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Bull."},{"key":"10.1016\/j.neulet.2017.06.052_bib0355","doi-asserted-by":"crossref","first-page":"3320","DOI":"10.1016\/j.bbagen.2014.08.012","article-title":"Methyl pyruvate rescues mitochondrial damage caused by SIGMAR1 mutation related to amyotrophic lateral sclerosis","volume":"1840","author":"Tagashira","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.neulet.2017.06.052_bib0360","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/j.bbamcr.2012.11.004","article-title":"A role for sequestosome 1\/p62 in mitochondrial dynamics, Import and genome integrity","volume":"1833","author":"Seibenhener","year":"2013","journal-title":"Biochim. Biophys. Acta \u2013 Mol. 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Phys."},{"key":"10.1016\/j.neulet.2017.06.052_bib0380","doi-asserted-by":"crossref","first-page":"10625","DOI":"10.1073\/pnas.91.22.10625","article-title":"Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization","volume":"91","author":"Pellerin","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.neulet.2017.06.052_bib0385","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1016\/j.cmet.2011.08.016","article-title":"Brain energy metabolism: focus on astrocyte-neuron metabolic cooperation","volume":"14","author":"B\u00e9langer","year":"2011","journal-title":"Cell Metab."},{"key":"10.1016\/j.neulet.2017.06.052_bib0390","doi-asserted-by":"crossref","first-page":"2627","DOI":"10.1093\/brain\/awr193","article-title":"Dysregulation of astrocyte-motoneuron cross-talk in mutant superoxide dismutase 1-related amyotrophic lateral sclerosis","volume":"134","author":"Ferraiuolo","year":"2011","journal-title":"Brain"},{"key":"10.1016\/j.neulet.2017.06.052_bib0395","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/nature11314","article-title":"Oligodendroglia metabolically support axons and contribute to neurodegeneration","volume":"487","author":"Lee","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.neulet.2017.06.052_bib0400","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1113\/jphysiol.2003.049478","article-title":"Mitochondrial formation of reactive oxygen species","volume":"552","author":"Turrens","year":"2003","journal-title":"J. Physiol. (Lond.)"},{"key":"10.1016\/j.neulet.2017.06.052_bib0405","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20081386","article-title":"How mitochondria produce reactive oxygen species","volume":"417","author":"Murphy","year":"2009","journal-title":"Biochem. J"},{"key":"10.1016\/j.neulet.2017.06.052_bib0410","doi-asserted-by":"crossref","first-page":"325","DOI":"10.5607\/en.2015.24.4.325","article-title":"The role of oxidative stress in neurodegenerative diseases","volume":"24","author":"Kim","year":"2015","journal-title":"Exp. Neurobiol."},{"key":"10.1016\/j.neulet.2017.06.052_bib0415","doi-asserted-by":"crossref","first-page":"428010","DOI":"10.1155\/2012\/428010","article-title":"Mechanism of oxidative stress in neurodegeneration","volume":"2012","author":"Gandhi","year":"2012","journal-title":"Oxid. Med. Cell. Longev."},{"key":"10.1016\/j.neulet.2017.06.052_bib0420","doi-asserted-by":"crossref","first-page":"646354","DOI":"10.1155\/2012\/646354","article-title":"Oxidative stress, mitochondrial dysfunction, and aging","volume":"2012","author":"Cui","year":"2012","journal-title":"J. Signal Transduc."},{"issue":"Suppl","key":"10.1016\/j.neulet.2017.06.052_bib0425","doi-asserted-by":"crossref","first-page":"S18","DOI":"10.1038\/nrn1434","article-title":"Oxidative stress in neurodegeneration: cause or consequence?","volume":"10","author":"Andersen","year":"2004","journal-title":"Nat. Med."},{"key":"10.1016\/j.neulet.2017.06.052_bib0430","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/j.freeradbiomed.2009.11.018","article-title":"Oxidative stress in ALS: Key role in motor neuron injury and therapeutic target","volume":"48","author":"Barber","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.neulet.2017.06.052_bib0435","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1002\/ana.410440419","article-title":"Presence of 4-hydroxynonenal in cerebrospinal fluid of patients with sporadic amyotrophic lateral sclerosis","volume":"44","author":"Smith","year":"1998","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.neulet.2017.06.052_bib0440","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.1212\/WNL.62.10.1758","article-title":"Increased lipid peroxidation in sera of ALS patients: a potential biomarker of disease burden","volume":"62","author":"Simpson","year":"2004","journal-title":"Neurology"},{"key":"10.1016\/j.neulet.2017.06.052_bib0445","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1080\/17482960801933942","article-title":"Oxidative stress biomarkers in sporadic ALS","volume":"9","author":"Mitsumoto","year":"2008","journal-title":"Amyotroph. Lateral Scler."},{"key":"10.1016\/j.neulet.2017.06.052_bib0450","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1016\/S0891-5849(00)00349-X","article-title":"Increased oxidative damage to DNA in ALS patients","volume":"29","author":"Bogdanov","year":"2000","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.neulet.2017.06.052_bib0455","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1002\/ana.410380424","article-title":"Oxidative damage to protein in sporadic motor neuron disease spinal cord","volume":"38","author":"Shaw","year":"1995","journal-title":"Ann. 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Neurol. Sci."},{"key":"10.1016\/j.neulet.2017.06.052_bib0480","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1159\/000121390","article-title":"Lack of evidence for oxidative stress in sporadic amyotrophic lateral sclerosis fibroblasts","volume":"6","author":"Sala","year":"2009","journal-title":"Neurodegener. Dis."},{"issue":"Suppl","key":"10.1016\/j.neulet.2017.06.052_bib0485","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/0022-510X(96)00070-6","article-title":"Evidence against increased oxidative stress in fibroblasts from patients with non-superoxide-dismutase-1 mutant familial amyotrophic lateral sclerosis","volume":"139","author":"Jansen","year":"1996","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.neulet.2017.06.052_bib0490","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1002\/ana.410430407","article-title":"Increased sensitivity of fibroblasts from amyotrophic lateral sclerosis patients to oxidative stress","volume":"43","author":"Aguirre","year":"1998","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.neulet.2017.06.052_bib0495","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1046\/j.1471-4159.1998.71052041.x","article-title":"Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis","volume":"71","author":"Andrus","year":"1998","journal-title":"J. Neurochem."},{"key":"10.1016\/j.neulet.2017.06.052_bib0500","doi-asserted-by":"crossref","first-page":"47551","DOI":"10.1074\/jbc.M207356200","article-title":"Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis","volume":"277","author":"Rakhit","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.neulet.2017.06.052_bib0505","doi-asserted-by":"crossref","first-page":"3947","DOI":"10.1093\/hmg\/ddt249","article-title":"Mitochondrial damage revealed by immunoselection for ALS-linked misfolded SOD1","volume":"22","author":"Pickles","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.neulet.2017.06.052_bib0510","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1186\/s40478-016-0313-8","article-title":"ALS-linked misfolded SOD1 species have divergent impacts on mitochondria","volume":"4","author":"Pickles","year":"2016","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.neulet.2017.06.052_bib0515","doi-asserted-by":"crossref","first-page":"5505","DOI":"10.1073\/pnas.1115009109","article-title":"Localization of a toxic form of superoxide dismutase 1 protein to pathologically affected tissues in familial ALS","volume":"109","author":"Brotherton","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.neulet.2017.06.052_bib0520","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.1038\/nn.2660","article-title":"Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS","volume":"13","author":"Bosco","year":"2010","journal-title":"Nat. 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(Lond.)"},{"key":"10.1016\/j.neulet.2017.06.052_bib0665","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.ceca.2009.12.002","article-title":"Calcium dysregulation in amyotrophic lateral sclerosis","volume":"47","author":"Grosskreutz","year":"2010","journal-title":"Cell Calcium"},{"key":"10.1016\/j.neulet.2017.06.052_bib0670","doi-asserted-by":"crossref","first-page":"147","DOI":"10.3389\/fncel.2014.00147","article-title":"The ER mitochondria calcium cycle and ER stress response as therapeutic targets in amyotrophic lateral sclerosis","volume":"8","author":"Tadic","year":"2014","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.neulet.2017.06.052_bib0675","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2017.02.004","article-title":"Neurobiology of axonal transport defects in motor neuron diseases: opportunities for translational research?","author":"De Vos","year":"2017","journal-title":"Neurobiol. 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A."},{"key":"10.1016\/j.neulet.2017.06.052_bib0910","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.neuron.2015.06.026","article-title":"Endolysosomal deficits augment mitochondria pathology in spinal motor neurons of asymptomatic fALS mice","volume":"87","author":"Xie","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.neulet.2017.06.052_bib0915","doi-asserted-by":"crossref","first-page":"1276","DOI":"10.15252\/embj.201593350","article-title":"Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death","volume":"35","author":"Sellier","year":"2016","journal-title":"EMBO J."},{"key":"10.1016\/j.neulet.2017.06.052_bib0920","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.15252\/embj.201694401","article-title":"The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy","volume":"35","author":"Webster","year":"2016","journal-title":"EMBO J."},{"key":"10.1016\/j.neulet.2017.06.052_bib0925","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1186\/s40478-016-0324-5","article-title":"The ALS\/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway","volume":"4","author":"Sullivan","year":"2016","journal-title":"Acta Neuropathol. 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