{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T08:26:43Z","timestamp":1793176003204,"version":"4.5.0"},"reference-count":93,"publisher":"Frontiers Media SA","funder":[{"DOI":"10.13039\/100013278","name":"JPND","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100013278","id-type":"DOI","asserted-by":"crossref"}]},{"name":"ARISLA"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cell. Neurosci."],"DOI":"10.3389\/fncel.2015.00336","type":"journal-article","created":{"date-parts":[[2015,8,25]],"date-time":"2015-08-25T04:21:44Z","timestamp":1440476504000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":151,"title":["SOD1 misplacing and mitochondrial dysfunction in amyotrophic lateral sclerosis pathogenesis"],"prefix":"10.3389","volume":"9","author":[{"given":"Francesco","family":"Tafuri","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dario","family":"Ronchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesca","family":"Magri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giacomo P.","family":"Comi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefania","family":"Corti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2015,8,25]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1016\/j.nbd.2008.08.010","article-title":"Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane","volume":"32","author":"Ahtoniemi","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"B2","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1007\/s10534-010-9392-3","article-title":"Copper depletion increases the mitochondrial-associated SOD1 in neuronal cells","volume":"24","author":"Arciello","year":"2011","journal-title":"Biometals"},{"key":"B3","doi-asserted-by":"publisher","first-page":"6410","DOI":"10.1021\/ac070585g","article-title":"RCADiA: simple automation platform for comparative multidimensional protein identification technology","volume":"79","author":"Bailey","year":"2007","journal-title":"Anal. Chem."},{"key":"B4","doi-asserted-by":"publisher","first-page":"e1677","DOI":"10.1371\/journal.pone.0001677","article-title":"SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization","volume":"3","author":"Banci","year":"2008","journal-title":"PLoS One"},{"key":"B5","doi-asserted-by":"publisher","first-page":"13555","DOI":"10.1073\/pnas.1207493109","article-title":"Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)","volume":"109","author":"Banci","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B6","doi-asserted-by":"publisher","first-page":"2329","DOI":"10.1093\/brain\/awu138","article-title":"A mitochondrial origin for frontotemporal dementia and amyotrophic lateral sclerosis through CHCHD10 involvement","volume":"137","author":"Bannwarth","year":"2014","journal-title":"Brain"},{"key":"B7","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1016\/j.neuron.2006.09.018","article-title":"ALS: a disease of motor neurons and their nonneuronal neighbors","volume":"52","author":"Boill\u00e9e","year":"2006","journal-title":"Neuron"},{"key":"B8","doi-asserted-by":"publisher","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":"B9","doi-asserted-by":"publisher","first-page":"723","DOI":"10.1146\/annurev.neuro.27.070203.144244","article-title":"Unraveling the mechanisms involved in motor neuron degeneration in Als","volume":"27","author":"Bruijn","year":"2004","journal-title":"Annu. Rev. Neurosci."},{"key":"B10","doi-asserted-by":"publisher","first-page":"668","DOI":"10.1016\/j.clinthera.2014.12.020","article-title":"Therapeutic development in amyotrophic lateral sclerosis","volume":"37","author":"Bucchia","year":"2015","journal-title":"Clin. Ther."},{"key":"B11","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1002\/ana.410430119","article-title":"Cytochrome c oxidase subunit I microdeletion in a patient with motor neuron disease","volume":"43","author":"Comi","year":"1998","journal-title":"Ann. Neurol."},{"key":"B12","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1016\/j.jns.2008.09.030","article-title":"Amyotrophic lateral sclerosis linked to a novel SOD1 mutation with muscle mitochondrial dysfunction","volume":"276","author":"Corti","year":"2009","journal-title":"J. Neurol. Sci."},{"key":"B13","doi-asserted-by":"publisher","first-page":"866","DOI":"10.1074\/jbc.m705657200","article-title":"Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis","volume":"283","author":"Cozzolino","year":"2008","journal-title":"J. Biol. Chem."},{"key":"B14","doi-asserted-by":"publisher","first-page":"1547","DOI":"10.1089\/ars.2009.2545","article-title":"Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity","volume":"11","author":"Cozzolino","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"B15","doi-asserted-by":"publisher","first-page":"31","DOI":"10.3389\/fncel.2015.00031","article-title":"Mitochondrial dynamism and the pathogenesis of amyotrophic lateral sclerosis","volume":"9","author":"Cozzolino","year":"2015","journal-title":"Front. Cell. Neurosci."},{"key":"B16","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1001\/archneurol.2010.128","article-title":"Mitochondrial respiratory chain dysfunction in muscle from patients with amyotrophic lateral sclerosis","volume":"67","author":"Crugnola","year":"2010","journal-title":"Arch. Neurol."},{"key":"B17","doi-asserted-by":"publisher","first-page":"23469","DOI":"10.1074\/jbc.272.38.23469","article-title":"The copper chaperone for superoxide dismutase","volume":"272","author":"Culotta","year":"1997","journal-title":"J. Biol. Chem."},{"key":"B18","doi-asserted-by":"publisher","first-page":"7142","DOI":"10.1073\/pnas.0602046103","article-title":"Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria","volume":"103","author":"Deng","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B19","doi-asserted-by":"publisher","DOI":"10.1016\/j.cca.2015.04.042","article-title":"Candidate genes for parkinson disease: lessons from pathogenesis","author":"De Rosa","year":"2015","journal-title":"Clin. Chim. Acta"},{"key":"B20","doi-asserted-by":"publisher","first-page":"594","DOI":"10.3410\/f.1159634.621028","article-title":"The mitochondrial disulfide relay system protein GFER is mutated in autosomal-recessive myopathy with cataract and combined respiratory-chain deficiency","volume":"84","author":"Di Fonzo","year":"2009","journal-title":"Am. J. Hum. Genet."},{"key":"B21","doi-asserted-by":"publisher","first-page":"13860","DOI":"10.1073\/pnas.0605814103","article-title":"Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials","volume":"103","author":"Ferri","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B22","doi-asserted-by":"publisher","first-page":"4529","DOI":"10.1093\/hmg\/ddq383","article-title":"Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity","volume":"19","author":"Ferri","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"B23","doi-asserted-by":"publisher","first-page":"454","DOI":"10.1016\/j.nbd.2008.08.004","article-title":"Inflammatory cytokines increase mitochondrial damage in motoneuronal cells expressing mutant SOD1","volume":"32","author":"Ferri","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"B24","doi-asserted-by":"publisher","first-page":"28052","DOI":"10.1074\/jbc.m304296200","article-title":"Factors controlling the uptake of yeast copper\/zinc superoxide dismutase into mitochondria","volume":"278","author":"Field","year":"2003","journal-title":"J. Biol. Chem."},{"key":"B25","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1093\/brain\/awq314","article-title":"SOD1 targeted to the mitochondrial intermembrane space prevents motor neuropathy in the Sod1 knockout mouse","volume":"134","author":"Fischer","year":"2011","journal-title":"Brain"},{"key":"B26","doi-asserted-by":"publisher","DOI":"10.1155\/2013\/742923","article-title":"The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond","volume":"742923","author":"Fischer","year":"2013","journal-title":"Int. J. Cell Biol."},{"key":"B27","doi-asserted-by":"publisher","first-page":"2723","DOI":"10.1113\/jphysiol.2012.247981","article-title":"Selective mitochondrial Ca2+ uptake deficit in disease endstage vulnerable motoneurons of the SOD1G93A mouse model of amyotrophic lateral sclerosis","volume":"591","author":"Fuchs","year":"2013","journal-title":"J. Physiol."},{"key":"B28","doi-asserted-by":"publisher","first-page":"8446","DOI":"10.1074\/jbc.M706111200","article-title":"Deleterious role of superoxide dismutase in the mitochondrial intermembrane space","volume":"283","author":"Goldsteins","year":"2008","journal-title":"J. Biol. Chem."},{"key":"B29","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1186\/1471-2334-7-131","article-title":"Expression of a Cu,Zn superoxide dismutase typical for familial amyotrophic lateral sclerosis increases the vulnerability of neuroblastoma cells to infectious injury","volume":"7","author":"Goos","year":"2007","journal-title":"BMC Infect. Dis."},{"key":"B30","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1093\/hmg\/dds399","article-title":"Expression of wild-type human superoxide dismutase-1 in mice causes amyotrophic lateral sclerosis","volume":"22","author":"Graffmo","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"B31","doi-asserted-by":"publisher","first-page":"1772","DOI":"10.1126\/science.8209258","article-title":"Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation","volume":"264","author":"Gurney","year":"1994","journal-title":"Science"},{"key":"B32","doi-asserted-by":"publisher","first-page":"3758","DOI":"10.1091\/mbc.e11-04-0296","article-title":"Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system","volume":"22","author":"Gro\u00df","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"B33","doi-asserted-by":"publisher","first-page":"1323","DOI":"10.1089\/ars.2010.3270","article-title":"Oxidation and reduction of cysteines in the intermembrane space of mitochondria: multiple facets of redox control","volume":"13","author":"Herrmann","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"B34","doi-asserted-by":"crossref","first-page":"RC215","DOI":"10.1523\/JNEUROSCI.22-06-j0001.2002","article-title":"Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS","volume":"22","author":"Higgins","year":"2002","journal-title":"J. Neurosci."},{"key":"B35","doi-asserted-by":"publisher","first-page":"15826","DOI":"10.1523\/jneurosci.1965-11.2011","article-title":"In vivo pathogenic role of mutant SOD1 localized in the mitochondrial intermembrane space","volume":"31","author":"Igoudjil","year":"2011","journal-title":"J. Neurosci."},{"key":"B36","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1016\/j.neuron.2010.07.019","article-title":"Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS","volume":"67","author":"Israelson","year":"2010","journal-title":"Neuron"},{"key":"B37","doi-asserted-by":"publisher","first-page":"218","DOI":"10.1016\/j.neuron.2015.02.034","article-title":"Macrophage migration inhibitory factor as a chaperone inhibiting accumulation of misfolded SOD1","volume":"86","author":"Israelson","year":"2015","journal-title":"Neuron"},{"key":"B38","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1007\/s004010100399","article-title":"CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations","volume":"102","author":"Jaarsma","year":"2001","journal-title":"Acta Neuropathol."},{"key":"B39","doi-asserted-by":"publisher","first-page":"478","DOI":"10.1124\/mol.108.050831","article-title":"Cu\/Zn superoxide dismutase typical for familial amyotrophic lateral sclerosis increases the vulnerability of mitochondria and perturbs Ca2+ homeostasis in SOD1G93A mice","volume":"75","author":"Jaiswal","year":"2009","journal-title":"Mol. Pharmacol."},{"key":"B40","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1186\/1471-2202-10-64","article-title":"Impairment of mitochondrial calcium handling in a mtSOD1 cell culture model of motoneuron disease","volume":"10","author":"Jaiswal","year":"2009","journal-title":"BMC Neurosci."},{"key":"B41","doi-asserted-by":"publisher","first-page":"12571","DOI":"10.1073\/pnas.220417997","article-title":"Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis","volume":"97","author":"Johnston","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B42","doi-asserted-by":"publisher","first-page":"1126","DOI":"10.1097\/01.jnen.0000248545.36046.3c","article-title":"Motor neuron disease in mice expressing the wild type-like D90A mutant superoxide dismutase-1","volume":"65","author":"Jonsson","year":"2006","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"B43","doi-asserted-by":"publisher","first-page":"7774","DOI":"10.1073\/pnas.0902505106","article-title":"Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS","volume":"106","author":"Karch","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B44","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1007\/s00401-007-0308-4","article-title":"Amyotrophic lateral sclerosis models and human neuropathology: similarities and differences","volume":"115","author":"Kato","year":"2008","journal-title":"Acta Neuropathol."},{"key":"B45","doi-asserted-by":"publisher","first-page":"3303","DOI":"10.1093\/hmg\/ddn226","article-title":"Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria","volume":"17","author":"Kawamata","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"B46","doi-asserted-by":"publisher","first-page":"1375","DOI":"10.1089\/ars.2010.3212","article-title":"Import, maturation and function of SOD1 and its copper chaperone CCS in the mitochondrial intermembrane space","volume":"13","author":"Kawamata","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"B47","doi-asserted-by":"publisher","first-page":"3749","DOI":"10.1091\/mbc.e11-04-0293","article-title":"Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol","volume":"22","author":"Kl\u00f6ppel","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"B48","doi-asserted-by":"publisher","first-page":"21146","DOI":"10.1073\/pnas.1014862107","article-title":"ALS-linked mutant superoxide dismutase 1 (SOD1) alters mitochondrial protein composition and decreases protein import","volume":"107","author":"Li","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B49","doi-asserted-by":"publisher","first-page":"9754","DOI":"10.1073\/pnas.0501957102","article-title":"Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants","volume":"102","author":"Lindberg","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B50","doi-asserted-by":"publisher","first-page":"5","DOI":"10.3410\/f.1022214.251768","article-title":"Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria","volume":"8","author":"Liu","year":"2004","journal-title":"Neuron"},{"key":"B51","doi-asserted-by":"publisher","first-page":"e82112","DOI":"10.1371\/journal.pone.0082112","article-title":"Defective mitochondrial dynamics is an early event in skeletal muscle of an amyotrophic lateral sclerosis mouse model","volume":"8","author":"Luo","year":"2013","journal-title":"PLoS One"},{"key":"B52","doi-asserted-by":"publisher","first-page":"4552","DOI":"10.1093\/hmg\/ddp421","article-title":"Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities","volume":"18","author":"Magran\u00e9","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"B53","doi-asserted-by":"publisher","first-page":"29626","DOI":"10.1074\/jbc.m203065200","article-title":"Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice","volume":"277","author":"Mattiazzi","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B54","doi-asserted-by":"publisher","first-page":"1059","DOI":"10.1016\/j.cell.2005.04.011","article-title":"A disulfide relay system in the intermembrane space of mitochondria that mediates protein import","volume":"121","author":"Mesecke","year":"2005","journal-title":"Cell"},{"key":"B55","doi-asserted-by":"publisher","first-page":"629","DOI":"10.1016\/s0092-8674(03)00926-7","article-title":"Integrated analysis of protein composition, tissue diversity and gene regulation in mouse mitochondria","volume":"115","author":"Mootha","year":"2003","journal-title":"Cell"},{"key":"B56","doi-asserted-by":"publisher","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":"B57","doi-asserted-by":"publisher","first-page":"28087","DOI":"10.1074\/jbc.m704465200","article-title":"Disulfide bond mediates aggregation, toxicity and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1","volume":"282","author":"Niwa","year":"2007","journal-title":"J. Biol. Chem."},{"key":"B58","doi-asserted-by":"publisher","first-page":"38388","DOI":"10.1074\/jbc.m105395200","article-title":"Subcellular distribution of superoxide dismutases (SOD) in rat liver Cu,Zn-SOD in mitochondria","volume":"276","author":"Okado-Matsumoto","year":"2001","journal-title":"J. Biol. Chem."},{"key":"B59","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1016\/j.brainres.2014.09.065","article-title":"Exploring new pathways of neurodegeneration in ALS: the role of mitochondria quality control","volume":"1607","author":"Palomo","year":"2015","journal-title":"Brain Res."},{"key":"B60","doi-asserted-by":"publisher","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":"B61","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.neuron.2004.06.021","article-title":"Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria","volume":"43","author":"Pasinelli","year":"2004","journal-title":"Neuron"},{"key":"B62","doi-asserted-by":"publisher","first-page":"2974","DOI":"10.1093\/hmg\/ddq202","article-title":"ALS-linked mutant SOD1 damages mitochondria by promoting conformational changes in Bcl-2","volume":"19","author":"Pedrini","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"B63","doi-asserted-by":"publisher","first-page":"1728","DOI":"10.1093\/hmg\/ddn063","article-title":"Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS","volume":"17","author":"Proescher","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"B64","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1038\/nn.3584","article-title":"State of play in amyotrophic lateral sclerosis genetics","volume":"17","author":"Renton","year":"2014","journal-title":"Nat. Neurosci."},{"key":"B65","doi-asserted-by":"publisher","first-page":"999","DOI":"10.1007\/s00018-013-1480-4","article-title":"Cellular therapy to target neuroinflammation in amyotrophic lateral sclerosis","volume":"71","author":"Rizzo","year":"2014","journal-title":"Cell. Mol. Life Sci."},{"key":"B66","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1038\/nrn3430","article-title":"The changing scene of amyotrophic lateral sclerosis","volume":"14","author":"Robberecht","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"B67","doi-asserted-by":"publisher","first-page":"10516","DOI":"10.1073\/pnas.0502515102","article-title":"Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis","volume":"102","author":"Rodriguez","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B68","doi-asserted-by":"publisher","first-page":"15932","DOI":"10.1074\/jbc.m112088200","article-title":"Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper\/Zinc superoxide dismutase","volume":"277","author":"Rodriguez","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B69","doi-asserted-by":"publisher","first-page":"3404","DOI":"10.1093\/brain\/aws258","article-title":"Next-generation sequencing reveals DGUOK mutations in adult patients with mitochondrial DNA multiple deletions","volume":"135","author":"Ronchi","year":"2012","journal-title":"Brain"},{"key":"B70","doi-asserted-by":"publisher","first-page":"e372","DOI":"10.1093\/brain\/awu384","article-title":"CHCHD10 mutations in italian patients with sporadic amyotrophic lateral sclerosis","volume":"138","author":"Ronchi","year":"2015","journal-title":"Brain"},{"key":"B71","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1038\/364362c0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"362","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"B72","doi-asserted-by":"publisher","first-page":"253","DOI":"10.3389\/fncel.2013.00253","article-title":"An emerging role for misfolded wild-type SOD1 insporadic ALS pathogenesis","volume":"7","author":"Rotunno","year":"2013","journal-title":"Front. Cell. Neurosci."},{"key":"B73","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1007\/s00401-004-0837-z","article-title":"Ultrastructural study of mitochondria in the spinal cord of transgenic mice with a G93A mutant SOD1 gene","volume":"107","author":"Sasaki","year":"2004","journal-title":"Acta Neuropathol."},{"key":"B74","doi-asserted-by":"publisher","first-page":"1954","DOI":"10.1212\/01.wnl.0000188760.53922.05","article-title":"Rapid disease progression correlates with instability of mutant SOD1 in familial ALS","volume":"65","author":"Sato","year":"2005","journal-title":"Neurology"},{"key":"B75","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1016\/j.neuron.2011.06.003","article-title":"Mitochondria: the next (neurode)generation","volume":"70","author":"Schon","year":"2011","journal-title":"Neuron"},{"key":"B76","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1038\/20959","article-title":"Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC","volume":"399","author":"Shimizu","year":"1999","journal-title":"Nature"},{"key":"B77","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1016\/j.nbd.2009.01.005","article-title":"Redox susceptibility of SOD1 mutants is associated with the differential response to CCS over-expression in vivo","volume":"34","author":"Son","year":"2009","journal-title":"Neurobiol. Dis."},{"key":"B78","doi-asserted-by":"publisher","first-page":"12267","DOI":"10.1074\/jbc.M708523200","article-title":"Isolated cytochrome","volume":"283","author":"Son","year":"2008","journal-title":"J. Biol. Chem."},{"key":"B79","doi-asserted-by":"publisher","first-page":"6072","DOI":"10.1073\/pnas.0610923104","article-title":"Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology","volume":"104","author":"Son","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B80","doi-asserted-by":"publisher","first-page":"38084","DOI":"10.1074\/jbc.M105296200","article-title":"A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage","volume":"276","author":"Sturtz","year":"2001","journal-title":"J. Biol. Chem."},{"key":"B81","doi-asserted-by":"publisher","first-page":"2430","DOI":"10.1038\/ncomms3430","article-title":"Human copper chaperone for superoxide dismutase 1 mediates its own oxidation-dependent import into mitochondria","volume":"4","author":"Suzuki","year":"2013","journal-title":"Nat. Commun."},{"key":"B82","doi-asserted-by":"publisher","first-page":"3568","DOI":"10.1093\/hmg\/dds188","article-title":"Mutant superoxide dismutase-1 indistinguishable from wild-type causes ALS","volume":"21","author":"Synofzik","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"B83","doi-asserted-by":"publisher","first-page":"50966","DOI":"10.1074\/jbc.m209356200","article-title":"Mitochondrial localization of mutant superoxide dismutase 1 triggers caspase-dependent cell death in a cellular model of familial amyotrophic lateral sclerosis","volume":"277","author":"Takeuchi","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B84","doi-asserted-by":"publisher","first-page":"11588","DOI":"10.1523\/JNEUROSCI.5385-12.2013","article-title":"Small peptides against the mutant SOD1\/Bcl-2 toxic mitochondrial complex restore mitochondrial function and cell viability in mutant SOD1-Mediated ALS","volume":"33","author":"Tan","year":"2013","journal-title":"J. Neurosci."},{"key":"B85","doi-asserted-by":"publisher","first-page":"1991","DOI":"10.1126\/science.1067122","article-title":"Toxic proteins in neurodegenerative disease","volume":"14","author":"Taylor","year":"2002","journal-title":"Science"},{"key":"B86","doi-asserted-by":"publisher","first-page":"4022","DOI":"10.1073\/pnas.0712209105","article-title":"Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria","volume":"105","author":"Vande Velde","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"B87","doi-asserted-by":"publisher","first-page":"4943","DOI":"10.1111\/febs.12409","article-title":"Mia40 and MINOS act in parallel with Ccs1 in the biogenesis of mitochondrial Sod1","volume":"280","author":"Varabyova","year":"2013","journal-title":"FEBS J."},{"key":"B88","doi-asserted-by":"publisher","first-page":"126","DOI":"10.3389\/fncel.2014.00126","article-title":"Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis","volume":"8","author":"Vehvil\u00e4inen","year":"2014","journal-title":"Front. Cell. Neurosci."},{"key":"B89","doi-asserted-by":"publisher","first-page":"2463","DOI":"10.1523\/jneurosci.4385-04.2005","article-title":"Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice","volume":"25","author":"Vijayvergiya","year":"2005","journal-title":"J. Neurosci."},{"key":"B90","doi-asserted-by":"publisher","first-page":"2753","DOI":"10.1093\/hmg\/ddg312","article-title":"Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature","volume":"12","author":"Wang","year":"2003","journal-title":"Hum. Mol. Genet."},{"key":"B91","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1006\/nbdi.2001.0471","article-title":"High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation","volume":"9","author":"Wang","year":"2002","journal-title":"Neurobiol. Dis."},{"key":"B92","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1016\/j.nbd.2013.10.027","article-title":"Wild-type Cu\/Zn superoxide dismutase stabilizes mutant variants by heterodimerization","volume":"62","author":"Weichert","year":"2014","journal-title":"Neurobiol. Dis."},{"key":"B93","doi-asserted-by":"publisher","first-page":"14157","DOI":"10.1073\/pnas.0700477104","article-title":"Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models","volume":"104","author":"Zetterstr\u00f6m","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U S A"}],"container-title":["Frontiers in Cellular Neuroscience"],"original-title":[],"deposited":{"date-parts":[[2020,5,15]],"date-time":"2020-05-15T15:13:00Z","timestamp":1589555580000},"score":1,"resource":{"primary":{"URL":"http:\/\/journal.frontiersin.org\/Article\/10.3389\/fncel.2015.00336\/abstract"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,8,25]]},"references-count":93,"URL":"https:\/\/doi.org\/10.3389\/fncel.2015.00336","relation":{},"ISSN":["1662-5102"],"issn-type":[{"value":"1662-5102","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,8,25]]}}}