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  • Atkin, J.D., Farg, M.A., Turner, B.J., Tomas, D., Lysaght, J.A., Nunan, J., Rembach, A., Nagley, P., Beart, P.M., Cheema, S.S. & Horne, M.K. (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, 3015230165.
  • Atkin, J.D., Farg, M.A., Walker, A.K., McLean, C., Tomas, D. & Horne, M.K. (2008) Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol. Dis., 30, 400407.
  • Bergemalm, D., Forsberg, K., Srivastava, V., Graffmo, K.S., Andersen, P.M., Brannstrom, T., Wingsle, G. & Marklund, S.L. (2010) Superoxide dismutase-1 and other proteins in inclusions from transgenic amyotrophic lateral sclerosis model mice. J. Neurochem., 114, 408418.
  • Berridge, M.J. (2002) The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium, 32, 235249.
  • Cashman, N.R., Durham, H.D., Blusztajn, J.K., Oda, K., Tabira, T., Shaw, I.T., Dahrouge, S. & Antel, J.P. (1992) Neuroblastoma × spinal cord (NSC) hybrid cell lines resemble developing motor neurons. Dev. Dyn., 194, 209221.
  • Cho, Y.M., Jang, Y.S., Jang, Y.M., Chung, S.M., Kim, H.S., Lee, J.H., Jeong, S.W., Kim, I.K., Kim, J.J., Kim, K.S. & Kwon, O.J. (2009) Induction of unfolded protein response during neuronal induction of rat bone marrow stromal cells and mouse embryonic stem cells. Exp. Mol. Med., 41, 440452.
  • Cox, D.J., Strudwick, N., Ali, A.A., Paton, A.W., Paton, J.C. & Schroder, M. (2011) Measuring signaling by the unfolded protein response. Methods Enzymol., 491, 261292.
  • Dudek, J., Benedix, J., Cappel, S., Greiner, M., Jalal, C., Muller, L. & Zimmermann, R. (2009) Functions and pathologies of BiP and its interaction partners. Cell. Mol. Life Sci., 66, 15561569.
  • Ferri, A., Cozzolino, M., Crosio, C., Nencini, M., Casciati, A., Gralla, E.B., Rotilio, G., Valentine, J.S. & Carri, M.T. (2006) Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials. Proc. Natl Acad. Sci. USA, 103, 1386013865.
  • Friedman, J.R., Lackner, L.L., West, M., DiBenedetto, J.R., Nunnari, J. & Voeltz, G.K. (2011) ER tubules mark sites of mitochondrial division. Science, 334, 358362.
  • Gong, Y.H., Parsadanian, A.S., Andreeva, A., Snider, W.D. & Elliott, J.L. (2000) Restricted expression of G86R Cu/Zn superoxide dismutase in astrocytes results in astrocytosis but does not cause motoneuron degeneration. J. Neurosci., 20, 660665.
  • Grosskreutz, J., Van Den, B.L. & Keller, B.U. (2010) Calcium dysregulation in amyotrophic lateral sclerosis. Cell Calcium, 47, 165174.
  • Guo, Y., Li, C., Wu, D., Wu, S., Yang, C., Liu, Y., Wu, H. & Li, Z. (2010) Ultrastructural diversity of inclusions and aggregations in the lumbar spinal cord of SOD1-G93A transgenic mice. Brain Res., 1353, 234244.
  • Gurney, M.E., Pu, H., Chiu, A.Y., Dal Canto, M.C., Polchow, C.Y., Alexander, D.D., Caliendo, J., Hentati, A., Kwon, Y.W. & Deng, H.X. (1994) Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science, 264, 17721775.
  • Haastert, K., Grosskreutz, J., Jaeckel, M., Laderer, C., Bufler, J., Grothe, C. & Claus, P. (2005) Rat embryonic motoneurons in long-term co-culture with Schwann cells-a system to investigate motoneuron diseases on a cellular level in vitro. J. Neurosci. Methods, 142, 275284.
  • Ilieva, E.V., Ayala, V., Jove, M., Dalfo, E., Cacabelos, D., Povedano, M., Bellmunt, M.J., Ferrer, I., Pamplona, R. & Portero-Otin, M. (2007) Oxidative and endoplasmic reticulum stress interplay in sporadic amyotrophic lateral sclerosis. Brain, 130, 31113123.
  • Ilieva, H., Polymenidou, M. & Cleveland, D.W. (2009) Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J. Cell Biol., 187, 761772.
  • Jonsson, P.A., Ernhill, K., Andersen, P.M., Bergemalm, D., Brannstrom, T., Gredal, O., Nilsson, P. & Marklund, S.L. (2004) Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis. Brain, 127, 7388.
  • Karch, C.M., Prudencio, M., Winkler, D.D., Hart, P.J. & Borchelt, D.R. (2009) Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc. Natl Acad. Sci. USA, 106, 77747779.
  • Kikuchi, H., Almer, G., Yamashita, S., Guegan, C., Nagai, M., Xu, Z., Sosunov, A.A., McKhann, G.M. & Przedborski, S. (2006) Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model. Proc. Natl Acad. Sci. USA, 103, 60256030.
  • Kozutsumi, Y., Segal, M., Normington, K., Gething, M.J. & Sambrook, J. (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature, 332, 462464.
  • Lee, A.H., Iwakoshi, N.N. & Glimcher, L.H. (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol., 23, 74487459.
  • Nagai, M., Re, D.B., Nagata, T., Chalazonitis, A., Jessell, T.M., Wichterle, H. & Przedborski, S. (2007) Astrocytes expressing ALS-linked mutated SOD1 release factors selectively toxic to motor neurons. Nat. Neurosci., 10, 615622.
  • Nagata, T., Ilieva, H., Murakami, T., Shiote, M., Narai, H., Ohta, Y., Hayashi, T., Shoji, M. & Abe, K. (2007) Increased ER stress during motor neuron degeneration in a transgenic mouse model of amyotrophic lateral sclerosis. Neurol. Res., 29, 767771.
  • Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B.A. & Yuan, J. (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature, 403, 98103.
  • Nishitoh, H., Kadowaki, H., Nagai, A., Maruyama, T., Yokota, T., Fukutomi, H., Noguchi, T., Matsuzawa, A., Takeda, K. & Ichijo, H. (2008) ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1. Genes Dev., 22, 14511464.
  • Oh, Y.K., Shin, K.S., Yuan, J. & Kang, S.J. (2008) Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells. J. Neurochem., 104, 9931005.
  • Papadeas, S.T., Kraig, S.E., O’Banion, C., Lepore, A.C. & Maragakis, N.J. (2011) Astrocytes carrying the superoxide dismutase 1 (SOD1G93A) mutation induce wild-type motor neuron degeneration in vivo. Proc. Natl Acad. Sci. USA, 108, 1780317808.
  • Parker, R., Phan, T., Baumeister, P., Roy, B., Cheriyath, V., Roy, A.L. & Lee, A.S. (2001) Identification of TFII-I as the endoplasmic reticulum stress response element binding factor ERSF: its autoregulation by stress and interaction with ATF6. Mol. Cell. Biol., 21, 32203233.
  • Philips, T. & Robberecht, W. (2011) Neuroinflammation in amyotrophic lateral sclerosis: role of glial activation in motor neuron disease. Lancet Neurol., 10, 253263.
  • Proescher, J.B., Son, M., Elliott, J.L. & Culotta, V.C. (2008) Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS. Hum. Mol. Genet., 17, 17281737.
  • Prudencio, M., Durazo, A., Whitelegge, J.P. & Borchelt, D.R. (2010) An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Hum. Mol. Genet., 19, 47744789.
  • Rothstein, J.D. (2009) Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann. Neurol., 65(Suppl 1), S3S9.
  • Saxena, S., Cabuy, E. & Caroni, P. (2009) A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci., 12, 627636.
  • Shaw, B.F. & Valentine, J.S. (2007) How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem. Sci., 32, 7885.
  • Sriburi, R., Jackowski, S., Mori, K. & Brewer, J.W. (2004) XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J. Cell Biol., 167, 3541.
  • Thuerauf, D.J., Morrison, L. & Glembotski, C.C. (2004) Opposing roles for ATF6alpha and ATF6beta in endoplasmic reticulum stress response gene induction. J. Biol. Chem., 279, 2107821084.
  • Thuerauf, D.J., Marcinko, M., Belmont, P.J. & Glembotski, C.C. (2007) Effects of the isoform-specific characteristics of ATF6 alpha and ATF6 beta on endoplasmic reticulum stress response gene expression and cell viability. J. Biol. Chem., 282, 2286522878.
  • Van Damme, P., Callewaert, G., Eggermont, J., Robberecht, W. & Van Den Bosch, L. (2003) Chloride influx aggravates Ca2+-dependent AMPA receptor-mediated motoneuron death. J. Neurosci., 23, 49424950.
  • Van Den Bosch, L., Vandenberghe, W., Klaassen, H., Van Houtte, E. & Robberecht, W. (2000) Ca(2+ )-permeable AMPA receptors and selective vulnerability of motor neurons. J. Neurol. Sci., 180, 2934.
  • Verkhratsky, A. (2005) Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons. Physiol. Rev., 85, 201279.
  • Vijayalakshmi, K., Alladi, P.A., Ghosh, S., Prasanna, V.K., Sagar, B.C., Nalini, A., Sathyaprabha, T.N. & Raju, T.R. (2011) Evidence of endoplasmic reticular stress in the spinal motor neurons exposed to CSF from sporadic amyotrophic lateral sclerosis patients. Neurobiol. Dis., 41, 695705.
  • Walker, A.K. (2010) Protein disulfide isomerase and the endoplasmic reticulum in amyotrophic lateral sclerosis. J. Neurosci., 30, 38653867.
  • Wang, Y., Shen, J., Arenzana, N., Tirasophon, W., Kaufman, R.J. & Prywes, R. (2000) Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. J. Biol. Chem., 275, 2701327020.
  • Watanabe, M., Dykes-Hoberg, M., Culotta, V.C., Price, D.L., Wong, P.C. & Rothstein, J.D. (2001) Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol. Dis., 8, 933941.
  • Yamanaka, K., Chun, S.J., Boillee, S., Fujimori-Tonou, N., Yamashita, H., Gutmann, D.H., Takahashi, R., Misawa, H. & Cleveland, D.W. (2008) Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis. Nat. Neurosci., 11, 251253.
  • Yoshida, H., Matsui, T., Yamamoto, A., Okada, T. & Mori, K. (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell, 107, 881891.
  • Yoshida, H., Oku, M., Suzuki, M. & Mori, K. (2006) pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J. Cell Biol., 172, 565575.