{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T04:47:33Z","timestamp":1790052453504,"version":"4.0.1"},"reference-count":151,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2025,2,26]],"date-time":"2025-02-26T00:00:00Z","timestamp":1740528000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100003130","name":"Research Foundation Flanders","doi-asserted-by":"publisher","award":["3G0H8318"],"award-info":[{"award-number":["3G0H8318"]}],"id":[{"id":"10.13039\/501100003130","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003130","name":"Research Foundation Flanders","doi-asserted-by":"publisher","award":["G0AC724N"],"award-info":[{"award-number":["G0AC724N"]}],"id":[{"id":"10.13039\/501100003130","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Funds W. Pyleman and Cremers-Opdebeeck"},{"DOI":"10.13039\/501100006282","name":"King Baudouin Foundation","doi-asserted-by":"publisher","award":["2023-J1141680-231086"],"award-info":[{"award-number":["2023-J1141680-231086"]}],"id":[{"id":"10.13039\/501100006282","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Ghent University Special Research Fund","award":["01N10319"],"award-info":[{"award-number":["01N10319"]}]},{"name":"Ghent University Fund"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,6,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>While neuropathological and genetic studies have established the crucial involvement of TDP-43 proteinopathy in the pathogenesis of amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD) and related neurodegenerative disorders, multiple studies have described the presence of TDP-43 inclusions in muscular disorders, including inclusion body myositis but also other related rimmed vacuole myopathies. In addition, TAR DNA-binding protein-43 (TDP-43) has been reported to be essential in normal muscle physiology as it is implicated in the formation of so-called amyloid-like myogranules during normal muscle regeneration after injury. However, genetic evidence supporting a primary role for TDP-43 proteinopathy in muscle disease has been missing.<\/jats:p>\n               <jats:p>In the present review we highlight recent landmark discoveries linking novel pathogenic TDP-43 variants [p.(W385IfsX10) and p.(G376V)] within the prion-like domain with unusual aggregation-propensity and muscle rather than neuronal pathology. We discuss these studies in the context of known TDP-43-related pathways in ALS\/FTD pathogenesis and show how they challenge some widely accepted views such as ALS as a pure neurogenic presynaptic neuromuscular disease and the direct correlation between TDP-43 aggregation-propensity and neurotoxicity. Finally, we discuss TDP-43 as part of a growing list of RNA-binding proteins including hnRNPA2B1 and hnRNPA1 as genetic causes of myopathies and relate this to the idea of \u2018multisystem proteinopathy\u2019.<\/jats:p>","DOI":"10.1093\/brain\/awaf076","type":"journal-article","created":{"date-parts":[[2025,3,4]],"date-time":"2025-03-04T20:50:58Z","timestamp":1741121458000},"page":"1876-1887","source":"Crossref","is-referenced-by-count":3,"title":["Myopathic aggregation-prone variants in the TDP-43 prion-like domain: genetics paving the way"],"prefix":"10.1093","volume":"148","author":[{"given":"Pedro","family":"Ervilha Pereira","sequence":"first","affiliation":[{"name":"Department of Biomolecular Medicine, Faculty of Medicine and Health Sciences, Ghent University , Ghent 9000 ,","place":["Belgium"]},{"name":"Centre for Medical Genetics, Ghent University Hospital , Ghent 9000 ,","place":["Belgium"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan L","family":"De Bleecker","sequence":"additional","affiliation":[{"name":"Department of Neurology, Ghent University Hospital , Ghent 9000 ,","place":["Belgium"]},{"name":"Department of Head and Skin, Faculty of Medicine and Health Sciences, Ghent University , Ghent 9000 ,","place":["Belgium"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elke","family":"Bogaert","sequence":"additional","affiliation":[{"name":"Department of Biomolecular Medicine, Faculty of Medicine and Health Sciences, Ghent University , Ghent 9000 ,","place":["Belgium"]},{"name":"Centre for Medical Genetics, Ghent University Hospital , Ghent 9000 ,","place":["Belgium"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6968-0572","authenticated-orcid":false,"given":"Bart","family":"Dermaut","sequence":"additional","affiliation":[{"name":"Department of Biomolecular Medicine, Faculty of Medicine and Health Sciences, Ghent University , Ghent 9000 ,","place":["Belgium"]},{"name":"Centre for Medical Genetics, Ghent University Hospital , Ghent 9000 ,","place":["Belgium"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2025,2,26]]},"reference":[{"key":"2025060300222486800_awaf076-B1","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":"2025060300222486800_awaf076-B2","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/s00401-012-1029-x","article-title":"The genetics and neuropathology of frontotemporal lobar degeneration","volume":"124","author":"Sieben","year":"2012","journal-title":"Acta Neuropathol"},{"key":"2025060300222486800_awaf076-B3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00401-009-0612-2","article-title":"Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update","volume":"119","author":"Mackenzie","year":"2010","journal-title":"Acta Neuropathol"},{"key":"2025060300222486800_awaf076-B4","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1186\/s13024-021-00503-x","article-title":"TDP-43 Pathology in Alzheimer\u2019s disease","volume":"16","author":"Meneses","year":"2021","journal-title":"Mol Neurodegener."},{"key":"2025060300222486800_awaf076-B5","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1007\/s11910-022-01232-4","article-title":"Limbic-predominant age-related TDP-43 encephalopathy: LATE-breaking updates in clinicopathologic features and biomarkers","volume":"22","author":"Duong","year":"2022","journal-title":"Curr Neurol Neurosci Rep."},{"key":"2025060300222486800_awaf076-B6","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1093\/jnen\/nlw033","article-title":"\u201cNew Old Pathologies\u201d: AD, PART, and cerebral age-related TDP-43 with sclerosis (CARTS)","volume":"75","author":"Nelson","year":"2016","journal-title":"J Neuropathol Exp Neurol"},{"key":"2025060300222486800_awaf076-B7","doi-asserted-by":"crossref","first-page":"3584","DOI":"10.1128\/jvi.69.6.3584-3596.1995","article-title":"Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs","volume":"69","author":"Ou","year":"1995","journal-title":"J Virol."},{"issue":"Suppl 1","key":"2025060300222486800_awaf076-B8","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1111\/jnc.13625","article-title":"Physiological functions and pathobiology of TDP-43 and FUS\/TLS proteins","volume":"138","author":"Ratti","year":"2016","journal-title":"J Neurochem."},{"key":"2025060300222486800_awaf076-B9","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":"2025060300222486800_awaf076-B10","doi-asserted-by":"crossref","first-page":"36337","DOI":"10.1074\/jbc.M104236200","article-title":"Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9","volume":"276","author":"Buratti","year":"2001","journal-title":"J Biol Chem."},{"key":"2025060300222486800_awaf076-B11","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.mcn.2013.03.001","article-title":"TDP-43 high throughput screening analyses in neurodegeneration: Advantages and pitfalls","volume":"56","author":"Buratti","year":"2013","journal-title":"Mol Cell Neurosci."},{"key":"2025060300222486800_awaf076-B12","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/nn.2778","article-title":"Characterizing the RNA targets and position-dependent splicing regulation by TDP-43","volume":"14","author":"Tollervey","year":"2011","journal-title":"Nat Neurosci."},{"key":"2025060300222486800_awaf076-B13","doi-asserted-by":"crossref","first-page":"2668","DOI":"10.1093\/nar\/gkr1082","article-title":"TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR","volume":"40","author":"Fiesel","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"2025060300222486800_awaf076-B14","doi-asserted-by":"crossref","first-page":"21510","DOI":"10.1073\/pnas.1211577110","article-title":"Misregulation of human sortilin splicing leads to the generation of a nonfunctional progranulin receptor","volume":"109","author":"Prudencio","year":"2012","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2025060300222486800_awaf076-B15","doi-asserted-by":"crossref","first-page":"8990","DOI":"10.1093\/nar\/gkv814","article-title":"TDP-43 affects splicing profiles and isoform production of genes involved in the apoptotic and mitotic cellular pathways","volume":"43","author":"De Conti","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"2025060300222486800_awaf076-B16","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1016\/j.bbagrm.2015.10.015","article-title":"From transcriptomic to protein level changes in TDP-43 and FUS loss-of-function cell models","volume":"1849","author":"Colombrita","year":"2015","journal-title":"Biochim Biophys Acta."},{"key":"2025060300222486800_awaf076-B17","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1038\/nature03120","article-title":"The microprocessor complex mediates the genesis of microRNAs","volume":"432","author":"Gregory","year":"2004","journal-title":"Nature"},{"key":"2025060300222486800_awaf076-B18","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.jsb.2009.06.006","article-title":"TDP-43 localizes in mRNA transcription and processing sites in mammalian neurons","volume":"167","author":"Casafont","year":"2009","journal-title":"J Struct Biol."},{"key":"2025060300222486800_awaf076-B19","doi-asserted-by":"crossref","first-page":"2268","DOI":"10.1111\/j.1742-4658.2010.07643.x","article-title":"Nuclear factor TDP-43 can affect selected microRNA levels","volume":"277","author":"Buratti","year":"2010","journal-title":"FEBS J."},{"key":"2025060300222486800_awaf076-B20","doi-asserted-by":"crossref","first-page":"3347","DOI":"10.1073\/pnas.1112427109","article-title":"TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes","volume":"109","author":"Kawahara","year":"2012","journal-title":"Proc Natl Acad Sci U S A."},{"key":"2025060300222486800_awaf076-B21","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1002\/hep.26310","article-title":"Tat-activating regulatory DNA-binding protein regulates glycolysis in hepatocellular carcinoma by regulating the platelet isoform of phosphofructokinase through microRNA 520","volume":"58","author":"Park","year":"2013","journal-title":"Hepatology"},{"key":"2025060300222486800_awaf076-B22","doi-asserted-by":"crossref","first-page":"e76055","DOI":"10.1371\/journal.pone.0076055","article-title":"Downregulation of microRNA-9 in iPSC-derived neurons of FTD\/ALS patients with TDP-43 mutations","volume":"8","author":"Zhang","year":"2013","journal-title":"PLoS One"},{"key":"2025060300222486800_awaf076-B23","doi-asserted-by":"crossref","first-page":"14263","DOI":"10.1074\/jbc.M114.561902","article-title":"The RNA-binding protein TDP-43 selectively disrupts microRNA-1\/206 incorporation into the RNA-induced silencing complex","volume":"289","author":"King","year":"2014","journal-title":"J Biol Chem."},{"key":"2025060300222486800_awaf076-B24","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1007\/s12035-013-8564-x","article-title":"TDP-43 regulates the microprocessor complex activity during in vitro neuronal differentiation","volume":"48","author":"Di Carlo","year":"2013","journal-title":"Mol Neurobiol."},{"key":"2025060300222486800_awaf076-B25","doi-asserted-by":"crossref","first-page":"4415","DOI":"10.1038\/emboj.2012.292","article-title":"Long non-coding RNA gadd7 interacts with TDP-43 and regulates Cdk6 mRNA decay","volume":"31","author":"Liu","year":"2012","journal-title":"EMBO J."},{"key":"2025060300222486800_awaf076-B26","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.bbrc.2015.08.027","article-title":"Regulation of MALAT1 expression by TDP43 controls the migration and invasion of non-small cell lung cancer cells in vitro","volume":"465","author":"Guo","year":"2015","journal-title":"Biochem Biophys Res Commun."},{"key":"2025060300222486800_awaf076-B27","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/j.cmet.2015.02.004","article-title":"A liver-enriched long non-coding RNA, lncLSTR, regulates systemic lipid metabolism in mice","volume":"21","author":"Li","year":"2015","journal-title":"Cell Metab."},{"key":"2025060300222486800_awaf076-B28","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1261\/rna.034777.112","article-title":"Neurodegenerative diseases: Quantitative predictions of protein-RNA interactions","volume":"19","author":"Cirillo","year":"2013","journal-title":"RNA"},{"key":"2025060300222486800_awaf076-B29","doi-asserted-by":"crossref","first-page":"e44099","DOI":"10.1371\/journal.pone.0044099","article-title":"Transposable elements in TDP-43-mediated neurodegenerative disorders","volume":"7","author":"Li","year":"2012","journal-title":"PLoS One"},{"key":"2025060300222486800_awaf076-B30","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.mcn.2007.03.007","article-title":"TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein","volume":"35","author":"Strong","year":"2007","journal-title":"Mol Cell Neurosci."},{"key":"2025060300222486800_awaf076-B31","doi-asserted-by":"crossref","first-page":"34097","DOI":"10.1074\/jbc.M110.154831","article-title":"Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS\/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA","volume":"285","author":"Kim","year":"2010","journal-title":"J Biol Chem."},{"key":"2025060300222486800_awaf076-B32","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1186\/1750-1326-6-64","article-title":"TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase 6","volume":"6","author":"Fiesel","year":"2011","journal-title":"Mol Neurodegener."},{"key":"2025060300222486800_awaf076-B33","doi-asserted-by":"crossref","first-page":"1280","DOI":"10.1080\/15476286.2014.996081","article-title":"TDP-43 regulates beta-adducin (Add2) transcript stability","volume":"11","author":"Costessi","year":"2014","journal-title":"RNA Biol."},{"key":"2025060300222486800_awaf076-B34","doi-asserted-by":"crossref","first-page":"15635","DOI":"10.1074\/jbc.M111.333450","article-title":"TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells","volume":"287","author":"Colombrita","year":"2012","journal-title":"J Biol Chem."},{"key":"2025060300222486800_awaf076-B35","doi-asserted-by":"crossref","first-page":"1","DOI":"10.5607\/en.2015.24.1.1","article-title":"Prion-like mechanism in amyotrophic lateral sclerosis: Are protein aggregates the key?","volume":"24","author":"Lee","year":"2015","journal-title":"Exp Neurobiol."},{"key":"2025060300222486800_awaf076-B36","doi-asserted-by":"crossref","first-page":"e71793","DOI":"10.1371\/journal.pone.0071793","article-title":"TDP-43, an ALS linked protein, regulates fat deposition and glucose homeostasis","volume":"8","author":"Stallings","year":"2013","journal-title":"PLoS One"},{"key":"2025060300222486800_awaf076-B37","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1093\/hmg\/ddr021","article-title":"TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1","volume":"20","author":"McDonald","year":"2011","journal-title":"Hum Mol Genet."},{"key":"2025060300222486800_awaf076-B38","doi-asserted-by":"crossref","first-page":"3703","DOI":"10.1093\/hmg\/dds205","article-title":"The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth","volume":"21","author":"Fallini","year":"2012","journal-title":"Hum Mol Genet."},{"key":"2025060300222486800_awaf076-B39","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.neuron.2013.12.018","article-title":"Axonal transport of TDP-43 mRNA granules is impaired by ALS-causing mutations","volume":"81","author":"Alami","year":"2014","journal-title":"Neuron"},{"key":"2025060300222486800_awaf076-B40","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1111\/j.1471-4159.2007.05190.x","article-title":"TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor","volume":"105","author":"Wang","year":"2008","journal-title":"J Neurochem."},{"key":"2025060300222486800_awaf076-B41","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1021\/pr901076y","article-title":"Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery","volume":"9","author":"Freibaum","year":"2010","journal-title":"J Proteome Res."},{"key":"2025060300222486800_awaf076-B42","doi-asserted-by":"crossref","first-page":"e17808","DOI":"10.1371\/journal.pone.0017808","article-title":"TDP-43 regulates Drosophila neuromuscular junctions growth by modulating Futsch\/MAP1B levels and synaptic microtubules organization","volume":"6","author":"Godena","year":"2011","journal-title":"PLoS One"},{"key":"2025060300222486800_awaf076-B43","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1007\/s00401-012-1006-4","article-title":"TDP-43 regulates the mammalian spinogenesis through translational repression of Rac1","volume":"124","author":"Majumder","year":"2012","journal-title":"Acta Neuropathol."},{"key":"2025060300222486800_awaf076-B44","doi-asserted-by":"crossref","first-page":"15962","DOI":"10.1523\/JNEUROSCI.2526-14.2014","article-title":"Futsch\/MAP1B mRNA is a translational target of TDP-43 and is neuroprotective in a Drosophila model of amyotrophic lateral sclerosis","volume":"34","author":"Coyne","year":"2014","journal-title":"J Neurosci."},{"key":"2025060300222486800_awaf076-B45","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.brainres.2016.02.022","article-title":"TBPH\/TDP-43 modulates translation of Drosophila futsch mRNA through an UG-rich sequence within its 5\u02b9UTR","volume":"1647","author":"Romano","year":"2016","journal-title":"Brain Res."},{"issue":"Pt 1","key":"2025060300222486800_awaf076-B46","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1093\/brain\/awv308","article-title":"MTHFSD and DDX58 are novel RNA-binding proteins abnormally regulated in amyotrophic lateral sclerosis","volume":"139","author":"MacNair","year":"2016","journal-title":"Brain."},{"key":"2025060300222486800_awaf076-B47","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1111\/j.1471-4159.2009.06383.x","article-title":"TDP-43 is recruited to stress granules in conditions of oxidative insult","volume":"111","author":"Colombrita","year":"2009","journal-title":"J Neurochem."},{"key":"2025060300222486800_awaf076-B48","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1083\/jcb.201302044","article-title":"Stress granules as crucibles of ALS pathogenesis","volume":"201","author":"Li","year":"2013","journal-title":"J Cell Biol."},{"key":"2025060300222486800_awaf076-B49","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.1093\/hmg\/ddt166","article-title":"The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation","volume":"22","author":"Zhang","year":"2013","journal-title":"Hum Mol Genet"},{"key":"2025060300222486800_awaf076-B50","doi-asserted-by":"crossref","first-page":"6196","DOI":"10.1038\/s41598-017-06263-3","article-title":"The N-terminal dimerization is required for TDP-43 splicing activity","volume":"7","author":"Jiang","year":"2017","journal-title":"Sci Rep"},{"key":"2025060300222486800_awaf076-B51","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1007\/s10571-009-9489-9","article-title":"TDP-43 dimerizes in human cells in culture","volume":"30","author":"Shiina","year":"2010","journal-title":"Cell Mol Neurobiol"},{"key":"2025060300222486800_awaf076-B52","doi-asserted-by":"crossref","first-page":"12590","DOI":"10.1002\/anie.201706769","article-title":"The N-terminal domain of ALS-linked TDP-43 assembles without misfolding","volume":"56","author":"Tsoi","year":"2017","journal-title":"Angew Chem Int Ed Engl"},{"key":"2025060300222486800_awaf076-B53","doi-asserted-by":"crossref","first-page":"9049","DOI":"10.1074\/jbc.M112.438564","article-title":"The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates","volume":"288","author":"Wang","year":"2013","journal-title":"J Biol Chem"},{"key":"2025060300222486800_awaf076-B54","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.bbrc.2012.07.071","article-title":"The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity","volume":"425","author":"Chang","year":"2012","journal-title":"Biochem Biophys Res Commun"},{"key":"2025060300222486800_awaf076-B55","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.neuron.2019.01.048","article-title":"RNA binding antagonizes neurotoxic phase transitions of TDP-43","volume":"102","author":"Mann","year":"2019","journal-title":"Neuron"},{"key":"2025060300222486800_awaf076-B56","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.1093\/nar\/gkp013","article-title":"Structural insights into TDP-43 in nucleic-acid binding and domain interactions","volume":"37","author":"Kuo","year":"2009","journal-title":"Nucleic Acids Res"},{"key":"2025060300222486800_awaf076-B57","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1038\/nsmb.2698","article-title":"Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43","volume":"20","author":"Lukavsky","year":"2013","journal-title":"Nat Struct Mol Biol"},{"key":"2025060300222486800_awaf076-B58","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1038\/sj.emboj.7601190","article-title":"Grabbing the message: Structural basis of mRNA 3'UTR recognition by Hrp1","volume":"25","author":"Perez-Canadillas","year":"2006","journal-title":"EMBO J"},{"key":"2025060300222486800_awaf076-B59","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/19242","article-title":"Structural basis for recognition of the tra mRNA precursor by the sex-lethal protein","volume":"398","author":"Handa","year":"1999","journal-title":"Nature"},{"key":"2025060300222486800_awaf076-B60","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/84131","article-title":"Structural basis for recognition of AU-rich element RNA by the HuD protein","volume":"8","author":"Wang","year":"2001","journal-title":"Nat Struct Biol"},{"key":"2025060300222486800_awaf076-B61","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1016\/j.celrep.2017.04.028","article-title":"High-resolution RNA maps suggest common principles of splicing and polyadenylation regulation by TDP-43","volume":"19","author":"Rot","year":"2017","journal-title":"Cell Rep"},{"key":"2025060300222486800_awaf076-B62","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/emboj.2010.310","article-title":"TDP-43 regulates its mRNA levels through a negative feedback loop","volume":"30","author":"Ayala","year":"2011","journal-title":"EMBO J"},{"key":"2025060300222486800_awaf076-B63","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.brainres.2012.01.016","article-title":"The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease","volume":"1462","author":"King","year":"2012","journal-title":"Brain Res"},{"key":"2025060300222486800_awaf076-B64","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1534\/genetics.111.137760","article-title":"Prions in yeast","volume":"191","author":"Liebman","year":"2012","journal-title":"Genetics"},{"key":"2025060300222486800_awaf076-B65","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","article-title":"TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"351","author":"Arai","year":"2006","journal-title":"Biochem Biophys Res Commun"},{"key":"2025060300222486800_awaf076-B66","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1038\/ng.132","article-title":"TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis","volume":"40","author":"Kabashi","year":"2008","journal-title":"Nat Genet."},{"key":"2025060300222486800_awaf076-B67","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1126\/science.1154584","article-title":"TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis","volume":"319","author":"Sreedharan","year":"2008","journal-title":"Science"},{"key":"2025060300222486800_awaf076-B68","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/S1474-4422(08)70071-1","article-title":"TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: A genetic and histopathological analysis","volume":"7","author":"Van Deerlin","year":"2008","journal-title":"Lancet Neurol."},{"key":"2025060300222486800_awaf076-B69","doi-asserted-by":"crossref","first-page":"7607","DOI":"10.1073\/pnas.0900688106","article-title":"Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity","volume":"106","author":"Zhang","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2025060300222486800_awaf076-B70","doi-asserted-by":"crossref","first-page":"10530","DOI":"10.1523\/JNEUROSCI.3421-07.2007","article-title":"Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43","volume":"27","author":"Zhang","year":"2007","journal-title":"J Neurosci"},{"key":"2025060300222486800_awaf076-B71","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/j.str.2016.07.007","article-title":"ALS mutations disrupt phase separation mediated by alpha-helical structure in the TDP-43 low-complexity C-terminal domain","volume":"24","author":"Conicella","year":"2016","journal-title":"Structure"},{"key":"2025060300222486800_awaf076-B72","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.neuron.2019.02.038","article-title":"Cytoplasmic TDP-43 de-mixing independent of stress granules drives inhibition of nuclear import, loss of nuclear TDP-43, and cell death","volume":"102","author":"Gasset-Rosa","year":"2019","journal-title":"Neuron"},{"key":"2025060300222486800_awaf076-B73","doi-asserted-by":"crossref","first-page":"105051","DOI":"10.1016\/j.nbd.2020.105051","article-title":"Chronic stress induces formation of stress granules and pathological TDP-43 aggregates in human ALS fibroblasts and iPSC-motoneurons","volume":"145","author":"Ratti","year":"2020","journal-title":"Neurobiol Dis."},{"key":"2025060300222486800_awaf076-B74","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1136\/jmg.2008.062463","article-title":"Contribution of TARDBP mutations to sporadic amyotrophic lateral sclerosis","volume":"46","author":"Daoud","year":"2009","journal-title":"J Med Genet"},{"key":"2025060300222486800_awaf076-B75","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1001\/archneur.65.9.1185","article-title":"Two German kindreds with familial amyotrophic lateral sclerosis due to TARDBP mutations","volume":"65","author":"K\u00fchnlein","year":"2008","journal-title":"Arch Neurol"},{"key":"2025060300222486800_awaf076-B76","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1136\/jnnp.2008.157677","article-title":"TDP-43 M311V mutation in familial amyotrophic lateral sclerosis","volume":"80","author":"Lemmens","year":"2009","journal-title":"J Neurol Neurosurg Psychiatry"},{"key":"2025060300222486800_awaf076-B77","doi-asserted-by":"crossref","first-page":"e1000193","DOI":"10.1371\/journal.pgen.1000193","article-title":"Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis","volume":"4","author":"Rutherford","year":"2008","journal-title":"PLoS Genet"},{"key":"2025060300222486800_awaf076-B78","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/nrn3121","article-title":"Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration","volume":"13","author":"Lee","year":"2011","journal-title":"Nat Rev Neurosci"},{"key":"2025060300222486800_awaf076-B79","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":"2025060300222486800_awaf076-B80","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1007\/s00401-017-1701-2","article-title":"Cryptic exon incorporation occurs in Alzheimer's brain lacking TDP-43 inclusion but exhibiting nuclear clearance of TDP-43","volume":"133","author":"Sun","year":"2017","journal-title":"Acta Neuropathol."},{"key":"2025060300222486800_awaf076-B81","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1080\/15548627.2018.1474311","article-title":"Cryptic exon splicing function of TARDBP interacts with autophagy in nervous tissue","volume":"14","author":"Torres","year":"2018","journal-title":"Autophagy"},{"key":"2025060300222486800_awaf076-B82","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/s41586-022-04424-7","article-title":"TDP-43 represses cryptic exon inclusion in the FTD-ALS gene UNC13A","volume":"603","author":"Ma","year":"2022","journal-title":"Nature"},{"key":"2025060300222486800_awaf076-B83","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/s41586-022-04436-3","article-title":"TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A","volume":"603","author":"Brown","year":"2022","journal-title":"Nature"},{"key":"2025060300222486800_awaf076-B84","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1002\/ana.24198","article-title":"C9orf72 and UNC13A are shared risk loci for amyotrophic lateral sclerosis and frontotemporal dementia: A genome-wide meta-analysis","volume":"76","author":"Diekstra","year":"2014","journal-title":"Ann Neurol."},{"key":"2025060300222486800_awaf076-B85","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1038\/ng.442","article-title":"Genome-wide association study identifies 19p13.3 (UNC13A) and 9p21.2 as susceptibility loci for sporadic amyotrophic lateral sclerosis","volume":"41","author":"van Es","year":"2009","journal-title":"Nat Genet."},{"key":"2025060300222486800_awaf076-B86","doi-asserted-by":"crossref","first-page":"eabi9196","DOI":"10.1126\/scitranslmed.abi9196","article-title":"Loss of TDP-43 function and rimmed vacuoles persist after T cell depletion in a xenograft model of sporadic inclusion body myositis","volume":"14","author":"Britson","year":"2022","journal-title":"Sci Transl Med."},{"key":"2025060300222486800_awaf076-B87","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s13024-016-0144-x","article-title":"Tdp-43 cryptic exons are highly variable between cell types","volume":"12","author":"Jeong","year":"2017","journal-title":"Mol Neurodegener."},{"key":"2025060300222486800_awaf076-B88","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1038\/s41586-018-0665-2","article-title":"TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle","volume":"563","author":"Vogler","year":"2018","journal-title":"Nature"},{"key":"2025060300222486800_awaf076-B89","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/s00401-008-0471-2","article-title":"TDP-43 accumulation is common in myopathies with rimmed vacuoles","volume":"117","author":"Kusters","year":"2009","journal-title":"Acta Neuropathol."},{"key":"2025060300222486800_awaf076-B90","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/s40478-018-0528-y","article-title":"Phosphorylated TDP-43 (pTDP-43) aggregates in the axial skeletal muscle of patients with sporadic and familial amyotrophic lateral sclerosis","volume":"6","author":"Cykowski","year":"2018","journal-title":"Acta Neuropathol Commun."},{"key":"2025060300222486800_awaf076-B91","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1001\/jamaneurol.2022.1113","article-title":"TDP-43 accumulation within intramuscular nerve bundles of patients with amyotrophic lateral sclerosis","volume":"79","author":"Kurashige","year":"2022","journal-title":"JAMA Neurol."},{"key":"2025060300222486800_awaf076-B92","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1186\/s40478-019-0824-1","article-title":"Phosphorylated TDP-43 aggregates in skeletal and cardiac muscle are a marker of myogenic degeneration in amyotrophic lateral sclerosis and various conditions","volume":"7","author":"Mori","year":"2019","journal-title":"Acta Neuropathol Commun."},{"key":"2025060300222486800_awaf076-B93","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1007\/s00401-023-02565-1","article-title":"C-terminal frameshift variant of TDP-43 with pronounced aggregation-propensity causes rimmed vacuole myopathy but not ALS\/FTD","volume":"145","author":"Ervilha Pereira","year":"2023","journal-title":"Acta Neuropathol"},{"key":"2025060300222486800_awaf076-B94","doi-asserted-by":"crossref","first-page":"1768","DOI":"10.1093\/brain\/awad410","article-title":"The new missense G376V-TDP-43 variant induces late-onset distal myopathy but not amyotrophic lateral sclerosis","volume":"147","author":"Zibold","year":"2023","journal-title":"Brain."},{"key":"2025060300222486800_awaf076-B95","doi-asserted-by":"crossref","first-page":"20329","DOI":"10.1074\/jbc.M109.010264","article-title":"TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity","volume":"284","author":"Johnson","year":"2009","journal-title":"J Biol Chem"},{"key":"2025060300222486800_awaf076-B96","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1002\/prot.26482","article-title":"Influence of ALS-linked M337V mutation on the conformational ensembles of TDP-43(321-340) peptide monomer and dimer","volume":"92","author":"Zeng","year":"2023","journal-title":"Proteins"},{"key":"2025060300222486800_awaf076-B97","doi-asserted-by":"crossref","first-page":"6696","DOI":"10.1074\/jbc.RA118.005889","article-title":"Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation","volume":"294","author":"French","year":"2019","journal-title":"J Biol Chem"},{"key":"2025060300222486800_awaf076-B98","doi-asserted-by":"crossref","first-page":"171","DOI":"10.4103\/2152-7806.169561","article-title":"A comprehensive review of amyotrophic lateral sclerosis","volume":"6","author":"Zarei","year":"2015","journal-title":"Surg Neurol Int."},{"key":"2025060300222486800_awaf076-B99","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1136\/jnnp.2007.131334","article-title":"TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia","volume":"79","author":"Weihl","year":"2008","journal-title":"J Neurol Neurosurg Psychiatry"},{"key":"2025060300222486800_awaf076-B100","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/ng718","article-title":"The UDP-N-acetylglucosamine 2-epimerase\/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy","volume":"29","author":"Eisenberg","year":"2001","journal-title":"Nat Genet"},{"key":"2025060300222486800_awaf076-B101","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1212\/WNL.0000000000001864","article-title":"SQSTM1 splice site mutation in distal myopathy with rimmed vacuoles","volume":"85","author":"Bucelli","year":"2015","journal-title":"Neurology"},{"key":"2025060300222486800_awaf076-B102","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.nmd.2024.07.008","article-title":"Defining the landscape of TIA1 and SQSTM1 digenic myopathy","volume":"42","author":"Panos-Basterra","year":"2024","journal-title":"Neuromuscul Disord"},{"key":"2025060300222486800_awaf076-B103","doi-asserted-by":"crossref","first-page":"121","DOI":"10.15252\/embj.201591998","article-title":"TDP-43 loss of function increases TFEB activity and blocks autophagosome-lysosome fusion","volume":"35","author":"Xia","year":"2016","journal-title":"EMBO J."},{"key":"2025060300222486800_awaf076-B104","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1002\/ana.410380504","article-title":"Inclusion body myositis and myopathies","volume":"38","author":"Griggs","year":"1995","journal-title":"Ann Neurol."},{"key":"2025060300222486800_awaf076-B105","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1212\/WNL.28.1.8","article-title":"Inclusion body myositis: A distinct variety of idiopathic inflammatory myopathy","volume":"28","author":"Carpenter","year":"1978","journal-title":"Neurology"},{"key":"2025060300222486800_awaf076-B106","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1007\/BF00687390","article-title":"Rimmed vacuoles","volume":"51","author":"Fukuhara","year":"1980","journal-title":"Acta Neuropathol"},{"issue":"Pt 1","key":"2025060300222486800_awaf076-B107","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1093\/brain\/115.1.249","article-title":"Strong immunoreactivity of cathepsin L at the site of rimmed vacuoles in diseased muscles","volume":"115","author":"Jimi","year":"1992","journal-title":"Brain"},{"key":"2025060300222486800_awaf076-B108","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/0960-8966(94)E0019-5","article-title":"Rimmed basophilic vacuoles and filamentous inclusions in neuromuscular disorders","volume":"5","author":"Jongen","year":"1995","journal-title":"Neuromuscul Disord"},{"key":"2025060300222486800_awaf076-B109","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/s00401-003-0774-2","article-title":"Expression of lysosome-related proteins and genes in the skeletal muscles of inclusion body myositis","volume":"107","author":"Kumamoto","year":"2004","journal-title":"Acta Neuropathol"},{"key":"2025060300222486800_awaf076-B110","first-page":"527","article-title":"Pathology of the inflammatory myopathies","volume":"2","author":"Karpati","year":"1993","journal-title":"Baillieres Clin Neurol"},{"key":"2025060300222486800_awaf076-B111","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1002\/mus.20584","article-title":"Nuclear membrane proteins are present within rimmed vacuoles in inclusion-body myositis","volume":"34","author":"Greenberg","year":"2006","journal-title":"Muscle Nerve."},{"key":"2025060300222486800_awaf076-B112","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s11926-010-0102-5","article-title":"Theories of the pathogenesis of inclusion body myositis","volume":"12","author":"Greenberg","year":"2010","journal-title":"Curr Rheumatol Rep"},{"key":"2025060300222486800_awaf076-B113","first-page":"874","article-title":"Conspicuous accumulation of a single-stranded DNA binding protein in skeletal muscle fibers in inclusion body myositis","volume":"144","author":"Nalbantoglu","year":"1994","journal-title":"Am J Pathol"},{"key":"2025060300222486800_awaf076-B114","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1002\/mus.21386","article-title":"Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis","volume":"40","author":"Salajegheh","year":"2009","journal-title":"Muscle Nerve"},{"key":"2025060300222486800_awaf076-B115","doi-asserted-by":"crossref","first-page":"4425","DOI":"10.1093\/brain\/awad202","article-title":"Skeletal muscle in amyotrophic lateral sclerosis","volume":"146","author":"Shefner","year":"2023","journal-title":"Brain."},{"key":"2025060300222486800_awaf076-B116","doi-asserted-by":"crossref","first-page":"4986","DOI":"10.1073\/pnas.1218311110","article-title":"Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth","volume":"110","author":"Schmid","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2025060300222486800_awaf076-B117","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/s00401-010-0659-0","article-title":"Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis","volume":"119","author":"Kraemer","year":"2010","journal-title":"Acta Neuropathol."},{"key":"2025060300222486800_awaf076-B118","doi-asserted-by":"crossref","first-page":"3883","DOI":"10.1093\/hmg\/ddt243","article-title":"Drosophila TDP-43 dysfunction in glia and muscle cells cause cytological and behavioural phenotypes that characterize ALS and FTLD","volume":"22","author":"Diaper","year":"2013","journal-title":"Hum Mol Genet"},{"key":"2025060300222486800_awaf076-B119","first-page":"184","article-title":"Muscleblind, BSF and TBPH are mislocalized in the muscle sarcomere of a Drosophila myotonic dystrophy model","volume":"6","author":"Llamusi","year":"2013","journal-title":"Dis Model Mech"},{"key":"2025060300222486800_awaf076-B120","doi-asserted-by":"crossref","first-page":"e1006805","DOI":"10.1371\/journal.pgen.1006805","article-title":"Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis","volume":"13","author":"Park","year":"2017","journal-title":"PLoS Genet."},{"key":"2025060300222486800_awaf076-B121","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.ymeth.2010.11.006","article-title":"TDP-43 toxicity in yeast","volume":"53","author":"Armakola","year":"2011","journal-title":"Methods"},{"key":"2025060300222486800_awaf076-B122","doi-asserted-by":"crossref","first-page":"39490","DOI":"10.1038\/srep39490","article-title":"An acridine derivative, [4,5-bis(N-carboxy methyl imidazolium)methylacridine] dibromide, shows anti-TDP-43 aggregation effect in ALS disease models","volume":"6","author":"Prasad","year":"2016","journal-title":"Sci Rep."},{"key":"2025060300222486800_awaf076-B123","doi-asserted-by":"crossref","first-page":"2092","DOI":"10.1038\/s41467-017-02017-x","article-title":"Endocytosis regulates TDP-43 toxicity and turnover","volume":"8","author":"Liu","year":"2017","journal-title":"Nat Commun."},{"key":"2025060300222486800_awaf076-B124","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1038\/nature22038","article-title":"Therapeutic reduction of ataxin-2 extends lifespan and reduces pathology in TDP-43 mice","volume":"544","author":"Becker","year":"2017","journal-title":"Nature"},{"key":"2025060300222486800_awaf076-B125","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1523\/JNEUROSCI.4988-09.2010","article-title":"Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis","volume":"30","author":"Barmada","year":"2010","journal-title":"J Neurosci."},{"key":"2025060300222486800_awaf076-B126","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/nsmb.2053","article-title":"An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity","volume":"18","author":"Guo","year":"2011","journal-title":"Nat Struct Mol Biol."},{"key":"2025060300222486800_awaf076-B127","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1093\/hmg\/ddt498","article-title":"TDP-43 Phosphorylation by casein kinase Iepsilon promotes oligomerization and enhances toxicity in vivo","volume":"23","author":"Choksi","year":"2014","journal-title":"Hum Mol Genet."},{"key":"2025060300222486800_awaf076-B128","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.brainres.2016.04.069","article-title":"The extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivo","volume":"1647","author":"Sasaguri","year":"2016","journal-title":"Brain Res."},{"key":"2025060300222486800_awaf076-B129","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1007\/s00401-015-1460-x","article-title":"Functional recovery in new mouse models of ALS\/FTLD after clearance of pathological cytoplasmic TDP-43","volume":"130","author":"Walker","year":"2015","journal-title":"Acta Neuropathol."},{"key":"2025060300222486800_awaf076-B130","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1172\/JCI44867","article-title":"Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice","volume":"121","author":"Igaz","year":"2011","journal-title":"J Clin Invest."},{"key":"2025060300222486800_awaf076-B131","doi-asserted-by":"crossref","first-page":"5154","DOI":"10.1093\/hmg\/ddv238","article-title":"PABPN1 suppresses TDP-43 toxicity in ALS disease models","volume":"24","author":"Chou","year":"2015","journal-title":"Hum Mol Genet."},{"key":"2025060300222486800_awaf076-B132","doi-asserted-by":"crossref","first-page":"4345","DOI":"10.1093\/hmg\/ddu152","article-title":"Distinct pathways leading to TDP-43-induced cellular dysfunctions","volume":"23","author":"Yamashita","year":"2014","journal-title":"Hum Mol Genet."},{"key":"2025060300222486800_awaf076-B133","doi-asserted-by":"crossref","first-page":"19230","DOI":"10.1038\/srep19230","article-title":"Interaction of RNA with a C-terminal fragment of the amyotrophic lateral sclerosis-associated TDP43 reduces cytotoxicity","volume":"6","author":"Kitamura","year":"2016","journal-title":"Sci Rep."},{"key":"2025060300222486800_awaf076-B134","doi-asserted-by":"crossref","first-page":"3641","DOI":"10.1074\/jbc.M112.433615","article-title":"Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins","volume":"288","author":"Watanabe","year":"2013","journal-title":"J Biol Chem."},{"key":"2025060300222486800_awaf076-B135","doi-asserted-by":"crossref","first-page":"eadp5730","DOI":"10.1126\/scitranslmed.adp5730","article-title":"Seeding-competent TDP-43 persists in human patient and mouse muscle","volume":"16","author":"Lynch","year":"2024","journal-title":"Sci Transl Med"},{"key":"2025060300222486800_awaf076-B136","doi-asserted-by":"crossref","first-page":"4162","DOI":"10.1038\/s41467-019-12101-z","article-title":"The mutational landscape of a prion-like domain","volume":"10","author":"Bolognesi","year":"2019","journal-title":"Nat Commun."},{"key":"2025060300222486800_awaf076-B137","doi-asserted-by":"crossref","first-page":"6826","DOI":"10.1074\/jbc.M109.061846","article-title":"TDP-43 is a developmentally regulated protein essential for early embryonic development","volume":"285","author":"Sephton","year":"2010","journal-title":"J Biol Chem."},{"key":"2025060300222486800_awaf076-B138","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1080\/17482960802146106","article-title":"ALSOD: The amyotrophic lateral sclerosis online database","volume":"9","author":"Wroe","year":"2008","journal-title":"Amyotroph Lateral Scler"},{"key":"2025060300222486800_awaf076-B139","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1007\/s00018-008-8532-1","article-title":"Nuclear functions of heterogeneous nuclear ribonucleoproteins A\/B","volume":"66","author":"He","year":"2009","journal-title":"Cell Mol Life Sci"},{"key":"2025060300222486800_awaf076-B140","doi-asserted-by":"crossref","first-page":"2306","DOI":"10.1038\/s41467-022-30015-1","article-title":"Heterozygous frameshift variants in HNRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy","volume":"13","author":"Kim","year":"2022","journal-title":"Nat Commun."},{"key":"2025060300222486800_awaf076-B141","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/nature11922","article-title":"Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS","volume":"495","author":"Kim","year":"2013","journal-title":"Nature"},{"key":"2025060300222486800_awaf076-B142","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.1212\/WNL.0b013e3182929fc3","article-title":"Motor neuron involvement in multisystem proteinopathy: Implications for ALS","volume":"80","author":"Benatar","year":"2013","journal-title":"Neurology"},{"key":"2025060300222486800_awaf076-B143","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1186\/s40478-014-0165-z","article-title":"Mitochondrial abnormalities and low grade inflammation are present in the skeletal muscle of a minority of patients with amyotrophic lateral sclerosis; an observational myopathology study","volume":"2","author":"Al-Sarraj","year":"2014","journal-title":"Acta Neuropathol Commun."},{"key":"2025060300222486800_awaf076-B144","doi-asserted-by":"crossref","first-page":"261","DOI":"10.3109\/21678421.2012.735239","article-title":"Mitochondrial genome aberrations in skeletal muscle of patients with motor neuron disease","volume":"14","author":"Artuso","year":"2013","journal-title":"Amyotroph Lateral Scler Frontotemporal Degener."},{"key":"2025060300222486800_awaf076-B145","doi-asserted-by":"crossref","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":"2025060300222486800_awaf076-B146","doi-asserted-by":"crossref","first-page":"165","DOI":"10.3109\/00207459108985432","article-title":"Muscle morphometry in amyotrophic lateral sclerosis","volume":"58","author":"Iwasaki","year":"1991","journal-title":"Int J Neurosci."},{"key":"2025060300222486800_awaf076-B147","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1111\/j.1600-0404.1997.tb00302.x","article-title":"DNA-fragmentation and apoptosis-related proteins of muscle cells in motor neuron disorders","volume":"96","author":"Tews","year":"1997","journal-title":"Acta Neurol Scand."},{"key":"2025060300222486800_awaf076-B148","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0022-510X(99)00236-1","article-title":"Visualization of defective mitochondrial function in skeletal muscle fibers of patients with sporadic amyotrophic lateral sclerosis","volume":"169","author":"Vielhaber","year":"1999","journal-title":"J Neurol Sci."},{"key":"2025060300222486800_awaf076-B149","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1111\/j.1471-4159.2006.04408.x","article-title":"Amyotrophic lateral sclerosis: All roads lead to Rome","volume":"101","author":"Gonzalez de Aguilar","year":"2007","journal-title":"J Neurochem."},{"key":"2025060300222486800_awaf076-B150","doi-asserted-by":"crossref","first-page":"240","DOI":"10.3109\/17482960902810890","article-title":"TDP-43 in skeletal muscle of patients affected with amyotrophic lateral sclerosis","volume":"11","author":"Soraru","year":"2010","journal-title":"Amyotroph Lateral Scler"},{"key":"2025060300222486800_awaf076-B151","doi-asserted-by":"crossref","first-page":"e13261","DOI":"10.1111\/bpa.13261","article-title":"Detection of pTDP-43 via routine muscle biopsy: A promising diagnostic biomarker for amyotrophic lateral sclerosis","volume":"34","author":"Zhang","year":"2024","journal-title":"Brain Pathol"}],"container-title":["Brain"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/brain\/advance-article-pdf\/doi\/10.1093\/brain\/awaf076\/62178661\/awaf076.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/brain\/article-pdf\/148\/6\/1876\/62178661\/awaf076.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/brain\/article-pdf\/148\/6\/1876\/62178661\/awaf076.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,6,3]],"date-time":"2025-06-03T04:22:55Z","timestamp":1748924575000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/brain\/article\/148\/6\/1876\/8043252"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2,26]]},"references-count":151,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2025,2,26]]},"published-print":{"date-parts":[[2025,6,3]]}},"URL":"https:\/\/doi.org\/10.1093\/brain\/awaf076","relation":{},"ISSN":["0006-8950","1460-2156"],"issn-type":[{"value":"0006-8950","type":"print"},{"value":"1460-2156","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2025,6]]},"published":{"date-parts":[[2025,2,26]]}}}