메뉴 건너뛰기




Volumn 9, Issue JUL, 2015, Pages

The unfolded protein response in multiple sclerosis

Author keywords

Demyelination; Endoplasmic reticulum stress; Experimental autoimmune encephalomyelitis; Multiple sclerosis; Oligodendrocytes; Pancreatic endoplasmic reticulum kinase; Remyelination; Unfolded protein response

Indexed keywords

ENZYME INHIBITOR; GAMMA INTERFERON; GSK 2606414; GSK 2656157; GUANABENZ; INITIATION FACTOR 2ALPHA; UNCLASSIFIED DRUG;

EID: 84938520346     PISSN: 16624548     EISSN: 1662453X     Source Type: Journal    
DOI: 10.3389/fnins.2015.00264     Document Type: Review
Times cited : (75)

References (132)
  • 1
    • 33744548450 scopus 로고    scopus 로고
    • Myelin biogenesis: sorting out protein trafficking
    • Anitei, M., and Pfeiffer, S. E. (2006). Myelin biogenesis: sorting out protein trafficking. Curr. Biol. 16, R418-R421. doi: 10.1016/j.cub.2006.05.010.
    • (2006) Curr. Biol , vol.16 , pp. R418-R421
    • Anitei, M.1    Pfeiffer, S.E.2
  • 2
    • 84861222698 scopus 로고    scopus 로고
    • The specialized unfolded protein response of B lymphocytes: ATF6α-independent development of antibody-secreting B cells
    • Aragon, I. V., Barrington, R. A., Jackowski, S., Mori, K., and Brewer, J. W. (2012). The specialized unfolded protein response of B lymphocytes: ATF6α-independent development of antibody-secreting B cells. Mol. Immunol. 51, 347-355. doi: 10.1016/j.molimm.2012.04.001.
    • (2012) Mol. Immunol , vol.51 , pp. 347-355
    • Aragon, I.V.1    Barrington, R.A.2    Jackowski, S.3    Mori, K.4    Brewer, J.W.5
  • 3
    • 84875235453 scopus 로고    scopus 로고
    • Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity
    • Atkins, C., Liu, Q., Minthorn, E., Zhang, S. Y., Figueroa, D. J., Moss, K., et al. (2013). Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity. Cancer. Res. 73, 1993-2002. doi: 10.1158/0008-5472.CAN-12-3109.
    • (2013) Cancer. Res , vol.73 , pp. 1993-2002
    • Atkins, C.1    Liu, Q.2    Minthorn, E.3    Zhang, S.Y.4    Figueroa, D.J.5    Moss, K.6
  • 4
    • 84866905708 scopus 로고    scopus 로고
    • Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK)
    • Axten, J. M., Medina, J. R., Feng, Y., Shu, A., Romeril, S. P., Grant, S. W., et al. (2012). Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK). J. Med. Chem. 55, 7193-7207. doi: 10.1021/jm300713s.
    • (2012) J. Med. Chem , vol.55 , pp. 7193-7207
    • Axten, J.M.1    Medina, J.R.2    Feng, Y.3    Shu, A.4    Romeril, S.P.5    Grant, S.W.6
  • 5
    • 33847223756 scopus 로고    scopus 로고
    • Interferon-gamma-oligodendrocyte interactions in the regulation of experimental autoimmune encephalomyelitis
    • Balabanov, R., Strand, K., Goswami, R., McMahon, E., Begolka, W., Miller, S. D., et al. (2007). Interferon-gamma-oligodendrocyte interactions in the regulation of experimental autoimmune encephalomyelitis. J. Neurosci. 27, 2013-2024. doi: 10.1523/JNEUROSCI.4689-06.2007.
    • (2007) J. Neurosci , vol.27 , pp. 2013-2024
    • Balabanov, R.1    Strand, K.2    Goswami, R.3    McMahon, E.4    Begolka, W.5    Miller, S.D.6
  • 6
    • 84877872994 scopus 로고    scopus 로고
    • Oligodendroglia and neurotrophic factors in neurodegeneration
    • Bankston, A. N., Mandler, M. D., and Feng, Y. (2013). Oligodendroglia and neurotrophic factors in neurodegeneration. Neurosci. Bull. 29, 216-228. doi: 10.1007/s12264-013-1321-3.
    • (2013) Neurosci. Bull , vol.29 , pp. 216-228
    • Bankston, A.N.1    Mandler, M.D.2    Feng, Y.3
  • 7
    • 1642281535 scopus 로고    scopus 로고
    • Relapsing and remitting multiple sclerosis: pathology of the newly forming lesion
    • Barnett, M. H., and Prineas, J. W. (2004). Relapsing and remitting multiple sclerosis: pathology of the newly forming lesion. Ann. Neurol. 55, 458-468. doi: 10.1002/ana.20016.
    • (2004) Ann. Neurol , vol.55 , pp. 458-468
    • Barnett, M.H.1    Prineas, J.W.2
  • 8
    • 35549010987 scopus 로고    scopus 로고
    • The origin and application of experimental autoimmune encephalomyelitis
    • Baxter, A. G. (2007). The origin and application of experimental autoimmune encephalomyelitis. Nat. Rev. Immunol. 7, 904-912. doi: 10.1038/nri2190.
    • (2007) Nat. Rev. Immunol , vol.7 , pp. 904-912
    • Baxter, A.G.1
  • 9
    • 67650000500 scopus 로고    scopus 로고
    • ATF6alpha induces XBP1-independent expansion of the endoplasmic reticulum
    • Bommiasamy, H., Back, S. H., Fagone, P., Lee, K., Meshinchi, S., Vink, E., et al. (2009). ATF6alpha induces XBP1-independent expansion of the endoplasmic reticulum. J. Cell. Sci. 122, 1626-1636. doi: 10.1242/jcs.045625.
    • (2009) J. Cell. Sci , vol.122 , pp. 1626-1636
    • Bommiasamy, H.1    Back, S.H.2    Fagone, P.3    Lee, K.4    Meshinchi, S.5    Vink, E.6
  • 10
    • 13644256191 scopus 로고    scopus 로고
    • A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress
    • Boyce, M., Bryant, K. F., Jousse, C., Long, K., Harding, H. P., Scheuner, D., et al. (2005). A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science 307, 935-939. doi: 10.1126/science.1101902.
    • (2005) Science , vol.307 , pp. 935-939
    • Boyce, M.1    Bryant, K.F.2    Jousse, C.3    Long, K.4    Harding, H.P.5    Scheuner, D.6
  • 11
    • 77649192930 scopus 로고    scopus 로고
    • Oligodendrocytes: biology and pathology
    • Bradl, M., and Lassmann, H. (2010). Oligodendrocytes: biology and pathology. Acta Neuropathol. 119, 37-53. doi: 10.1007/s00401-009-0601-5.
    • (2010) Acta Neuropathol , vol.119 , pp. 37-53
    • Bradl, M.1    Lassmann, H.2
  • 12
    • 12344256887 scopus 로고    scopus 로고
    • Building an antibody factory: a job for the unfolded protein response
    • Brewer, J. W., and Hendershot, L. M. (2005). Building an antibody factory: a job for the unfolded protein response. Nat. Immunol. 6, 23-29. doi: 10.1038/ni1149.
    • (2005) Nat. Immunol , vol.6 , pp. 23-29
    • Brewer, J.W.1    Hendershot, L.M.2
  • 13
    • 84903795970 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease
    • Cao, S. S., and Kaufman, R. J. (2014). Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease. Antioxid. Redox Signal. 21, 396-413. doi: 10.1089/ars.2014.5851.
    • (2014) Antioxid. Redox Signal , vol.21 , pp. 396-413
    • Cao, S.S.1    Kaufman, R.J.2
  • 14
    • 2642538541 scopus 로고    scopus 로고
    • Immunohistochemical localization of phosphorylated protein kinase R and phosphorylated eukaryotic initiation factor-2 alpha in the central nervous system of SJL mice with experimental allergic encephalomyelitis
    • Chakrabarty, A., Danley, M. M., and LeVine, S. M. (2004). Immunohistochemical localization of phosphorylated protein kinase R and phosphorylated eukaryotic initiation factor-2 alpha in the central nervous system of SJL mice with experimental allergic encephalomyelitis. J. Neurosci. Res. 76, 822-833. doi: 10.1002/jnr.20125.
    • (2004) J. Neurosci. Res , vol.76 , pp. 822-833
    • Chakrabarty, A.1    Danley, M.M.2    LeVine, S.M.3
  • 15
    • 19344369610 scopus 로고    scopus 로고
    • Quantifying immunohistochemical staining of phospho-eIF2alpha, heme oxygenase-2 and NADPH cytochrome P450 reductase in oligodendrocytes during experimental autoimmune encephalomyelitis
    • Chakrabarty, A., Fleming, K. K., Marquis, J. G., and LeVine, S. M. (2005). Quantifying immunohistochemical staining of phospho-eIF2alpha, heme oxygenase-2 and NADPH cytochrome P450 reductase in oligodendrocytes during experimental autoimmune encephalomyelitis. J. Neurosci. Methods 144, 227-234. doi: 10.1016/j.jneumeth.2004.11.010.
    • (2005) J. Neurosci. Methods , vol.144 , pp. 227-234
    • Chakrabarty, A.1    Fleming, K.K.2    Marquis, J.G.3    LeVine, S.M.4
  • 16
    • 84886749523 scopus 로고    scopus 로고
    • IRE1: ER stress sensor and cell fate executor
    • Chen, Y., and Brandizzi, F. (2013). IRE1: ER stress sensor and cell fate executor. Trends Cell Biol. 23, 547-555. doi: 10.1016/j.tcb.2013.06.005.
    • (2013) Trends Cell Biol , vol.23 , pp. 547-555
    • Chen, Y.1    Brandizzi, F.2
  • 17
    • 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. (2012). 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
  • 18
    • 0030135421 scopus 로고    scopus 로고
    • Targeted CNS expression of interferon-gamma in transgenic mice leads to hypomyelination, reactive gliosis, and abnormal cerebellar development
    • Corbin, J. G., Kelly, D., Rath, E. M., Baerwald, K. D., Suzuki, K., and Popko, B. (1996). Targeted CNS expression of interferon-gamma in transgenic mice leads to hypomyelination, reactive gliosis, and abnormal cerebellar development. Mol. Cell Neurosci. 7, 354-370. doi: 10.1006/mcne.1996.0026.
    • (1996) Mol. Cell Neurosci , vol.7 , pp. 354-370
    • Corbin, J.G.1    Kelly, D.2    Rath, E.M.3    Baerwald, K.D.4    Suzuki, K.5    Popko, B.6
  • 20
    • 33645980003 scopus 로고    scopus 로고
    • Endoplasmic reticulum: a metabolic compartment
    • Csala, M., Bánhegyi, G., and Benedetti, A. (2006). Endoplasmic reticulum: a metabolic compartment. FEBS Lett. 580, 2160-2165. doi: 10.1016/j.febslet.2006.03.050.
    • (2006) FEBS Lett , vol.580 , pp. 2160-2165
    • Csala, M.1    Bánhegyi, G.2    Benedetti, A.3
  • 21
    • 79959503183 scopus 로고    scopus 로고
    • Expression profiles of endoplasmic reticulum stress-related molecules in demyelinating lesions and multiple sclerosis
    • Cunnea, P., Mháille, A. N., McQuaid, S., Farrell, M., McMahon, J., and Fitz Gerald, U. (2011). Expression profiles of endoplasmic reticulum stress-related molecules in demyelinating lesions and multiple sclerosis. Mult. Scler. 17, 808-818. doi: 10.1177/1352458511399114.
    • (2011) Mult. Scler , vol.17 , pp. 808-818
    • Cunnea, P.1    Mháille, A.N.2    McQuaid, S.3    Farrell, M.4    McMahon, J.5    Fitz Gerald, U.6
  • 22
    • 0037328719 scopus 로고    scopus 로고
    • Heat shock protein 70 associations with myelin basic protein and proteolipid protein in multiple sclerosis brains
    • Cwiklinska, H., Mycko, M. P., Luvsannorov, O., Walkowiak, B., Brosnan, C. F., Raine, C. S., et al. (2003). Heat shock protein 70 associations with myelin basic protein and proteolipid protein in multiple sclerosis brains. Int. Immunol. 15, 241-249. doi: 10.1093/intimm/dxg022.
    • (2003) Int. Immunol , vol.15 , pp. 241-249
    • Cwiklinska, H.1    Mycko, M.P.2    Luvsannorov, O.3    Walkowiak, B.4    Brosnan, C.F.5    Raine, C.S.6
  • 24
    • 8644282751 scopus 로고    scopus 로고
    • Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2
    • Deng, J., Lu, P. D., Zhang, Y., Scheuner, D., Kaufman, R. J., Sonenberg, N., et al. (2004). Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Mol. Cell. Biol. 24, 10161-10168. doi: 10.1128/MCB.24.23.10161-10168.2004.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 10161-10168
    • Deng, J.1    Lu, P.D.2    Zhang, Y.3    Scheuner, D.4    Kaufman, R.J.5    Sonenberg, N.6
  • 26
    • 80555133285 scopus 로고    scopus 로고
    • Neuroinflammation and endoplasmic reticulum stress are coregulated by crocin to prevent demyelination and neurodegeneration
    • Deslauriers, A. M., Afkhami-Goli, A., Paul, A. M., Bhat, R. K., Acharjee, S., Ellestad, K. K., et al. (2011). Neuroinflammation and endoplasmic reticulum stress are coregulated by crocin to prevent demyelination and neurodegeneration. J. Immunol. 187, 4788-4799. doi: 10.4049/jimmunol.1004111.
    • (2011) J. Immunol , vol.187 , pp. 4788-4799
    • Deslauriers, A.M.1    Afkhami-Goli, A.2    Paul, A.M.3    Bhat, R.K.4    Acharjee, S.5    Ellestad, K.K.6
  • 27
    • 80053252011 scopus 로고    scopus 로고
    • Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders
    • Doyle, K. M., Kennedy, D., Gorman, A. M., Gupta, S., Healy, S. J., and Samali, A. (2011). Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders. J. Cell. Mol. Med. 15, 2025-2039. doi: 10.1111/j.1582-4934.2011.01374.x.
    • (2011) J. Cell. Mol. Med , vol.15 , pp. 2025-2039
    • Doyle, K.M.1    Kennedy, D.2    Gorman, A.M.3    Gupta, S.4    Healy, S.J.5    Samali, A.6
  • 28
    • 78549234073 scopus 로고    scopus 로고
    • Mechanisms of neuronal dysfunction and degeneration in multiple sclerosis
    • Dutta, R., and Trapp, B. D. (2011). Mechanisms of neuronal dysfunction and degeneration in multiple sclerosis. Prog. Neurobiol. 93, 1-12. doi: 10.1016/j.pneurobio.2010.09.005.
    • (2011) Prog. Neurobiol , vol.93 , pp. 1-12
    • Dutta, R.1    Trapp, B.D.2
  • 30
    • 0029671318 scopus 로고    scopus 로고
    • Mice with a disrupted IFN-gamma gene are susceptible to the induction of experimental autoimmune encephalomyelitis (EAE)
    • Ferber, I. A., Brocke, S., Taylor-Edwards, C., Ridgway, W., Dinisco, C., Steinman, L., et al. (1996). Mice with a disrupted IFN-gamma gene are susceptible to the induction of experimental autoimmune encephalomyelitis (EAE). J. Immunol. 156, 5-7.
    • (1996) J. Immunol , vol.156 , pp. 5-7
    • Ferber, I.A.1    Brocke, S.2    Taylor-Edwards, C.3    Ridgway, W.4    Dinisco, C.5    Steinman, L.6
  • 31
    • 0036720034 scopus 로고    scopus 로고
    • Why does remyelination fail in multiple sclerosis?
    • Franklin, R. J. (2002). Why does remyelination fail in multiple sclerosis? Nat. Rev. Neurosci. 3, 705-714. doi: 10.1038/nrn917.
    • (2002) Nat. Rev. Neurosci , vol.3 , pp. 705-714
    • Franklin, R.J.1
  • 32
    • 54249124952 scopus 로고    scopus 로고
    • Remyelination in the CNS: from biology to therapy
    • Franklin, R. J., and Ffrench-Constant, C. (2008). Remyelination in the CNS: from biology to therapy. Nat. Rev. Neurosci. 9, 839-855. doi: 10.1038/nrn2480.
    • (2008) Nat. Rev. Neurosci , vol.9 , pp. 839-855
    • Franklin, R.J.1    Ffrench-Constant, C.2
  • 33
    • 33644607018 scopus 로고    scopus 로고
    • Multiple sclerosis-the plaque and its pathogenesis
    • Frohman, E. M., Racke, M. K., and Raine, C. S. (2006). Multiple sclerosis-the plaque and its pathogenesis. N. Engl. J. Med. 354, 942-955. doi: 10.1056/NEJMra052130.
    • (2006) N. Engl. J. Med , vol.354 , pp. 942-955
    • Frohman, E.M.1    Racke, M.K.2    Raine, C.S.3
  • 34
    • 84862977176 scopus 로고    scopus 로고
    • An IFN-γ-stimulated ATF6-C/EBP-β-signaling pathway critical for the expression of Death Associated Protein Kinase 1 and induction of autophagy
    • Gade, P., Ramachandran, G., Maachani, U. B., Rizzo, M. A., Okada, T., Prywes, R., et al. (2012). An IFN-γ-stimulated ATF6-C/EBP-β-signaling pathway critical for the expression of Death Associated Protein Kinase 1 and induction of autophagy. Proc. Natl. Acad. Sci. U.S.A. 109, 10316-10321. doi: 10.1073/pnas.1119273109.
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 10316-10321
    • Gade, P.1    Ramachandran, G.2    Maachani, U.B.3    Rizzo, M.A.4    Okada, T.5    Prywes, R.6
  • 35
    • 35548935675 scopus 로고    scopus 로고
    • The unfolded protein response of B-lymphocytes: PERK-independent development of antibody-secreting cells
    • Gass, J. N., Jiang, H. Y., Wek, R. C., and Brewer, J. W. (2008). The unfolded protein response of B-lymphocytes: PERK-independent development of antibody-secreting cells. Mol. Immunol. 45, 1035-1043. doi: 10.1016/j.molimm.2007.07.029.
    • (2008) Mol. Immunol , vol.45 , pp. 1035-1043
    • Gass, J.N.1    Jiang, H.Y.2    Wek, R.C.3    Brewer, J.W.4
  • 36
    • 77950363010 scopus 로고    scopus 로고
    • Mechanisms underlying inflammation in neurodegeneration
    • Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., and Gage, F. H. (2010). Mechanisms underlying inflammation in neurodegeneration. Cell 140, 918-934. doi: 10.1016/j.cell.2010.02.016.
    • (2010) Cell , vol.140 , pp. 918-934
    • Glass, C.K.1    Saijo, K.2    Winner, B.3    Marchetto, M.C.4    Gage, F.H.5
  • 37
    • 84899925732 scopus 로고    scopus 로고
    • Roles for ATF6 and the sarco/endoplasmic reticulum protein quality control system in the heart
    • Glembotski, C. C. (2014). Roles for ATF6 and the sarco/endoplasmic reticulum protein quality control system in the heart. J. Mol. Cell Cardiol. 71, 11-15. doi: 10.1016/j.yjmcc.2013.09.018.
    • (2014) J. Mol. Cell Cardiol , vol.71 , pp. 11-15
    • Glembotski, C.C.1
  • 38
    • 33746729791 scopus 로고    scopus 로고
    • Understanding pathogenesis and therapy of multiple sclerosis via animal models: 70 years of merits and culprits in experimental autoimmune encephalomyelitis research
    • Gold, R., Linington, C., and Lassmann, H. (2006). Understanding pathogenesis and therapy of multiple sclerosis via animal models: 70 years of merits and culprits in experimental autoimmune encephalomyelitis research. Brain 129, 1953-1971. doi: 10.1093/brain/awl075.
    • (2006) Brain , vol.129 , pp. 1953-1971
    • Gold, R.1    Linington, C.2    Lassmann, H.3
  • 39
    • 67349216357 scopus 로고    scopus 로고
    • Autoimmune T cell responses in the central nervous system
    • Goverman, J. (2009). Autoimmune T cell responses in the central nervous system. Nat. Rev. Immunol. 9, 393-407. doi: 10.1038/nri2550.
    • (2009) Nat. Rev. Immunol , vol.9 , pp. 393-407
    • Goverman, J.1
  • 40
    • 70450214826 scopus 로고    scopus 로고
    • CHOP and the endoplasmic reticulum stress response in myelinating glia
    • Gow, A., and Wrabetz, L. (2009). CHOP and the endoplasmic reticulum stress response in myelinating glia. Curr. Opin. Neurobiol. 19, 505-510. doi: 10.1016/j.conb.2009.08.007.
    • (2009) Curr. Opin. Neurobiol , vol.19 , pp. 505-510
    • Gow, A.1    Wrabetz, L.2
  • 41
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding, H. P., Calfon, M., Urano, F., Novoa, I., and Ron, D. (2002). Transcriptional and translational control in the mammalian unfolded protein response. Annu. Rev. Cell. Dev. Biol. 18, 575-599. doi: 10.1146/annurev.cellbio.18.011402.160624.
    • (2002) Annu. Rev. Cell. Dev. Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 42
    • 0035787914 scopus 로고    scopus 로고
    • Translational regulation in the cellular response to biosynthetic load on the endoplasmic reticulum
    • Harding, H. P., Novoa, I., Bertolotti, A., Zeng, H., Zhang, Y., Urano, F., et al. (2001). Translational regulation in the cellular response to biosynthetic load on the endoplasmic reticulum. Cold Spring Harb. Symp. Quant. Biol. 66, 499-508. doi: 10.1101/sqb.2001.66.499.
    • (2001) Cold Spring Harb. Symp. Quant. Biol , vol.66 , pp. 499-508
    • Harding, H.P.1    Novoa, I.2    Bertolotti, A.3    Zeng, H.4    Zhang, Y.5    Urano, F.6
  • 43
    • 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
  • 44
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M., et al. (2003). An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell. 11, 619-633. doi: 10.1016/S1097-2765(03)00105-9.
    • (2003) Mol. Cell , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3    Novoa, I.4    Lu, P.D.5    Calfon, M.6
  • 45
    • 84871759394 scopus 로고    scopus 로고
    • Uncoupling proteostasis and development in vitro with a small molecule inhibitor of the pancreatic endoplasmic reticulum kinase, PERK
    • Harding, H. P., Zyryanova, A. F., and Ron, D. (2012). Uncoupling proteostasis and development in vitro with a small molecule inhibitor of the pancreatic endoplasmic reticulum kinase, PERK. J. Biol. Chem. 287, 44338-44344. doi: 10.1074/jbc.M112.428987.
    • (2012) J. Biol. Chem , vol.287 , pp. 44338-44344
    • Harding, H.P.1    Zyryanova, A.F.2    Ron, D.3
  • 46
    • 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
  • 47
    • 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
  • 48
    • 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
  • 49
    • 0034142394 scopus 로고    scopus 로고
    • Targeted expression of baculovirus p35 caspase inhibitor in oligodendrocytes protects mice against autoimmune-mediated demyelination
    • Hisahara, S., Araki, T., Sugiyama, F., Yagami, K., Suzuki, M., Abe, K., et al. (2000). Targeted expression of baculovirus p35 caspase inhibitor in oligodendrocytes protects mice against autoimmune-mediated demyelination. EMBO J. 19, 341-348. doi: 10.1093/emboj/19.3.341.
    • (2000) EMBO J , vol.19 , pp. 341-348
    • Hisahara, S.1    Araki, T.2    Sugiyama, F.3    Yagami, K.4    Suzuki, M.5    Abe, K.6
  • 50
    • 0037491616 scopus 로고    scopus 로고
    • Caspase-mediated oligodendrocyte cell death in the pathogenesis of autoimmune demyelination
    • Hisahara, S., Okano, H., and Miura, M. (2003). Caspase-mediated oligodendrocyte cell death in the pathogenesis of autoimmune demyelination. Neurosci. Res. 46, 387-397. doi: 10.1016/S0168-0102(03)00127-5.
    • (2003) Neurosci. Res , vol.46 , pp. 387-397
    • Hisahara, S.1    Okano, H.2    Miura, M.3
  • 51
    • 27144460509 scopus 로고    scopus 로고
    • Apoptosis of Oligodendrocytes via Fas and TNF-R1 Is a Key Event in the Induction of Experimental Autoimmune Encephalomyelitis
    • Hövelmeyer, N., Hao, Z., Kranidioti, K., Kassiotis, G., Buch, T., Frommer, F., et al. (2005). Apoptosis of Oligodendrocytes via Fas and TNF-R1 Is a Key Event in the Induction of Experimental Autoimmune Encephalomyelitis. J. Immunol. 175, 5875-5884. doi: 10.4049/jimmunol.175.9.5875.
    • (2005) J. Immunol , vol.175 , pp. 5875-5884
    • Hövelmeyer, N.1    Hao, Z.2    Kranidioti, K.3    Kassiotis, G.4    Buch, T.5    Frommer, F.6
  • 52
    • 33645815074 scopus 로고    scopus 로고
    • Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression
    • Hu, P., Han, Z., Couvillon, A. D., Kaufman, R. J., and Exton, J. H. (2006). Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression. Mol. Cell. Biol. 26, 3071-3084. doi: 10.1128/MCB.26.8.3071-3084.2006.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 3071-3084
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3    Kaufman, R.J.4    Exton, J.H.5
  • 53
    • 84896319455 scopus 로고    scopus 로고
    • Genetic inactivation of PERK signaling in mouse oligodendrocytes: normal developmental myelination with increased susceptibility to inflammatory demyelination
    • Hussien, Y., Cavener, D. R., and Popko, B. (2014). Genetic inactivation of PERK signaling in mouse oligodendrocytes: normal developmental myelination with increased susceptibility to inflammatory demyelination. Glia 62, 680-691. doi: 10.1002/glia.22634.
    • (2014) Glia , vol.62 , pp. 680-691
    • Hussien, Y.1    Cavener, D.R.2    Popko, B.3
  • 54
    • 0037385313 scopus 로고    scopus 로고
    • Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1
    • Iwakoshi, N. N., Lee, A. H., Vallabhajosyula, P., Otipoby, K. L., Rajewsky, K., and Glimcher, L. H. (2003). Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat. Immunol. 4, 321-329. doi: 10.1038/ni907.
    • (2003) Nat. Immunol , vol.4 , pp. 321-329
    • Iwakoshi, N.N.1    Lee, A.H.2    Vallabhajosyula, P.3    Otipoby, K.L.4    Rajewsky, K.5    Glimcher, L.H.6
  • 55
    • 0043133837 scopus 로고    scopus 로고
    • Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses
    • Jiang, H. Y., Wek, S. A., McGrath, B. C., Scheuner, D., Kaufman, R. J., Cavener, D. R., et al. (2003). Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses. Mol. Cell. Biol. 23, 5651-5663. doi: 10.1128/MCB.23.16.5651-5663.2003.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 5651-5663
    • Jiang, H.Y.1    Wek, S.A.2    McGrath, B.C.3    Scheuner, D.4    Kaufman, R.J.5    Cavener, D.R.6
  • 56
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin, M., and Lin, A. (2002). NF-kappaB at the crossroads of life and death. Nat. Immunol. 3, 221-227. doi: 10.1038/ni0302-221.
    • (2002) Nat. Immunol , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 57
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • Kaufman, R. J. (1999). Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211-1233. doi: 10.1101/gad.13.10.1211.
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 58
    • 78751556358 scopus 로고    scopus 로고
    • Control of NF-κB and inflammation by the unfolded protein response
    • Kitamura, M. (2011). Control of NF-κB and inflammation by the unfolded protein response. Int. Rev. Immunol. 30, 4-15. doi: 10.3109/08830185.2010.522281.
    • (2011) Int. Rev. Immunol , vol.30 , pp. 4-15
    • Kitamura, M.1
  • 59
    • 0034487540 scopus 로고    scopus 로고
    • Regional hypomyelination and dysplasia in transgenic mice with astrocyte-directed expression of interferon-gamma
    • LaFerla, F. M., Sugarman, M. C., Lane, T. E., and Leissring, M. A. (2000). Regional hypomyelination and dysplasia in transgenic mice with astrocyte-directed expression of interferon-gamma. J. Mol. Neurosci. 15, 45-59. doi: 10.1385/JMN:15:1:45.
    • (2000) J. Mol. Neurosci , vol.15 , pp. 45-59
    • LaFerla, F.M.1    Sugarman, M.C.2    Lane, T.E.3    Leissring, M.A.4
  • 60
    • 77955656367 scopus 로고    scopus 로고
    • Axonal and neuronal pathology in multiple sclerosis: what have we learnt from animal models
    • Lassmann, H. (2010). Axonal and neuronal pathology in multiple sclerosis: what have we learnt from animal models. Exp. Neurol. 225, 2-8. doi: 10.1016/j.expneurol.2009.10.009.
    • (2010) Exp. Neurol , vol.225 , pp. 2-8
    • Lassmann, H.1
  • 61
    • 33846806080 scopus 로고    scopus 로고
    • A little stress is good: IFN-gamma, demyelination, and multiple sclerosis
    • Lees, J. R., and Cross, A. H. (2007). A little stress is good: IFN-gamma, demyelination, and multiple sclerosis. J. Clin. Invest. 117, 297-299. doi: 10.1172/JCI31254.
    • (2007) J. Clin. Invest , vol.117 , pp. 297-299
    • Lees, J.R.1    Cross, A.H.2
  • 62
    • 84925147662 scopus 로고    scopus 로고
    • Impaired eIF2B activity in oligodendrocytes contributes to VWMD pathogenesis
    • Lin, W. (2015). Impaired eIF2B activity in oligodendrocytes contributes to VWMD pathogenesis. Neural. Regen. Res. 10, 195-197 doi: 10.4103/1673-5374.152366.
    • (2015) Neural. Regen. Res , vol.10 , pp. 195-197
    • Lin, W.1
  • 63
    • 33846811702 scopus 로고    scopus 로고
    • The integrated stress response prevents demyelination by protecting oligodendrocytes against immune-mediated damage
    • Lin, W., Bailey, S. L., Ho, H., Harding, H. P., Ron, D., Miller, S. D., et al. (2007). The integrated stress response prevents demyelination by protecting oligodendrocytes against immune-mediated damage. J. Clin. Invest. 117, 448-456. doi: 10.1172/JCI29571.
    • (2007) J. Clin. Invest , vol.117 , pp. 448-456
    • Lin, W.1    Bailey, S.L.2    Ho, H.3    Harding, H.P.4    Ron, D.5    Miller, S.D.6
  • 64
    • 22344435167 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-gamma
    • Lin, W., Harding, H. P., Ron, D., and Popko, B. (2005). Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-gamma. J. Cell. Biol. 169, 603-612. doi: 10.1083/jcb.200502086.
    • (2005) J. Cell. Biol , vol.169 , pp. 603-612
    • Lin, W.1    Harding, H.P.2    Ron, D.3    Popko, B.4
  • 65
    • 33646232737 scopus 로고    scopus 로고
    • Interferon-gamma inhibits central nervous system remyelination through a process modulated by endoplasmic reticulum stress
    • Lin, W., Kemper, A., Dupree, J. L., Harding, H. P., Ron, D., and Popko, B. (2006). Interferon-gamma inhibits central nervous system remyelination through a process modulated by endoplasmic reticulum stress. Brain 129, 1306-1318. doi: 10.1093/brain/awl044.
    • (2006) Brain , vol.129 , pp. 1306-1318
    • Lin, W.1    Kemper, A.2    Dupree, J.L.3    Harding, H.P.4    Ron, D.5    Popko, B.6
  • 66
    • 8544260349 scopus 로고    scopus 로고
    • Interferon-gamma induced medulloblastoma in the developing cerebellum
    • Lin, W., Kemper, A., McCarthy, K. D., Pytel, P., Wang, J. P., Campbell, I. L., et al. (2004). Interferon-gamma induced medulloblastoma in the developing cerebellum. J. Neurosci. 24, 10074-10083. doi: 10.1523/JNEUROSCI.2604-04.2004.
    • (2004) J. Neurosci , vol.24 , pp. 10074-10083
    • Lin, W.1    Kemper, A.2    McCarthy, K.D.3    Pytel, P.4    Wang, J.P.5    Campbell, I.L.6
  • 67
    • 55349142516 scopus 로고    scopus 로고
    • Enhanced integrated stress response promotes myelinating oligodendrocyte survival in response to interferon-gamma
    • Lin, W., Kunkler, P. E., Harding, H. P., Ron, D., Kraig, R. P., and Popko, B. (2008). Enhanced integrated stress response promotes myelinating oligodendrocyte survival in response to interferon-gamma. Am. J. Pathol. 173, 1508-1517. doi: 10.2353/ajpath.2008.080449.
    • (2008) Am. J. Pathol , vol.173 , pp. 1508-1517
    • Lin, W.1    Kunkler, P.E.2    Harding, H.P.3    Ron, D.4    Kraig, R.P.5    Popko, B.6
  • 68
    • 77955477978 scopus 로고    scopus 로고
    • Interferon-γ inhibits central nervous system myelination through both STAT1-dependent and STAT1-independent pathways
    • Lin, W., and Lin, Y. (2010). Interferon-γ inhibits central nervous system myelination through both STAT1-dependent and STAT1-independent pathways. J. Neurosci. Res. 88, 2569-2577. doi: 10.1002/jnr.22425.
    • (2010) J. Neurosci. Res , vol.88 , pp. 2569-2577
    • Lin, W.1    Lin, Y.2
  • 69
    • 84876001820 scopus 로고    scopus 로고
    • Oligodendrocyte-specific activation of PERK signaling protects mice against experimental autoimmune encephalomyelitis
    • Lin, W., Lin, Y., Li, J., Fenstermaker, A. G., Way, S. W., Clayton, B., et al. (2013). Oligodendrocyte-specific activation of PERK signaling protects mice against experimental autoimmune encephalomyelitis. J. Neurosci. 33, 5980-5991. doi: 10.1523/JNEUROSCI.1636-12.2013.
    • (2013) J. Neurosci , vol.33 , pp. 5980-5991
    • Lin, W.1    Lin, Y.2    Li, J.3    Fenstermaker, A.G.4    Way, S.W.5    Clayton, B.6
  • 70
    • 63649109017 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disorders of myelinating cells
    • Lin, W., and Popko, B. (2009). Endoplasmic reticulum stress in disorders of myelinating cells. Nat. Neurosci. 12, 379-385. doi: 10.1038/nn.2273.
    • (2009) Nat. Neurosci , vol.12 , pp. 379-385
    • Lin, W.1    Popko, B.2
  • 71
    • 84892179950 scopus 로고    scopus 로고
    • PERK activation preserves the viability and function of remyelinating oligodendrocytes in immune-mediated demyelinating diseases
    • Lin, Y., Huang, G., Jamison, S., Li, J., Harding, H. P., Ron, D., et al. (2014a). PERK activation preserves the viability and function of remyelinating oligodendrocytes in immune-mediated demyelinating diseases. Am. J. Pathol. 184, 507-519. doi: 10.1016/j.ajpath.2013.10.009.
    • (2014) Am. J. Pathol , vol.184 , pp. 507-519
    • Lin, Y.1    Huang, G.2    Jamison, S.3    Li, J.4    Harding, H.P.5    Ron, D.6
  • 72
    • 84860523529 scopus 로고    scopus 로고
    • Interferon-γ activates nuclear factor-κ B in oligodendrocytes through a process mediated by the unfolded protein response
    • Lin, Y., Jamison, S., and Lin, W. (2012). Interferon-γ activates nuclear factor-κ B in oligodendrocytes through a process mediated by the unfolded protein response. PLoS ONE 7:e36408. doi: 10.1371/journal.pone.0036408.
    • (2012) PLoS ONE , vol.7
    • Lin, Y.1    Jamison, S.2    Lin, W.3
  • 73
    • 84906898010 scopus 로고    scopus 로고
    • Impaired eukaryotic translation initiation factor 2B activity specifically in oligodendrocytes reproduces the pathology of vanishing white matter disease in mice
    • Lin, Y., Pang, X., Huang, G., Jamison, S., Fang, J., Harding, H. P., et al. (2014b). Impaired eukaryotic translation initiation factor 2B activity specifically in oligodendrocytes reproduces the pathology of vanishing white matter disease in mice. J. Neurosci. 34, 12182-12191. doi: 10.1523/JNEUROSCI.1373-14.2014.
    • (2014) J. Neurosci , vol.34 , pp. 12182-12191
    • Lin, Y.1    Pang, X.2    Huang, G.3    Jamison, S.4    Fang, J.5    Harding, H.P.6
  • 74
    • 0842285401 scopus 로고    scopus 로고
    • Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2
    • Lu, P. D., Jousse, C., Marciniak, S. J., Zhang, Y., Novoa, I., Scheuner, D., et al. (2004). Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2. EMBO J. 23, 169-179. doi: 10.1038/sj.emboj.7600030.
    • (2004) EMBO J , vol.23 , pp. 169-179
    • Lu, P.D.1    Jousse, C.2    Marciniak, S.J.3    Zhang, Y.4    Novoa, I.5    Scheuner, D.6
  • 75
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak, S. J., and Ron, D. (2006). Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86, 1133-1149. doi: 10.1152/physrev.00015.2006.
    • (2006) Physiol. Rev , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 76
    • 10644233167 scopus 로고    scopus 로고
    • CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum
    • Marciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., et al. (2004). CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev. 18, 3066-3077. doi: 10.1101/gad.1250704.
    • (2004) Genes Dev , vol.18 , pp. 3066-3077
    • Marciniak, S.J.1    Yun, C.Y.2    Oyadomari, S.3    Novoa, I.4    Zhang, Y.5    Jungreis, R.6
  • 77
    • 0035198691 scopus 로고    scopus 로고
    • The neurotoxicant, cuprizone, as a model to study demyelination and remyelination in the central nervous system
    • Matsushima, G. K., and Morell, P. (2001). The neurotoxicant, cuprizone, as a model to study demyelination and remyelination in the central nervous system. Brain Pathol. 11, 107-116. doi: 10.1111/j.1750-3639.2001.tb00385.x.
    • (2001) Brain Pathol , vol.11 , pp. 107-116
    • Matsushima, G.K.1    Morell, P.2
  • 78
    • 84899937866 scopus 로고    scopus 로고
    • Getting RIDD of RNA: IRE1 in cell fate regulation
    • Maurel, M., Chevet, E., Tavernier, J., and Gerlo, S. (2014). Getting RIDD of RNA: IRE1 in cell fate regulation. Trends Biochem. Sci. 39, 245-554. doi: 10.1016/j.tibs.2014.02.008.
    • (2014) Trends Biochem. Sci , vol.39 , pp. 245-554
    • Maurel, M.1    Chevet, E.2    Tavernier, J.3    Gerlo, S.4
  • 79
    • 84884753706 scopus 로고    scopus 로고
    • Nuclear factor kappa B (NF-κB) in multiple sclerosis pathology
    • McGuire, C., Prinz, M., Beyaert, R., and van Loo, G. (2013). Nuclear factor kappa B (NF-κB) in multiple sclerosis pathology. Trends Mol. Med. 19, 604-613. doi: 10.1016/j.molmed.2013.08.001.
    • (2013) Trends Mol. Med , vol.19 , pp. 604-613
    • McGuire, C.1    Prinz, M.2    Beyaert, R.3    van Loo, G.4
  • 80
    • 78650652403 scopus 로고    scopus 로고
    • Oligodendrocyte-specific FADD deletion protects mice from autoimmune-mediated demyelination
    • McGuire, C., Volckaert, T., Wolke, U., Sze, M., de Rycke, R., Waisman, A., et al. (2010). Oligodendrocyte-specific FADD deletion protects mice from autoimmune-mediated demyelination. J. Immunol. 185, 7646-7653. doi: 10.4049/jimmunol.1000930.
    • (2010) J. Immunol , vol.185 , pp. 7646-7653
    • McGuire, C.1    Volckaert, T.2    Wolke, U.3    Sze, M.4    de Rycke, R.5    Waisman, A.6
  • 81
    • 84867007198 scopus 로고    scopus 로고
    • Increased expression of ER stress-and hypoxia-associated molecules in grey matter lesions in multiple sclerosis
    • McMahon, J. M., McQuaid, S., Reynolds, R., and Fitz Gerald, U. F. (2012). Increased expression of ER stress-and hypoxia-associated molecules in grey matter lesions in multiple sclerosis. Mult. Scler. 18, 1437-1447. doi: 10.1177/1352458512438455.
    • (2012) Mult. Scler , vol.18 , pp. 1437-1447
    • McMahon, J.M.1    McQuaid, S.2    Reynolds, R.3    Fitz Gerald, U.F.4
  • 82
    • 84907157987 scopus 로고    scopus 로고
    • PERK-dependent activation of JAK1 and STAT3 contributes to endoplasmic reticulum stress-induced inflammation
    • Meares, G. P., Liu, Y., Rajbhandari, R., Qin, H., Nozell, S. E., Mobley, J. A., et al. (2014). PERK-dependent activation of JAK1 and STAT3 contributes to endoplasmic reticulum stress-induced inflammation. Mol. Cell Biol. 34, 3911-3925. doi: 10.1128/MCB.00980-14.
    • (2014) Mol. Cell Biol , vol.34 , pp. 3911-3925
    • Meares, G.P.1    Liu, Y.2    Rajbhandari, R.3    Qin, H.4    Nozell, S.E.5    Mobley, J.A.6
  • 83
    • 0026601932 scopus 로고
    • Inflammatory leukocytes and cytokines in the peptide-induced disease of experimental allergic encephalomyelitis in SJL and B10.PL mice
    • Merrill, J. E., Kono, D. H., Clayton, J., Ando, D. G., Hinton, D. R., and Hofman, F. M. (1992). Inflammatory leukocytes and cytokines in the peptide-induced disease of experimental allergic encephalomyelitis in SJL and B10.PL mice. Proc. Natl. Aacd. Sci. U.S.A. 89, 574-578. doi: 10.1073/pnas.89.2.574.
    • (1992) Proc. Natl. Aacd. Sci. U.S.A , vol.89 , pp. 574-578
    • Merrill, J.E.1    Kono, D.H.2    Clayton, J.3    Ando, D.G.4    Hinton, D.R.5    Hofman, F.M.6
  • 84
    • 41649097176 scopus 로고    scopus 로고
    • Increased expression of endoplasmic reticulum stress-related signaling pathway molecules in multiple sclerosis lesions
    • Mháille, A. N., McQuaid, S., Windebank, A., Cunnea, P., McMahon, J., Samali, A., et al. (2008). Increased expression of endoplasmic reticulum stress-related signaling pathway molecules in multiple sclerosis lesions. J. Neuropathol. Exp. Neurol. 67, 200-211. doi: 10.1097/NEN.0b013e318165b239.
    • (2008) J. Neuropathol. Exp. Neurol , vol.67 , pp. 200-211
    • Mháille, A.N.1    McQuaid, S.2    Windebank, A.3    Cunnea, P.4    McMahon, J.5    Samali, A.6
  • 85
    • 84877824588 scopus 로고    scopus 로고
    • NF-κB signaling pathways: role in nervous system physiology and pathology
    • Mincheva-Tasheva, S., and Soler, R. M. (2013). NF-κB signaling pathways: role in nervous system physiology and pathology. Neuroscientist 19, 175-194. doi: 10.1177/1073858412444007.
    • (2013) Neuroscientist , vol.19 , pp. 175-194
    • Mincheva-Tasheva, S.1    Soler, R.M.2
  • 86
    • 0027102387 scopus 로고
    • T cells in the lesion of experimental autoimmune encephalomyelitis. Enrichment for reactivities to myelin basic protein and to heat shock proteins
    • Mor, F., and Cohen, I. R. (1992). T cells in the lesion of experimental autoimmune encephalomyelitis. Enrichment for reactivities to myelin basic protein and to heat shock proteins. J. Clin. Invest. 90, 2447-2455. doi: 10.1172/JCI116136.
    • (1992) J. Clin. Invest , vol.90 , pp. 2447-2455
    • Mor, F.1    Cohen, I.R.2
  • 87
    • 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
  • 88
    • 1842782996 scopus 로고    scopus 로고
    • Anti-inflammatory properties of pro-inflammatory interferon-gamma
    • Mühl, H., and Pfeilschifter, J. (2003). Anti-inflammatory properties of pro-inflammatory interferon-gamma. Int. Immunopharmacol. 3, 1247-1255. doi: 10.1016/S1567-5769(03)00131-0.
    • (2003) Int. Immunopharmacol , vol.3 , pp. 1247-1255
    • Mühl, H.1    Pfeilschifter, J.2
  • 89
    • 2642539885 scopus 로고    scopus 로고
    • Microarray gene expression profiling of chronic active and inactive lesions in multiple sclerosis
    • Mycko, M. P., Papoian, R., Boschert, U., Raine, C. S., and Selmaj, K. W. (2004). Microarray gene expression profiling of chronic active and inactive lesions in multiple sclerosis. Clin. Neurol. Neurosurg. 106, 223-229. doi: 10.1016/j.clineuro.2004.02.019.
    • (2004) Clin. Neurol. Neurosurg , vol.106 , pp. 223-229
    • Mycko, M.P.1    Papoian, R.2    Boschert, U.3    Raine, C.S.4    Selmaj, K.W.5
  • 90
    • 84925267195 scopus 로고    scopus 로고
    • Myelination of the nervous system: mechanisms and functions
    • Nave, K. A., and Werner, H. B. (2014). Myelination of the nervous system: mechanisms and functions. Annu. Rev. Cell Dev. Biol. 30, 503-533. doi: 10.1146/annurev-cellbio-100913-013101.
    • (2014) Annu. Rev. Cell Dev. Biol , vol.30 , pp. 503-533
    • Nave, K.A.1    Werner, H.B.2
  • 91
    • 85005870165 scopus 로고    scopus 로고
    • Calreticulin and other components of endoplasmic reticulum stress in rat and human inflammatory demyelination
    • Ní Fhlathartaigh, M., McMahon, J., Reynolds, R., Connolly, D., Higgins, E., Fitzgerald, U., et al. (2013). Calreticulin and other components of endoplasmic reticulum stress in rat and human inflammatory demyelination. Acta Neuropathol. Commun. 1:37. doi: 10.1186/2051-5960-1-37.
    • (2013) Acta Neuropathol. Commun , vol.1 , pp. 37
    • Ní Fhlathartaigh, M.1    McMahon, J.2    Reynolds, R.3    Connolly, D.4    Higgins, E.5    Fitzgerald, U.6
  • 92
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa, I., Zeng, H., Harding, H. P., and Ron, D. (2001). Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J. Cell. Biol. 153, 1011-1022. doi: 10.1083/jcb.153.5.1011.
    • (2001) J. Cell. Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 93
    • 84879368095 scopus 로고    scopus 로고
    • Restoring endoplasmic reticulum homeostasis improves functional recovery after spinal cord injury
    • Ohri, S. S., Hetman, M., and Whittemore, S. R. (2013). Restoring endoplasmic reticulum homeostasis improves functional recovery after spinal cord injury. Neurobiol. Dis. 58, 29-37. doi: 10.1016/j.nbd.2013.04.021.
    • (2013) Neurobiol. Dis , vol.58 , pp. 29-37
    • Ohri, S.S.1    Hetman, M.2    Whittemore, S.R.3
  • 94
    • 0023221133 scopus 로고
    • Treatment of multiple sclerosis with gamma interferon: exacerbations associated with activation of the immune system
    • Panitch, H. S., Hirsch, R. L., Schindler, J., and Johnson, K. P. (1987). Treatment of multiple sclerosis with gamma interferon: exacerbations associated with activation of the immune system. Neurology 37, 1097-1102. doi: 10.1212/WNL.37.7.1097.
    • (1987) Neurology , vol.37 , pp. 1097-1102
    • Panitch, H.S.1    Hirsch, R.L.2    Schindler, J.3    Johnson, K.P.4
  • 95
    • 61649099869 scopus 로고    scopus 로고
    • Substantial archaeocortical atrophy and neuronal loss in multiple sclerosis
    • Papadopoulos, D., Dukes, S., Patel, R., Nicholas, R., Vora, A., and Reynolds, R. (2009). Substantial archaeocortical atrophy and neuronal loss in multiple sclerosis. Brain Pathol. 19, 238-253. doi: 10.1111/j.1750-3639.2008.00177.x.
    • (2009) Brain Pathol , vol.19 , pp. 238-253
    • Papadopoulos, D.1    Dukes, S.2    Patel, R.3    Nicholas, R.4    Vora, A.5    Reynolds, R.6
  • 96
    • 70450207226 scopus 로고    scopus 로고
    • Protein synthesis and its control in neuronal cells with a focus on vanishing white matter disease
    • Pavitt, G. D., and Proud, C. G. (2009). Protein synthesis and its control in neuronal cells with a focus on vanishing white matter disease. Biochem. Soc. Trans. 37, 1298-1310. doi: 10.1042/BST0371298.
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 1298-1310
    • Pavitt, G.D.1    Proud, C.G.2
  • 97
    • 0027193569 scopus 로고
    • The oligodendrocyte and its many cellular processes
    • Pfeiffer, S. E., Warrington, A. E., and Bansal, R. (1993). The oligodendrocyte and its many cellular processes. Trends Cell. Biol. 3, 191-197. doi: 10.1016/0962-8924(93)90213-K.
    • (1993) Trends Cell. Biol , vol.3 , pp. 191-197
    • Pfeiffer, S.E.1    Warrington, A.E.2    Bansal, R.3
  • 98
    • 84856884830 scopus 로고    scopus 로고
    • Pathology of demyelinating diseases
    • Popescu, B. F., and Lucchinetti, C. F. (2012). Pathology of demyelinating diseases. Annu. Rev. Pathol. 7, 185-217. doi: 10.1146/annurev-pathol-011811-132443.
    • (2012) Annu. Rev. Pathol , vol.7 , pp. 185-217
    • Popescu, B.F.1    Lucchinetti, C.F.2
  • 99
    • 0032904541 scopus 로고    scopus 로고
    • Oligodendroglial response to the immune cytokine interferon gamma
    • Popko, B., and Baerwald, K. D. (1999). Oligodendroglial response to the immune cytokine interferon gamma. Neurochem. Res. 24, 331-338. doi: 10.1023/A:1022586726510.
    • (1999) Neurochem. Res , vol.24 , pp. 331-338
    • Popko, B.1    Baerwald, K.D.2
  • 100
    • 0031063399 scopus 로고    scopus 로고
    • The effects of interferon-gamma on the central nervous system
    • Popko, B., Corbin, J. G., Baerwald, K. D., Dupree, J., and Garcia, A. M. (1997). The effects of interferon-gamma on the central nervous system. Mol. Neurobiol. 14, 19-35. doi: 10.1007/BF02740619.
    • (1997) Mol. Neurobiol , vol.14 , pp. 19-35
    • Popko, B.1    Corbin, J.G.2    Baerwald, K.D.3    Dupree, J.4    Garcia, A.M.5
  • 101
    • 84864434405 scopus 로고    scopus 로고
    • Oligodendrocytes and the early multiple sclerosis lesion
    • Prineas, J. W., and Parratt, J. D. (2012). Oligodendrocytes and the early multiple sclerosis lesion. Ann. Neurol. 72, 18-31. doi: 10.1002/ana.23634.
    • (2012) Ann. Neurol , vol.72 , pp. 18-31
    • Prineas, J.W.1    Parratt, J.D.2
  • 102
    • 79251504265 scopus 로고    scopus 로고
    • Detecting and quantitating physiological endoplasmic reticulum stress
    • Qi, L., Yang, L., and Chen, H. (2011). Detecting and quantitating physiological endoplasmic reticulum stress. Methods Enzymol. 490, 137-146. doi: 10.1016/B978-0-12-385114-7.00008-8.
    • (2011) Methods Enzymol , vol.490 , pp. 137-146
    • Qi, L.1    Yang, L.2    Chen, H.3
  • 103
    • 0036476551 scopus 로고    scopus 로고
    • Stat1-dependent and-independent pathways in IFN-gamma-dependent signaling
    • Ramana, C. V., Gil, M. P., Schreiber, R. D., and Stark, G. R. (2002). Stat1-dependent and-independent pathways in IFN-gamma-dependent signaling. Trends Immunol. 23, 96-101. doi: 10.1016/S1471-4906(01)02118-4.
    • (2002) Trends Immunol , vol.23 , pp. 96-101
    • Ramana, C.V.1    Gil, M.P.2    Schreiber, R.D.3    Stark, G.R.4
  • 104
    • 79958279017 scopus 로고    scopus 로고
    • Overexpression of the dominant-negative form of interferon regulatory factor 1 in oligodendrocytes protects against experimental autoimmune encephalomyelitis
    • Ren, Z., Wang, Y., Tao, D., Liebenson, D., Liggett, T., Goswami, R., et al. (2011). Overexpression of the dominant-negative form of interferon regulatory factor 1 in oligodendrocytes protects against experimental autoimmune encephalomyelitis. J. Neurosci. 31, 8329-8341. doi: 10.1523/JNEUROSCI.1028-11.2011.
    • (2011) J. Neurosci , vol.31 , pp. 8329-8341
    • Ren, Z.1    Wang, Y.2    Tao, D.3    Liebenson, D.4    Liggett, T.5    Goswami, R.6
  • 105
    • 33646042221 scopus 로고    scopus 로고
    • Defective translation initiation causes vanishing of cerebral white matter
    • Scheper, G. C., Proud, C. G., and van der Knaap, M. S. (2006). Defective translation initiation causes vanishing of cerebral white matter. Trends Mol. Med. 12, 159-166. doi: 10.1016/j.molmed.2006.02.006.
    • (2006) Trends Mol. Med , vol.12 , pp. 159-166
    • Scheper, G.C.1    Proud, C.G.2    van der Knaap, M.S.3
  • 106
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schröder, M. (2008). Endoplasmic reticulum stress responses. Cell Mol. Life Sci. 65, 862-894. doi: 10.1007/s00018-007-7383-5.
    • (2008) Cell Mol. Life Sci , vol.65 , pp. 862-894
    • Schröder, M.1
  • 107
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J., Chen, X., Hendershot, L., and Prywes, R. (2002). ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3, 99-111. doi: 10.1016/S1534-5807(02)00203-4.
    • (2002) Dev. Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 108
    • 77950862182 scopus 로고    scopus 로고
    • Multiple sclerosis-candidate mechanisms underlying CNS atrophy
    • Siffrin, V., Vogt, J., Radbruch, H., Nitsch, R., and Zipp, F. (2010). Multiple sclerosis-candidate mechanisms underlying CNS atrophy. Trends Neurosci. 33, 202-210. doi: 10.1016/j.tins.2010.01.002.
    • (2010) Trends Neurosci , vol.33 , pp. 202-210
    • Siffrin, V.1    Vogt, J.2    Radbruch, H.3    Nitsch, R.4    Zipp, F.5
  • 109
    • 0037079142 scopus 로고    scopus 로고
    • The unfolded protein response modulates disease severity in Pelizaeus-Merzbacher disease
    • Southwood, C. M., Garbern, J., Jiang, W., and Gow, A. (2002). The unfolded protein response modulates disease severity in Pelizaeus-Merzbacher disease. Neuron 36, 585-596. doi: 10.1016/S0896-6273(02)01045-0.
    • (2002) Neuron , vol.36 , pp. 585-596
    • Southwood, C.M.1    Garbern, J.2    Jiang, W.3    Gow, A.4
  • 110
    • 5444222234 scopus 로고    scopus 로고
    • XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum
    • Sriburi, R., Jackowski, S., Mori, K., and Brewer, J. W. (2004). XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J. Cell. Biol. 167, 35-41. doi: 10.1083/jcb.200406136.
    • (2004) J. Cell. Biol , vol.167 , pp. 35-41
    • Sriburi, R.1    Jackowski, S.2    Mori, K.3    Brewer, J.W.4
  • 111
    • 0033231305 scopus 로고    scopus 로고
    • Assessment of animal models for MS and demyelinating disease in the design of rational therapy
    • Steinman, L. (1999). Assessment of animal models for MS and demyelinating disease in the design of rational therapy. Neuron 24, 511-514. doi: 10.1016/S0896-6273(00)81107-1.
    • (1999) Neuron , vol.24 , pp. 511-514
    • Steinman, L.1
  • 112
    • 0041625961 scopus 로고    scopus 로고
    • Quantifying the early stages of remyelination following cuprizone-induced demyelination
    • Stidworthy, M. F., Genoud, S., Suter, U., Mantei, N., and Franklin, R. J. (2003). Quantifying the early stages of remyelination following cuprizone-induced demyelination. Brain Pathol. 13, 329-339. doi: 10.1111/j.1750-3639.2003.tb00032.x.
    • (2003) Brain Pathol , vol.13 , pp. 329-339
    • Stidworthy, M.F.1    Genoud, S.2    Suter, U.3    Mantei, N.4    Franklin, R.J.5
  • 113
    • 84855767695 scopus 로고    scopus 로고
    • Mechanism-based screen for G1/S checkpoint activators identifies a selective activator of EIF2AK3/PERK signalling
    • Stockwell, S. R., Platt, G., Barrie, S. E., Zoumpoulidou, G., Te Poele, R. H., Aherne, G. W., et al. (2012). Mechanism-based screen for G1/S checkpoint activators identifies a selective activator of EIF2AK3/PERK signalling. PLoS ONE 7:e28568. doi: 10.1371/journal.pone.0028568.
    • (2012) PLoS ONE , vol.7
    • Stockwell, S.R.1    Platt, G.2    Barrie, S.E.3    Zoumpoulidou, G.4    Te Poele, R.H.5    Aherne, G.W.6
  • 114
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas, I., and Ron, D. (2011). Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell. Biol. 13, 184-190. doi: 10.1038/ncb0311-184.
    • (2011) Nat. Cell. Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 115
    • 48249139449 scopus 로고    scopus 로고
    • Multiple sclerosis: an immune or neurodegenerative disorder?
    • Trapp, B. D., and Nave, K. A. (2008). Multiple sclerosis: an immune or neurodegenerative disorder? Annu. Rev. Neurosci. 31, 247-269. doi: 10.1146/annurev.neuro.30.051606.094313.
    • (2008) Annu. Rev. Neurosci , vol.31 , pp. 247-269
    • Trapp, B.D.1    Nave, K.A.2
  • 116
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler, P., Harding, H. P., Ron, D., and Bertolotti, A. (2011). Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 332, 91-94. doi: 10.1126/science.1201396.
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 118
    • 84862731075 scopus 로고    scopus 로고
    • Shifting imaging targets in multiple sclerosis: from inflammation to neurodegeneration
    • Vigeveno, R. M., Wiebenga, O. T., Wattjes, M. P., Geurts, J. J., and Barkhof, F. (2012). Shifting imaging targets in multiple sclerosis: from inflammation to neurodegeneration. J. Magn. Reson. Imaging. 36, 1-19. doi: 10.1002/jmri.23578.
    • (2012) J. Magn. Reson. Imaging , vol.36 , pp. 1-19
    • Vigeveno, R.M.1    Wiebenga, O.T.2    Wattjes, M.P.3    Geurts, J.J.4    Barkhof, F.5
  • 119
    • 70350044493 scopus 로고    scopus 로고
    • Lower motor neuron loss in multiple sclerosis and experimental autoimmune encephalomyelitis
    • Vogt, J., Paul, F., Aktas, O., Müller-Wielsch, K., Dörr, J., Dörr, S., et al. (2009). Lower motor neuron loss in multiple sclerosis and experimental autoimmune encephalomyelitis. Ann. Neurol. 66, 310-322. doi: 10.1002/ana.21719.
    • (2009) Ann. Neurol , vol.66 , pp. 310-322
    • Vogt, J.1    Paul, F.2    Aktas, O.3    Müller-Wielsch, K.4    Dörr, J.5    Dörr, S.6
  • 120
    • 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
  • 121
    • 84908344184 scopus 로고    scopus 로고
    • Guanabenz, which enhances the unfolded protein response, ameliorates mutant SOD1-induced amyotrophic lateral sclerosis
    • Wang, L., Popko, B., Tixier, E., and Roos, R. P. (2014). Guanabenz, which enhances the unfolded protein response, ameliorates mutant SOD1-induced amyotrophic lateral sclerosis. Neurobiol. Dis. 71, 317-324. doi: 10.1016/j.nbd.2014.08.010.
    • (2014) Neurobiol. Dis , vol.71 , pp. 317-324
    • Wang, L.1    Popko, B.2    Tixier, E.3    Roos, R.P.4
  • 122
    • 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
  • 123
    • 84863740827 scopus 로고    scopus 로고
    • The impact of the unfolded protein response on human disease
    • Wang, S., and Kaufman, R. J. (2012). The impact of the unfolded protein response on human disease. J. Cell. Biol. 197, 857-867. doi: 10.1083/jcb.201110131.
    • (2012) J. Cell. Biol , vol.197 , pp. 857-867
    • Wang, S.1    Kaufman, R.J.2
  • 124
    • 84924891315 scopus 로고    scopus 로고
    • Pharmaceutical integrated stress response enhancement protects oligodendrocytes and provides a potential multiple sclerosis therapeutic
    • Way, S. W., Podojil, J. R., Clayton, B. L., Zaremba, A., Collins, T. L., Kunjamma, R. B., et al. (2015). Pharmaceutical integrated stress response enhancement protects oligodendrocytes and provides a potential multiple sclerosis therapeutic. Nat. Commun. 6, 6532. doi: 10.1038/ncomms7532.
    • (2015) Nat. Commun , vol.6 , pp. 6532
    • Way, S.W.1    Podojil, J.R.2    Clayton, B.L.3    Zaremba, A.4    Collins, T.L.5    Kunjamma, R.B.6
  • 125
    • 79953043284 scopus 로고    scopus 로고
    • Co-expression of miRNA targeting the expression of PERK, but not PKR, enhances cellular immunity from an HIV-1 Env DNA vaccine
    • Wheatley, A. K., Kramski, M., Alexander, M. R., Toe, J. G., Center, R. J., and Purcell, D. F. (2011). Co-expression of miRNA targeting the expression of PERK, but not PKR, enhances cellular immunity from an HIV-1 Env DNA vaccine. PLoS ONE 6:e18225. doi: 10.1371/journal.pone.0018225.
    • (2011) PLoS ONE , vol.6
    • Wheatley, A.K.1    Kramski, M.2    Alexander, M.R.3    Toe, J.G.4    Center, R.J.5    Purcell, D.F.6
  • 126
    • 14744292802 scopus 로고    scopus 로고
    • The changing face of cytokines in the brain: perspectives from EAE
    • Wheeler, R. D., and Owens, T. (2005). The changing face of cytokines in the brain: perspectives from EAE. Curr. Pharm. Des. 11, 1031-1037. doi: 10.2174/1381612053381657.
    • (2005) Curr. Pharm. Des , vol.11 , pp. 1031-1037
    • Wheeler, R.D.1    Owens, T.2
  • 127
    • 0030587910 scopus 로고    scopus 로고
    • IFN-gamma plays a critical down-regulatory role in the induction and effector phase of myelin oligodendrocyte glycoprotein-induced autoimmune encephalomyelitis
    • Willenborg, D. O., Fordham, S., Bernard, C. C., Cowden, W. B., and Ramshaw, I. A. (1996). IFN-gamma plays a critical down-regulatory role in the induction and effector phase of myelin oligodendrocyte glycoprotein-induced autoimmune encephalomyelitis. J. Immunol. 157, 3223-3227.
    • (1996) J. Immunol , vol.157 , pp. 3223-3227
    • Willenborg, D.O.1    Fordham, S.2    Bernard, C.C.3    Cowden, W.B.4    Ramshaw, I.A.5
  • 128
    • 0019781220 scopus 로고
    • Ultrastructural changes accompanying the growth of isolated oligodendrocytes
    • Wollmann, R. L., Szuchet, S., Barlow, J., and Jerkovic, M. (1981). Ultrastructural changes accompanying the growth of isolated oligodendrocytes. J. Neurosci. Res. 6, 757-769. doi: 10.1002/jnr.490060610.
    • (1981) J. Neurosci. Res , vol.6 , pp. 757-769
    • Wollmann, R.L.1    Szuchet, S.2    Barlow, J.3    Jerkovic, M.4
  • 129
    • 73349141743 scopus 로고    scopus 로고
    • Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling
    • Woo, C. W., Cui, D., Arellano, J., Dorweiler, B., Harding, H., Fitzgerald, K. A., et al. (2009). Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling. Nat. Cell. Biol. 11, 1473-1480. doi: 10.1038/ncb1996.
    • (2009) Nat. Cell. Biol , vol.11 , pp. 1473-1480
    • Woo, C.W.1    Cui, D.2    Arellano, J.3    Dorweiler, B.4    Harding, H.5    Fitzgerald, K.A.6
  • 130
    • 77956232915 scopus 로고    scopus 로고
    • Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress
    • Yamamoto, K., Takahara, K., Oyadomari, S., Okada, T., Sato, T., Harada, A., et al. (2010). Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress. Mol. Biol. Cell. 21, 2975-2986. doi: 10.1091/mbc.E09-02-0133.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2975-2986
    • Yamamoto, K.1    Takahara, K.2    Oyadomari, S.3    Okada, T.4    Sato, T.5    Harada, A.6
  • 131
    • 70350011787 scopus 로고    scopus 로고
    • NF-kappa B, a potential therapeutic target for the treatment of multiple sclerosis
    • Yan, J., and Greer, J. M. (2008). NF-kappa B, a potential therapeutic target for the treatment of multiple sclerosis. CNS Neurol. Disord. Drug Targets 7, 536-557. doi: 10.2174/187152708787122941.
    • (2008) CNS Neurol. Disord. Drug Targets , vol.7 , pp. 536-557
    • Yan, J.1    Greer, J.M.2
  • 132
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang, K., and Kaufman, R. J. (2008). From endoplasmic-reticulum stress to the inflammatory response. Nature 454, 455-462. doi: 10.1038/nature07203.
    • (2008) Nature , vol.454 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.