메뉴 건너뛰기




Volumn 10, Issue , 2017, Pages

The endoplasmic reticulum unfolded protein response in neurodegenerative disorders and its potential therapeutic significance

Author keywords

ER stress; Neurodegenerative diseases; Protein misfolding disorders; Therapeutic targets; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; AUTOPHAGY RELATED PROTEIN 12; AUTOPHAGY RELATED PROTEIN 5; BECLIN 1; CALCIUM ION; CALRETICULIN; COPPER ZINC SUPEROXIDE DISMUTASE; CYCLIN DEPENDENT KINASE 5; DIBENZOYLMETHANE DERIVATIVE; GLUCOSE REGULATED PROTEIN 78; GLUCOSYLCERAMIDASE; GLUCOSYLCERAMIDE; GUANABENZ; MESSENGER RNA; OPTINEURIN; RAB PROTEIN; REACTIVE OXYGEN METABOLITE; RNA 28S; SALUBRINAL; SECRETORY PROTEIN; SEQUESTOSOME 1; THIOREDOXIN; TRANSCRIPTION FACTOR FKHR; TRAZODONE; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UNINDEXED DRUG; X BOX BINDING PROTEIN 1;

EID: 85021447128     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2017.00187     Document Type: Review
Times cited : (135)

References (190)
  • 1
    • 84878333056 scopus 로고    scopus 로고
    • Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation
    • Abisambra, J. F., Jinwal, U. K., Blair, L. J., O’Leary, J. C. I. I. I., Li, Q., Brady, S., et al. (2013). Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation. J. Neurosci. 33, 9498–9507. doi: 10.1523/JNEUROSCI.5397-12.2013
    • (2013) J. Neurosci. , vol.33 , pp. 9498-9507
    • Abisambra, J.F.1    Jinwal, U.K.2    Blair, L.J.3    O’Leary, J.C.I.I.I.4    Li, Q.5    Brady, S.6
  • 2
    • 34250794495 scopus 로고    scopus 로고
    • XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks
    • Acosta-Alvear, D., Zhou, Y., Blais, A., Tsikitis, M., Lents, N. H., Arias, C., et al. (2007). XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks. Mol. Cell 27, 53–66. doi: 10.1016/j.molcel.2007.06.011
    • (2007) Mol. Cell , vol.27 , pp. 53-66
    • Acosta-Alvear, D.1    Zhou, Y.2    Blais, A.3    Tsikitis, M.4    Lents, N.H.5    Arias, C.6
  • 3
    • 84887621906 scopus 로고    scopus 로고
    • Paneth cells as a site of origin for intestinal inflammation
    • Adolph, T. E., Tomczak, M. F., Niederreiter, L., Ko, H. J., Bock, J., Martinez-Naves, E., et al. (2013). Paneth cells as a site of origin for intestinal inflammation. Nature 503, 272–276. doi: 10.1038/nature12599
    • (2013) Nature , vol.503 , pp. 272-276
    • Adolph, T.E.1    Tomczak, M.F.2    Niederreiter, L.3    Ko, H.J.4    Bock, J.5    Martinez-Naves, E.6
  • 4
    • 33645957634 scopus 로고    scopus 로고
    • A point mutation at the calreticulin gene core promoter conserved sequence in a case of schizophrenia
    • Aghajani, A., Rahimi, A., Fadai, F., Ebrahimi, A., Najmabadi, H., and Ohadi, M. (2006). A point mutation at the calreticulin gene core promoter conserved sequence in a case of schizophrenia. Am. J. Med. Genet. B Neuropsychiatr. Genet. 141B, 294–295. doi: 10.1002/ajmg.b.30300
    • (2006) Am. J. Med. Genet. B Neuropsychiatr. Genet , vol.141B , pp. 294-295
    • Aghajani, A.1    Rahimi, A.2    Fadai, F.3    Ebrahimi, A.4    Najmabadi, H.5    Ohadi, M.6
  • 5
    • 84155163741 scopus 로고    scopus 로고
    • A mutation in sigma-1 receptor causes juvenile amyotrophic lateral sclerosis
    • Al-Saif, A., Al-Mohanna, F., and Bohlega, S. (2011). A mutation in sigma-1 receptor causes juvenile amyotrophic lateral sclerosis. Ann. Neurol. 70, 913–919. doi: 10.1002/ana.22534
    • (2011) Ann. Neurol. , vol.70 , pp. 913-919
    • Al-Saif, A.1    Al-Mohanna, F.2    Bohlega, S.3
  • 7
    • 70350323730 scopus 로고    scopus 로고
    • Endoplasmic Reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments
    • Amodio, G., Renna, M., Paladino, S., Venturi, C., Tacchetti, C., Moltedo, O., et al. (2009). Endoplasmic Reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments. Int. J. Biochem. Cell Biol. 41, 2511–2521. doi: 10.1016/j.biocel.2009.08.006
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 2511-2521
    • Amodio, G.1    Renna, M.2    Paladino, S.3    Venturi, C.4    Tacchetti, C.5    Moltedo, O.6
  • 8
    • 84978374862 scopus 로고    scopus 로고
    • Remondelli P. Identification of a microRNA (miR-663a) induced by ER stress and its target gene PLOD3 by a combined microRNome and proteome approach
    • Amodio, G., Sasso, E., D’Ambrosio, C., Scaloni, A., Moltedo, O., Franceschelli, S., et al. (2016). Remondelli P. Identification of a microRNA (miR-663a) induced by ER stress and its target gene PLOD3 by a combined microRNome and proteome approach. Cell Biol. Toxicol. 32, 285–303. doi: 10.1007/s10565-016-9335-z
    • (2016) Cell Biol. Toxicol , vol.32 , pp. 285-303
    • Amodio, G.1    Sasso, E.2    D’Ambrosio, C.3    Scaloni, A.4    Moltedo, O.5    Franceschelli, S.6
  • 9
    • 84884280837 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs
    • Amodio, G., Venditti, R., De Matteis, M. A., Moltedo, O., Pignataro, P., and Remondelli, P. (2013). Endoplasmic reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs. FEBS Lett. 587, 3261–3266. doi: 10.1016/j.febslet.2013.08.021
    • (2013) FEBS Lett , vol.587 , pp. 3261-3266
    • Amodio, G.1    Venditti, R.2    De Matteis, M.A.3    Moltedo, O.4    Pignataro, P.5    Remondelli, P.6
  • 10
    • 80755133370 scopus 로고    scopus 로고
    • Clinical genetics of amyotrophic lateral sclerosis: What do we really know?
    • Andersen, P. M., and Al-Chalabi, A. (2011). Clinical genetics of amyotrophic lateral sclerosis: what do we really know? Nat. Rev. Neurol. 7, 603–615. doi: 10.1038/nrneurol.2011.150
    • (2011) Nat. Rev. Neurol. , vol.7 , pp. 603-615
    • Andersen, P.M.1    Al-Chalabi, A.2
  • 11
    • 84866556522 scopus 로고    scopus 로고
    • Protein aggregates in Huntington’s disease
    • Arrasate, M., and Finkbeiner, S. (2012). Protein aggregates in Huntington’s disease. Exp. Neurol. 238, 1–11. doi: 10.1016/j.expneurol.2011.12.013
    • (2012) Exp. Neurol , vol.238 , pp. 1-11
    • Arrasate, M.1    Finkbeiner, S.2
  • 12
    • 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, J. D., Farg, M. A., Turner, B. J., Tomas, D., Lysaght, J. A., Nunan, J., et al. (2006). Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J. Biol. Chem. 281, 30152–30165. doi: 10.1074/jbc.M603393200
    • (2006) J. Biol. Chem. , vol.281 , pp. 30152-30165
    • Atkin, J.D.1    Farg, M.A.2    Turner, B.J.3    Tomas, D.4    Lysaght, J.A.5    Nunan, J.6
  • 13
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W. E., Morimoto, R. I., Dillin, A., and Kelly, J. W. (2008). Adapting proteostasis for disease intervention. Science 319, 916–919. doi: 10.1126/science. 1141448
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 14
    • 84885455062 scopus 로고    scopus 로고
    • The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression
    • B’Chir, W., Maurin, A. C., Carraro, V., Averous, J., Jousse, C., Muranishi, Y., et al. (2013). The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression. Nucleic Acids Res. 41, 7683–7699. doi: 10.1093/nar/gkt563
    • (2013) Nucleic Acids Res , vol.41 , pp. 7683-7699
    • B’Chir, W.1    Maurin, A.C.2    Carraro, V.3    Averous, J.4    Jousse, C.5    Muranishi, Y.6
  • 15
    • 84856954609 scopus 로고    scopus 로고
    • The homocysteine-inducible endoplasmic reticulum (ER) stress protein Herp counteracts mutant α-synuclein-induced ER stress via the homeostatic regulation of ER-resident calcium release channel proteins
    • Belal, C., Ameli, N. J., El Kommos, A., Bezalel, S., Al’Khafaji, A. M., Mughal, M. R., et al. (2012). The homocysteine-inducible endoplasmic reticulum (ER) stress protein Herp counteracts mutant α-synuclein-induced ER stress via the homeostatic regulation of ER-resident calcium release channel proteins. Hum. Mol. Genet. 21, 963–977. doi: 10.1093/hmg/ddr502
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 963-977
    • Belal, C.1    Ameli, N.J.2    El Kommos, A.3    Bezalel, S.4    Al’Khafaji, A.M.5    Mughal, M.R.6
  • 16
    • 79551647443 scopus 로고    scopus 로고
    • Induction of the unfolded protein response by α-synuclein in experimental models of Parkinson’s disease
    • Bellucci, A., Navarria, L., Zaltieri, M., Falarti, E., Bodei, S., Sigala, S., et al. (2011). Induction of the unfolded protein response by α-synuclein in experimental models of Parkinson’s disease. J. Neurochem. 116, 588–605. doi: 10.1111/j.1471-4159.2010.07143.x
    • (2011) J. Neurochem. , vol.116 , pp. 588-605
    • Bellucci, A.1    Navarria, L.2    Zaltieri, M.3    Falarti, E.4    Bodei, S.5    Sigala, S.6
  • 17
    • 0038125598 scopus 로고    scopus 로고
    • Calcium signalling: Dynamics, homeostasis and remodeling
    • Berridge, M. J., Bootman, M. D., and Roderick, H. L. (2003). Calcium signalling: dynamics, homeostasis and remodeling. Nat. Rev. Mol. Cell Biol. 4, 517–529. doi: 10.1038/nrm1155
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 517-529
    • Berridge, M.J.1    Bootman, M.D.2    Roderick, H.L.3
  • 18
    • 4344648874 scopus 로고    scopus 로고
    • Activating transcription factor 4 is translationally regulated by hypoxic stress
    • Blais, J. D., Filipenko, V., Bi, M., Harding, H. P., Ron, D., Koumenis, C., et al. (2004). Activating transcription factor 4 is translationally regulated by hypoxic stress. Mol. Cell. Biol. 24, 7469–7482. doi: 10.1128/MCB.24.17.7469-7482.2004
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7469-7482
    • Blais, J.D.1    Filipenko, V.2    Bi, M.3    Harding, H.P.4    Ron, D.5    Koumenis, C.6
  • 19
    • 79954417075 scopus 로고    scopus 로고
    • Parkin is transcriptionally regulated by ATF4: Evidence for an interconnection between mitochondrial stress and ER stress
    • Bouman, L., Schlierf, A., Lutz, A. K., Shan, J., Deinlein, A., Kast, J., et al. (2011). Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress. Cell Death Differ. 18, 769–782. doi: 10.1038/cdd.2010.142
    • (2011) Cell Death Differ , vol.18 , pp. 769-782
    • Bouman, L.1    Schlierf, A.2    Lutz, A.K.3    Shan, J.4    Deinlein, A.5    Kast, J.6
  • 20
    • 84938517319 scopus 로고    scopus 로고
    • Early Neurodegeneration in the Brain of a Child Without Functional PKR-like Endoplasmic Reticulum Kinase
    • Bruch, J., Kurz, C., Vasiljevic, A., Nicolino, M., Arzberger, T., and Höglinger, G. U. (2015). Early Neurodegeneration in the Brain of a Child Without Functional PKR-like Endoplasmic Reticulum Kinase. J. Neuropathol. Exp. Neurol. 74, 850–857. doi: 10.1097/NEN.0000000000000224
    • (2015) J. Neuropathol. Exp. Neurol. , vol.74 , pp. 850-857
    • Bruch, J.1    Kurz, C.2    Vasiljevic, A.3    Nicolino, M.4    Arzberger, T.5    Höglinger, G.U.6
  • 21
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., et al. (2002). IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415, 92–96. doi: 10.1038/415092a
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6
  • 23
    • 85016139631 scopus 로고    scopus 로고
    • Mitofusin-mediated ER stress triggers neurodegeneration in pink1/parkin models of Parkinson’s disease
    • Celardo, I., Costa, A. C., Lehmann, S., Jones, C., Wood, N., Mencacci, N. E., et al. (2016). Mitofusin-mediated ER stress triggers neurodegeneration in pink1/parkin models of Parkinson’s disease. Cell Death Dis. 7, e2271. doi: 10.1038/cddis.2016.173
    • (2016) Cell Death Dis , vol.7
    • Celardo, I.1    Costa, A.C.2    Lehmann, S.3    Jones, C.4    Wood, N.5    Mencacci, N.E.6
  • 24
    • 83455243339 scopus 로고    scopus 로고
    • Autophagy dysregulation in amyotrophic lateral sclerosis
    • Chen, S., Zhang, X., Song, L., and Le, W. (2012). Autophagy dysregulation in amyotrophic lateral sclerosis. Brain Pathol. 22, 110–116. doi: 10.1111/j.1750-3639.2011.00546.x
    • (2012) Brain Pathol , vol.22 , pp. 110-116
    • Chen, S.1    Zhang, X.2    Song, L.3    Le, W.4
  • 25
    • 82055164052 scopus 로고    scopus 로고
    • Dantrolene is neuroprotective in Huntington’s disease transgenic mouse model
    • Chen, X., Wu, J., Lvovskaya, S., Herndon, E., Supnet, C., and Bezprozvanny, I. (2011). Dantrolene is neuroprotective in Huntington’s disease transgenic mouse model. Mol. Neurodegener. 6, 81. doi: 10.1186/1750-1326-6-81
    • (2011) Mol. Neurodegener. , vol.6 , pp. 81
    • Chen, X.1    Wu, J.2    Lvovskaya, S.3    Herndon, E.4    Supnet, C.5    Bezprozvanny, I.6
  • 26
    • 57649232173 scopus 로고    scopus 로고
    • Functional alterations of the ubiquitin-proteasome system in motor neurons of a mouse model of familial amyotrophic lateral sclerosis
    • Cheroni, C., Marino, M., Tortarolo, M., Veglianese, P., De Biasi, S., Fontana, E., et al. (2009). Functional alterations of the ubiquitin-proteasome system in motor neurons of a mouse model of familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 18, 82–96. doi: 10.1093/hmg/ddn319
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 82-96
    • Cheroni, C.1    Marino, M.2    Tortarolo, M.3    Veglianese, P.4    De Biasi, S.5    Fontana, E.6
  • 27
    • 84992183855 scopus 로고    scopus 로고
    • Parkin and PINK1 Patient iPSC-derived midbrain dopamine neurons exhibit mitochondrial dysfunction and alpha-synuclein accumulation
    • Chung, S. Y., Kishinevsky, S., Mazzulli, J. R., Graziotto, J., Mrejeru, A., Mosharov, E. V., et al. (2016). Parkin and PINK1 Patient iPSC-derived midbrain dopamine neurons exhibit mitochondrial dysfunction and alpha-synuclein accumulation. Stem Cell Rep. 7, 664–677. doi: 10.1016/j.stemcr.2016.08.012
    • (2016) Stem Cell Rep , vol.7 , pp. 664-677
    • Chung, S.Y.1    Kishinevsky, S.2    Mazzulli, J.R.3    Graziotto, J.4    Mrejeru, A.5    Mosharov, E.V.6
  • 28
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham, D. E. (2007). Calcium signaling. Cell 13, 1047–1058. doi: 10.1016/j.cell. 2007.11.028
    • (2007) Cell , vol.13 , pp. 1047-1058
    • Clapham, D.E.1
  • 29
    • 84863230467 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is important for the manifestations of α-synucleinopathy in vivo
    • Colla, E., Coune, P., Liu, Y., Pletnikova, O., Troncoso, J. C., Iwatsubo, T., et al. (2012a). Endoplasmic reticulum stress is important for the manifestations of α-synucleinopathy in vivo. J. Neurosci. 32, 3306–3320. doi: 10.1523/JNEUROSCI.5367-11.2012
    • (2012) J. Neurosci. , vol.32 , pp. 3306-3320
    • Colla, E.1    Coune, P.2    Liu, Y.3    Pletnikova, O.4    Troncoso, J.C.5    Iwatsubo, T.6
  • 30
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic α-synuclein oligomer within endoplasmic reticulum occurs in α-synucleinopathy in vivo
    • Colla, E., Jensen, P. H., Pletnikova, O., Troncoso, J. C., Glabe, C., and Lee, M. K. (2012b). Accumulation of toxic α-synuclein oligomer within endoplasmic reticulum occurs in α-synucleinopathy in vivo. J. Neurosci. 32, 3301–3305. doi: 10.1523/JNEUROSCI.5368-11.2012
    • (2012) J. Neurosci. , vol.32 , pp. 3301-3305
    • Colla, E.1    Jensen, P.H.2    Pletnikova, O.3    Troncoso, J.C.4    Glabe, C.5    Lee, M.K.6
  • 31
    • 33746533924 scopus 로고    scopus 로고
    • α-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson’s models
    • Cooper, A. A., Gitler, A. D., Cashikar, A., Haynes, C. M., Hill, K. J., Bhullar, B., et al. (2006). α-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson’s models. Science 313, 324–328. doi: 10.1126/science.1129462
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1    Gitler, A.D.2    Cashikar, A.3    Haynes, C.M.4    Hill, K.J.5    Bhullar, B.6
  • 32
    • 0141752795 scopus 로고    scopus 로고
    • Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival
    • Cullinan, S. B., Zhang, D., Hannink, M., Arvisais, E., Kaufman, R. J., and Diehl, J. A. (2003). Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. Mol. Cell. Biol. 23, 7198–7209. doi: 10.1128/MCB.23.20.7198-7209. 2003
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7198-7209
    • Cullinan, S.B.1    Zhang, D.2    Hannink, M.3    Arvisais, E.4    Kaufman, R.J.5    Diehl, J.A.6
  • 33
    • 84982803301 scopus 로고    scopus 로고
    • C9orf72 hexanucleotide expansions are associated with altered endoplasmic reticulum calcium homeostasis, and stress granule formation in induced pluripotent stem cell-derived neurons from patients with amyotrophic lateral sclerosis, and frontotemporal dementia
    • Dafinca, R., Scaber, J., Ababneh, N., Lalic, T., Weir, G., Christian, H., et al. (2016). C9orf72 hexanucleotide expansions are associated with altered endoplasmic reticulum calcium homeostasis, and stress granule formation in induced pluripotent stem cell-derived neurons from patients with amyotrophic lateral sclerosis, and frontotemporal dementia. Stem Cells 34, 2063–2078. doi: 10.1002/stem.2388
    • (2016) Stem Cells , vol.34 , pp. 2063-2078
    • Dafinca, R.1    Scaber, J.2    Ababneh, N.3    Lalic, T.4    Weir, G.5    Christian, H.6
  • 34
    • 84927619395 scopus 로고    scopus 로고
    • Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit
    • Das, I., Krzyzosiak, A., Schneider, K., Wrabetz, L., D’Antonio, M., Barry, N., et al. (2015). Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit. Science 348, 239–242. doi: 10.1126/science.aaa4484
    • (2015) Science , vol.348 , pp. 239-242
    • Das, I.1    Krzyzosiak, A.2    Schneider, K.3    Wrabetz, L.4    D’Antonio, M.5    Barry, N.6
  • 35
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., et al. (2011). Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72, 245–256. doi: 10.1016/j.neuron.2011.09.011
    • (2011) Neuron , vol.72 , pp. 245-256
    • Dejesus-Hernandez, M.1    Mackenzie, I.R.2    Boeve, B.F.3    Boxer, A.L.4    Baker, M.5    Rutherford, N.J.6
  • 36
    • 33845381075 scopus 로고    scopus 로고
    • Mutant huntingtin impairs the post-Golgi trafficking of brain-derived neurotrophic factor but not its Val66Met polymorphism
    • del Toro, D., Canals, J. M., Ginés, S., Kojima, M., Egea, G., and Alberch, J. (2006). Mutant huntingtin impairs the post-Golgi trafficking of brain-derived neurotrophic factor but not its Val66Met polymorphism. J. Neurosci. 26, 12748– 12757. doi: 10.1523/JNEUROSCI.3873-06.2006
    • (2006) J. Neurosci , vol.26
    • Del Toro, D.1    Canals, J.M.2    Ginés, S.3    Kojima, M.4    Egea, G.5    Alberch, J.6
  • 37
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • Deng, H. X., Chen, W., Hong, S. T., Boycott, K. M., Gorrie, G. H., Siddique, N., et al. (2011). Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 477, 211–215. doi: 10.1038/nature10353
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1    Chen, W.2    Hong, S.T.3    Boycott, K.M.4    Gorrie, G.H.5    Siddique, N.6
  • 38
    • 84885398154 scopus 로고    scopus 로고
    • Deletion of the eIF2α Kinase GCN2 fails to rescue the memory decline associated with Alzheimer’s disease
    • Devi, L., and Ohno, M. (2013). Deletion of the eIF2α Kinase GCN2 fails to rescue the memory decline associated with Alzheimer’s disease. PLoS ONE 8:e77335. doi: 10.1371/journal.pone.0077335
    • (2013) Plos ONE , vol.8
    • Devi, L.1    Ohno, M.2
  • 39
    • 34247253057 scopus 로고    scopus 로고
    • Altered subcellular distribution of the Alzheimer’s amyloid precursor protein under stress conditions
    • Domingues, S. C., Henriques, A. G., Wu, W., Da Cruz e Silva, E. F., and Da Cruz e Silva, O. A. (2007). Altered subcellular distribution of the Alzheimer’s amyloid precursor protein under stress conditions. Ann. N. Y. Acad. Sci 1096, 184–195. doi: 10.1196/annals.1397.085
    • (2007) Ann. N. Y. Acad. Sci , vol.1096 , pp. 184-195
    • Domingues, S.C.1    Henriques, A.G.2    Wu, W.3    Da Cruz E Silva, E.F.4    Da Cruz E Silva, O.A.5
  • 40
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald, M. L., and Lindquist, S. (2008). Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev. 22, 3308–3319. doi: 10.1101/gad.1673408
    • (2008) Genes Dev , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 41
    • 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., Sévalle, J., Corti, O., Brice, A., et al. (2013). 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. 126, 2124–2133. doi: 10.1242/jcs.127340
    • (2013) J. Cell Sci. , vol.126 , pp. 2124-2133
    • Duplan, E.1    Giaime, E.2    Viotti, J.3    Sévalle, J.4    Corti, O.5    Brice, A.6
  • 43
    • 79953148080 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress sensor, ATF6α, protects against neurotoxin-induced dopaminergic neuronal death
    • Egawa, N., Yamamoto, K., Inoue, H., Hikawa, R., Nishi, K., Mori, K., et al. (2011). The endoplasmic reticulum stress sensor, ATF6α, protects against neurotoxin-induced dopaminergic neuronal death. J. Biol. Chem. 286, 7947–7957. doi: 10.1074/jbc.M110.156430
    • (2011) J. Biol. Chem. , vol.286 , pp. 7947-7957
    • Egawa, N.1    Yamamoto, K.2    Inoue, H.3    Hikawa, R.4    Nishi, K.5    Mori, K.6
  • 44
    • 85017476767 scopus 로고    scopus 로고
    • From dysfunctional endoplasmic reticulum-mitochondria coupling to neurodegeneration
    • [Epub ahead of print]
    • Erpapazoglou, Z., Mouton-Liger, F., and Corti, O. (2017). From dysfunctional endoplasmic reticulum-mitochondria coupling to neurodegeneration. Neurochem. Int. doi: 10.1016/j.neuint.2017.03.021 [Epub ahead of print].
    • (2017) Neurochem. Int. Doi
    • Erpapazoglou, Z.1    Mouton-Liger, F.2    Corti, O.3
  • 45
    • 84866748196 scopus 로고    scopus 로고
    • Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase
    • Farg, M. A., Soo, K. Y., Walker, A. K., Pham, H., Orian, J., Horne, M. K., et al. (2012). Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase. Neurobiol. Aging 33, 2855–2868. doi: 10.1016/j.neurobiolaging.2012.02.009
    • (2012) Neurobiol. Aging , vol.33 , pp. 2855-2868
    • Farg, M.A.1    Soo, K.Y.2    Walker, A.K.3    Pham, H.4    Orian, J.5    Horne, M.K.6
  • 46
    • 84901038797 scopus 로고    scopus 로고
    • C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking
    • Farg, M. A., Sundaramoorthy, V., Sultana, J. M., Yang, S., Atkinson, R. A., Levina, V., et al. (2014). C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking. Hum. Mol. Genet. 23, 3579–3595. doi: 10.1093/hmg/ddu068
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 3579-3595
    • Farg, M.A.1    Sundaramoorthy, V.2    Sultana, J.M.3    Yang, S.4    Atkinson, R.A.5    Levina, V.6
  • 47
    • 77952308995 scopus 로고    scopus 로고
    • A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum
    • Fasana, E., Fossati, M., Ruggiano, A., Brambillasca, S., Hoogenraad, C. C., Navone, F., et al. (2010). A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum. FASEB J. 24, 1419–1430. doi: 10.1096/fj.09-147850
    • (2010) FASEB J , vol.24 , pp. 1419-1430
    • Fasana, E.1    Fossati, M.2    Ruggiano, A.3    Brambillasca, S.4    Hoogenraad, C.C.5    Navone, F.6
  • 48
    • 80855130688 scopus 로고    scopus 로고
    • Making connections: Pathology and genetics link amyotrophic lateral sclerosis with frontotemporal lobe dementia
    • Fecto, F., and Siddique, T. (2011). Making connections: pathology and genetics link amyotrophic lateral sclerosis with frontotemporal lobe dementia. J. Mol. Neurosci. 45, 663–675. doi: 10.1007/s12031-011-9637-9
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 663-675
    • Fecto, F.1    Siddique, T.2
  • 49
    • 84960803232 scopus 로고    scopus 로고
    • ER stress and autophagic perturbations lead to elevated extracellular alpha-Synuclein in GBA-N370S Parkinson’s iPSC-Derived Dopamine Neurons
    • Fernandes, H. J., Hartfield, E. M., Christian, H. C., Emmanoulidou, E., Zheng, Y., Booth, H., et al. (2016). ER stress and autophagic perturbations lead to elevated extracellular alpha-Synuclein in GBA-N370S Parkinson’s iPSC-Derived Dopamine Neurons. Stem Cell Rep. 6, 342–356. doi: 10.1016/j.stemcr. 2016.01.013
    • (2016) Stem Cell Rep , vol.6 , pp. 342-356
    • Fernandes, H.J.1    Hartfield, E.M.2    Christian, H.C.3    Emmanoulidou, E.4    Zheng, Y.5    Booth, H.6
  • 50
    • 78349312360 scopus 로고    scopus 로고
    • Impaired ATF6α processing, decreased Rheb and neuronal cell cycle re-entry in Huntington’s disease
    • Fernandez-Fernandez, M. R., Ferrer, I., and Lucas, J. J. (2011). Impaired ATF6α processing, decreased Rheb and neuronal cell cycle re-entry in Huntington’s disease. Neurobiol. Dis. 41, 23–32. doi: 10.1016/j.nbd.2010.08.014
    • (2011) Neurobiol. Dis. , vol.41 , pp. 23-32
    • Fernandez-Fernandez, M.R.1    Ferrer, I.2    Lucas, J.J.3
  • 51
    • 84862303631 scopus 로고    scopus 로고
    • ER stress inhibits neuronal death by promoting autophagy
    • Fouillet, A., Levet, C., Virgone, A., Robin, M., Dourlen, P., Rieusset, J., et al. (2012). ER stress inhibits neuronal death by promoting autophagy. Autophagy 8, 915–926. doi: 10.4161/auto.19716
    • (2012) Autophagy , vol.8 , pp. 915-926
    • Fouillet, A.1    Levet, C.2    Virgone, A.3    Robin, M.4    Dourlen, P.5    Rieusset, J.6
  • 52
    • 84931345859 scopus 로고    scopus 로고
    • Phenotypic assays identify azoramide as a small-molecule modulator of the unfolded protein response with antidiabetic activity
    • Fu, S., Yalcin, A., Lee, G. Y., Li, P., Fan, J., Arruda, A. P., et al. (2015). Phenotypic assays identify azoramide as a small-molecule modulator of the unfolded protein response with antidiabetic activity. Sci. Transl. Med. 7, 292ra98. doi: 10.1126/scitranslmed.aaa9134
    • (2015) Sci. Transl. Med. , vol.7
    • Fu, S.1    Yalcin, A.2    Lee, G.Y.3    Li, P.4    Fan, J.5    Arruda, A.P.6
  • 55
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert, M., Clavaguera, F., and Tolnay, M. (2010). The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci. 33, 317–325. doi: 10.1016/j.tins.2010.04.003
    • (2010) Trends Neurosci , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 56
    • 84863498486 scopus 로고    scopus 로고
    • Glucose regulated protein 78 diminishes α-synuclein neurotoxicity in a rat model of Parkinson disease
    • Gorbatyuk, M. S., Shabashvili, A., Chen, W., Meyers, C., Sullivan, L. F., Salganik, M., et al. (2012). Glucose regulated protein 78 diminishes α-synuclein neurotoxicity in a rat model of Parkinson disease. Mol. Ther. 20, 1327–1337. doi: 10.1038/mt.2012.28
    • (2012) Mol. Ther. , vol.20 , pp. 1327-1337
    • Gorbatyuk, M.S.1    Shabashvili, A.2    Chen, W.3    Meyers, C.4    Sullivan, L.F.5    Salganik, M.6
  • 57
    • 84897143522 scopus 로고    scopus 로고
    • To be or not to be? How selective autophagy and cell death govern cell fate
    • Green, D. R., and Levine, B. (2014). To be or not to be? How selective autophagy and cell death govern cell fate. Cell 157, 65–75. doi: 10.1016/j.cell.2014.02.049
    • (2014) Cell , vol.157 , pp. 65-75
    • Green, D.R.1    Levine, B.2
  • 58
    • 84973164070 scopus 로고    scopus 로고
    • Up-regulation of activating transcription factor 4 induces severe loss of dopamine nigral neurons in a rat model of Parkinson’s disease
    • Gully, J. C., Sergeyev, V. G., Bhootada, Y., Mendez-Gomez, H., Meyers, C. A., Zolotukhin, S., et al. (2016). Up-regulation of activating transcription factor 4 induces severe loss of dopamine nigral neurons in a rat model of Parkinson’s disease. Neurosci. Lett. 627, 36–41. doi: 10.1016/j.neulet.2016.05.039
    • (2016) Neurosci. Lett. , vol.627 , pp. 36-41
    • Gully, J.C.1    Sergeyev, V.G.2    Bhootada, Y.3    Mendez-Gomez, H.4    Meyers, C.A.5    Zolotukhin, S.6
  • 59
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer’s amyloid β-peptide
    • Haass, C., and Selkoe, D. J. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid β-peptide. Nat. Rev. Mol. Cell Biol. 8, 101–112. doi: 10.1038/nrm2101
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 60
    • 84988811921 scopus 로고    scopus 로고
    • Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity
    • Halliday, M., Radford, H., Sekine, Y., Moreno, J., Verity, N., le Quesne, J., et al. (2015). Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity. Cell Death Dis. 6, e1672. doi: 10.1038/cddis.2015.49
    • (2015) Cell Death Dis , vol.6
    • Halliday, M.1    Radford, H.2    Sekine, Y.3    Moreno, J.4    Verity, N.5    Le Quesne, J.6
  • 61
    • 85020602496 scopus 로고    scopus 로고
    • Repurposed drugs targeting eIF2α-P-mediated translational repression prevent neurodegeneration in mice
    • Halliday, M., Radford, H., Zents, K. A. M., Molloy, C., Moreno, J. A., Verity, N. C., et al. (2017). Repurposed drugs targeting eIF2α-P-mediated translational repression prevent neurodegeneration in mice. Brain 140, 1768–1783. doi: 10.1093/brain/awx074
    • (2017) Brain , vol.140 , pp. 1768-1783
    • Halliday, M.1    Radford, H.2    Zents, K.A.M.3    Molloy, C.4    Moreno, J.A.5    Verity, N.C.6
  • 62
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H. P., Zhang, Y., and Ron, D. (1999). Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397, 271–274. doi: 10.1038/16729
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 63
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324–332. doi: 10.1038/nature10317
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 64
    • 84868135034 scopus 로고    scopus 로고
    • ATF6α promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson’s disease
    • Hashida, K., Kitao, Y., Sudo, H., Awa, Y., Maeda, S., Mori, K., et al. (2012). ATF6α promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson’s disease. PLoS ONE 7:e47950. doi: 10.1371/journal.pone.0047950
    • (2012) Plos ONE , vol.7
    • Hashida, K.1    Kitao, Y.2    Sudo, H.3    Awa, Y.4    Maeda, S.5    Mori, K.6
  • 65
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze, K., Yoshida, H., Yanagi, H., Yura, T., and Mori, K. (1999). Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell 10, 3787–3799. doi: 10.1091/mbc.10.11.3787
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 66
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz, C. (2012). The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89–102. doi: 10.1038/nrm3270
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 89-102
    • Hetz, C.1
  • 67
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz, C., Chevet, E., and Harding, H. P. (2013). Targeting the unfolded protein response in disease. Nat. Rev. Drug Discov. 12, 703–719. doi: 10.1038/nrd3976
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 703-719
    • Hetz, C.1    Chevet, E.2    Harding, H.P.3
  • 68
    • 38649108109 scopus 로고    scopus 로고
    • Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis
    • Hetz, C., Lee, A. H., Gonzalez-Romero, D., Thielen, P., Castilla, J., Soto, C., et al. (2008). Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proc. Natl. Acad. Sci. U.S.A. 105, 757–762. doi: 10.1073/pnas.0711094105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 757-762
    • Hetz, C.1    Lee, A.H.2    Gonzalez-Romero, D.3    Thielen, P.4    Castilla, J.5    Soto, C.6
  • 69
    • 80054722420 scopus 로고    scopus 로고
    • The unfolded protein response: Integrating stress signals through the stress sensor IRE1
    • Hetz, C., Martinon, F., Rodriguez, D., and Glimcher, L. H. (2011). The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91, 1219–1243. doi: 10.1152/physrev.00001.2011
    • (2011) α. Physiol. Rev. , vol.91 , pp. 1219-1243
    • Hetz, C.1    Martinon, F.2    Rodriguez, D.3    Glimcher, L.H.4
  • 70
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz, C., and Mollereau, B. (2014). Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 15, 233–249. doi: 10.1038/nrn3689
    • (2014) Nat. Rev. Neurosci. , vol.15 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 71
    • 34250766661 scopus 로고    scopus 로고
    • The proapoptotic BCL-2 family member BIM mediates motoneuron loss in a model of amyotrophic lateral sclerosis
    • Hetz, C., Thielen, P., Fisher, J., Pasinelli, P., Brown, R. H., Korsmeyer, S., et al. (2007). The proapoptotic BCL-2 family member BIM mediates motoneuron loss in a model of amyotrophic lateral sclerosis. Cell Death Differ. 14, 1386–1389. doi: 10.1038/sj.cdd.4402166
    • (2007) Cell Death Differ , vol.14 , pp. 1386-1389
    • Hetz, C.1    Thielen, P.2    Fisher, J.3    Pasinelli, P.4    Brown, R.H.5    Korsmeyer, S.6
  • 72
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz, C., Thielen, P., Matus, S., Nassif, M., Court, F., Kiffin, R., et al. (2009). XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev. 23, 2294–2306. doi: 10.1101/gad.1830709
    • (2009) Genes Dev , vol.23 , pp. 2294-2306
    • Hetz, C.1    Thielen, P.2    Matus, S.3    Nassif, M.4    Court, F.5    Kiffin, R.6
  • 73
    • 78649954745 scopus 로고    scopus 로고
    • Mechanism of ER stress-induced brain damage by IP3 receptor
    • Higo, T., Hamada, K., Hisatsune, C., Nukina, N., Hashikawa, T., Hattori, M., et al. (2010). Mechanism of ER stress-induced brain damage by IP3 receptor. Neuron 68, 865–878. doi: 10.1016/j.neuron.2010.11.010
    • (2010) Neuron , vol.68 , pp. 865-878
    • Higo, T.1    Hamada, K.2    Hisatsune, C.3    Nukina, N.4    Hashikawa, T.5    Hattori, M.6
  • 74
    • 84957922325 scopus 로고    scopus 로고
    • Progesterone exerts neuroprotective effects against Aβ-induced neuroinflammation by attenuating ER stress in astrocytes
    • Hong, Y., Wang, X., Sun, S., Xue, G., Li, J., and Hou, Y. (2016). Progesterone exerts neuroprotective effects against Aβ-induced neuroinflammation by attenuating ER stress in astrocytes. Int. Immunopharmacol. 33, 83–89. doi: 10.1016/j.intimp. 2016.02.002
    • (2016) Int. Immunopharmacol. , vol.33 , pp. 83-89
    • Hong, Y.1    Wang, X.2    Sun, S.3    Xue, G.4    Li, J.5    Hou, Y.6
  • 75
    • 85015646151 scopus 로고    scopus 로고
    • Blockade of RyRs in the ER Attenuates 6-OHDA-induced calcium overload, cellular hypo-excitability and apoptosis in dopaminergic neurons
    • Huang, L., Xue, Y., Feng, D., Yang, R., Nie, T., Zhu, G., et al. (2017). Blockade of RyRs in the ER Attenuates 6-OHDA-induced calcium overload, cellular hypo-excitability and apoptosis in dopaminergic neurons. Front. Cell Neurosci. 11:52. doi: 10.3389/fncel.2017.00052
    • (2017) Front. Cell Neurosci , vol.11 , pp. 52
    • Huang, L.1    Xue, Y.2    Feng, D.3    Yang, R.4    Nie, T.5    Zhu, G.6
  • 76
    • 0035147411 scopus 로고    scopus 로고
    • Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress
    • Iwawaki, T., Hosoda, A., Okuda, T., Kamigori, Y., Nomura-Furuwatari, C., Kimata, Y., et al. (2001). Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress. Nat. Cell Biol. 3, 158–164. doi: 10.1038/35055065
    • (2001) Nat. Cell Biol , vol.3 , pp. 158-164
    • Iwawaki, T.1    Hosoda, A.2    Okuda, T.3    Kamigori, Y.4    Nomura-Furuwatari, C.5    Kimata, Y.6
  • 78
    • 0141730405 scopus 로고    scopus 로고
    • Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder
    • Kakiuchi, C., Iwamoto, K., Ishiwata, M., Bundo, M., Kasahara, T., Kusumi, I., et al. (2003). Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder. Nat. Genet. 35, 171–175. doi: 10.1038/ng1235
    • (2003) Nat. Genet. , vol.35 , pp. 171-175
    • Kakiuchi, C.1    Iwamoto, K.2    Ishiwata, M.3    Bundo, M.4    Kasahara, T.5    Kusumi, I.6
  • 79
    • 33749554133 scopus 로고    scopus 로고
    • Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8)
    • Kanekura, K., Nishimoto, I., Aiso, S., and Matsuoka, M. (2006). Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8). J. Biol. Chem. 281, 30223–30233. doi: 10.1074/jbc.M605049200
    • (2006) J. Biol. Chem. , vol.281 , pp. 30223-30233
    • Kanekura, K.1    Nishimoto, I.2    Aiso, S.3    Matsuoka, M.4
  • 80
    • 0033258544 scopus 로고    scopus 로고
    • Presinilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
    • Katayama, T., Imaizumi, K., Sato, N., Miyoshi, K., Kudo, T., Hitomi, J., et al. (1999). Presinilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Nat. Cell Biol. 1, 479–485. doi: 10.1038/70265
    • (1999) Nat. Cell Biol. , vol.1 , pp. 479-485
    • Katayama, T.1    Imaizumi, K.2    Sato, N.3    Miyoshi, K.4    Kudo, T.5    Hitomi, J.6
  • 81
    • 33645798615 scopus 로고    scopus 로고
    • Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model
    • Kikuchi, H., Almer, G., Yamashita, S., Guégan, C., Nagai, M., Xu, Z., et al. (2006). Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model. Proc. Natl. Acad. Sci. U.S.A. 103, 6025–6030. doi: 10.1073/pnas.0509227103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6025-6030
    • Kikuchi, H.1    Almer, G.2    Yamashita, S.3    Guégan, C.4    Nagai, M.5    Xu, Z.6
  • 82
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • Knowles, T. P., Vendruscolo, M., and Dobson, C. M. (2014). The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 15, 384–396. doi: 10.1038/nrm3810
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 384-396
    • Knowles, T.P.1    Vendruscolo, M.2    Dobson, C.M.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., Ueno, T., Isoai, A., Kumagai, H., et al. (2007). ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ. 14, 230–239. doi: 10.1038/sj.cdd.4401984
    • (2007) Cell Death Differ , vol.14 , pp. 230-239
    • Kouroku, Y.1    Fujita, E.2    Tanida, I.3    Ueno, T.4    Isoai, A.5    Kumagai, H.6
  • 84
    • 27844495164 scopus 로고    scopus 로고
    • Molecular basis of programmed cell death involved in neurodegeneration
    • Krantic, S., Mechawar, N., Reix, S., and Quirion, R. (2005). Molecular basis of programmed cell death involved in neurodegeneration. Trends Neurosci. 28, 670–676. doi: 10.1016/j.tins.2005.09.011
    • (2005) Trends Neurosci , vol.28 , pp. 670-676
    • Krantic, S.1    Mechawar, N.2    Reix, S.3    Quirion, R.4
  • 86
    • 38049170584 scopus 로고    scopus 로고
    • A molecular chaperone inducer protects neurons from ER stress
    • Kudo, T., Kanemoto, S., Hara, H., Morimoto, N., Morihara, T., Kimura, R., et al. (2008). A molecular chaperone inducer protects neurons from ER stress. Cell Death Differ. 15, 364–375. doi: 10.1038/sj.cdd.4402276
    • (2008) Cell Death Differ , vol.15 , pp. 364-375
    • Kudo, T.1    Kanemoto, S.2    Hara, H.3    Morimoto, N.4    Morihara, T.5    Kimura, R.6
  • 87
    • 84880331334 scopus 로고    scopus 로고
    • The ALS8 protein VAPB interacts with the ER–Golgi recycling protein YIF1A and regulates membrane delivery into dendrites
    • Kuijpers, M., Yu, K. L., Teuling, E., Akhmanova, A., Jaarsma, D., Hoogenraad, C. C., et al. (2013). The ALS8 protein VAPB interacts with the ER–Golgi recycling protein YIF1A and regulates membrane delivery into dendrites. EMBO J. 32, 2056–2072. doi: 10.1038/emboj.2013.131
    • (2013) EMBO J , vol.32 , pp. 2056-2072
    • Kuijpers, M.1    Yu, K.L.2    Teuling, E.3    Akhmanova, A.4    Jaarsma, D.5    Hoogenraad, C.C.6
  • 88
    • 84875991370 scopus 로고    scopus 로고
    • Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis
    • Kwok, C. T., Morris, A. G., Frampton, J., Smith, B., Shaw, C. E., and de Belleroche, J. (2013). Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis. Free Radic. Biol. Med. 58, 81–86. doi: 10.1016/j.freeradbiomed.2013.01.001
    • (2013) Free Radic. Biol. Med. , vol.58 , pp. 81-86
    • Kwok, C.T.1    Morris, A.G.2    Frampton, J.3    Smith, B.4    Shaw, C.E.5    De Belleroche, J.6
  • 89
    • 84949512969 scopus 로고    scopus 로고
    • ENC1 modulates the aggregation and neurotoxicity of mutant huntingtin through p62 Under ER stress
    • Lee, H., Ahn, H. H., Lee, W., Oh, Y., Choi, H., Shim, S. M., et al. (2016). ENC1 modulates the aggregation and neurotoxicity of mutant huntingtin through p62 Under ER stress. Mol. Neurobiol. 53, 6620–6634. doi: 10.1007/s12035-015-9557-8
    • (2016) Mol. Neurobiol. , vol.53 , pp. 6620-6634
    • Lee, H.1    Ahn, H.H.2    Lee, W.3    Oh, Y.4    Choi, H.5    Shim, S.M.6
  • 90
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations
    • Lee, J. H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., and Peterhoff, C. M. (2010). Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell 141, 1146–1158. doi: 10.1016/j.cell.2010. 05.008
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1    Yu, W.H.2    Kumar, A.3    Lee, S.4    Mohan, P.S.5    Peterhoff, C.M.6
  • 91
    • 84991222851 scopus 로고    scopus 로고
    • Activation of HIPK2 promotes ER stress-mediated neurodegeneration in amyotrophic lateral sclerosis
    • Lee, S., Shang, Y., Redmond, S. A., Urisman, A., Tang, A. A., and Li, K. H. (2016). Activation of HIPK2 promotes ER stress-mediated neurodegeneration in amyotrophic lateral sclerosis. Neuron 91, 41–55. doi: 10.1016/j.neuron.2016. 05.021
    • (2016) Neuron , vol.91 , pp. 41-55
    • Lee, S.1    Shang, Y.2    Redmond, S.A.3    Urisman, A.4    Tang, A.A.5    Li, K.H.6
  • 92
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: Progress and prognosis
    • Lindquist, S. L., and Kelly, J. W. (2011). Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb. Perspect. Biol. 3:a004507. doi: 10.1101/cshperspect.a004507
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 93
    • 84875632050 scopus 로고    scopus 로고
    • Polymorphism -116C/G of human X-box-binding protein 1 promoter is associated with risk of Alzheimer’s disease
    • Liu, S. Y., Wang, W., Cai, Z. Y., Yao, L. F., Chen, Z. W., Wang, C. Y., et al. (2013). Polymorphism -116C/G of human X-box-binding protein 1 promoter is associated with risk of Alzheimer’s disease. CNS Neurosci. Ther. 19, 229–234. doi: 10.1111/cns.12064
    • (2013) CNS Neurosci. Ther. , vol.19 , pp. 229-234
    • Liu, S.Y.1    Wang, W.2    Cai, Z.Y.3    Yao, L.F.4    Chen, Z.W.5    Wang, C.Y.6
  • 95
    • 84889656503 scopus 로고    scopus 로고
    • TNF -α mediates PKR-dependent memory impairment and brain IRS-1 inhibition induced by Alzheimer’s β-amyloid oligomers in mice and monkeys
    • Lourenco, M. V., Clarke, J. R., Frozza, R. L., Bomfim, T. R., Forny-Germano, L., Batista, A. F., et al. (2013). TNF -α mediates PKR-dependent memory impairment and brain IRS-1 inhibition induced by Alzheimer’s β-amyloid oligomers in mice and monkeys. Cell Metab. 18, 831–843. doi: 10.1016/j.cmet. 2013.11.002
    • (2013) Cell Metab , vol.18 , pp. 831-843
    • Lourenco, M.V.1    Clarke, J.R.2    Frozza, R.L.3    Bomfim, T.R.4    Forny-Germano, L.5    Batista, A.F.6
  • 96
    • 78249273602 scopus 로고    scopus 로고
    • Sigma nonopioid intracellular receptor 1 mutations cause frontotemporal lobar degeneration-motor neuron disease
    • Luty, A. A., Kwok, J. B., Dobson-Stone, C., Loy, C. T., Coupland, K. G., Karlstrom, H., et al. (2010). Sigma nonopioid intracellular receptor 1 mutations cause frontotemporal lobar degeneration-motor neuron disease. Ann. Neurol. 68, 639–649. doi: 10.1002/ana.22274
    • (2010) Ann. Neurol. , vol.68 , pp. 639-649
    • Luty, A.A.1    Kwok, J.B.2    Dobson-Stone, C.3    Loy, C.T.4    Coupland, K.G.5    Karlstrom, H.6
  • 97
    • 84883453343 scopus 로고    scopus 로고
    • Suppression of eIF2α kinases alleviates Alzheimer’s disease-related plasticity and memory deficits
    • Ma, T., Trinh, M. A., Wexler, A. J., Bourbon, C., Gatti, E., Pierre, P., et al. (2013). Suppression of eIF2α kinases alleviates Alzheimer’s disease-related plasticity and memory deficits. Nat. Neurosci. 16, 1299–1305. doi: 10.1038/nn.3486
    • (2013) Nat. Neurosci. , vol.16 , pp. 1299-1305
    • Ma, T.1    Trinh, M.A.2    Wexler, A.J.3    Bourbon, C.4    Gatti, E.5    Pierre, P.6
  • 98
    • 77956700757 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress defined by activated unfolded protein response in multiple system atrophy
    • Makioka, K., Yamazaki, T., Fujita, Y., Takatama, M., Nakazato, Y., and Okamoto, K. (2010). Involvement of endoplasmic reticulum stress defined by activated unfolded protein response in multiple system atrophy. J. Neurol. Sci. 297, 60–65. doi: 10.1016/j.jns.2010.06.019
    • (2010) J. Neurol. Sci. , vol.297 , pp. 60-65
    • Makioka, K.1    Yamazaki, T.2    Fujita, Y.3    Takatama, M.4    Nakazato, Y.5    Okamoto, K.6
  • 99
    • 79960361814 scopus 로고    scopus 로고
    • Recent advances in the genetics of Parkinson’s disease
    • Martin, I., Dawson, V. L., and Dawson, T. M. (2011). Recent advances in the genetics of Parkinson’s disease. Annu. Rev. Genomics Hum. Genet. 12, 301–325. doi: 10.1146/annurev-genom-082410-101440
    • (2011) Annu. Rev. Genomics Hum. Genet. , vol.12 , pp. 301-325
    • Martin, I.1    Dawson, V.L.2    Dawson, T.M.3
  • 100
    • 84864866226 scopus 로고    scopus 로고
    • Hormesis: Protecting neurons against cellular stress in Parkinson disease
    • Matus, S., Castillo, K., and Hetz, C. (2012). Hormesis: protecting neurons against cellular stress in Parkinson disease. Autophagy 8, 997–1001. doi: 10.4161/auto. 20748
    • (2012) Autophagy , vol.8 , pp. 997-1001
    • Matus, S.1    Castillo, K.2    Hetz, C.3
  • 101
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: A glimpse into the ER
    • Matus, S., Glimcher, L. H., and Hetz, C. (2011). Protein folding stress in neurodegenerative diseases: a glimpse into the ER. Curr. Opin. Cell Biol. 23, 239–252. doi: 10.1016/j.ceb.2011.01.003
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 239-252
    • Matus, S.1    Glimcher, L.H.2    Hetz, C.3
  • 102
    • 84880423261 scopus 로고    scopus 로고
    • Functional role of the transcription factor ATF4 in the pathogenesis of amyotrophic lateral sclerosis
    • Matus, S., Lopez, E., Valenzuela, V., and Hetz, C. (2013). Functional role of the transcription factor ATF4 in the pathogenesis of amyotrophic lateral sclerosis. PLoS ONE 8:e66672. doi: 10.1371/journal.pone.0066672
    • (2013) Plos ONE , vol.8
    • Matus, S.1    Lopez, E.2    Valenzuela, V.3    Hetz, C.4
  • 103
    • 73449097110 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system reveals a homeostatic switch to activate autophagy
    • Matus, S., Nassif, M., Glimcher, L. H., and Hetz, C. (2009). XBP-1 deficiency in the nervous system reveals a homeostatic switch to activate autophagy. Autophagy 5, 1226–1228. doi: 10.4161/auto.5.8.10247
    • (2009) Autophagy , vol.5 , pp. 1226-1228
    • Matus, S.1    Nassif, M.2    Glimcher, L.H.3    Hetz, C.4
  • 104
    • 79960009804 scopus 로고    scopus 로고
    • Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies
    • Mazzulli, J. R., Xu, Y. H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., et al. (2011). Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell 146, 37–52. doi: 10.1016/j.cell.2011.06.001
    • (2011) Cell , vol.146 , pp. 37-52
    • Mazzulli, J.R.1    Xu, Y.H.2    Sun, Y.3    Knight, A.L.4    McLean, P.J.5    Caldwell, G.A.6
  • 105
    • 84883605293 scopus 로고    scopus 로고
    • Insights on altered mitochondrial function and dynamics in the pathogenesis of neurodegeneration
    • McInnes, J. (2013). Insights on altered mitochondrial function and dynamics in the pathogenesis of neurodegeneration. Transl. Neurodegener. 2:12. doi: 10.1186/2047-9158-2-12
    • (2013) Transl. Neurodegener. , vol.2 , pp. 12
    • McInnes, J.1
  • 107
    • 84929903016 scopus 로고    scopus 로고
    • Compromised autophagy and neurodegenerative diseases
    • Menzies, F. M., Fleming, A., and Rubinsztein, D. C. (2015). Compromised autophagy and neurodegenerative diseases. Nat. Rev. Neurosci. 16, 345–357. doi: 10.1038/nrn3961
    • (2015) Nat. Rev. Neurosci. , vol.16 , pp. 345-357
    • Menzies, F.M.1    Fleming, A.2    Rubinsztein, D.C.3
  • 108
    • 23144451257 scopus 로고    scopus 로고
    • ERAD: The long road to destruction
    • Meusser, B., Hirsch, C., Jarosch, E., and Sommer, T. (2005). ERAD: the long road to destruction. Nat. Cell Biol. 7, 766–772. doi: 10.1038/ncb0805-766
    • (2005) Nat. Cell Biol. , vol.7 , pp. 766-772
    • Meusser, B.1    Hirsch, C.2    Jarosch, E.3    Sommer, T.4
  • 109
    • 33845311194 scopus 로고    scopus 로고
    • ATF4 regulates γ-secretase activity during amino acid imbalance
    • Mitsuda, T., Hayakawa, Y., Itoh, M., Ohta, K., and Nakagawa, T. (2007). ATF4 regulates γ-secretase activity during amino acid imbalance. Biochem. Biophys. Res. Commun. 352, 722–727. doi: 10.1016/j.bbrc.2006.11.075
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 722-727
    • Mitsuda, T.1    Hayakawa, Y.2    Itoh, M.3    Ohta, K.4    Nakagawa, T.5
  • 110
    • 84878980614 scopus 로고    scopus 로고
    • Establishing links between ER-hormesis and cancer
    • Mollereau, B. (2013). Establishing links between ER-hormesis and cancer. Mol. Cell Biol. 33, 2372–2374. doi: 10.1128/MCB.00315-13
    • (2013) Mol. Cell Biol , vol.33 , pp. 2372-2374
    • Mollereau, B.1
  • 111
    • 84885463900 scopus 로고    scopus 로고
    • Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice
    • Moreno, J. A., Halliday, M., Molloy, C., Radford, H., Verity, N., Axten, J. M., et al. (2013). Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice. Sci. Transl. Med. 5, 206ra138. doi: 10.1126/scitranslmed.3006767
    • (2013) Sci. Transl. Med. , vol.5
    • Moreno, J.A.1    Halliday, M.2    Molloy, C.3    Radford, H.4    Verity, N.5    Axten, J.M.6
  • 112
    • 84861450392 scopus 로고    scopus 로고
    • Sustained translational repression by eIF2α-P mediates prion neurodegeneration
    • Moreno, J. A., Radford, H., Peretti, D., Steinert, J. R., Verity, N., Martin, M. G., et al. (2012). Sustained translational repression by eIF2α-P mediates prion neurodegeneration. Nature 485, 507–511. doi: 10.1038/nature11058
    • (2012) Nature , vol.485 , pp. 507-511
    • Moreno, J.A.1    Radford, H.2    Peretti, D.3    Steinert, J.R.4    Verity, N.5    Martin, M.G.6
  • 113
    • 71949098172 scopus 로고    scopus 로고
    • Signalling pathways in the unfolded protein response: Development from yeast to mammals
    • Mori, K. (2009). Signalling pathways in the unfolded protein response: development from yeast to mammals. J. Biochem. 146, 743–750. doi: 10.1093/jb/mvp166
    • (2009) J. Biochem. , vol.146 , pp. 743-750
    • Mori, K.1
  • 114
    • 84897865656 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein, VAP, is required for ER protein quality control
    • Moustaqim-Barrette, A., Lin, Y. Q., Pradhan, S., Neely, G. G., Bellen, H. J., and Tsuda, H. (2014). The amyotrophic lateral sclerosis 8 protein, VAP, is required for ER protein quality control. Hum. Mol. Genet. 23, 1975–1989. doi: 10.1093/hmg/ddt594
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 1975-1989
    • Moustaqim-Barrette, A.1    Lin, Y.Q.2    Pradhan, S.3    Neely, G.G.4    Bellen, H.J.5    Tsuda, H.6
  • 115
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., et al. (2000). Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature 403, 98–103. doi: 10.1038/47513
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6
  • 116
    • 84964345529 scopus 로고    scopus 로고
    • β-Asarone Inhibits IRE1/XBP1 Endoplasmic Reticulum Stress Pathway in 6-OHDA-Induced Parkinsonian Rats
    • Ning, B., Deng, M., Zhang, Q., Wang, N., and Fang, Y. (2016). β-Asarone Inhibits IRE1/XBP1 Endoplasmic Reticulum Stress Pathway in 6-OHDA-Induced Parkinsonian Rats. Neurochem. Res. 41, 2097–2101. doi: 10.1007/s11064-016-1922-0
    • (2016) Neurochem. Res. , vol.41 , pp. 2097-2101
    • Ning, B.1    Deng, M.2    Zhang, Q.3    Wang, N.4    Fang, Y.5
  • 117
    • 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., Maruyama, T., Yokota, T., Fukutomi, H., et al. (2008). ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1. Genes Dev. 22, 1451–1464. doi: 10.1101/gad.1640108
    • (2008) Genes Dev , vol.22 , pp. 1451-1464
    • Nishitoh, H.1    Kadowaki, H.2    Nagai, A.3    Maruyama, T.4    Yokota, T.5    Fukutomi, H.6
  • 118
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., et al. (2002). ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16, 1345–1355. doi: 10.1101/gad.992302
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6
  • 119
    • 0033598996 scopus 로고    scopus 로고
    • A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
    • Niwa, M., Sidrauski, C., Kaufman, R. J., and Walter, P. (1999). A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell 99, 691–702. doi: 10.1016/S0092-8674(00) 81667-0
    • (1999) Cell , vol.99 , pp. 691-702
    • Niwa, M.1    Sidrauski, C.2    Kaufman, R.J.3    Walter, P.4
  • 120
    • 57649245230 scopus 로고    scopus 로고
    • Phosphorylation of the translation initiation factor eIF2α increases BACE1 levels and promotes amyloidogenesis
    • O’Connor, T., Sadleir, K. R., Maus, E., Velliquette, R. A., Zhao, J., Cole, S. L., et al. (2008). Phosphorylation of the translation initiation factor eIF2α increases BACE1 levels and promotes amyloidogenesis. Neuron 60, 988–1009. doi: 10.1016/j.neuron.2008.10.047
    • (2008) Neuron , vol.60 , pp. 988-1009
    • O’Connor, T.1    Sadleir, K.R.2    Maus, E.3    Velliquette, R.A.4    Zhao, J.5    Cole, S.L.6
  • 121
    • 17144417669 scopus 로고    scopus 로고
    • TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death
    • Ohoka, N., Yoshii, S., Hattori, T., Onozaki, K., and Hayashi, H. (2005). TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. EMBO J. 24, 1243–1255. doi: 10.1038/sj.emboj. 7600596
    • (2005) EMBO J , vol.24 , pp. 1243-1255
    • Ohoka, N.1    Yoshii, S.2    Hattori, T.3    Onozaki, K.4    Hayashi, H.5
  • 122
    • 84855896629 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress enhances γ-secretase activity
    • Ohta, K., Mizuno, A., Li, S., Itoh, M., Ueda, M., Ohta, E., et al. (2011). Endoplasmic reticulum stress enhances γ-secretase activity. Biochem. Biophys. Res. Commun. 416, 362–366. doi: 10.1016/j.bbrc.2011.11.042
    • (2011) Biochem. Biophys. Res. Commun. , vol.416 , pp. 362-366
    • Ohta, K.1    Mizuno, A.2    Li, S.3    Itoh, M.4    Ueda, M.5    Ohta, E.6
  • 123
    • 85016158513 scopus 로고    scopus 로고
    • The endoplasmic reticulum chaperone GRP78/BiP modulates prion propagation in vitro and in vivo
    • Park, K. W., Eun Kim, G. M., Morales, R., Moreno-Gonzalez, I., Concha-Marambio, L., Lee, A. S., et al. (2017). The endoplasmic reticulum chaperone GRP78/BiP modulates prion propagation in vitro and in vivo. Sci. Rep. 7:44723. doi: 10.1038/srep44723
    • (2017) Sci. Rep. , vol.7
    • Park, K.W.1    Eun Kim, G.M.2    Morales, R.3    Moreno-Gonzalez, I.4    Concha-Marambio, L.5    Lee, A.S.6
  • 124
    • 84958979045 scopus 로고    scopus 로고
    • Protein folding and misfolding, endoplasmic reticulum stress in neurodegenerative diseases: In trace of novel drug targets
    • Penke, B., Bogár, F., and Fülöp, L. (2016). Protein folding and misfolding, endoplasmic reticulum stress in neurodegenerative diseases: in trace of novel drug targets. Curr. Protein Pept. Sci. 17, 169–182. doi: 10.2174/1389203716666151102104653
    • (2016) Curr. Protein Pept. Sci. , vol.17 , pp. 169-182
    • Penke, B.1    Bogár, F.2    Fülöp, L.3
  • 126
    • 34250758642 scopus 로고    scopus 로고
    • ER stress triggers apoptosis by activating BH3-only protein Bim
    • Puthalakath, H., O’Reilly, L. A., Gunn, P., Lee, L., Kelly, P. N., Huntington, N. D., et al. (2007). ER stress triggers apoptosis by activating BH3-only protein Bim. Cell 129, 1337–1349. doi: 10.1016/j.cell.2007.04.027
    • (2007) Cell , vol.129 , pp. 1337-1349
    • Puthalakath, H.1    O’Reilly, L.A.2    Gunn, P.3    Lee, L.4    Kelly, P.N.5    Huntington, N.D.6
  • 127
    • 34547961744 scopus 로고    scopus 로고
    • Regulation of ERGIC-53 gene transcription in response to Endoplasmic Reticulum stress
    • Renna, M., Caporaso, M. G., Bonatti, S., Kaufman, R. J., and Remondelli, P. (2007). Regulation of ERGIC-53 gene transcription in response to Endoplasmic Reticulum stress. J. Biol. Chem. 282, 22499–22512. doi: 10.1074/jbc. M703778200
    • (2007) J. Biol. Chem. , vol.282 , pp. 22499-22512
    • Renna, M.1    Caporaso, M.G.2    Bonatti, S.3    Kaufman, R.J.4    Remondelli, P.5
  • 128
    • 33748690946 scopus 로고    scopus 로고
    • Nitric oxide-induced endoplasmic reticulum stress activates the expression of cargo receptor proteins and alters the glycoprotein transport to the Golgi complex
    • Renna, M., Faraonio, R., Bonatti, S., De Stefano, D., Carnuccio, R., Tajana, G., et al. (2006). Nitric oxide-induced endoplasmic reticulum stress activates the expression of cargo receptor proteins and alters the glycoprotein transport to the Golgi complex. Int. J. Biochem. Cell Biol. 38, 2040–2048. doi: 10.1016/j. biocel.2006.05.016
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 2040-2048
    • Renna, M.1    Faraonio, R.2    Bonatti, S.3    De Stefano, D.4    Carnuccio, R.5    Tajana, G.6
  • 129
    • 79551546749 scopus 로고    scopus 로고
    • Autophagic substrate clearance requires activity of the Syntaxin-5 SNARE complex
    • Renna, M., Schaffner, C., Winslow, A. R., Menzies, F. M., Peden, A. A., Floto, R. A., et al. (2011). Autophagic substrate clearance requires activity of the Syntaxin-5 SNARE complex. J. Cell Sci. 124, 469–482. doi: 10.1242/jcs.076489
    • (2011) J. Cell Sci. , vol.124 , pp. 469-482
    • Renna, M.1    Schaffner, C.2    Winslow, A.R.3    Menzies, F.M.4    Peden, A.A.5    Floto, R.A.6
  • 130
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D., and Walter, P. (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519–529. doi: 10.1038/nrm2199
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 133
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein, D. C., Codogno, P., and Levine, B. (2012). Autophagy modulation as a potential therapeutic target for diverse diseases. Nat. Rev. Drug Discov. 11, 709–730. doi: 10.1038/nrd3802
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 134
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • Rutkowski, D. T., Arnold, S. M., Miller, C. N., Wu, J., Li, J., Gunnison, K. M., et al. (2006). Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. PLoS Biol. 4:e374. doi: 10.1371/journal.pbio.0040374
    • (2006) Plos Biol , vol.4
    • Rutkowski, D.T.1    Arnold, S.M.2    Miller, C.N.3    Wu, J.4    Li, J.5    Gunnison, K.M.6
  • 135
    • 84885456003 scopus 로고    scopus 로고
    • The ire-1 ER stress-response pathway is required for normal secretory-protein metabolism in C. Elegans
    • Safra, M., Ben-Hamo, S., Kenyon, C., and Henis-Korenblit, S. (2013). The ire-1 ER stress-response pathway is required for normal secretory-protein metabolism in C. elegans. J. Cell Sci. 126, 4136–4146. doi: 10.1242/jcs.123000
    • (2013) J. Cell Sci. , vol.126 , pp. 4136-4146
    • Safra, M.1    Ben-Hamo, S.2    Kenyon, C.3    Henis-Korenblit, S.4
  • 136
    • 67650233672 scopus 로고    scopus 로고
    • Caenorhabditits elegans LRK-1 and PINK-1 act antagonistically in stress response and neurite outgrowth
    • Samann, J., Hegermann, J., von Gromoff, E., Eimer, S., Baumeister, R., Schmidt, E., et al. (2009). Caenorhabditits elegans LRK-1 and PINK-1 act antagonistically in stress response and neurite outgrowth. J. Biol. Chem. 284, 16482–16491. doi: 10.1074/jbc.M808255200
    • (2009) J. Biol. Chem. , vol.284 , pp. 16482-16491
    • Samann, J.1    Hegermann, J.2    Von Gromoff, E.3    Eimer, S.4    Baumeister, R.5    Schmidt, E.6
  • 137
    • 84983339547 scopus 로고    scopus 로고
    • Parkinson disease-linked GBA mutation effects reversed by molecular chaperones in human cell and fly models
    • Sanchez-Martinez, A., Beavan, M., Gegg, M. E., Chau, K. Y., Whitworth, A. J., and Schapira, A. H. (2016). Parkinson disease-linked GBA mutation effects reversed by molecular chaperones in human cell and fly models. Sci. Rep. 6:31380. doi: 10.1038/srep31380
    • (2016) Sci. Rep , vol.6
    • Sanchez-Martinez, A.1    Beavan, M.2    Gegg, M.E.3    Chau, K.Y.4    Whitworth, A.J.5    Schapira, A.H.6
  • 138
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena, S., Cabuy, E., and Caroni, P. (2009). A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci. 12, 627–636. doi: 10.1038/nn.2297
    • (2009) Nat. Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 139
    • 84939562716 scopus 로고    scopus 로고
    • The unfolded protein response in neurodegenerative diseases: A neuropathological perspective
    • Scheper, W., and Hoozemans, J. J. (2015). The unfolded protein response in neurodegenerative diseases: a neuropathological perspective. Acta Neuropathol. 130, 315–331. doi: 10.1007/s00401-015-1462-8
    • (2015) Acta Neuropathol , vol.130 , pp. 315-331
    • Scheper, W.1    Hoozemans, J.J.2
  • 140
    • 84911899819 scopus 로고    scopus 로고
    • Amyloid-β(Peptides are generated in mitochondria-associated endoplasmic reticulum membranes
    • Schreiner, B., Hedskog, L., Wiehager, B., and Ankarcrona, M. (2015). Amyloid-β(peptides are generated in mitochondria-associated endoplasmic reticulum membranes). J. Alzheimers Dis. 43, 369–374. doi: 10.3233/JAD-132543
    • (2015) J. Alzheimers Dis , vol.43 , pp. 369-374
    • Schreiner, B.1    Hedskog, L.2    Wiehager, B.3    Ankarcrona, M.4
  • 141
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M., and Kaufman, R. J. (2005). The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739–789. doi: 10.1146/annurev.biochem.73. 011303.074134
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 142
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J. (2003). Folding proteins in fatal ways. Nature 426, 900–904. doi: 10.1038/nature02264
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 143
    • 84963940232 scopus 로고    scopus 로고
    • Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death
    • Sellier, C., Campanari, M. L., Julie Corbier, C., Gaucherot, A., Kolb-Cheynel, I., Oulad-Abdelghani, M., et al. (2016). Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death. EMBO J. 35, 1276–1297. doi: 10.15252/embj.201593350
    • (2016) EMBO J , vol.35 , pp. 1276-1297
    • Sellier, C.1    Campanari, M.L.2    Julie Corbier, C.3    Gaucherot, A.4    Kolb-Cheynel, I.5    Oulad-Abdelghani, M.6
  • 144
    • 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, J. A., Wang, S., Lei, S., Birnbaumer, L., et al. (2012). Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling. J. Clin. Invest. 122, 1354–1367. doi: 10.1172/JCI61332
    • (2012) J. Clin. Invest. , vol.122 , pp. 1354-1367
    • Selvaraj, S.1    Sun, Y.2    Watt, J.A.3    Wang, S.4    Lei, S.5    Birnbaumer, L.6
  • 145
    • 84881530677 scopus 로고    scopus 로고
    • Pharmacological brake-release of mRNA translation enhances cognitive memory
    • Sidrauski, C., Acosta-Alvear, D., Khoutorsky, A., Vedantham, P., Hearn, B. R., Li, H., et al. (2013). Pharmacological brake-release of mRNA translation enhances cognitive memory. eLife 2:e00498. doi: 10.7554/eLife.00498
    • (2013) Elife , vol.2
    • Sidrauski, C.1    Acosta-Alvear, D.2    Khoutorsky, A.3    Vedantham, P.4    Hearn, B.R.5    Li, H.6
  • 146
    • 84964694840 scopus 로고    scopus 로고
    • The small molecule ISRIB reverses the effects of eIF2α phosphorylation on translation and stress granule assembly
    • Sidrauski, C., McGeachy, A. M., Ingolia, N. T., and Walter, P. (2015). The small molecule ISRIB reverses the effects of eIF2α phosphorylation on translation and stress granule assembly. eLife 4, e05033. doi: 10.7554/eLife.05033.131
    • (2015) Elife , vol.4
    • Sidrauski, C.1    McGeachy, A.M.2    Ingolia, N.T.3    Walter, P.4
  • 147
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia, R., and Braakman, I. (2003). Quality control in the endoplasmic reticulum protein factory. Nature 426, 891–894. doi: 10.1038/nature02262
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 149
    • 84861559058 scopus 로고    scopus 로고
    • Transmissible proteins: Expanding the prion heresy
    • Soto, C. (2012). Transmissible proteins: expanding the prion heresy. Cell 149, 968–977. doi: 10.1016/j.cell.2012.05.007
    • (2012) Cell , vol.149 , pp. 968-977
    • Soto, C.1
  • 150
    • 5644240873 scopus 로고    scopus 로고
    • Heat Shock induces preferential translation of ERGIC-53 and affects its recycling pathway
    • Spatuzza, C., Renna, M., Faraonio, R., Cardinali, G., Martire, G., Bonatti, S., et al. (2004). Heat Shock induces preferential translation of ERGIC-53 and affects its recycling pathway. J. Biol. Chem. 279, 42535–42544. doi: 10.1074/jbc. M401860200
    • (2004) J. Biol. Chem. , vol.279 , pp. 42535-42544
    • Spatuzza, C.1    Renna, M.2    Faraonio, R.3    Cardinali, G.4    Martire, G.5    Bonatti, S.6
  • 151
    • 51649103992 scopus 로고    scopus 로고
    • Prion pathogenesis is independent of caspase-12
    • Steele, A. D., Hetz, C., Yi, C. H., Jackson, W. S., Borkowski, A. W., Yuan, J., et al. (2007). Prion pathogenesis is independent of caspase-12. Prion 1, 243–247. doi: 10.4161/pri.1.4.5551
    • (2007) Prion , vol.1 , pp. 243-247
    • Steele, A.D.1    Hetz, C.2    Yi, C.H.3    Jackson, W.S.4    Borkowski, A.W.5    Yuan, J.6
  • 152
    • 58549088349 scopus 로고    scopus 로고
    • ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB
    • Suzuki, H., Kanekura, K., Levine, T. P., Kohno, K., Olkkonen, V. M., Aiso, S., et al. (2009). ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB. J. Neurochem. 108, 973–985. doi: 10.1111/j.0022-3042.2008.05857.x
    • (2009) J. Neurochem , vol.108 , pp. 973-985
    • Suzuki, H.1    Kanekura, K.2    Levine, T.P.3    Kohno, K.4    Olkkonen, V.M.5    Aiso, S.6
  • 153
    • 0041963057 scopus 로고    scopus 로고
    • Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1
    • Tang, T. S., Tu, H., Chan, E. Y., Maximov, A., Wang, Z., Wellington, C. L., et al. (2003). Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39, 227–239. doi: 10.1016/S0896-6273(03)00366-0
    • (2003) Neuron , vol.39 , pp. 227-239
    • Tang, T.S.1    Tu, H.2    Chan, E.Y.3    Maximov, A.4    Wang, Z.5    Wellington, C.L.6
  • 154
    • 84876533723 scopus 로고    scopus 로고
    • Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: Genetics and neuropathology
    • Teyssou, E., Takeda, T., Lebon, V., Boillée, S., Doukouré, B., Bataillon, G., et al. (2013). Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology. Acta Neuropathol. 125, 511–522. doi: 10.1007/s00401-013-1090-0
    • (2013) Acta Neuropathol , vol.125 , pp. 511-522
    • Teyssou, E.1    Takeda, T.2    Lebon, V.3    Boillée, S.4    Doukouré, B.5    Bataillon, G.6
  • 155
    • 77952900626 scopus 로고    scopus 로고
    • α-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi, N., Helm, J. R., Nycz, D. C., Bentley, M., Liang, Y., and Hay, J. C. (2010). α-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol. Biol. Cell 21, 1850–1863. doi: 10.1091/mbc.E09-09-0801
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 156
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres, M., Castillo, K., Armisén, R., Stutzin, A., Soto, C., and Hetz, C. (2010). Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS ONE 5:e15658. doi: 10.1371/journal.pone. 0015658
    • (2010) Plos ONE , vol.5
    • Torres, M.1    Castillo, K.2    Armisén, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 157
    • 12144249923 scopus 로고    scopus 로고
    • Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis
    • Turner, B. J., Atkin, J. D., Farg, M. A., Zang, D. W., Rembach, A., Lopes, E. C., et al. (2005). Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J. Neurosci. 25, 108–117. doi: 10.1523/JNEUROSCI.4253-04.2005
    • (2005) J. Neurosci. , vol.25 , pp. 108-117
    • Turner, B.J.1    Atkin, J.D.2    Farg, M.A.3    Zang, D.W.4    Rembach, A.5    Lopes, E.C.6
  • 158
    • 80052254663 scopus 로고    scopus 로고
    • Mutant Atp13a2 proteins involved in parkinsonism are degraded by ER-associated degradation and sensitize cells to ER-stress induced cell death
    • Ugolino, J., Fang, S., Kubisch, C., and Monteiro, M. J. (2011). Mutant Atp13a2 proteins involved in parkinsonism are degraded by ER-associated degradation and sensitize cells to ER-stress induced cell death. Hum. Mol. Genet. 20, 3565–3577. doi: 10.1093/hmg/ddr274
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 3565-3577
    • Ugolino, J.1    Fang, S.2    Kubisch, C.3    Monteiro, M.J.4
  • 159
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani, M., Sik, A., Sakurai, T., Nukina, N., Takahashi, R., and Julien, J. P. (2006). Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci. 9, 108–118. doi: 10.1038/nn1603
    • (2006) Nat. Neurosci. , vol.9 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.P.6
  • 160
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of α-synuclein aggregation
    • Uversky, V. N. (2007). Neuropathology, biochemistry, and biophysics of α-synuclein aggregation. J. Neurochem. 103, 17–37. doi: 10.1111/j.1471-4159. 2007.04764.x
    • (2007) J. Neurochem. , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 161
    • 84892408458 scopus 로고    scopus 로고
    • Mechanisms of protein-folding diseases at a glance
    • Valastyan, J. S., and Lindquist, S. (2014). Mechanisms of protein-folding diseases at a glance. Dis. Model Mech. 7, 9–14. doi: 10.1242/dmm.013474
    • (2014) Dis. Model Mech. , vol.7 , pp. 9-14
    • Valastyan, J.S.1    Lindquist, S.2
  • 162
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson’s disease caused by mutations in PINK1
    • Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M., Harvey, K., Gispert, S., et al. (2004). Hereditary early-onset Parkinson’s disease caused by mutations in PINK1. Science 304, 1158–1160. doi: 10.1126/science.1096284
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3    Muqit, M.M.4    Harvey, K.5    Gispert, S.6
  • 163
    • 0038182518 scopus 로고    scopus 로고
    • P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling
    • van Huizen, R., Martindale, J. L., Gorospe, M., and Holbrook, N. J. (2003). P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling. J. Biol. Chem. 278, 15558–15564. doi: 10.1074/jbc.M212074200
    • (2003) J. Biol. Chem. , vol.278 , pp. 15558-15564
    • Van Huizen, R.1    Martindale, J.L.2    Gorospe, M.3    Holbrook, N.J.4
  • 164
    • 84860471873 scopus 로고    scopus 로고
    • Targeting the UPR transcription factor XBP1 protects against Huntington’s disease through the regulation of FoxO1 and autophagy
    • Vidal, R. L., Figueroa, A., Court, F. A., Thielen, P., Molina, C., Wirth, C., et al. (2012). Targeting the UPR transcription factor XBP1 protects against Huntington’s disease through the regulation of FoxO1 and autophagy. Hum. Mol. Genet. 21, 2245–2262. doi: 10.1093/hmg/dds040
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2245-2262
    • Vidal, R.L.1    Figueroa, A.2    Court, F.A.3    Thielen, P.4    Molina, C.5    Wirth, C.6
  • 165
    • 84864878269 scopus 로고    scopus 로고
    • Crosstalk between the UPR and autophagy pathway contributes to handling cellular stress in neurodegenerative disease
    • Vidal, R. L., and Hetz, C. (2012). Crosstalk between the UPR and autophagy pathway contributes to handling cellular stress in neurodegenerative disease. Autophagy 8, 970–972. doi: 10.4161/auto.20139
    • (2012) Autophagy , vol.8 , pp. 970-972
    • Vidal, R.L.1    Hetz, C.2
  • 166
    • 84908386761 scopus 로고    scopus 로고
    • Targeting autophagy in neurodegenerative diseases
    • Vidal, R. L., Matus, S., Bargsted, L., and Hetz, C. (2014). Targeting autophagy in neurodegenerative diseases. Trends Pharmacol. Sci. 35, 583–591. doi: 10.1016/j. tips.2014.09.002
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 583-591
    • Vidal, R.L.1    Matus, S.2    Bargsted, L.3    Hetz, C.4
  • 167
    • 84942615942 scopus 로고    scopus 로고
    • Guanabenz treatment accelerates disease in a mutant SOD1 mouse model of ALS
    • Vieira, F. G., Ping, Q., Moreno, A. J., Kidd, J. D., Thompson, K., Jiang, B., et al. (2015). Guanabenz treatment accelerates disease in a mutant SOD1 mouse model of ALS. PLoS ONE 10:e0135570. doi: 10.1371/journal.pone.0135570
    • (2015) Plos ONE , vol.10
    • Vieira, F.G.1    Ping, Q.2    Moreno, A.J.3    Kidd, J.D.4    Thompson, K.5    Jiang, B.6
  • 168
    • 84948405715 scopus 로고    scopus 로고
    • Dysfunction of Endoplasmic Reticulum (ER) and Mitochondria (MT) in Alzheimer’s Disease: The role of the ER-MT cross-talk
    • Volgyi, K., Juhász, G., Kovacs, Z., and Penke, B. (2015). Dysfunction of Endoplasmic Reticulum (ER) and Mitochondria (MT) in Alzheimer’s Disease: the role of the ER-MT cross-talk. Curr. Alzheimer Res. 12, 655–672. doi: 10. 2174/1567205012666150710095035
    • (2015) Curr. Alzheimer Res. , vol.12 , pp. 655-672
    • Volgyi, K.1    Juhász, G.2    Kovacs, Z.3    Penke, B.4
  • 169
    • 84903774616 scopus 로고    scopus 로고
    • Loss of function of the ALS protein SigR1 leads to ER pathology associated with defective autophagy and lipid raft disturbances
    • Vollrath, J. T., Sechi, A., Dreser, A., Katona, I., Wiemuth, D., Vervoorts, J., et al. (2014). Loss of function of the ALS protein SigR1 leads to ER pathology associated with defective autophagy and lipid raft disturbances. Cell Death Dis. 5, e1290. doi: 10.1038/cddis.2014.243
    • (2014) Cell Death Dis , vol.5
    • Vollrath, J.T.1    Sechi, A.2    Dreser, A.3    Katona, I.4    Wiemuth, D.5    Vervoorts, J.6
  • 170
    • 74249084267 scopus 로고    scopus 로고
    • Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis
    • Walker, A. K., Farg, M. A., Bye, C. R., McLean, C. A., Horne, M. K., and Atkin, J. D. (2010). Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis. Brain 133, 105–116. doi: 10.1093/brain/awp267
    • (2010) Brain , vol.133 , pp. 105-116
    • Walker, A.K.1    Farg, M.A.2    Bye, C.R.3    McLean, C.A.4    Horne, M.K.5    Atkin, J.D.6
  • 171
    • 84896710448 scopus 로고    scopus 로고
    • ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation
    • Walker, A. K., Soo, K. Y., Sundaramoorthy, V., Parakh, S., Ma, Y., and Farg, M. A. (2013). ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PLoS ONE 8:e81170. doi: 10.1371/journal.pone.0081170
    • (2013) Plos ONE , vol.8
    • Walker, A.K.1    Soo, K.Y.2    Sundaramoorthy, V.3    Parakh, S.4    Ma, Y.5    Farg, M.A.6
  • 172
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P., and Ron, D. (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081–1086. doi: 10.1126/science.1209038
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 173
    • 79551584057 scopus 로고    scopus 로고
    • The unfolded protein response in familial amyotrophic lateral sclerosis
    • Wang, L., Popko, B., and Roos, R. P. (2011). The unfolded protein response in familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 20, 1008–1015. doi: 10.1093/hmg/ddq546
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1008-1015
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 174
    • 84906712846 scopus 로고    scopus 로고
    • The impact of the endoplasmic reticulum protein-folding environment on cancer development
    • Wang, M., and Kaufman, R. J. (2014). The impact of the endoplasmic reticulum protein-folding environment on cancer development. Nat. Rev. Cancer 14, 581–597. doi: 10.1038/nrc3800
    • (2014) Nat. Rev. Cancer , vol.14 , pp. 581-597
    • Wang, M.1    Kaufman, R.J.2
  • 175
    • 9644297858 scopus 로고    scopus 로고
    • Rotenone induces apoptosis via activation of bad in human dopaminergic SH-SY5Y cells
    • Watabe, M., and Nakaki, T. (2004). Rotenone induces apoptosis via activation of bad in human dopaminergic SH-SY5Y cells. J. Pharmacol. Exp. Ther. 311, 948–953. doi: 10.1124/jpet.104.071381
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 948-953
    • Watabe, M.1    Nakaki, T.2
  • 176
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong, E., and Cuervo, A. M. (2010). Autophagy gone awry in neurodegenerative diseases. Nat. Neurosci. 13, 805–811. doi: 10.1038/nn.2575
    • (2010) Nat. Neurosci. , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 177
    • 84860513477 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and prion diseases
    • Xu, K., and Zhu, X. P. (2012). Endoplasmic reticulum stress and prion diseases. Rev. Neurosci. 23, 79–84. doi: 10.1515/rns.2011.062
    • (2012) Rev. Neurosci , vol.23 , pp. 79-84
    • Xu, K.1    Zhu, X.P.2
  • 178
    • 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, M. J., and Fang, S. (2010). Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS ONE 5:e8905. doi: 10.1371/journal.pone.0008905
    • (2010) Plos ONE , vol.5
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 179
    • 84969849520 scopus 로고    scopus 로고
    • Rescue of glaucomatous neurodegeneration by differentially modulating neuronal endoplasmic reticulum stress molecules
    • Yang, L., Li, S., Miao, L., Huang, H., Liang, F., Teng, X., et al. (2016). Rescue of glaucomatous neurodegeneration by differentially modulating neuronal endoplasmic reticulum stress molecules. J. Neurosci. 36, 5891–5903. doi: 10.1523/JNEUROSCI.3709-15.2016
    • (2016) J. Neurosci. , vol.36 , pp. 5891-5903
    • Yang, L.1    Li, S.2    Miao, L.3    Huang, H.4    Liang, F.5    Teng, X.6
  • 180
    • 84963680128 scopus 로고    scopus 로고
    • Repression of the eIF2α kinase PERK alleviates mGluR-LTD impairments in a mouse model of Alzheimer’s disease
    • Yang, W., Zhou, X., Zimmermann, H. R., Cavener, D. R., Klann, E., and Ma, T. (2016). Repression of the eIF2α kinase PERK alleviates mGluR-LTD impairments in a mouse model of Alzheimer’s disease. Neurobiol. Aging 41, 19–24. doi: 10.1016/j.neurobiolaging.2016.02.005
    • (2016) Neurobiol. Aging , vol.41 , pp. 19-24
    • Yang, W.1    Zhou, X.2    Zimmermann, H.R.3    Cavener, D.R.4    Klann, E.5    Ma, T.6
  • 181
    • 0032475957 scopus 로고    scopus 로고
    • The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Aβ40 and Aβ42 secretion
    • Yang, Y., Turner, R. S., and Gaut, J. R. (1998). The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Aβ40 and Aβ42 secretion. J. Biol. Chem. 273, 25552–25555. doi: 10.1074/jbc.273.40.25552
    • (1998) J. Biol. Chem. , vol.273 , pp. 25552-25555
    • Yang, Y.1    Turner, R.S.2    Gaut, J.R.3
  • 182
    • 84865966647 scopus 로고    scopus 로고
    • JNK3 perpetuates metabolic stress induced by Aβ peptides
    • Yoon, S. O., Park, D. J., Ryu, J. C., Ozer, H. G., Tep, C., Shin, Y. J., et al. (2012). JNK3 perpetuates metabolic stress induced by Aβ peptides. Neuron 75, 824–837. doi: 10.1016/j.neuron.2012.06.024
    • (2012) Neuron , vol.75 , pp. 824-837
    • Yoon, S.O.1    Park, D.J.2    Ryu, J.C.3    Ozer, H.G.4    Tep, C.5    Shin, Y.J.6
  • 183
    • 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, M. A., Kramp, K., Huang, Y., Hisamoto, N., et al. (2011). Dysregulated LRRK2 signaling in response to endoplasmic reticulum stress leads to dopaminergic neuron degeneration in C. elegans. PLoS ONE 6:e22354. doi: 10.1371/journal.pone.0022354
    • (2011) Plos ONE , vol.6
    • Yuan, Y.1    Cao, P.2    Smith, M.A.3    Kramp, K.4    Huang, Y.5    Hisamoto, N.6
  • 184
    • 84963556483 scopus 로고    scopus 로고
    • Stromal Interaction Molecule 1 rescues store-operated calcium entry and protects NG115-401L cells against cell death induced by endoplasmic reticulum and mitochondrial oxidative stress
    • Zhang, C., and Thomas, T. W. (2016). Stromal Interaction Molecule 1 rescues store-operated calcium entry and protects NG115-401L cells against cell death induced by endoplasmic reticulum and mitochondrial oxidative stress. Neurochem. Int. 97, 137–145. doi: 10.1016/j.neuint.2016.04.002
    • (2016) Neurochem. Int. , vol.97 , pp. 137-145
    • Zhang, C.1    Thomas, T.W.2
  • 185
    • 33645996396 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum and the unfolded protein response
    • Zhang, K., and Kaufman, R. J. (2006). Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb. Exp. Pharmacol. 172, 69–91. doi: 10.1007/3-540-29717-0_3
    • (2006) Handb. Exp. Pharmacol. , vol.172 , pp. 69-91
    • Zhang, K.1    Kaufman, R.J.2
  • 186
    • 33745844503 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in health and disease
    • Zhao, L., and Ackerman, S. L. (2006). Endoplasmic reticulum stress in health and disease. Curr. Opin. Cell Biol. 18, 444–452. doi: 10.1016/j.ceb.2006.06.005
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 444-452
    • Zhao, L.1    Ackerman, S.L.2
  • 187
    • 84876416042 scopus 로고    scopus 로고
    • XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells
    • Zhao, Y., Li, X., Cai, M. Y., Ma, K., Yang, J., Zhou, J., et al. (2013). XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells. Cell Res. 23, 491–507. doi: 10.1038/cr.2013.2
    • (2013) Cell Res , vol.23 , pp. 491-507
    • Zhao, Y.1    Li, X.2    Cai, M.Y.3    Ma, K.4    Yang, J.5    Zhou, J.6
  • 188
    • 79952381078 scopus 로고    scopus 로고
    • Regulation of glucose omeostasis through a XBP-1-FoxO1 interaction
    • Zhou, Y., Lee, J., Reno, C. M., Sun, C., Park, S. W., Chung, J., et al. (2011). Regulation of glucose omeostasis through a XBP-1-FoxO1 interaction. Nat. Med. 17, 356–365. doi: 10.1038/nm.2293
    • (2011) Nat. Med. , vol.17 , pp. 356-365
    • Zhou, Y.1    Lee, J.2    Reno, C.M.3    Sun, C.4    Park, S.W.5    Chung, J.6
  • 189
    • 84937426124 scopus 로고    scopus 로고
    • Allicin improves endoplasmic reticulum stress-related cognitive deficits via PERK/Nrf2 antioxidative signaling pathway
    • Zhu, Y. F., Li, X. H., Yuan, Z. P., Li, C. Y., Tian, R. B., Jia, W., et al. (2015). Allicin improves endoplasmic reticulum stress-related cognitive deficits via PERK/Nrf2 antioxidative signaling pathway. Eur. J. Pharmacol. 762, 239–246. doi: 10.1016/j.ejphar.2015.06.002
    • (2015) Eur. J. Pharmacol. , vol.762 , pp. 239-246
    • Zhu, Y.F.1    Li, X.H.2    Yuan, Z.P.3    Li, C.Y.4    Tian, R.B.5    Jia, W.6
  • 190
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H., et al. (1998). CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev. 12, 982–995. doi: 10.1101/gad.12.7.982
    • (1998) Genes Dev , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Lightfoot, R.T.5    Remotti, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.