{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T05:14:15Z","timestamp":1792818855892,"version":"4.5.0"},"reference-count":50,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,31]],"date-time":"2025-12-31T00:00:00Z","timestamp":1767139200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002915","name":"Foundation for Medical Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002915","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["bmn.com","clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Neurobiology"],"published-print":{"date-parts":[[2026,4]]},"DOI":"10.1016\/j.conb.2025.103163","type":"journal-article","created":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T08:02:59Z","timestamp":1768982579000},"page":"103163","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"special_numbering":"C","title":["ALS-related proteinopathies: From TDP-43 to mitochondrial proteinopathies"],"prefix":"10.1016","volume":"97","author":[{"given":"Emmanuelle C.","family":"Genin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6138-4867","authenticated-orcid":false,"given":"V\u00e9ronique","family":"Paquis-Flucklinger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.conb.2025.103163_bib1","doi-asserted-by":"crossref","first-page":"1918","DOI":"10.1111\/ene.14393","article-title":"Amyotrophic lateral sclerosis: a clinical review","volume":"27","author":"Masrori","year":"2020","journal-title":"Eur J Neurol"},{"key":"10.1016\/j.conb.2025.103163_sref2","doi-asserted-by":"crossref","first-page":"1981","DOI":"10.3390\/genes14111981","article-title":"Mitochondria, a key target in amyotrophic lateral sclerosis pathogenesis","volume":"14","author":"Genin","year":"2023","journal-title":"Genes"},{"key":"10.1016\/j.conb.2025.103163_bib3","doi-asserted-by":"crossref","DOI":"10.3390\/ijms241613006","article-title":"Decoding neurodegeneration: a comprehensive review of molecular mechanisms, genetic influences, and therapeutic innovations","volume":"24","author":"Voicu","year":"2023","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.conb.2025.103163_bib4","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2021.783624","article-title":"Proteinopathies as hallmarks of impaired gene expression, proteostasis and mitochondrial function in amyotrophic lateral sclerosis","volume":"15","author":"Benson","year":"2021","journal-title":"Front Neurosci"},{"key":"10.1016\/j.conb.2025.103163_bib5","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/j.neuron.2013.07.033","article-title":"Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis","volume":"79","author":"Ling","year":"2013","journal-title":"Neuron"},{"key":"10.1016\/j.conb.2025.103163_bib6","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/nrneurol.2010.18","article-title":"TAR DNA-binding protein 43 in neurodegenerative disease","volume":"6","author":"Chen-Plotkin","year":"2010","journal-title":"Nat Rev Neurol"},{"key":"10.1016\/j.conb.2025.103163_bib7","first-page":"232","article-title":"Molecular neuropathology of TDP-43 proteinopathies","volume":"10","author":"Neumann","year":"2009","journal-title":"Int J Math Stat"},{"key":"10.1016\/j.conb.2025.103163_bib8","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1126\/science.1134108","article-title":"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"314","author":"Neumann","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.conb.2025.103163_bib9","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1002\/ana.21154","article-title":"TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease","volume":"61","author":"Amador-Ortiz","year":"2007","journal-title":"Ann Neurol"},{"key":"10.1016\/j.conb.2025.103163_bib10","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1002\/mds.29048","article-title":"TDP-43 proteinopathy presenting with typical symptoms of Parkinson's disease","volume":"37","author":"Yamashita","year":"2022","journal-title":"Mov Disord"},{"key":"10.1016\/j.conb.2025.103163_bib11","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s00401-007-0261-2","article-title":"Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases","volume":"114","author":"Nakashima-Yasuda","year":"2007","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.conb.2025.103163_sref12","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1038\/s41593-024-01850-w","article-title":"Aberrant splicing in Huntington's disease accompanies disrupted TDP-43 activity and altered m6A RNA modification","volume":"28","author":"Nguyen","year":"2025","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.conb.2025.103163_bib13","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3389\/fnmol.2019.00025","article-title":"Molecular mechanisms of TDP-43 misfolding and pathology in amyotrophic lateral sclerosis","volume":"12","author":"Prasad","year":"2019","journal-title":"Front Mol Neurosci"},{"key":"10.1016\/j.conb.2025.103163_sref14","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1093\/hmg\/ddac206","article-title":"Stress granule assembly in vivo is deficient in the CNS of mutant TDP-43 ALS mice","volume":"32","author":"Dubinski","year":"2023","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.conb.2025.103163_bib15","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1126\/science.aab0983","article-title":"TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD","volume":"349","author":"Ling","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.conb.2025.103163_bib16","doi-asserted-by":"crossref","DOI":"10.3390\/ijms241512176","article-title":"Nuclear expression of TDP-43 is linked with morphology and ubiquitylation of cytoplasmic aggregates in amyotrophic lateral sclerosis","volume":"24","author":"Yabata","year":"2023","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.conb.2025.103163_sref17","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1007\/s00401-024-02705-1","article-title":"RNA aptamer reveals nuclear TDP-43 pathology is an early aggregation event that coincides with STMN-2 cryptic splicing and precedes clinical manifestation in ALS","volume":"147","author":"Spence","year":"2024","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.conb.2025.103163_bib18","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2025.107124","article-title":"The potential role of misfolded wild-type SOD1 protein in sporadic amyotrophic lateral sclerosis (ALS): a review of the evidence","volume":"216","author":"Marlow","year":"2025","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.conb.2025.103163_bib19","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.conb.2025.103163_bib20","doi-asserted-by":"crossref","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":"10.1016\/j.conb.2025.103163_bib21","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.conb.2025.103163_bib22","doi-asserted-by":"crossref","first-page":"8180","DOI":"10.1038\/s41598-022-12098-4","article-title":"Nuclear RNA transcript levels modulate nucleocytoplasmic distribution of ALS\/FTD-associated protein FUS","volume":"12","author":"Tsai","year":"2022","journal-title":"Sci Rep"},{"key":"10.1016\/j.conb.2025.103163_bib23","doi-asserted-by":"crossref","first-page":"6889","DOI":"10.1093\/nar\/gkaa410","article-title":"FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention","volume":"48","author":"Humphrey","year":"2020","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.conb.2025.103163_sref24","doi-asserted-by":"crossref","first-page":"5810","DOI":"10.1093\/nar\/gkad319","article-title":"Cytoplasmic aggregation of mutant FUS causes multistep RNA splicing perturbations in the course of motor neuron pathology","volume":"51","author":"Rezvykh","year":"2023","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.conb.2025.103163_bib25","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1093\/jnen\/nlac004","article-title":"Widespread mislocalization of FUS is associated with mitochondrial abnormalities in skeletal muscle in amyotrophic lateral sclerosis with FUS mutations","volume":"81","author":"Yu","year":"2022","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.1016\/j.conb.2025.103163_bib26","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1126\/science.1232927","article-title":"The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD\/ALS","volume":"339","author":"Mori","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.conb.2025.103163_bib27","doi-asserted-by":"crossref","first-page":"17573","DOI":"10.1074\/jbc.RA120.015012","article-title":"Wildtype \u03c31 receptor and the receptor agonist improve ALS-associated mutation-induced insolubility and toxicity","volume":"295","author":"Shinoda","year":"2020","journal-title":"J Biol Chem"},{"key":"10.1016\/j.conb.2025.103163_bib28","doi-asserted-by":"crossref","DOI":"10.3389\/fncel.2021.661447","article-title":"C9ORF72: what it Is, what it does, and why it matters","volume":"15","author":"Smeyers","year":"2021","journal-title":"Front Cell Neurosci"},{"key":"10.1016\/j.conb.2025.103163_bib29","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2017.00035","article-title":"The role of dipeptide repeats in C9ORF72-Related ALS-FTD","volume":"10","author":"Freibaum","year":"2017","journal-title":"Front Mol Neurosci"},{"key":"10.1016\/j.conb.2025.103163_bib30","doi-asserted-by":"crossref","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":"10.1016\/j.conb.2025.103163_bib31","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1186\/s40478-022-01386-9","article-title":"Modulation of synaptic plasticity, motor unit physiology, and TDP-43 pathology by CHCHD10","volume":"10","author":"Liu","year":"2022","journal-title":"Acta Neuropathol Commun"},{"key":"10.1016\/j.conb.2025.103163_bib32","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2024.106498","article-title":"CHCHD10S59L\/+ mouse model: behavioral and neuropathological features of frontotemporal dementia","volume":"195","author":"Genin","year":"2024","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.conb.2025.103163_bib33","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1007\/s00401-019-01989-y","article-title":"ALS\/FTD mutant CHCHD10 mice reveal a tissue-specific toxic gain-of-function and mitochondrial stress response","volume":"138","author":"Anderson","year":"2019","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.conb.2025.103163_bib34","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/s00401-019-01988-z","article-title":"Mitochondrial defect in muscle precedes neuromuscular junction degeneration and motor neuron death in CHCHD10S59L\/+ mouse","volume":"138","author":"Genin","year":"2019","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.conb.2025.103163_bib35","doi-asserted-by":"crossref","first-page":"3415","DOI":"10.1093\/brain\/awac197","article-title":"CHCHD10 and SLP2 control the stability of the PHB complex: a key factor for motor neuron viability","volume":"145","author":"Genin","year":"2022","journal-title":"Brain"},{"key":"10.1016\/j.conb.2025.103163_bib36","doi-asserted-by":"crossref","DOI":"10.1212\/NXG.0000000000000394","article-title":"Neuropathologic description of CHCHD10 mutated amyotrophic lateral sclerosis","volume":"6","author":"Keith","year":"2020","journal-title":"Neurol Genet"},{"key":"10.1016\/j.conb.2025.103163_bib37","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1021\/acschemneuro.2c00011","article-title":"Structures of the wild-type and S59L mutant CHCHD10 proteins important in amyotrophic lateral sclerosis-frontotemporal dementia","volume":"13","author":"Alici","year":"2022","journal-title":"ACS Chem Neurosci"},{"key":"10.1016\/j.conb.2025.103163_bib38","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.nbd.2018.07.027","article-title":"Loss of MICOS complex integrity and mitochondrial damage, but not TDP-43 mitochondrial localisation, are likely associated with severity of CHCHD10-related diseases","volume":"119","author":"Genin","year":"2018","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.conb.2025.103163_bib39","doi-asserted-by":"crossref","first-page":"71","DOI":"10.3390\/cells8010071","article-title":"Prohibitins: a critical role in mitochondrial functions and implication in diseases","volume":"8","author":"Signorile","year":"2019","journal-title":"Cells"},{"key":"10.1016\/j.conb.2025.103163_bib40","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1016\/j.bbamcr.2008.02.006","article-title":"SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability","volume":"1783","author":"Da Cruz","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.conb.2025.103163_bib41","doi-asserted-by":"crossref","first-page":"1844","DOI":"10.15252\/embr.201642698","article-title":"The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i-AAA protease YME1L","volume":"17","author":"Wai","year":"2016","journal-title":"EMBO Rep"},{"key":"10.1016\/j.conb.2025.103163_sref42","article-title":"SLP2\/PHB aggregates in ALS mouse models and patients: implications beyond CHCHD10-Associated motor neuron disease","volume":"26","author":"Genin","year":"2025","journal-title":"Int J Math Stat"},{"key":"10.1016\/j.conb.2025.103163_bib43","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a033951","article-title":"Functional modules of the proteostasis network","volume":"12","author":"Jayaraj","year":"2020","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"10.1016\/j.conb.2025.103163_bib44","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.biocel.2016.07.019","article-title":"The ubiquitin-proteasome system and autophagy: coordinated and independent activities","volume":"79","author":"Cohen-Kaplan","year":"2016","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/j.conb.2025.103163_bib45","doi-asserted-by":"crossref","first-page":"1811","DOI":"10.15252\/embj.201796697","article-title":"Molecular definitions of autophagy and related processes","volume":"36","author":"Galluzzi","year":"2017","journal-title":"EMBO J"},{"key":"10.1016\/j.conb.2025.103163_bib46","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1038\/s41580-019-0101-y","article-title":"The proteostasis network and its decline in ageing","volume":"20","author":"Hipp","year":"2019","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.conb.2025.103163_bib47","doi-asserted-by":"crossref","DOI":"10.1155\/2020\/5497046","article-title":"Proteostasis failure in neurodegenerative diseases: focus on oxidative stress","volume":"2020","author":"H\u00f6hn","year":"2020","journal-title":"Oxid Med Cell Longev"},{"key":"10.1016\/j.conb.2025.103163_bib48","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.15252\/embr.201642195","article-title":"The integrated stress response","volume":"17","author":"Pakos-Zebrucka","year":"2016","journal-title":"EMBO Rep"},{"key":"10.1016\/j.conb.2025.103163_bib49","doi-asserted-by":"crossref","first-page":"2797","DOI":"10.1093\/brain\/awx248","article-title":"Humanized mutant FUS drives progressive motor neuron degeneration without aggregation in \u2018FUSDelta14\u2019 knockin mice","volume":"140","author":"Devoy","year":"2017","journal-title":"Brain"},{"key":"10.1016\/j.conb.2025.103163_bib50","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1093\/brain\/awz078","article-title":"The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?","volume":"142","author":"Hergesheimer","year":"2019","journal-title":"Brain"}],"container-title":["Current Opinion in Neurobiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959438825001941?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959438825001941?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T01:18:49Z","timestamp":1772241529000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959438825001941"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4]]},"references-count":50,"alternative-id":["S0959438825001941"],"URL":"https:\/\/doi.org\/10.1016\/j.conb.2025.103163","relation":{},"ISSN":["0959-4388"],"issn-type":[{"value":"0959-4388","type":"print"}],"subject":[],"published":{"date-parts":[[2026,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"ALS-related proteinopathies: From TDP-43 to mitochondrial proteinopathies","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Neurobiology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.conb.2025.103163","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"103163"}}