 , Issue.2 , pp. 322-332
    • Habelhah, H.1    Takahashi, S.2    Cho, S.G.3    Kadoya, T.4    Watanabe, T.5    Ronai, Z.6
  • 29
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F, Wang X, Bertolotti A, et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287(5453): 664-6.
    • (2000) Science , vol.287 , Issue.5453 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3
  • 30
    • 84868525253 scopus 로고    scopus 로고
    • IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2
    • Upton JP, Wang L, Han D, et al. IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2. Science 2012; 338(6108): 818-22.
    • (2012) Science , vol.338 , Issue.6108 , pp. 818-822
    • Upton, J.P.1    Wang, L.2    Han, D.3
  • 31
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • Cullinan SB, Diehl JA. PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J Biol Chem 2004; 279(19): 20108- 17.
    • (2004) J Biol Chem , vol.279 , Issue.19 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 32
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz C. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 2012; 13(2): 89-102.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.2 , pp. 89-102
    • Hetz, C.1
  • 33
    • 79953146630 scopus 로고    scopus 로고
    • Selective abrogation of BiP/GRP78 blunts activation of NF-kappaB through the ATF6 branch of the UPR: Involvement of C/EBPbeta and mTORdependent dephosphorylation of Akt
    • Nakajima S, Hiramatsu N, Hayakawa K, et al. Selective abrogation of BiP/GRP78 blunts activation of NF-kappaB through the ATF6 branch of the UPR: involvement of C/EBPbeta and mTORdependent dephosphorylation of Akt. Mol Cell Biol 2011; 31(8): 1710-8.
    • (2011) Mol Cell Biol , vol.31 , Issue.8 , pp. 1710-1718
    • Nakajima, S.1    Hiramatsu, N.2    Hayakawa, K.3
  • 34
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N, et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403(6765): 98-103.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3
  • 35
    • 0035976923 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced cysteine protease activation in cortical neurons: Effect of an Alzheimer's disease-linked presenilin-1 knock-in mutation
    • Siman R, Flood DG, Thinakaran G, Neumar RW. Endoplasmic reticulum stress-induced cysteine protease activation in cortical neurons: effect of an Alzheimer's disease-linked presenilin-1 knock-in mutation. J Biol Chem 2001; 276(48): 44736-43.
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 44736-44743
    • Siman, R.1    Flood, D.G.2    Thinakaran, G.3    Neumar, R.W.4
  • 36
    • 0036744969 scopus 로고    scopus 로고
    • Neuronal apoptosis induced by endoplasmic reticulum stress
    • Chen L, Gao X. Neuronal apoptosis induced by endoplasmic reticulum stress. Neurochem Res 2002; 27(9): 891-8.
    • (2002) Neurochem Res , vol.27 , Issue.9 , pp. 891-898
    • Chen, L.1    Gao, X.2
  • 37
    • 0037096823 scopus 로고    scopus 로고
    • Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation
    • Kouroku Y, Fujita E, Jimbo A, et al. Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation. Hum Mol Genet 2002; 11(13): 1505-15.
    • (2002) Hum Mol Genet , vol.11 , Issue.13 , pp. 1505-1515
    • Kouroku, Y.1    Fujita, E.2    Jimbo, A.3
  • 38
    • 1342305497 scopus 로고    scopus 로고
    • Caspase-12 and ER-stressmediated apoptosis: The story so far
    • Szegezdi E, Fitzgerald U, Samali A. Caspase-12 and ER-stressmediated apoptosis: the story so far. Ann NY Acad Sci 2003; 1010: 186-94.
    • (2003) Ann NY Acad Sci , vol.1010 , pp. 186-194
    • Szegezdi, E.1    Fitzgerald, U.2    Samali, A.3
  • 39
    • 33645141853 scopus 로고    scopus 로고
    • ER stress and neurodegenerative diseases
    • Lindholm D, Wootz H, Korhonen L. ER stress and neurodegenerative diseases. Cell Death Differ 2006; 13(3): 385-92.
    • (2006) Cell Death Differ , vol.13 , Issue.3 , pp. 385-392
    • Lindholm, D.1    Wootz, H.2    Korhonen, L.3
  • 40
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T, Imaizumi K, Oono K, et al. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 2001; 276(17): 13935-40.
    • (2001) J Biol Chem , vol.276 , Issue.17 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3
  • 41
    • 84894432757 scopus 로고    scopus 로고
    • Glucose deprivation induces reticulum stress by the PERK pathway and caspase-7- and calpain-mediated caspase-12 activation
    • de la Cadena SG, Hernandez-Fonseca K, Camacho-Arroyo I, Massieu L. Glucose deprivation induces reticulum stress by the PERK pathway and caspase-7- and calpain-mediated caspase-12 activation. Apoptosis 2014; 19(3): 414-27.
    • (2014) Apoptosis , vol.19 , Issue.3 , pp. 414-427
    • de la Cadena, S.G.1    Hernandez-Fonseca, K.2    Camacho-Arroyo, I.3    Massieu, L.4
  • 42
    • 33646175602 scopus 로고    scopus 로고
    • Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice
    • Saleh M, Mathison JC, Wolinski MK, et al. Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice. Nature 2006; 440(7087): 1064-8.
    • (2006) Nature , vol.440 , Issue.7087 , pp. 1064-1068
    • Saleh, M.1    Mathison, J.C.2    Wolinski, M.K.3
  • 44
    • 0037007141 scopus 로고    scopus 로고
    • The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum
    • Breckenridge DG, Nguyen M, Kuppig S, Reth M, Shore GC. The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum. Proc Natl Acad Sci USA 2002; 99(7): 4331-6.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.7 , pp. 4331-4336
    • Breckenridge, D.G.1    Nguyen, M.2    Kuppig, S.3    Reth, M.4    Shore, G.C.5
  • 45
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge DG, Stojanovic M, Marcellus RC, Shore GC. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J Cell Biol 2003; 160(7): 1115- 27.
    • (2003) J Cell Biol , vol.160 , Issue.7 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 46
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao RV, Ellerby HM, Bredesen DE. Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ 2004; 11(4): 372-80.
    • (2004) Cell Death Differ , vol.11 , Issue.4 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 47
    • 0033816610 scopus 로고    scopus 로고
    • Caspaseresistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria
    • Nguyen M, Breckenridge DG, Ducret A, Shore GC. Caspaseresistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria. Mol Cell Biol 2000; 20(18): 6731-40.
    • (2000) Mol Cell Biol , vol.20 , Issue.18 , pp. 6731-6740
    • Nguyen, M.1    Breckenridge, D.G.2    Ducret, A.3    Shore, G.C.4
  • 48
    • 0037418238 scopus 로고    scopus 로고
    • JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
    • Lei K, Davis RJ. JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. Proc Natl Acad Sci USA 2003; 100(5): 2432-7.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.5 , pp. 2432-2437
    • Lei, K.1    Davis, R.J.2
  • 49
    • 0037860975 scopus 로고    scopus 로고
    • JNK-mediated BIM phosphorylation potentiates BAX-dependent apoptosis
    • Putcha GV, Le S, Frank S, et al. JNK-mediated BIM phosphorylation potentiates BAX-dependent apoptosis. Neuron 2003; 38(6): 899-914.
    • (2003) Neuron , vol.38 , Issue.6 , pp. 899-914
    • Putcha, G.V.1    Le, S.2    Frank, S.3
  • 50
    • 0033499801 scopus 로고    scopus 로고
    • BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M
    • Yamamoto K, Ichijo H, Korsmeyer SJ. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol 1999; 19(12): 8469- 78.
    • (1999) Mol Cell Biol , vol.19 , Issue.12 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 51
    • 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, et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002; 16(11): 1345-55.
    • (2002) Genes Dev , vol.16 , Issue.11 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3
  • 52
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S, Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ 2004; 11(4): 381-9.
    • (2004) Cell Death Differ , vol.11 , Issue.4 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 53
    • 33646166316 scopus 로고    scopus 로고
    • The role of the endoplasmic reticulum in the accumulation of beta-amyloid peptide in Alzheimer's disease
    • Ghribi O. The role of the endoplasmic reticulum in the accumulation of beta-amyloid peptide in Alzheimer's disease. Curr Mol Med 2006; 6(1): 119-33.
    • (2006) Curr Mol Med , vol.6 , Issue.1 , pp. 119-133
    • Ghribi, O.1
  • 55
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state
    • McCullough KD, Martindale JL, Klotz LO, Aw TY, Holbrook NJ. Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001; 21(4): 1249-59.
    • (2001) Mol Cell Biol , vol.21 , Issue.4 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 56
    • 84877578475 scopus 로고    scopus 로고
    • ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
    • Han J, Back SH, Hur J, et al. ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death. Nat Cell Biol 2013; 15(5): 481-90.
    • (2013) Nat Cell Biol , vol.15 , Issue.5 , pp. 481-490
    • Han, J.1    Back, S.H.2    Hur, J.3
  • 57
    • 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 KT, et al. 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(6): 783-92.
    • (2009) J Cell Biol , vol.186 , Issue.6 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3
  • 58
    • 0037418843 scopus 로고    scopus 로고
    • BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis
    • Scorrano L, Oakes SA, Opferman JT, et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis. Science 2003; 300(5616): 135-9.
    • (2003) Science , vol.300 , Issue.5616 , pp. 135-139
    • Scorrano, L.1    Oakes, S.A.2    Opferman, J.T.3
  • 59
    • 3342984659 scopus 로고    scopus 로고
    • Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate
    • Chen R, Valencia I, Zhong F, et al. Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate. J Cell Biol 2004; 166(2): 193-203.
    • (2004) J Cell Biol , vol.166 , Issue.2 , pp. 193-203
    • Chen, R.1    Valencia, I.2    Zhong, F.3
  • 60
    • 84905049169 scopus 로고    scopus 로고
    • Calcium trafficking integrates endoplasmic reticulum function with mitochondrial bioenergetics
    • Kaufman RJ, Malhotra JD. Calcium trafficking integrates endoplasmic reticulum function with mitochondrial bioenergetics. Biochim Biophys Acta 2014; 1843(10): 2233-9.
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.10 , pp. 2233-2239
    • Kaufman, R.J.1    Malhotra, J.D.2
  • 61
    • 11844284861 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
    • Oakes SA, Scorrano L, Opferman JT, et al. Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc Natl Acad Sci USA 2005; 102(1): 105-10.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.1 , pp. 105-110
    • Oakes, S.A.1    Scorrano, L.2    Opferman, J.T.3
  • 62
    • 10044264391 scopus 로고    scopus 로고
    • Calcium and mitochondria: Mechanisms and functions of a troubled relationship
    • Bianchi K, Rimessi A, Prandini A, Szabadkai G, Rizzuto R. Calcium and mitochondria: mechanisms and functions of a troubled relationship. Biochim Biophys Acta 2004; 1742(1-3): 119-31.
    • (2004) Biochim Biophys Acta , vol.1742 , Issue.1-3 , pp. 119-131
    • Bianchi, K.1    Rimessi, A.2    Prandini, A.3    Szabadkai, G.4    Rizzuto, R.5
  • 63
    • 34547941644 scopus 로고    scopus 로고
    • Evolution of calcium homeostasis: From birth of the first cell to an omnipresent signalling system
    • Case RM, Eisner D, Gurney A, Jones O, Muallem S, Verkhratsky A. Evolution of calcium homeostasis: from birth of the first cell to an omnipresent signalling system. Cell Calcium 2007; 42(4-5): 345-50.
    • (2007) Cell Calcium , vol.42 , Issue.4-5 , pp. 345-350
    • Case, R.M.1    Eisner, D.2    Gurney, A.3    Jones, O.4    Muallem, S.5    Verkhratsky, A.6
  • 64
    • 0031710975 scopus 로고    scopus 로고
    • Modulation of cell calcium signals by mitochondria
    • Jouaville LS, Ichas F, Mazat JP. Modulation of cell calcium signals by mitochondria. Mol Cell Biochem 1998; 184(1-2): 371-6.
    • (1998) Mol Cell Biochem , vol.184 , Issue.1-2 , pp. 371-376
    • Jouaville, L.S.1    Ichas, F.2    Mazat, J.P.3
  • 65
    • 33845692166 scopus 로고    scopus 로고
    • Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
    • Szabadkai G, Bianchi K, Varnai P, et al. Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels. J Cell Biol 2006; 175(6): 901-11.
    • (2006) J Cell Biol , vol.175 , Issue.6 , pp. 901-911
    • Szabadkai, G.1    Bianchi, K.2    Varnai, P.3
  • 66
    • 84873248602 scopus 로고    scopus 로고
    • In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM)
    • Poston CN, Krishnan SC, Bazemore-Walker CR. In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM). J Proteomics 2013; 79: 219-30.
    • (2013) J Proteomics , vol.79 , pp. 219-230
    • Poston, C.N.1    Krishnan, S.C.2    Bazemore-Walker, C.R.3
  • 67
    • 84905031945 scopus 로고    scopus 로고
    • Ca-mediated regulation of VDAC1 expression levels is associated with cell death induction
    • Weisthal S, Keinan N, Ben-Hail D, Arif T, Shoshan-Barmatz V. Ca-mediated regulation of VDAC1 expression levels is associated with cell death induction. Biochim Biophys Acta 2014; 1843(10): 2270-81.
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.10 , pp. 2270-2281
    • Weisthal, S.1    Keinan, N.2    Ben-Hail, D.3    Arif, T.4    Shoshan-Barmatz, V.5
  • 68
    • 84891393224 scopus 로고    scopus 로고
    • The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter
    • Pan X, Liu J, Nguyen T, et al. The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter. Nat Cell Biol 2013; 15(12): 1464-72.
    • (2013) Nat Cell Biol , vol.15 , Issue.12 , pp. 1464-1472
    • Pan, X.1    Liu, J.2    Nguyen, T.3
  • 69
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • Huang Y, Wang KK. The calpain family and human disease. Trends Mol Med 2001; 7(8): 355-62.
    • (2001) Trends Mol Med , vol.7 , Issue.8 , pp. 355-362
    • Huang, Y.1    Wang, K.K.2
  • 70
    • 0032480260 scopus 로고    scopus 로고
    • Bax cleavage is mediated by calpain during drug-induced apoptosis
    • Wood DE, Thomas A, Devi LA, et al. Bax cleavage is mediated by calpain during drug-induced apoptosis. Oncogene 1998; 17(9): 1069-78.
    • (1998) Oncogene , vol.17 , Issue.9 , pp. 1069-1078
    • Wood, D.E.1    Thomas, A.2    Devi, L.A.3
  • 71
    • 0035903235 scopus 로고    scopus 로고
    • Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion
    • Chen M, He H, Zhan S, Krajewski S, Reed JC, Gottlieb RA. Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion. J Biol Chem 2001; 276(33): 30724-8.
    • (2001) J Biol Chem , vol.276 , Issue.33 , pp. 30724-30728
    • Chen, M.1    He, H.2    Zhan, S.3    Krajewski, S.4    Reed, J.C.5    Gottlieb, R.A.6
  • 72
    • 0036125351 scopus 로고    scopus 로고
    • Lipids, cardiolipin and apoptosis: A greasy licence to kill
    • Esposti MD. Lipids, cardiolipin and apoptosis: a greasy licence to kill. Cell Death Differ 2002; 9(3): 234-6.
    • (2002) Cell Death Differ , vol.9 , Issue.3 , pp. 234-236
    • Esposti, M.D.1
  • 73
  • 74
  • 75
    • 4944222095 scopus 로고    scopus 로고
    • Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2+ waves and protects against Ca2+- mediated apoptosis
    • Szabadkai G, Simoni AM, Chami M, Wieckowski MR, Youle RJ, Rizzuto R. Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2+ waves and protects against Ca2+- mediated apoptosis. Mol Cell 2004; 16(1): 59-68.
    • (2004) Mol Cell , vol.16 , Issue.1 , pp. 59-68
    • Szabadkai, G.1    Simoni, A.M.2    Chami, M.3    Wieckowski, M.R.4    Youle, R.J.5    Rizzuto, R.6
  • 76
    • 0033537768 scopus 로고    scopus 로고
    • Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD
    • Wang HG, Pathan N, Ethell IM, et al. Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD. Science 1999; 284(5412): 339-43.
    • (1999) Science , vol.284 , Issue.5412 , pp. 339-343
    • Wang, H.G.1    Pathan, N.2    Ethell, I.M.3
  • 77
    • 27144487808 scopus 로고    scopus 로고
    • The endoplasmic reticulum gateway to apoptosis by Bcl-X(L) modulation of the InsP3R
    • White C, Li C, Yang J, et al. The endoplasmic reticulum gateway to apoptosis by Bcl-X(L) modulation of the InsP3R. Nat Cell Biol 2005; 7(10): 1021-8.
    • (2005) Nat Cell Biol , vol.7 , Issue.10 , pp. 1021-1028
    • White, C.1    Li, C.2    Yang, J.3
  • 78
    • 0033595816 scopus 로고    scopus 로고
    • Apoptosis of T cells mediated by Ca2+-induced release of the transcription factor MEF2
    • Youn HD, Sun L, Prywes R, Liu JO. Apoptosis of T cells mediated by Ca2+-induced release of the transcription factor MEF2. Science 1999; 286(5440): 790-3.
    • (1999) Science , vol.286 , Issue.5440 , pp. 790-793
    • Youn, H.D.1    Sun, L.2    Prywes, R.3    Liu, J.O.4
  • 80
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • Ogata M, Hino S, Saito A, et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 2006; 26(24): 9220-31.
    • (2006) Mol Cell Biol , vol.26 , Issue.24 , pp. 9220-9231
    • Ogata, M.1    Hino, S.2    Saito, A.3
  • 81
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding WX, Ni HM, Gao W, et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007; 171(2): 513-24.
    • (2007) Am J Pathol , vol.171 , Issue.2 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3
  • 82
    • 74949118681 scopus 로고    scopus 로고
    • The unfolded protein response protects human tumor cells during hypoxia through regulation of the autophagy genes MAP1LC3B and ATG5
    • Rouschop KM, van den Beucken T, Dubois L, et al. The unfolded protein response protects human tumor cells during hypoxia through regulation of the autophagy genes MAP1LC3B and ATG5. J Clin Invest 2010; 120(1): 127-41.
    • (2010) J Clin Invest , vol.120 , Issue.1 , pp. 127-141
    • Rouschop, K.M.1    van den Beucken, T.2    Dubois, L.3
  • 83
    • 33846211417 scopus 로고    scopus 로고
    • ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation
    • Kouroku Y, Fujita E, Tanida I, et al. ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ 2007; 14(2): 230-9.
    • (2007) Cell Death Differ , vol.14 , Issue.2 , pp. 230-239
    • Kouroku, Y.1    Fujita, E.2    Tanida, I.3
  • 84
    • 0037039442 scopus 로고    scopus 로고
    • Regulation of starvationand virus-induced autophagy by the eIF2alpha kinase signaling pathway
    • Talloczy Z, Jiang W, Virgin HW, et al. Regulation of starvationand virus-induced autophagy by the eIF2alpha kinase signaling pathway. Proc Natl Acad Sci USA 2002; 99(1): 190-5.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.1 , pp. 190-195
    • Talloczy, Z.1    Jiang, W.2    Virgin, H.W.3
  • 85
    • 84885455062 scopus 로고    scopus 로고
    • The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression
    • B'Chir W, Maurin AC, Carraro V, et al. The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression. Nucleic Acids Res 2013; 41(16): 7683-99.
    • (2013) Nucleic Acids Res , vol.41 , Issue.16 , pp. 7683-7699
    • B'Chir, W.1    Maurin, A.C.2    Carraro, V.3
  • 86
    • 84863296660 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress, the unfolded protein response, autophagy, and the integrated regulation of breast cancer cell fate
    • Clarke R, Cook KL, Hu R, et al. Endoplasmic reticulum stress, the unfolded protein response, autophagy, and the integrated regulation of breast cancer cell fate. Cancer Res 2012; 72(6): 1321-31.
    • (2012) Cancer Res , vol.72 , Issue.6 , pp. 1321-1331
    • Clarke, R.1    Cook, K.L.2    Hu, R.3
  • 87
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer G, Marino G, Levine B. Autophagy and the integrated stress response. Mol Cell 2010; 40(2): 280-93.
    • (2010) Mol Cell , vol.40 , Issue.2 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 88
    • 50249137038 scopus 로고    scopus 로고
    • Induction of macroautophagy by exogenously introduced calcium
    • Gao W, Ding WX, Stolz DB, Yin XM. Induction of macroautophagy by exogenously introduced calcium. Autophagy 2008; 4(6): 754-61.
    • (2008) Autophagy , vol.4 , Issue.6 , pp. 754-761
    • Gao, W.1    Ding, W.X.2    Stolz, D.B.3    Yin, X.M.4
  • 89
    • 33846189759 scopus 로고    scopus 로고
    • Control of macroautophagy by calcium, calmodulin-dependent kinase kinasebeta, and Bcl-2
    • Hoyer-Hansen M, Bastholm L, Szyniarowski P, et al. Control of macroautophagy by calcium, calmodulin-dependent kinase kinasebeta, and Bcl-2. Mol Cell 2007; 25(2): 193-205.
    • (2007) Mol Cell , vol.25 , Issue.2 , pp. 193-205
    • Hoyer-Hansen, M.1    Bastholm, L.2    Szyniarowski, P.3
  • 90
    • 79251587803 scopus 로고    scopus 로고
    • Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
    • Egan DF, Shackelford DB, Mihaylova MM, et al. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 2011; 331(6016): 456-61.
    • (2011) Science , vol.331 , Issue.6016 , pp. 456-461
    • Egan, D.F.1    Shackelford, D.B.2    Mihaylova, M.M.3
  • 91
    • 84865712631 scopus 로고    scopus 로고
    • Modulating macroautophagy: A neuronal perspective
    • Johnson CW, Melia TJ, Yamamoto A. Modulating macroautophagy: a neuronal perspective. Future Med Chem 2012; 4(13): 1715-31.
    • (2012) Future Med Chem , vol.4 , Issue.13 , pp. 1715-1731
    • Johnson, C.W.1    Melia, T.J.2    Yamamoto, A.3
  • 92
    • 84874904524 scopus 로고    scopus 로고
    • The role of calcium stores in apoptosis and autophagy
    • Smaili SS, Pereira GJ, Costa MM, et al. The role of calcium stores in apoptosis and autophagy. Curr Mol Med 2013; 13(2): 252-65.
    • (2013) Curr Mol Med , vol.13 , Issue.2 , pp. 252-265
    • Smaili, S.S.1    Pereira, G.J.2    Costa, M.M.3
  • 93
    • 34548037901 scopus 로고    scopus 로고
    • Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium
    • Hoyer-Hansen M, Jaattela M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 2007; 14(9): 1576-82.
    • (2007) Cell Death Differ , vol.14 , Issue.9 , pp. 1576-1582
    • Hoyer-Hansen, M.1    Jaattela, M.2
  • 94
    • 77955824765 scopus 로고    scopus 로고
    • An intimate liaison: Spatial organization of the endoplasmic reticulum-mitochondria relationship
    • de Brito OM, Scorrano L. An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship. EMBO J 2010; 29(16): 2715-23.
    • (2010) EMBO J , vol.29 , Issue.16 , pp. 2715-2723
    • de Brito, O.M.1    Scorrano, L.2
  • 95
    • 84883451708 scopus 로고    scopus 로고
    • The molecular hug between the ER and the mitochondria
    • Kornmann B. The molecular hug between the ER and the mitochondria. Curr Opin Cell Biol 2013; 25(4): 443-8.
    • (2013) Curr Opin Cell Biol , vol.25 , Issue.4 , pp. 443-448
    • Kornmann, B.1
  • 96
    • 84904967279 scopus 로고    scopus 로고
    • New functions of mitochondria associated membranes in cellular signaling
    • van Vliet AR, Verfaillie T, Agostinis P. New functions of mitochondria associated membranes in cellular signaling. Biochim Biophys Acta 2014; 1843(10): 2253-62.
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.10 , pp. 2253-2262
    • van Vliet, A.R.1    Verfaillie, T.2    Agostinis, P.3
  • 97
    • 84908082447 scopus 로고    scopus 로고
    • Stress-responsive regulation of mitochondria through the ER unfolded protein response
    • Rainbolt TK, Saunders JM, Wiseman RL. Stress-responsive regulation of mitochondria through the ER unfolded protein response. Trends Endocrinol Metab 2014; 25(10): 528-37.
    • (2014) Trends Endocrinol Metab , vol.25 , Issue.10 , pp. 528-537
    • Rainbolt, T.K.1    Saunders, J.M.2    Wiseman, R.L.3
  • 98
    • 29144463168 scopus 로고    scopus 로고
    • Agonist-induced regulation of mitochondrial and endoplasmic reticulum motility
    • Brough D, Schell MJ, Irvine RF. Agonist-induced regulation of mitochondrial and endoplasmic reticulum motility. Biochem J 2005; 392(Pt 2): 291-7.
    • (2005) Biochem J , vol.392 , pp. 291-297
    • Brough, D.1    Schell, M.J.2    Irvine, R.F.3
  • 99
    • 79960898591 scopus 로고    scopus 로고
    • Mitochondria and endoplasmic reticulum: Mitochondria-endoplasmic reticulum interplay in type 2 diabetes pathophysiology
    • Rieusset J. Mitochondria and endoplasmic reticulum: mitochondria-endoplasmic reticulum interplay in type 2 diabetes pathophysiology. Int J Biochem Cell Biol 2011; 43(9): 1257-62.
    • (2011) Int J Biochem Cell Biol , vol.43 , Issue.9 , pp. 1257-1262
    • Rieusset, J.1
  • 101
    • 79960310339 scopus 로고    scopus 로고
    • Increased ER-mitochondrial coupling promotes mitochondrial respiration and bioenergetics during early phases of ER stress
    • Bravo R, Vicencio JM, Parra V, et al. Increased ER-mitochondrial coupling promotes mitochondrial respiration and bioenergetics during early phases of ER stress. J Cell Sci 2011; 124(Pt 13): 2143- 52.
    • (2011) J Cell Sci , vol.124 , pp. 2143-2152
    • Bravo, R.1    Vicencio, J.M.2    Parra, V.3
  • 102
    • 84870063016 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress impairs insulin signaling through mitochondrial damage in SH-SY5Y cells
    • Koo HJ, Piao Y, Pak YK. Endoplasmic reticulum stress impairs insulin signaling through mitochondrial damage in SH-SY5Y cells. Neurosignals 2012; 20(4): 265-80.
    • (2012) Neurosignals , vol.20 , Issue.4 , pp. 265-280
    • Koo, H.J.1    Piao, Y.2    Pak, Y.K.3
  • 103
    • 84939876537 scopus 로고    scopus 로고
    • Enhanced Amyloidogenic Processing of Amyloid Precursor Protein and Cell Death Under Prolonged Endoplasmic Reticulum Stress in Brain Endothelial Cells
    • in press
    • Placido AI, Oliveira CR, Moreira PI, Pereira CM. Enhanced Amyloidogenic Processing of Amyloid Precursor Protein and Cell Death Under Prolonged Endoplasmic Reticulum Stress in Brain Endothelial Cells. Mol Neurobiol. 2014; in press.
    • (2014) Mol Neurobiol
    • Placido, A.I.1    Oliveira, C.R.2    Moreira, P.I.3    Pereira, C.M.4
  • 104
    • 84883271527 scopus 로고    scopus 로고
    • Mfn2 modulates the UPR and mitochondrial function via repression of PERK
    • Munoz JP, Ivanova S, Sanchez-Wandelmer J, et al. Mfn2 modulates the UPR and mitochondrial function via repression of PERK. EMBO J 2013; 32(17): 2348-61.
    • (2013) EMBO J , vol.32 , Issue.17 , pp. 2348-2361
    • Munoz, J.P.1    Ivanova, S.2    Sanchez-Wandelmer, J.3
  • 105
    • 84861774361 scopus 로고    scopus 로고
    • Sensing endoplasmic reticulum stress by protein kinase RNA-like endoplasmic reticulum kinase promotes adaptive mitochondrial DNA biogenesis and cell survival via heme oxygenase-1/carbon monoxide activity
    • Zheng M, Kim SK, Joe Y, et al. Sensing endoplasmic reticulum stress by protein kinase RNA-like endoplasmic reticulum kinase promotes adaptive mitochondrial DNA biogenesis and cell survival via heme oxygenase-1/carbon monoxide activity. FASEB J 2012; 26(6): 2558-68.
    • (2012) FASEB J , vol.26 , Issue.6 , pp. 2558-2568
    • Zheng, M.1    Kim, S.K.2    Joe, Y.3
  • 106
    • 84870984470 scopus 로고    scopus 로고
    • PERK is required at the ERmitochondrial contact sites to convey apoptosis after ROS-based ER stress
    • Verfaillie T, Rubio N, Garg AD, et al. PERK is required at the ERmitochondrial contact sites to convey apoptosis after ROS-based ER stress. Cell Death Differ 2012; 19(11): 1880-91.
    • (2012) Cell Death Differ , vol.19 , Issue.11 , pp. 1880-1891
    • Verfaillie, T.1    Rubio, N.2    Garg, A.D.3
  • 107
    • 77950676470 scopus 로고    scopus 로고
    • The role of protein quality control in mitochondrial protein homeostasis under oxidative stress
    • Bender T, Leidhold C, Ruppert T, Franken S, Voos W. The role of protein quality control in mitochondrial protein homeostasis under oxidative stress. Proteomics 2010; 10(7): 1426-43.
    • (2010) Proteomics , vol.10 , Issue.7 , pp. 1426-1443
    • Bender, T.1    Leidhold, C.2    Ruppert, T.3    Franken, S.4    Voos, W.5
  • 108
    • 18444390287 scopus 로고    scopus 로고
    • Transmission of cell stress from endoplasmic reticulum to mitochondria: Enhanced expression of Lon protease
    • Hori O, Ichinoda F, Tamatani T, et al. Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease. J Cell Biol 2002; 157(7): 1151-60.
    • (2002) J Cell Biol , vol.157 , Issue.7 , pp. 1151-1160
    • Hori, O.1    Ichinoda, F.2    Tamatani, T.3
  • 109
    • 63049095076 scopus 로고    scopus 로고
    • Mitochondrial Lon protease is a human stress protein
    • Ngo JK, Davies KJ. Mitochondrial Lon protease is a human stress protein. Free Radic Biol Med 2009; 46(8): 1042-8.
    • (2009) Free Radic Biol Med , vol.46 , Issue.8 , pp. 1042-1048
    • Ngo, J.K.1    Davies, K.J.2
  • 110
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota DA, Davies KJ. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 2002; 4(9): 674-80.
    • (2002) Nat Cell Biol , vol.4 , Issue.9 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 111
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska A, Koehler CM, Milenkovic D, Lithgow T, Pfanner N. Importing mitochondrial proteins: machineries and mechanisms. Cell 2009; 138(4): 628-44.
    • (2009) Cell , vol.138 , Issue.4 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 112
    • 84858955705 scopus 로고    scopus 로고
    • Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system
    • Iosefson O, Sharon S, Goloubinoff P, Azem A. Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system. Cell Stress Chaperones 2012; 17(1): 57- 66.
    • (2012) Cell Stress Chaperones , vol.17 , Issue.1 , pp. 57-66
    • Iosefson, O.1    Sharon, S.2    Goloubinoff, P.3    Azem, A.4
  • 113
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: From proteomics to functional mechanisms
    • Schmidt O, Pfanner N, Meisinger C. Mitochondrial protein import: from proteomics to functional mechanisms. Nat Rev Mol Cell Biol 2010; 11(9): 655-67.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.9 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 115
    • 85048240730 scopus 로고    scopus 로고
    • The unfolded protein response is activated in disease-affected brain regions in progressive supranuclear palsy and Alzheimer's disease
    • Stutzbach LD, Xie SX, Naj AC, et al. The unfolded protein response is activated in disease-affected brain regions in progressive supranuclear palsy and Alzheimer's disease. Acta Neuropathol Commun 2013; 1(1): 31.
    • (2013) Acta Neuropathol Commun , vol.1 , Issue.1 , pp. 31
    • Stutzbach, L.D.1    Xie, S.X.2    Naj, A.C.3
  • 116
    • 24344489466 scopus 로고    scopus 로고
    • The unfolded protein response is activated in Alzheimer's disease
    • Hoozemans JJ, Veerhuis R, Van Haastert ES, et al. The unfolded protein response is activated in Alzheimer's disease. Acta Neuropathol 2005; 110(2): 165-72.
    • (2005) Acta Neuropathol , vol.110 , Issue.2 , pp. 165-172
    • Hoozemans, J.J.1    Veerhuis, R.2    Van Haastert, E.S.3
  • 117
    • 84875632050 scopus 로고    scopus 로고
    • Polymorphism-116C/G of Human X-box-Binding Protein 1 Promoter is Associated with Risk of Alzheimer's Disease
    • Sheng-Yuan Liu WW, Zhi-You Cai, Li-Fen Yao, Zhong-Wei Chen, Chang-Yi Wang, Bin Zhao, Ke-Shen Li. Polymorphism-116C/G of Human X-box-Binding Protein 1 Promoter is Associated with Risk of Alzheimer's Disease. CNS Neurosci Ther 2013; 19(4): 229-34.
    • (2013) CNS Neurosci Ther , vol.19 , Issue.4 , pp. 229-234
    • Sheng-Yuan Liu, W.W.1    Cai, Z.-Y.2    Yao, L.-F.3    Chen, Z.-W.4    Wang, C.-Y.5    Zhao, B.6    Li, K.-S.7
  • 118
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of amyloidbeta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • Resende R, Ferreiro E, Pereira C, Resende de Oliveira C. Neurotoxic effect of oligomeric and fibrillar species of amyloidbeta peptide 1-42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death. Neuroscience 2008; 155(3): 725-37.
    • (2008) Neuroscience , vol.155 , Issue.3 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Resende de Oliveira, C.4
  • 119
    • 84866452758 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress occurs downstream of GluN2B subunit of N-methyl-daspartate receptor in mature hippocampal cultures treated with amyloid-beta oligomers
    • Costa RO, Lacor PN, Ferreira IL, et al. Endoplasmic reticulum stress occurs downstream of GluN2B subunit of N-methyl-daspartate receptor in mature hippocampal cultures treated with amyloid-beta oligomers. Aging Cell 2012; 11(5): 823-33.
    • (2012) Aging Cell , vol.11 , Issue.5 , pp. 823-833
    • Costa, R.O.1    Lacor, P.N.2    Ferreira, I.L.3
  • 120
    • 0031982670 scopus 로고    scopus 로고
    • Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease
    • Mattson MP, Guo Q, Furukawa K, Pedersen WA. Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease. J Neurochem 1998; 70(1): 1-14.
    • (1998) J Neurochem , vol.70 , Issue.1 , pp. 1-14
    • Mattson, M.P.1    Guo, Q.2    Furukawa, K.3    Pedersen, W.A.4
  • 121
    • 84885165023 scopus 로고    scopus 로고
    • Suppression of amyloid-beta production by 24S-hydroxycholesterol via inhibition of intracellular amyloid precursor protein trafficking
    • Urano Y, Ochiai S, Noguchi N. Suppression of amyloid-beta production by 24S-hydroxycholesterol via inhibition of intracellular amyloid precursor protein trafficking. FASEB J 2013; 27(10): 4305-15.
    • (2013) FASEB J , vol.27 , Issue.10 , pp. 4305-4315
    • Urano, Y.1    Ochiai, S.2    Noguchi, N.3
  • 122
    • 33646101021 scopus 로고    scopus 로고
    • Altered localization of amyloid precursor protein under endoplasmic reticulum stress
    • Kudo T, Okumura M, Imaizumi K, et al. Altered localization of amyloid precursor protein under endoplasmic reticulum stress. Biochem Biophys Res Commun 2006; 344(2): 525-30.
    • (2006) Biochem Biophys Res Commun , vol.344 , Issue.2 , pp. 525-530
    • Kudo, T.1    Okumura, M.2    Imaizumi, K.3
  • 123
    • 67349098681 scopus 로고    scopus 로고
    • Low molecular weight Abeta induces collapse of endoplasmic reticulum
    • Lai CS, Preisler J, Baum L, et al. Low molecular weight Abeta induces collapse of endoplasmic reticulum. Mol Cell Neurosci 2009; 41(1): 32-43.
    • (2009) Mol Cell Neurosci , vol.41 , Issue.1 , pp. 32-43
    • Lai, C.S.1    Preisler, J.2    Baum, L.3
  • 124
    • 84903445250 scopus 로고    scopus 로고
    • Crosstalk between endoplasmic reticulum stress and protein misfolding in neurodegenerative diseases
    • Pereira C. Crosstalk between endoplasmic reticulum stress and protein misfolding in neurodegenerative diseases. ISRN Cell Biol 2013; 2013: 22.
    • (2013) ISRN Cell Biol , vol.2013 , pp. 22
    • Pereira, C.1
  • 125
    • 84863242250 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces tau pathology and forms a vicious cycle: Implication in Alzheimer's disease pathogenesis
    • Ho YS, Yang X, Lau JC, Hung CH, Wuwongse S, Zhang Q, et al. Endoplasmic reticulum stress induces tau pathology and forms a vicious cycle: implication in Alzheimer's disease pathogenesis. J Alzheimers Dis 2012; 28(4): 839-54.
    • (2012) J Alzheimers Dis , vol.28 , Issue.4 , pp. 839-854
    • Ho, Y.S.1    Yang, X.2    Lau, J.C.3    Hung, C.H.4    Wuwongse, S.5    Zhang, Q.6
  • 126
    • 59449087438 scopus 로고    scopus 로고
    • Neuroprotective effects of donepezil through inhibition of GSK-3 activity in amyloid-beta-induced neuronal cell death
    • Noh MY, Koh SH, Kim Y, Kim HY, Cho GW, Kim SH. Neuroprotective effects of donepezil through inhibition of GSK-3 activity in amyloid-beta-induced neuronal cell death. J Neurochem 2009; 108(5): 1116-25.
    • (2009) J Neurochem , vol.108 , Issue.5 , pp. 1116-1125
    • Noh, M.Y.1    Koh, S.H.2    Kim, Y.3    Kim, H.Y.4    Cho, G.W.5    Kim, S.H.6
  • 127
    • 84878333056 scopus 로고    scopus 로고
    • Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation
    • Abisambra JF, Jinwal UK, Blair LJ, et al. Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation. J Neurosci 2013; 33(22): 9498- 507.
    • (2013) J Neurosci , vol.33 , Issue.22 , pp. 9498-9507
    • Abisambra, J.F.1    Jinwal, U.K.2    Blair, L.J.3
  • 128
    • 79960672046 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca2+ handling in excitable cells in health and disease
    • Stutzmann GE, Mattson MP. Endoplasmic reticulum Ca2+ handling in excitable cells in health and disease. Pharmacol Rev 2011; 63(3): 700-27.
    • (2011) Pharmacol Rev , vol.63 , Issue.3 , pp. 700-727
    • Stutzmann, G.E.1    Mattson, M.P.2
  • 129
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny I, Mattson MP. Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci 2008; 31(9): 454-63.
    • (2008) Trends Neurosci , vol.31 , Issue.9 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 131
    • 38049162500 scopus 로고    scopus 로고
    • Involvement of mitochondria in endoplasmic reticulum stressinduced apoptotic cell death pathway triggered by the prion peptide PrP(106-126)
    • Ferreiro E, Costa R, Marques S, Cardoso SM, Oliveira CR, Pereira CM. Involvement of mitochondria in endoplasmic reticulum stressinduced apoptotic cell death pathway triggered by the prion peptide PrP(106-126). J Neurochem 2008; 104(3): 766-76.
    • (2008) J Neurochem , vol.104 , Issue.3 , pp. 766-776
    • Ferreiro, E.1    Costa, R.2    Marques, S.3    Cardoso, S.M.4    Oliveira, C.R.5    Pereira, C.M.6
  • 132
    • 57649245230 scopus 로고    scopus 로고
    • Phosphorylation of the translation initiation factor eIF2alpha increases BACE1 levels and promotes amyloidogenesis
    • O'Connor T, Sadleir KR, Maus E, et al. Phosphorylation of the translation initiation factor eIF2alpha increases BACE1 levels and promotes amyloidogenesis. Neuron 2008; 60(6): 988-1009.
    • (2008) Neuron , vol.60 , Issue.6 , pp. 988-1009
    • O'Connor, T.1    Sadleir, K.R.2    Maus, E.3
  • 133
    • 71749121998 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a trigger of Alzheimer's disease pathophysiology
    • Moreira PI, Carvalho C, Zhu X, Smith MA, Perry G. Mitochondrial dysfunction is a trigger of Alzheimer's disease pathophysiology. Biochim Biophys Acta 2010; 1802(1): 2-10.
    • (2010) Biochim Biophys Acta , vol.1802 , Issue.1 , pp. 2-10
    • Moreira, P.I.1    Carvalho, C.2    Zhu, X.3    Smith, M.A.4    Perry, G.5
  • 134
    • 84903304059 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in Alzheimer's disease
    • Wang X, Wang W, Li L, Perry G, Lee HG, Zhu X. Oxidative stress and mitochondrial dysfunction in Alzheimer's disease. Biochim Biophys Acta 2014; 1842(8): 1240-7.
    • (2014) Biochim Biophys Acta , vol.1842 , Issue.8 , pp. 1240-1247
    • Wang, X.1    Wang, W.2    Li, L.3    Perry, G.4    Lee, H.G.5    Zhu, X.6
  • 135
    • 73649098791 scopus 로고    scopus 로고
    • Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria
    • Area-Gomez E, de Groof AJ, Boldogh I, et al. Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria. Am J Pathol 2009; 175(5): 1810-6.
    • (2009) Am J Pathol , vol.175 , Issue.5 , pp. 1810-1816
    • Area-Gomez, E.1    de Groof, A.J.2    Boldogh, I.3
  • 136
    • 45249117227 scopus 로고    scopus 로고
    • Mechanism of Ca2+ disruption in Alzheimer's disease by presenilin regulation of InsP3 receptor channel gating
    • Cheung KH, Shineman D, Muller M, et al. Mechanism of Ca2+ disruption in Alzheimer's disease by presenilin regulation of InsP3 receptor channel gating. Neuron 2008; 58(6): 871-83.
    • (2008) Neuron , vol.58 , Issue.6 , pp. 871-883
    • Cheung, K.H.1    Shineman, D.2    Muller, M.3
  • 137
    • 33748140720 scopus 로고    scopus 로고
    • Presenilins form ER Ca2+ leak channels, a function disrupted by familial Alzheimer's diseaselinked mutations
    • Tu H, Nelson O, Bezprozvanny A, et al. Presenilins form ER Ca2+ leak channels, a function disrupted by familial Alzheimer's diseaselinked mutations. Cell 2006; 126(5): 981-93.
    • (2006) Cell , vol.126 , Issue.5 , pp. 981-993
    • Tu, H.1    Nelson, O.2    Bezprozvanny, A.3
  • 138
    • 84876117473 scopus 로고    scopus 로고
    • Calcium and endoplasmic reticulummitochondria tethering in neurodegeneration
    • Cali T, Ottolini D, Brini M. Calcium and endoplasmic reticulummitochondria tethering in neurodegeneration. DNA Cell Biol 2013; 32(4): 140-6.
    • (2013) DNA Cell Biol , vol.32 , Issue.4 , pp. 140-146
    • Cali, T.1    Ottolini, D.2    Brini, M.3
  • 139
    • 84859156397 scopus 로고    scopus 로고
    • Presenilin-2 modulation of ER-mitochondria interactions: FAD mutations, mechanisms and pathological consequences
    • Zampese E, Fasolato C, Pozzan T, Pizzo P. Presenilin-2 modulation of ER-mitochondria interactions: FAD mutations, mechanisms and pathological consequences. Commun Integr Biol 2011; 4(3): 357-60.
    • (2011) Commun Integr Biol , vol.4 , Issue.3 , pp. 357-360
    • Zampese, E.1    Fasolato, C.2    Pozzan, T.3    Pizzo, P.4
  • 140
    • 84866455663 scopus 로고    scopus 로고
    • Ca2+ dysregulation in neurons from transgenic mice expressing mutant presenilin 2
    • Kipanyula MJ, Contreras L, Zampese E, et al. Ca2+ dysregulation in neurons from transgenic mice expressing mutant presenilin 2. Aging Cell 2012; 11(5): 885-93.
    • (2012) Aging Cell , vol.11 , Issue.5 , pp. 885-893
    • Kipanyula, M.J.1    Contreras, L.2    Zampese, E.3
  • 142
    • 84893146602 scopus 로고    scopus 로고
    • Down-regulation of mortalin exacerbates Abeta-mediated mitochondrial fragmentation and dysfunction
    • Park SJ, Shin JH, Jeong JI, et al. Down-regulation of mortalin exacerbates Abeta-mediated mitochondrial fragmentation and dysfunction. J Biol Chem 2014; 289(4): 2195-204.
    • (2014) J Biol Chem , vol.289 , Issue.4 , pp. 2195-2204
    • Park, S.J.1    Shin, J.H.2    Jeong, J.I.3
  • 144
    • 4444237848 scopus 로고    scopus 로고
    • Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology
    • Conn KJ, Gao W, McKee A, et al. Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology. Brain Res 2004; 1022(1-2): 164-72.
    • (2004) Brain Res , vol.1022 , Issue.1-2 , pp. 164-172
    • Conn, K.J.1    Gao, W.2    McKee, A.3
  • 145
    • 70350043611 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (herp) is up-regulated in parkinsonian substantia nigra and present in the core of Lewy bodies
    • Slodzinski H, Moran LB, Michael GJ, et al. Homocysteine-induced endoplasmic reticulum protein (herp) is up-regulated in parkinsonian substantia nigra and present in the core of Lewy bodies. Clin Neuropathol 2009; 28(5): 333-43.
    • (2009) Clin Neuropathol , vol.28 , Issue.5 , pp. 333-343
    • Slodzinski, H.1    Moran, L.B.2    Michael, G.J.3
  • 146
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: A glimpse into the ER
    • Matus S, Glimcher LH, Hetz C. Protein folding stress in neurodegenerative diseases: a glimpse into the ER. Curr Opin Cell Biol 2011; 23(2): 239-52.
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.2 , pp. 239-252
    • Matus, S.1    Glimcher, L.H.2    Hetz, C.3
  • 147
    • 84899844505 scopus 로고    scopus 로고
    • Control of dopaminergic neuron survival by the unfolded protein response transcription factor XBP1
    • Valdes P, Mercado G, Vidal RL, et al. Control of dopaminergic neuron survival by the unfolded protein response transcription factor XBP1. Proc Natl Acad Sci USA 2014; 111(18): 6804-9.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.18 , pp. 6804-6809
    • Valdes, P.1    Mercado, G.2    Vidal, R.L.3
  • 148
    • 79551647443 scopus 로고    scopus 로고
    • Induction of the unfolded protein response by alpha-synuclein in experimental models of Parkinson's disease
    • Bellucci A, Navarria L, Zaltieri M, et al. Induction of the unfolded protein response by alpha-synuclein in experimental models of Parkinson's disease. J Neurochem 2011; 116(4): 588-605.
    • (2011) J Neurochem , vol.116 , Issue.4 , pp. 588-605
    • Bellucci, A.1    Navarria, L.2    Zaltieri, M.3
  • 149
    • 84875259777 scopus 로고    scopus 로고
    • An ERcentric view of Parkinson's disease
    • Mercado G, Valdes P, Hetz C. An ERcentric view of Parkinson's disease. Trends Mol Med 2013; 19(3): 165-75.
    • (2013) Trends Mol Med , vol.19 , Issue.3 , pp. 165-175
    • Mercado, G.1    Valdes, P.2    Hetz, C.3
  • 150
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz WA, O'Malley KL. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 2003; 278(21): 19367-77.
    • (2003) J Biol Chem , vol.278 , Issue.21 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 151
    • 84863230467 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is important for the manifestations of alpha-synucleinopathy in vivo
    • Colla E, Coune P, Liu Y, et al. Endoplasmic reticulum stress is important for the manifestations of alpha-synucleinopathy in vivo. J Neurosci 2012; 32(10): 3306-20.
    • (2012) J Neurosci , vol.32 , Issue.10 , pp. 3306-3320
    • Colla, E.1    Coune, P.2    Liu, Y.3
  • 152
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo
    • Colla E, Jensen PH, Pletnikova O, Troncoso JC, Glabe C, Lee MK. Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo. J Neurosci 2012; 32(10): 3301-5.
    • (2012) J Neurosci , vol.32 , Issue.10 , pp. 3301-3305
    • Colla, E.1    Jensen, P.H.2    Pletnikova, O.3    Troncoso, J.C.4    Glabe, C.5    Lee, M.K.6
  • 153
    • 33746533924 scopus 로고    scopus 로고
    • Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models
    • Cooper AA, Gitler AD, Cashikar A, et al. Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 2006; 313(5785): 324-8.
    • (2006) Science , vol.313 , Issue.5785 , pp. 324-328
    • Cooper, A.A.1    Gitler, A.D.2    Cashikar, A.3
  • 154
    • 77949438990 scopus 로고    scopus 로고
    • Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models
    • Su LJ, Auluck PK, Outeiro TF, et al. Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models. Dis Model Mech 2010; 3(3-4): 194-208.
    • (2010) Dis Model Mech , vol.3 , Issue.3-4 , pp. 194-208
    • Su, L.J.1    Auluck, P.K.2    Outeiro, T.F.3
  • 155
    • 77952900626 scopus 로고    scopus 로고
    • Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi N, Helm JR, Nycz DC, Bentley M, Liang Y, Hay JC. Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol Biol Cell 2010; 21(11): 1850-63.
    • (2010) Mol Biol Cell , vol.21 , Issue.11 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 157
    • 84856954609 scopus 로고    scopus 로고
    • The homocysteineinducible endoplasmic reticulum (ER) stress protein Herp counteracts mutant alpha-synuclein-induced ER stress via the homeostatic regulation of ER-resident calcium release channel proteins
    • Belal C, Ameli NJ, El Kommos A, et al. The homocysteineinducible endoplasmic reticulum (ER) stress protein Herp counteracts mutant alpha-synuclein-induced ER stress via the homeostatic regulation of ER-resident calcium release channel proteins. Hum Mol Genet 2012; 21(5): 963-77.
    • (2012) Hum Mol Genet , vol.21 , Issue.5 , pp. 963-977
    • Belal, C.1    Ameli, N.J.2    El Kommos, A.3
  • 158
    • 84859717205 scopus 로고    scopus 로고
    • Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling
    • Selvaraj S, Sun Y, Watt JA, et al. Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling. J Clin Invest 2012; 122(4): 1354-67.
    • (2012) J Clin Invest , vol.122 , Issue.4 , pp. 1354-1367
    • Selvaraj, S.1    Sun, Y.2    Watt, J.A.3
  • 159
    • 77957283003 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 is associated with the endoplasmic reticulum in dopaminergic neurons and accumulates in the core of Lewy bodies in Parkinson disease
    • Vitte J, Traver S, Maues De Paula A, et al. Leucine-rich repeat kinase 2 is associated with the endoplasmic reticulum in dopaminergic neurons and accumulates in the core of Lewy bodies in Parkinson disease. J Neuropathol Exp Neurol 2010; 69(9): 959- 72.
    • (2010) J Neuropathol Exp Neurol , vol.69 , Issue.9 , pp. 959-972
    • Vitte, J.1    Traver, S.2    Maues De Paula, A.3
  • 160
    • 79961078072 scopus 로고    scopus 로고
    • Dysregulated LRRK2 signaling in response to endoplasmic reticulum stress leads to dopaminergic neuron degeneration in C. elegans
    • Yuan Y, Cao P, Smith MA, et al. Dysregulated LRRK2 signaling in response to endoplasmic reticulum stress leads to dopaminergic neuron degeneration in C. elegans. PLoS One 2011; 6(8): e22354.
    • (2011) PLoS One , vol.6 , Issue.8
    • Yuan, Y.1    Cao, P.2    Smith, M.A.3
  • 161
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai YC, Fishman PS, Thakor NV, Oyler GA. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J Biol Chem 2003; 278(24): 22044-55.
    • (2003) J Biol Chem , vol.278 , Issue.24 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 162
    • 84886581781 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in neurodegeneration: A new approach to therapy
    • Halliday M, Mallucci GR. Targeting the unfolded protein response in neurodegeneration: A new approach to therapy. Neuropharmacology 2014; 76 Pt A: 169-74.
    • (2014) Neuropharmacology , vol.76 , pp. 169-174
    • Halliday, M.1    Mallucci, G.R.2
  • 163
    • 84876098997 scopus 로고    scopus 로고
    • The Parkinson diseaserelated protein DJ-1 counteracts mitochondrial impairment induced by the tumour suppressor protein p53 by enhancing endoplasmic reticulum-mitochondria tethering
    • Ottolini D, Cali T, Negro A, Brini M. The Parkinson diseaserelated protein DJ-1 counteracts mitochondrial impairment induced by the tumour suppressor protein p53 by enhancing endoplasmic reticulum-mitochondria tethering. Hum Mol Genet 2013; 22(11): 2152-68.
    • (2013) Hum Mol Genet , vol.22 , Issue.11 , pp. 2152-2168
    • Ottolini, D.1    Cali, T.2    Negro, A.3    Brini, M.4
  • 164
    • 25444514752 scopus 로고    scopus 로고
    • Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress
    • Li HM, Niki T, Taira T, Iguchi-Ariga SM, Ariga H. Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress. Free Radic Res 2005; 39(10): 1091-9.
    • (2005) Free Radic Res , vol.39 , Issue.10 , pp. 1091-1099
    • Li, H.M.1    Niki, T.2    Taira, T.3    Iguchi-Ariga, S.M.4    Ariga, H.5
  • 165
    • 34249704608 scopus 로고    scopus 로고
    • Identification of novel proteins associated with both alpha-synuclein and DJ-1
    • Jin J, Li GJ, Davis J, et al. Identification of novel proteins associated with both alpha-synuclein and DJ-1. Mol Cell Proteomics 2007; 6(5): 845-59.
    • (2007) Mol Cell Proteomics , vol.6 , Issue.5 , pp. 845-859
    • Jin, J.1    Li, G.J.2    Davis, J.3
  • 166
    • 84861554724 scopus 로고    scopus 로고
    • alpha-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions
    • Cali T, Ottolini D, Negro A, Brini M. alpha-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions. J Biol Chem 2012; 287(22): 17914-29.
    • (2012) J Biol Chem , vol.287 , Issue.22 , pp. 17914-17929
    • Cali, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 167
    • 84891410019 scopus 로고    scopus 로고
    • alpha-Synuclein is localized to mitochondria-associated ER membranes
    • Guardia-Laguarta C, Area-Gomez E, Rub C, et al. alpha-Synuclein is localized to mitochondria-associated ER membranes. J Neurosci 2014; 34(1): 249-59.
    • (2014) J Neurosci , vol.34 , Issue.1 , pp. 249-259
    • Guardia-Laguarta, C.1    Area-Gomez, E.2    Rub, C.3
  • 168
    • 84873254580 scopus 로고    scopus 로고
    • Enhanced parkin levels favor ER-mitochondria crosstalk and guarantee Ca2+ transfer to sustain cell bioenergetics
    • Cali T, Ottolini D, Negro A, Brini M. Enhanced parkin levels favor ER-mitochondria crosstalk and guarantee Ca2+ transfer to sustain cell bioenergetics. Biochim Biophys Acta 2013; 1832(4): 495-508.
    • (2013) Biochim Biophys Acta , vol.1832 , Issue.4 , pp. 495-508
    • Cali, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 169
    • 27744483960 scopus 로고    scopus 로고
    • siRNA-mediated inhibition of endogenous Huntington disease gene expression induces an aberrant configuration of the ER network in vitro
    • Omi K, Hachiya NS, Tokunaga K, Kaneko K. siRNA-mediated inhibition of endogenous Huntington disease gene expression induces an aberrant configuration of the ER network in vitro. Biochem Biophys Res Commun 2005; 338(2): 1229-35.
    • (2005) Biochem Biophys Res Commun , vol.338 , Issue.2 , pp. 1229-1235
    • Omi, K.1    Hachiya, N.S.2    Tokunaga, K.3    Kaneko, K.4
  • 170
    • 67650566385 scopus 로고    scopus 로고
    • Rrs1 is involved in endoplasmic reticulum stress response in Huntington disease
    • Carnemolla A, Fossale E, Agostoni E, et al. Rrs1 is involved in endoplasmic reticulum stress response in Huntington disease. J Biol Chem 2009; 284(27): 18167-73.
    • (2009) J Biol Chem , vol.284 , Issue.27 , pp. 18167-18173
    • Carnemolla, A.1    Fossale, E.2    Agostoni, E.3
  • 171
    • 78650827764 scopus 로고    scopus 로고
    • Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease
    • Vidal R, Caballero B, Couve A, Hetz C. Converging pathways in the occurrence of endoplasmic reticulum (ER) stress in Huntington's disease. Curr Mol Med 2011; 11(1): 1-12.
    • (2011) Curr Mol Med , vol.11 , Issue.1 , pp. 1-12
    • Vidal, R.1    Caballero, B.2    Couve, A.3    Hetz, C.4
  • 172
    • 38049053467 scopus 로고    scopus 로고
    • A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy
    • Atwal RS, Truant R. A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy 2008; 4(1): 91-3.
    • (2008) Autophagy , vol.4 , Issue.1 , pp. 91-93
    • Atwal, R.S.1    Truant, R.2
  • 173
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
    • Atwal RS, Xia J, Pinchev D, Taylor J, Epand RM, Truant R. Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum Mol Genet 2007; 16(21): 2600-15.
    • (2007) Hum Mol Genet , vol.16 , Issue.21 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3    Taylor, J.4    Epand, R.M.5    Truant, R.6
  • 174
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • Panov AV, Gutekunst CA, Leavitt BR, et al. Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat Neurosci 2002; 5(8): 731-6.
    • (2002) Nat Neurosci , vol.5 , Issue.8 , pp. 731-736
    • Panov, A.V.1    Gutekunst, C.A.2    Leavitt, B.R.3
  • 175
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald ML, Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev 2008; 22(23): 3308-19.
    • (2008) Genes Dev , vol.22 , Issue.23 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 176
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang H, Liu C, Zhong Y, Luo S, Monteiro MJ, Fang S. Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS One 2010; 5(1): e8905.
    • (2010) PLoS One , vol.5 , Issue.1
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 177
    • 78649954745 scopus 로고    scopus 로고
    • Mechanism of ER stressinduced brain damage by IP(3) receptor
    • Higo T, Hamada K, Hisatsune C, et al. Mechanism of ER stressinduced brain damage by IP(3) receptor. Neuron 2010; 68(5): 865- 78.
    • (2010) Neuron , vol.68 , Issue.5 , pp. 865-878
    • Higo, T.1    Hamada, K.2    Hisatsune, C.3
  • 178
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • Atkin JD, Farg MA, Walker AK, McLean C, Tomas D, Horne MK. Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol Dis 2008; 30(3): 400-7.
    • (2008) Neurobiol Dis , vol.30 , Issue.3 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5    Horne, M.K.6
  • 179
    • 77950853379 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis
    • Sasaki S. Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 2010; 69(4): 346-55.
    • (2010) J Neuropathol Exp Neurol , vol.69 , Issue.4 , pp. 346-355
    • Sasaki, S.1
  • 180
    • 33749563294 scopus 로고    scopus 로고
    • Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1
    • Atkin JD, Farg MA, Turner BJ, et al. Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J Biol Chem 2006; 281(40): 30152-65.
    • (2006) J Biol Chem , vol.281 , Issue.40 , pp. 30152-30165
    • Atkin, J.D.1    Farg, M.A.2    Turner, B.J.3
  • 181
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtypeselective ER stress in disease manifestations of FALS mice
    • Saxena S, Cabuy E, Caroni P. A role for motoneuron subtypeselective ER stress in disease manifestations of FALS mice. Nat Neurosci 2009; 12(5): 627-36.
    • (2009) Nat Neurosci , vol.12 , Issue.5 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 182
    • 33646176558 scopus 로고    scopus 로고
    • ER stress and UPR in familial amyotrophic lateral sclerosis
    • Turner BJ, Atkin JD. ER stress and UPR in familial amyotrophic lateral sclerosis. Curr Mol Med 2006; 6(1): 79-86.
    • (2006) Curr Mol Med , vol.6 , Issue.1 , pp. 79-86
    • Turner, B.J.1    Atkin, J.D.2
  • 183
    • 0346034856 scopus 로고    scopus 로고
    • Mutant SOD1 linked to familial amyotrophic lateral sclerosis, but not wild-type SOD1, induces ER stress in COS7 cells and transgenic mice
    • Tobisawa S, Hozumi Y, Arawaka S, et al. Mutant SOD1 linked to familial amyotrophic lateral sclerosis, but not wild-type SOD1, induces ER stress in COS7 cells and transgenic mice. Biochem Biophys Res Commun 2003; 303(2): 496-503.
    • (2003) Biochem Biophys Res Commun , vol.303 , Issue.2 , pp. 496-503
    • Tobisawa, S.1    Hozumi, Y.2    Arawaka, S.3
  • 184
    • 12144249923 scopus 로고    scopus 로고
    • Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis
    • Turner BJ, Atkin JD, Farg MA, et al. Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J Neurosci 2005; 25(1): 108-17.
    • (2005) J Neurosci , vol.25 , Issue.1 , pp. 108-117
    • Turner, B.J.1    Atkin, J.D.2    Farg, M.A.3
  • 185
    • 46749107070 scopus 로고    scopus 로고
    • The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS
    • Urushitani M, Ezzi SA, Matsuo A, Tooyama I, Julien JP. The endoplasmic reticulum-Golgi pathway is a target for translocation and aggregation of mutant superoxide dismutase linked to ALS. FASEB J 2008; 22(7): 2476-87.
    • (2008) FASEB J , vol.22 , Issue.7 , pp. 2476-2487
    • Urushitani, M.1    Ezzi, S.A.2    Matsuo, A.3    Tooyama, I.4    Julien, J.P.5
  • 186
    • 80052081196 scopus 로고    scopus 로고
    • Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis
    • Walker AK, Atkin JD. Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis. IUBMB Life 2011; 63(9): 754-63.
    • (2011) IUBMB Life , vol.63 , Issue.9 , pp. 754-763
    • Walker, A.K.1    Atkin, J.D.2
  • 187
    • 44849124411 scopus 로고    scopus 로고
    • ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1
    • Nishitoh H, Kadowaki H, Nagai A, et al. ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1. Genes Dev 2008; 22(11): 1451-64.
    • (2008) Genes Dev , vol.22 , Issue.11 , pp. 1451-1464
    • Nishitoh, H.1    Kadowaki, H.2    Nagai, A.3
  • 188
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 2004; 429(6994): 841-7.
    • (2004) Nature , vol.429 , Issue.6994 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 189
    • 84923189622 scopus 로고    scopus 로고
    • Marinesco-Sjogren syndrome protein SIL1 regulates motor neuron subtype-selective ER stress in ALS
    • Filezac de L'Etang A, Maharjan N, Cordeiro Brana M, et al. Marinesco-Sjogren syndrome protein SIL1 regulates motor neuron subtype-selective ER stress in ALS. Nat Neurosci 2015; 18(2): 227-38.
    • (2015) Nat Neurosci , vol.18 , Issue.2 , pp. 227-238
    • Filezac de L'Etang, A.1    Maharjan, N.2    Cordeiro Brana, M.3
  • 190
    • 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(20): 5435-45.
    • (2003) EMBO J , vol.22 , Issue.20 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 191
    • 0037121618 scopus 로고    scopus 로고
    • Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease
    • Yoo BC, Krapfenbauer K, Cairns N, Belay G, Bajo M, Lubec G. Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease. Neurosci Lett 2002; 334(3): 196-200.
    • (2002) Neurosci Lett , vol.334 , Issue.3 , pp. 196-200
    • Yoo, B.C.1    Krapfenbauer, K.2    Cairns, N.3    Belay, G.4    Bajo, M.5    Lubec, G.6
  • 192
    • 56349096340 scopus 로고    scopus 로고
    • Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model
    • Dossena S, Imeri L, Mangieri M, et al. Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model. Neuron 2008; 60(4): 598- 609.
    • (2008) Neuron , vol.60 , Issue.4 , pp. 598-609
    • Dossena, S.1    Imeri, L.2    Mangieri, M.3
  • 193
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres M, Castillo K, Armisen R, Stutzin A, Soto C, Hetz C. Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS One 2010; 5(12): e15658.
    • (2010) PLoS One , vol.5 , Issue.12
    • Torres, M.1    Castillo, K.2    Armisen, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 194
    • 2642541799 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum Ca2+ release through ryanodine and inositol 1,4,5- triphosphate receptors in the neurotoxic effects induced by the amyloid-beta peptide
    • Ferreiro E, Oliveira CR, Pereira C. Involvement of endoplasmic reticulum Ca2+ release through ryanodine and inositol 1,4,5- triphosphate receptors in the neurotoxic effects induced by the amyloid-beta peptide. J Neurosci Res 2004; 76(6): 872-80.
    • (2004) J Neurosci Res , vol.76 , Issue.6 , pp. 872-880
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.3
  • 195
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • Ferreiro E, Resende R, Costa R, Oliveira CR, Pereira CM. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol Dis 2006; 23(3): 669-78.
    • (2006) Neurobiol Dis , vol.23 , Issue.3 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.M.5
  • 196
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • Orsi A, Fioriti L, Chiesa R, Sitia R. Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. J Biol Chem 2006; 281(41): 30431-8.
    • (2006) J Biol Chem , vol.281 , Issue.41 , pp. 30431-30438
    • Orsi, A.1    Fioriti, L.2    Chiesa, R.3    Sitia, R.4
  • 197
    • 79551507564 scopus 로고    scopus 로고
    • Familial CJD associated PrP mutants within transmembrane region induced Ctm-PrP retention in ER and triggered apoptosis by ER stress in SH-SY5Y cells
    • Wang X, Shi Q, Xu K, et al. Familial CJD associated PrP mutants within transmembrane region induced Ctm-PrP retention in ER and triggered apoptosis by ER stress in SH-SY5Y cells. PLoS One 2011; 6(1): e14602.
    • (2011) PLoS One , vol.6 , Issue.1
    • Wang, X.1    Shi, Q.2    Xu, K.3
  • 198
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz C, Chevet E, Harding HP. Targeting the unfolded protein response in disease. Nat Rev Drug Discov 2013; 12(9): 703-19.
    • (2013) Nat Rev Drug Discov , vol.12 , Issue.9 , pp. 703-719
    • Hetz, C.1    Chevet, E.2    Harding, H.P.3
  • 199
    • 84858332177 scopus 로고    scopus 로고
    • Salubrinal attenuates beta-amyloid-induced neuronal death and microglial activation by inhibition of the NF-kappaB pathway
    • Huang X, Chen Y, Zhang H, Ma Q, Zhang YW, Xu H. Salubrinal attenuates beta-amyloid-induced neuronal death and microglial activation by inhibition of the NF-kappaB pathway. Neurobiol Aging 2012; 33(5): 1007 e9-17.
    • (2012) Neurobiol Aging , vol.33 , Issue.5 , pp. 9-17
    • Huang, X.1    Chen, Y.2    Zhang, H.3    Ma, Q.4    Zhang, Y.W.5    Xu, H.6
  • 200
    • 84879368095 scopus 로고    scopus 로고
    • Restoring endoplasmic reticulum homeostasis improves functional recovery after spinal cord injury
    • Ohri SS, Hetman M, Whittemore SR. Restoring endoplasmic reticulum homeostasis improves functional recovery after spinal cord injury. Neurobiol Dis 2013; 58: 29-37.
    • (2013) Neurobiol Dis , vol.58 , pp. 29-37
    • Ohri, S.S.1    Hetman, M.2    Whittemore, S.R.3
  • 201
    • 33846577831 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress inhibition protects against excitotoxic neuronal injury in the rat brain
    • Sokka AL, Putkonen N, Mudo G, et al. Endoplasmic reticulum stress inhibition protects against excitotoxic neuronal injury in the rat brain. J Neurosci 2007; 27(4): 901-8.
    • (2007) J Neurosci , vol.27 , Issue.4 , pp. 901-908
    • Sokka, A.L.1    Putkonen, N.2    Mudo, G.3
  • 202
    • 84861450392 scopus 로고    scopus 로고
    • Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration
    • Moreno JA, Radford H, Peretti D, et al. Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration. Nature 2012; 485(7399): 507-11.
    • (2012) Nature , vol.485 , Issue.7399 , pp. 507-511
    • Moreno, J.A.1    Radford, H.2    Peretti, D.3
  • 203
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler P, Harding HP, Ron D, Bertolotti A. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 2011; 332(6025): 91-4.
    • (2011) Science , vol.332 , Issue.6025 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 204
    • 84885463900 scopus 로고    scopus 로고
    • Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice
    • Moreno JA, Halliday M, Molloy C, et al. Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice. Sci Transl Med 2013; 5(206): 206ra138.
    • (2013) Sci Transl Med , vol.5 , Issue.206
    • Moreno, J.A.1    Halliday, M.2    Molloy, C.3
  • 205
    • 84881530677 scopus 로고    scopus 로고
    • Pharmacological brake-release of mRNA translation enhances cognitive memory
    • Sidrauski C, Acosta-Alvear D, Khoutorsky A, et al. Pharmacological brake-release of mRNA translation enhances cognitive memory. Elife 2013; 2: e00498.
    • (2013) Elife , vol.2
    • Sidrauski, C.1    Acosta-Alvear, D.2    Khoutorsky, A.3
  • 206
    • 84895811770 scopus 로고    scopus 로고
    • Memory loss in Alzheimer's disease: Are the alterations in the UPR network involved in the cognitive impairment?
    • Duran-Aniotz C, Martinez G, Hetz C. Memory loss in Alzheimer's disease: are the alterations in the UPR network involved in the cognitive impairment? Front Aging Neurosci 2014; 6: 8.
    • (2014) Front Aging Neurosci , vol.6 , pp. 8
    • Duran-Aniotz, C.1    Martinez, G.2    Hetz, C.3
  • 207
    • 79952283168 scopus 로고    scopus 로고
    • Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response
    • Ali MM, Bagratuni T, Davenport EL, et al. Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response. EMBO J 2011; 30(5): 894-905.
    • (2011) EMBO J , vol.30 , Issue.5 , pp. 894-905
    • Ali, M.M.1    Bagratuni, T.2    Davenport, E.L.3
  • 208
    • 80052668828 scopus 로고    scopus 로고
    • Peptides derived from the bifunctional kinase/RNase enzyme IRE1alpha modulate IRE1alpha activity and protect cells from endoplasmic reticulum stress
    • Bouchecareilh M, Higa A, Fribourg S, Moenner M, Chevet E. Peptides derived from the bifunctional kinase/RNase enzyme IRE1alpha modulate IRE1alpha activity and protect cells from endoplasmic reticulum stress. FASEB J 2011; 25(9): 3115-29.
    • (2011) FASEB J , vol.25 , Issue.9 , pp. 3115-3129
    • Bouchecareilh, M.1    Higa, A.2    Fribourg, S.3    Moenner, M.4    Chevet, E.5
  • 209
    • 68049110633 scopus 로고    scopus 로고
    • IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • Han D, Lerner AG, Vande Walle L, et al. IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 2009; 138(3): 562-75.
    • (2009) Cell , vol.138 , Issue.3 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande Walle, L.3
  • 210
    • 78349265743 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress as a therapeutic target in cardiovascular disease
    • Minamino T, Komuro I, Kitakaze M. Endoplasmic reticulum stress as a therapeutic target in cardiovascular disease. Circ Res 2010; 107(9): 1071-82.
    • (2010) Circ Res , vol.107 , Issue.9 , pp. 1071-1082
    • Minamino, T.1    Komuro, I.2    Kitakaze, M.3
  • 211
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie prion protein
    • Tatzelt J, Prusiner SB, Welch WJ. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J 1996; 15(23): 6363-73.
    • (1996) EMBO J , vol.15 , Issue.23 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 212
    • 78650191883 scopus 로고    scopus 로고
    • Sodium 4- phenylbutyrate protects against spinal cord ischemia by inhibition of endoplasmic reticulum stress
    • Mizukami T, Orihashi K, Herlambang B, et al. Sodium 4- phenylbutyrate protects against spinal cord ischemia by inhibition of endoplasmic reticulum stress. J Vasc Surg 2010; 52(6): 1580-6.
    • (2010) J Vasc Surg , vol.52 , Issue.6 , pp. 1580-1586
    • Mizukami, T.1    Orihashi, K.2    Herlambang, B.3
  • 213
    • 84908334942 scopus 로고    scopus 로고
    • Neuroprotective effect of the chemical chaperone, trehalose in a chronic MPTP-induced Parkinson's disease mouse model
    • Sarkar S, Chigurupati S, Raymick J, et al. Neuroprotective effect of the chemical chaperone, trehalose in a chronic MPTP-induced Parkinson's disease mouse model. Neurotoxicology 2014; 44: 250- 62.
    • (2014) Neurotoxicology , vol.44 , pp. 250-262
    • Sarkar, S.1    Chigurupati, S.2    Raymick, J.3
  • 214
    • 34249814605 scopus 로고    scopus 로고
    • Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone
    • Inden M, Kitamura Y, Takeuchi H, et al. Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone. J Neurochem 2007; 101(6): 1491-504.
    • (2007) J Neurochem , vol.101 , Issue.6 , pp. 1491-1504
    • Inden, M.1    Kitamura, Y.2    Takeuchi, H.3
  • 215
    • 84868089556 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid prevents MPTP-induced dopaminergic cell death in a mouse model of Parkinson's disease
    • Castro-Caldas M, Carvalho AN, Rodrigues E, et al. Tauroursodeoxycholic acid prevents MPTP-induced dopaminergic cell death in a mouse model of Parkinson's disease. Mol Neurobiol 2012; 46(2): 475-86.
    • (2012) Mol Neurobiol , vol.46 , Issue.2 , pp. 475-486
    • Castro-Caldas, M.1    Carvalho, A.N.2    Rodrigues, E.3
  • 216
    • 70350150325 scopus 로고    scopus 로고
    • A chemical chaperone, sodium 4-phenylbutyric acid, attenuates the pathogenic potency in human alpha-synuclein A30P + A53T transgenic mice
    • Ono K, Ikemoto M, Kawarabayashi T, et al. A chemical chaperone, sodium 4-phenylbutyric acid, attenuates the pathogenic potency in human alpha-synuclein A30P + A53T transgenic mice. Parkinson Relat Disord 2009; 15(9): 649-54.
    • (2009) Parkinson Relat Disord , vol.15 , Issue.9 , pp. 649-654
    • Ono, K.1    Ikemoto, M.2    Kawarabayashi, T.3
  • 217
    • 84867485621 scopus 로고    scopus 로고
    • TUDCA, a bile acid, attenuates amyloid precursor protein processing and amyloid-beta deposition in APP/PS1 mice
    • Nunes AF, Amaral JD, Lo AC, et al. TUDCA, a bile acid, attenuates amyloid precursor protein processing and amyloid-beta deposition in APP/PS1 mice. Mol Neurobiol 2012; 45(3): 440-54.
    • (2012) Mol Neurobiol , vol.45 , Issue.3 , pp. 440-454
    • Nunes, A.F.1    Amaral, J.D.2    Lo, A.C.3
  • 218
    • 84867741036 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid (TUDCA) supplementation prevents cognitive impairment and amyloid deposition in APP/PS1 mice
    • Lo AC, Callaerts-Vegh Z, Nunes AF, Rodrigues CM, D'Hooge R. Tauroursodeoxycholic acid (TUDCA) supplementation prevents cognitive impairment and amyloid deposition in APP/PS1 mice. Neurobiol Dis 2013; 50: 21-9.
    • (2013) Neurobiol Dis , vol.50 , pp. 21-29
    • Lo, A.C.1    Callaerts-Vegh, Z.2    Nunes, A.F.3    Rodrigues, C.M.4    D'Hooge, R.5
  • 219
    • 84869091863 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid suppresses amyloid beta-induced synaptic toxicity in vitro and in APP/PS1 mice
    • Ramalho RM, Nunes AF, Dias RB, et al. Tauroursodeoxycholic acid suppresses amyloid beta-induced synaptic toxicity in vitro and in APP/PS1 mice. Neurobiol Aging 2013; 34(2): 551-61.
    • (2013) Neurobiol Aging , vol.34 , Issue.2 , pp. 551-561
    • Ramalho, R.M.1    Nunes, A.F.2    Dias, R.B.3
  • 221
    • 77952881391 scopus 로고    scopus 로고
    • Phenylbutyric acid prevents rats from electroconvulsion-induced memory deficit with alterations of memory-related proteins and tau hyperphosphorylation
    • Yao Z, Guo Z, Yang C, et al. Phenylbutyric acid prevents rats from electroconvulsion-induced memory deficit with alterations of memory-related proteins and tau hyperphosphorylation. Neuroscience 2010; 168(2): 405-15.
    • (2010) Neuroscience , vol.168 , Issue.2 , pp. 405-415
    • Yao, Z.1    Guo, Z.2    Yang, C.3
  • 222
    • 0036677435 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease
    • Keene CD, Rodrigues CM, Eich T, Chhabra MS, Steer CJ, Low WC. Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease. Proc Natl Acad Sci USA 2002; 99(16): 10671-6.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.16 , pp. 10671-10676
    • Keene, C.D.1    Rodrigues, C.M.2    Eich, T.3    Chhabra, M.S.4    Steer, C.J.5    Low, W.C.6
  • 223
    • 78149339310 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis pathogenesis: A journey through the secretory pathway
    • Nassif M, Matus S, Castillo K, Hetz C. Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway. Antioxid Redox Signal 2010; 13(12): 1955-89.
    • (2010) Antioxid Redox Signal , vol.13 , Issue.12 , pp. 1955-1989
    • Nassif, M.1    Matus, S.2    Castillo, K.3    Hetz, C.4
  • 224
    • 34249092704 scopus 로고    scopus 로고
    • Calcium and neurodegeneration
    • Mattson MP. Calcium and neurodegeneration. Aging Cell 2007; 6(3): 337-50.
    • (2007) Aging Cell , vol.6 , Issue.3 , pp. 337-350
    • Mattson, M.P.1
  • 225
    • 0036071866 scopus 로고    scopus 로고
    • A calcium channel blocker nicardipine protects neurons from zinc-induced toxicity in rat hippocampus
    • Demir S, Bagirici F, Marangoz C. A calcium channel blocker nicardipine protects neurons from zinc-induced toxicity in rat hippocampus. Neurosci Res Commun 2002; 30(3): 7.
    • (2002) Neurosci Res Commun , vol.30 , Issue.3 , pp. 7
    • Demir, S.1    Bagirici, F.2    Marangoz, C.3
  • 226
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
    • Sarkar S, Perlstein EO, Imarisio S, et al. Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat Chem Biol 2007; 3(6): 331-8.
    • (2007) Nat Chem Biol , vol.3 , Issue.6 , pp. 331-338
    • Sarkar, S.1    Perlstein, E.O.2    Imarisio, S.3
  • 227
    • 84868021206 scopus 로고    scopus 로고
    • Sigma-1R agonist improves motor function and motoneuron survival in ALS mice
    • Mancuso R, Olivan S, Rando A, Casas C, Osta R, Navarro X. Sigma-1R agonist improves motor function and motoneuron survival in ALS mice. Neurotherapeutics 2012; 9(4): 814-26.
    • (2012) Neurotherapeutics , vol.9 , Issue.4 , pp. 814-826
    • Mancuso, R.1    Olivan, S.2    Rando, A.3    Casas, C.4    Osta, R.5    Navarro, X.6
  • 228
    • 84886816838 scopus 로고    scopus 로고
    • Neuroprotective effects of the Sigma-1 receptor (S1R) agonist PRE-084, in a mouse model of motor neuron disease not linked to SOD1 mutation
    • Peviani M, Salvaneschi E, Bontempi L, et al. Neuroprotective effects of the Sigma-1 receptor (S1R) agonist PRE-084, in a mouse model of motor neuron disease not linked to SOD1 mutation. Neurobiol Dis 2014; 62: 218-32.
    • (2014) Neurobiol Dis , vol.62 , pp. 218-232
    • Peviani, M.1    Salvaneschi, E.2    Bontempi, L.3
  • 229
    • 84890919596 scopus 로고    scopus 로고
    • SA4503, a sigma-1 receptor agonist, suppresses motor neuron damage in in vitro and in vivo amyotrophic lateral sclerosis models
    • Ono Y, Tanaka H, Takata M, et al. SA4503, a sigma-1 receptor agonist, suppresses motor neuron damage in in vitro and in vivo amyotrophic lateral sclerosis models. Neurosci Lett 2014; 559: 174-8.
    • (2014) Neurosci Lett , vol.559 , pp. 174-178
    • Ono, Y.1    Tanaka, H.2    Takata, M.3
  • 230
    • 84883313329 scopus 로고    scopus 로고
    • Mithramycin, an agent for developing new therapeutic drugs for neurodegenerative diseases
    • Osada N, Kosuge Y, Ishige K, Ito Y. Mithramycin, an agent for developing new therapeutic drugs for neurodegenerative diseases. J Pharmacol Sci 2013; 122(4): 251-6.
    • (2013) J Pharmacol Sci , vol.122 , Issue.4 , pp. 251-256
    • Osada, N.1    Kosuge, Y.2    Ishige, K.3    Ito, Y.4
  • 231
    • 79957858568 scopus 로고    scopus 로고
    • Neuroprotective effect of mithramycin against endoplasmic reticulum stress-induced neurotoxicity in organotypic hippocampal slice cultures
    • Kosuge Y, Taniguchi Y, Imai T, Ishige K, Ito Y. Neuroprotective effect of mithramycin against endoplasmic reticulum stress-induced neurotoxicity in organotypic hippocampal slice cultures. Neuropharmacology 2011; 61(1-2): 252-61.
    • (2011) Neuropharmacology , vol.61 , Issue.1-2 , pp. 252-261
    • Kosuge, Y.1    Taniguchi, Y.2    Imai, T.3    Ishige, K.4    Ito, Y.5
  • 233
    • 48249157930 scopus 로고    scopus 로고
    • ER stress is involved in Abeta-induced GSK-3beta activation and tau phosphorylation
    • Resende R, Ferreiro E, Pereira C, Oliveira CR. ER stress is involved in Abeta-induced GSK-3beta activation and tau phosphorylation. J Neurosci Res 2008; 86(9): 2091-9.
    • (2008) J Neurosci Res , vol.86 , Issue.9 , pp. 2091-2099
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Oliveira, C.R.4
  • 234
    • 84860439512 scopus 로고    scopus 로고
    • Dantrolene ameliorates cognitive decline and neuropathology in Alzheimer triple transgenic mice
    • Peng J, Liang G, Inan S, et al. Dantrolene ameliorates cognitive decline and neuropathology in Alzheimer triple transgenic mice. Neurosci Lett 2012; 516(2): 274-9.
    • (2012) Neurosci Lett , vol.516 , Issue.2 , pp. 274-279
    • Peng, J.1    Liang, G.2    Inan, S.3
  • 235
    • 84864403738 scopus 로고    scopus 로고
    • Dantrolene is neuroprotective in vitro, but does not affect survival in SOD1(G(9)(3)A) mice
    • Staats KA, Van Rillaer M, Scheveneels W, et al. Dantrolene is neuroprotective in vitro, but does not affect survival in SOD1(G(9)(3)A) mice. Neuroscience 2012; 220: 26-31.
    • (2012) Neuroscience , vol.220 , pp. 26-31
    • Staats, K.A.1    Van Rillaer, M.2    Scheveneels, W.3
  • 236
    • 84860471873 scopus 로고    scopus 로고
    • Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy
    • Vidal RL, Figueroa A, Court FA, et al. Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy. Hum Mol Genet 2012; 21(10): 2245-62.
    • (2012) Hum Mol Genet , vol.21 , Issue.10 , pp. 2245-2262
    • Vidal, R.L.1    Figueroa, A.2    Court, F.A.3


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