{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T04:45:48Z","timestamp":1782708348670,"version":"3.54.5"},"reference-count":64,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2026,5,22]],"date-time":"2026-05-22T00:00:00Z","timestamp":1779408000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,5,22]],"date-time":"2026-05-22T00:00:00Z","timestamp":1779408000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Neurochem Res"],"published-print":{"date-parts":[[2026,6]]},"DOI":"10.1007\/s11064-026-04770-2","type":"journal-article","created":{"date-parts":[[2026,5,22]],"date-time":"2026-05-22T07:48:40Z","timestamp":1779436120000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["TDP-43 Acetylation at the Neuroimmune Interface: A Hypothesis-Driven Framework for Peripheral Inflammatory Stratotypes in ALS"],"prefix":"10.1007","volume":"51","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-5390-568X","authenticated-orcid":false,"given":"Guido Attilio","family":"Condorelli","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-5055-5420","authenticated-orcid":false,"given":"Alessio","family":"Iozzia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-3622-385X","authenticated-orcid":false,"given":"Deborah","family":"Bonifacio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5568-3780","authenticated-orcid":false,"given":"Anamaria","family":"Pelin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,5,22]]},"reference":[{"issue":"5796","key":"4770_CR1","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1126\/science.1134108","volume":"314","author":"M Neumann","year":"2006","unstructured":"Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT et al (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and ALS. Science 314(5796):130\u2013133. https:\/\/doi.org\/10.1126\/science.1134108","journal-title":"Science"},{"issue":"3","key":"4770_CR2","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","volume":"351","author":"T Arai","year":"2006","unstructured":"Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H et al (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and ALS. Biochem Biophys Res Commun 351(3):602\u2013611. https:\/\/doi.org\/10.1016\/j.bbrc.2006.10.093","journal-title":"Biochem Biophys Res Commun"},{"issue":"3","key":"4770_CR3","doi-asserted-by":"publisher","first-page":"416","DOI":"10.1016\/j.neuron.2013.07.033","volume":"79","author":"SC Ling","year":"2013","unstructured":"Ling SC, Polymenidou M, Cleveland DW (2013) Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 79(3):416\u2013438. https:\/\/doi.org\/10.1016\/j.neuron.2013.07.033","journal-title":"Neuron"},{"key":"4770_CR4","doi-asserted-by":"publisher","first-page":"5845","DOI":"10.1038\/ncomms6845","volume":"6","author":"TJ Cohen","year":"2015","unstructured":"Cohen TJ, Hwang AW, Restrepo CR, Yuan CX, Trojanowski JQ, Lee VMY (2015) An acetylation switch controls TDP-43 function and aggregation propensity. Nat Commun 6:5845. https:\/\/doi.org\/10.1038\/ncomms6845","journal-title":"Nat Commun"},{"key":"4770_CR5","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1038\/s41467-017-00088-4","volume":"8","author":"P Wang","year":"2017","unstructured":"Wang P, Wander CM, Yuan C-X, Bereman MS, Cohen TJ (2017) Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program. Nat Commun 8:82. https:\/\/doi.org\/10.1038\/s41467-017-00088-4","journal-title":"Nat Commun"},{"issue":"6529","key":"4770_CR6","doi-asserted-by":"publisher","first-page":"eabb4309","DOI":"10.1126\/science.abb4309","volume":"371","author":"H Yu","year":"2021","unstructured":"Yu H, Lu S, Gasior K, Singh D, Vazquez-Sanchez S, Tapia O et al (2021) HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells. Science 371(6529):eabb4309. https:\/\/doi.org\/10.1126\/science.abb4309","journal-title":"Science"},{"issue":"2","key":"4770_CR7","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1002\/glia.20919","volume":"58","author":"W Zhao","year":"2010","unstructured":"Zhao W, Beers DR, Henkel JS, Zhang W, Urushitani M, Julien J-P et al (2010) Extracellular mutant SOD1 induces microglial-mediated motoneuron injury. Glia 58(2):231\u2013243. https:\/\/doi.org\/10.1002\/glia.20919","journal-title":"Glia"},{"issue":"11","key":"4770_CR8","doi-asserted-by":"publisher","first-page":"1132","DOI":"10.3390\/brainsci14111132","volume":"14","author":"E Pongr\u00e1cov\u00e1","year":"2024","unstructured":"Pongr\u00e1cov\u00e1 E, Buratti E, Romano M (2024) Prion-like spreading of disease in TDP-43 proteinopathies. Brain Sci 14(11):1132. https:\/\/doi.org\/10.3390\/brainsci14111132","journal-title":"Brain Sci"},{"issue":"12","key":"4770_CR9","doi-asserted-by":"publisher","first-page":"3187","DOI":"10.1093\/brain\/aww237","volume":"139","author":"Y Iguchi","year":"2016","unstructured":"Iguchi Y, Eid L, Parent M, Soucy G, Bareil C, Riku Y et al (2016) Exosome secretion is a key pathway for clearance of pathological TDP-43. Brain 139(12):3187\u20133201. https:\/\/doi.org\/10.1093\/brain\/aww237","journal-title":"Brain"},{"issue":"5\u20136","key":"4770_CR10","doi-asserted-by":"publisher","first-page":"351","DOI":"10.3109\/21678421.2014.905606","volume":"15","author":"E Feneberg","year":"2014","unstructured":"Feneberg E, Steinacker P, Lehnert S, Schneider A, Walther P, Thal DR, Linsenmeier M, Ludolph AC, Otto M (2014) Limited role of free TDP-43 as a diagnostic tool in neurodegenerative diseases. Amyotroph Lateral Scler Frontotemporal Degener 15(5\u20136):351\u2013356. https:\/\/doi.org\/10.3109\/21678421.2014.905606","journal-title":"Amyotroph Lateral Scler Frontotemporal Degener"},{"key":"4770_CR11","doi-asserted-by":"publisher","first-page":"487","DOI":"10.3389\/fnins.2018.00487","volume":"12","author":"D Sproviero","year":"2018","unstructured":"Sproviero D, La Salvia S, Giannini M, Crippa V, Gagliardi S, Bernuzzi S et al (2018) Pathological proteins are transported by extracellular vesicles of sporadic amyotrophic lateral sclerosis patients. Front Neurosci 12:487. https:\/\/doi.org\/10.3389\/fnins.2018.00487","journal-title":"Front Neurosci"},{"issue":"7","key":"4770_CR12","doi-asserted-by":"publisher","first-page":"e0182002","DOI":"10.1371\/journal.pone.0182002","volume":"12","author":"MP Gustafson","year":"2017","unstructured":"Gustafson MP, Staff NP, Bornschlegl S, Butler GW, Maas ML, Kazamel M et al (2017) Comprehensive immune profiling reveals substantial immune system alterations in a subset of patients with amyotrophic lateral sclerosis. PLoS ONE 12(7):e0182002. https:\/\/doi.org\/10.1371\/journal.pone.0182002","journal-title":"PLoS ONE"},{"issue":"4","key":"4770_CR13","doi-asserted-by":"publisher","first-page":"e242","DOI":"10.1212\/NXI.0000000000000242","volume":"3","author":"BJ Murdock","year":"2016","unstructured":"Murdock BJ, Bender DE, Kashlan SR, Figueroa-Romero C, Backus C, Callaghan BC et al (2016) Increased ratio of circulating neutrophils to monocytes in amyotrophic lateral sclerosis. Neurol Neuroimmunol Neuroinflamm 3(4):e242. https:\/\/doi.org\/10.1212\/NXI.0000000000000242","journal-title":"Neurol Neuroimmunol Neuroinflamm"},{"key":"4770_CR14","doi-asserted-by":"publisher","first-page":"301","DOI":"10.3389\/fnmol.2019.00301","volume":"12","author":"L Fran\u00e7ois-Moutal","year":"2019","unstructured":"Fran\u00e7ois-Moutal L, Perez-Miller S, Scott DD, Miranda VG, Mollasalehi N, Khanna M (2019) Structural insights into TDP-43 and effects of post-translational modifications. Front Mol Neurosci 12:301. https:\/\/doi.org\/10.3389\/fnmol.2019.00301","journal-title":"Front Mol Neurosci"},{"key":"4770_CR15","doi-asserted-by":"publisher","first-page":"2558","DOI":"10.1038\/s41467-023-38168-4","volume":"14","author":"A Ramachandran","year":"2023","unstructured":"Ramachandran A, Saunders C, Koren J et al (2023) Acetylation drives TDP-43 pathogenesis and its modulation induces disease reversal. Nat Commun 14:2558. https:\/\/doi.org\/10.1038\/s41467-023-38168-4","journal-title":"Nat Commun"},{"key":"4770_CR16","doi-asserted-by":"publisher","DOI":"10.1101\/2025.02.28.639952","author":"SC Saunders","year":"2025","unstructured":"Saunders S C, Rocha-Rangel PV, Desai R, Quadri Z, Liu H, Hunt J Jr et al (2025) Citrullination of TDP-43 is a key post-translation modification associated with structural and functional changes and progressive pathology in TDP-43 mouse models and human proteinopathies. bioRxiv. https:\/\/doi.org\/10.1101\/2025.02.28.639952","journal-title":"bioRxiv"},{"key":"4770_CR17","doi-asserted-by":"publisher","unstructured":"Hans F, Eckert M, von Zweydorf F, Gloeckner CJ, Kahle PJ (2018) Identification and characterization of ubiquitinylation sites in TAR DNA-binding protein of 43\u00a0kDa (TDP-43). Journal of Biological Chemistry. 293(41):16083\u201316099. https:\/\/doi.org\/10.1074\/jbc.RA118.003440","DOI":"10.1074\/jbc.RA118.003440"},{"key":"4770_CR18","doi-asserted-by":"publisher","unstructured":"Buratti E (2018) TDP-43 post-translational modifications in health and disease. Expert Opinion on Therapeutic Targets. 22(3):279\u2013293. https:\/\/doi.org\/10.1080\/14728222.2018.1439923","DOI":"10.1080\/14728222.2018.1439923"},{"key":"4770_CR19","doi-asserted-by":"publisher","unstructured":"Eck RJ, Kraemer BC, Liachko NF (2021) Regulation of TDP-43 phosphorylation in aging and disease. GeroScience. 43(4):1605\u20131614. https:\/\/doi.org\/10.1007\/s11357-021-00383-5","DOI":"10.1007\/s11357-021-00383-5"},{"key":"4770_CR20","doi-asserted-by":"publisher","unstructured":"Farina S, Esposito F, Battistoni M, Biamonti G, Francia S (2021) Post-translational modifications modulate proteinopathies of TDP-43, FUS and hnRNP-A\/B in amyotrophic lateral sclerosis. Frontiers in Molecular Biosciences. 8:693325. https:\/\/doi.org\/10.3389\/fmolb.2021.693325","DOI":"10.3389\/fmolb.2021.693325"},{"key":"4770_CR21","doi-asserted-by":"publisher","first-page":"279","DOI":"10.3389\/fneur.2020.00279","volume":"11","author":"PA McCombe","year":"2020","unstructured":"McCombe PA et al (2020) The peripheral immune system and amyotrophic lateral sclerosis. Front Neurol 11:279. https:\/\/doi.org\/10.3389\/fneur.2020.00279","journal-title":"Front Neurol"},{"issue":"52","key":"4770_CR22","doi-asserted-by":"publisher","first-page":"36186","DOI":"10.1074\/jbc.M805932200","volume":"283","author":"C Cook","year":"2008","unstructured":"Cook C, Zhang Y-J, Xu Y-F, Dickson DW, Petrucelli L (2008) TDP-43 in glial cytoplasmic inclusions is phosphorylated and truncated in frontotemporal lobar degeneration with ubiquitin-positive inclusions. J Biol Chem 283(52):36186\u201336193. https:\/\/doi.org\/10.1074\/jbc.M805932200","journal-title":"J Biol Chem"},{"issue":"1","key":"4770_CR23","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1186\/s12974-025-03347-0","volume":"22","author":"E \u00c1lvarez-S\u00e1nchez","year":"2025","unstructured":"\u00c1lvarez-S\u00e1nchez E, Carbayo \u00c1, Valle-Tamayo N, Mu\u00f1oz L, Aumatell J, Torres S et al (2025) Single-cell RNA sequencing highlights the role of distinct natural killer subsets in sporadic amyotrophic lateral sclerosis. J Neuroinflammation 22(1):15. https:\/\/doi.org\/10.1186\/s12974-025-03347-0","journal-title":"J Neuroinflammation"},{"key":"4770_CR24","doi-asserted-by":"publisher","first-page":"5941","DOI":"10.1038\/s41598-020-62756-8","volume":"10","author":"Z Jin","year":"2020","unstructured":"Jin Z et al (2020) Peripheral proinflammatory Th1\/Th17 immune cell shift is linked to disease severity in amyotrophic lateral sclerosis. Sci Rep 10:5941. https:\/\/doi.org\/10.1038\/s41598-020-62756-8","journal-title":"Sci Rep"},{"key":"4770_CR25","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1016\/j.bbi.2025.06.021","volume":"129","author":"G Risby-Jones","year":"2025","unstructured":"Risby-Jones G, Marallag J, Jagaraj CJ, Atkin JD, Walker AK, Woodruff TM, Lee JD, Fung JN (2025) IL-6 trans-signalling is elevated in ALS models and drives TDP-43 induced inflammatory responses in microglia. Brain Behav Immun 129:296\u2013304. https:\/\/doi.org\/10.1016\/j.bbi.2025.06.021","journal-title":"Brain Behav Immun"},{"key":"4770_CR26","doi-asserted-by":"publisher","first-page":"1193507","DOI":"10.3389\/fimmu.2023.1193507","volume":"14","author":"A Ramachandran","year":"2023","unstructured":"Ramachandran A, Ray P, Mantri S et al (2023) Low T cell reactivity to TDP-43 peptides in ALS. Front Immunol 14:1193507. https:\/\/doi.org\/10.3389\/fimmu.2023.1193507","journal-title":"Front Immunol"},{"issue":"3","key":"4770_CR27","doi-asserted-by":"publisher","first-page":"516","DOI":"10.3390\/cells11030516","volume":"11","author":"E Casarotto","year":"2022","unstructured":"Casarotto E, Sproviero D, Corridori E et al (2022) Neurodegenerative disease-associated TDP-43 fragments are extracellularly secreted with CASA complex proteins. Cells 11(3):516. https:\/\/doi.org\/10.3390\/cells11030516","journal-title":"Cells"},{"issue":"7899","key":"4770_CR28","doi-asserted-by":"publisher","first-page":"124","DOI":"10.1038\/s41586-022-04424-7","volume":"603","author":"XR Ma","year":"2022","unstructured":"Ma XR, Prudencio M, Koike Y, Vatsavayai SC, Kim G, Harbinski F et al (2022) TDP-43 represses cryptic exon inclusion in the FTD\u2013ALS gene UNC13A. Nature 603(7899):124\u2013130. https:\/\/doi.org\/10.1038\/s41586-022-04424-7","journal-title":"Nature"},{"issue":"1","key":"4770_CR29","doi-asserted-by":"publisher","first-page":"27","DOI":"10.3934\/biophy.2016.1.27","volume":"3","author":"A Didonna","year":"2016","unstructured":"Didonna A, Benetti F (2016) Post-translational modifications in neurodegeneration. AIMS Biophys 3(1):27\u201349. https:\/\/doi.org\/10.3934\/biophy.2016.1.27","journal-title":"AIMS Biophys"},{"issue":"1","key":"4770_CR30","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1186\/s13024-023-00608-5","volume":"18","author":"PR Mehta","year":"2023","unstructured":"Mehta PR, Brown AL, Ward ME, Fratta P (2023) The era of cryptic exons: implications for ALS\u2013FTD. Mol Neurodegener 18(1):16. https:\/\/doi.org\/10.1186\/s13024-023-00608-5","journal-title":"Mol Neurodegener"},{"issue":"734","key":"4770_CR31","doi-asserted-by":"publisher","first-page":"eadg7162","DOI":"10.1126\/scitranslmed.adg7162","volume":"16","author":"S Seddighi","year":"2024","unstructured":"Seddighi S, Qi YA, Brown AL, Wilkins OG, Bereda C, Belair C et al (2024) Mis-spliced transcripts generate de novo proteins in TDP-43-related ALS\/FTD. Sci Transl Med 16(734):eadg7162. https:\/\/doi.org\/10.1126\/scitranslmed.adg7162","journal-title":"Sci Transl Med"},{"issue":"2","key":"4770_CR32","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1038\/s41591-023-02788-5","volume":"30","author":"KE Irwin","year":"2024","unstructured":"Irwin KE, Jasin P, Braunstein KE, Sinha IR, Garret MA, Bowden KD et al (2024) A fluid biomarker reveals loss of TDP-43 splicing repression in presymptomatic ALS\u2013FTD. Nat Med 30(2):382\u2013393. https:\/\/doi.org\/10.1038\/s41591-023-02788-5","journal-title":"Nat Med"},{"key":"4770_CR33","doi-asserted-by":"publisher","unstructured":"Chizari S, Zanovello M, Kong S et al (2025) TDP-43 pathology induces CD8\u207a T cell activation through cryptic epitope recognition. bioRxiv. https:\/\/doi.org\/10.1101\/2025.06.22.660773","DOI":"10.1101\/2025.06.22.660773"},{"issue":"4","key":"4770_CR34","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1083\/jcb.201504057","volume":"211","author":"MS Feiler","year":"2015","unstructured":"Feiler MS, Strobel B, Freischmidt A, Helferich AM, Kappel J, Brewer BM, Li D, Thal DR, Walther P, Ludolph AC, Danzer KM, Weishaupt JH (2015) TDP-43 is intercellularly transmitted across axon terminals. J Cell Biol 211(4):897\u2013911. https:\/\/doi.org\/10.1083\/jcb.201504057","journal-title":"J Cell Biol"},{"issue":"37","key":"4770_CR35","doi-asserted-by":"publisher","first-page":"4121","DOI":"10.2174\/0929867324666170223153115","volume":"24","author":"A Richters","year":"2017","unstructured":"Richters A, Koehler AN (2017) Epigenetic modulation using small molecules - targeting histone acetyltransferases in disease. Curr Med Chem 24(37):4121\u20134150. https:\/\/doi.org\/10.2174\/0929867324666170223153115","journal-title":"Curr Med Chem"},{"issue":"9","key":"4770_CR36","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1038\/nrd4360","volume":"13","author":"KJ Falkenberg","year":"2014","unstructured":"Falkenberg KJ, Johnstone RW (2014) Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat Rev Drug Discov 13(9):673\u2013691. https:\/\/doi.org\/10.1038\/nrd4360","journal-title":"Nat Rev Drug Discov"},{"key":"4770_CR37","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1016\/j.bcp.2015.12.010","volume":"102","author":"T Van den Bosch","year":"2016","unstructured":"Van den Bosch T, Boichenko A, Leus NGJ et al (2016) The histone acetyltransferase p300 inhibitor C646 reduces pro-inflammatory gene expression and inhibits histone deacetylases. Biochem Pharmacol 102:130\u2013140. https:\/\/doi.org\/10.1016\/j.bcp.2015.12.010","journal-title":"Biochem Pharmacol"},{"issue":"3","key":"4770_CR38","doi-asserted-by":"publisher","first-page":"636","DOI":"10.1016\/j.cell.2020.09.020","volume":"183","author":"C-H Yu","year":"2020","unstructured":"Yu C-H, Davidson S, Harapas CR, Hilton JB, Mlodzianoski MJ, Laohamonthonkul P, Louis C, Low RRJ, Moecking J, De Nardo D, Balka KR, Calleja DJ, Moghaddas F, Ni E, McLean CA, Samson AL, Tyebji S, Tonkin CJ, Bye CR, Turner BJ et al (2020) TDP-43 triggers mitochondrial DNA release via mPTP to activate cGAS\/STING in ALS. Cell 183(3):636\u2013649e18. https:\/\/doi.org\/10.1016\/j.cell.2020.09.020","journal-title":"Cell"},{"issue":"2","key":"4770_CR39","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1038\/s41593-017-0047-3","volume":"21","author":"C-C Chou","year":"2018","unstructured":"Chou C-C, Zhang Y, Umoh ME, Vaughan SW, Lorenzini I, Liu F, Sayegh M, Donlin-Asp PG, Chen YH, Duong DM, Seyfried NT, Powers MA, Kukar T, Hales CM, Gearing M, Cairns NJ, Boylan KB, Dickson DW, Rademakers R, Zhang Y-J, Petrucelli L, Cook C, Song H, Yu G, Ling SC (2018) TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS\/FTD. Nat Neurosci 21(2):228\u2013239. https:\/\/doi.org\/10.1038\/s41593-017-0047-3","journal-title":"Nat Neurosci"},{"issue":"12","key":"4770_CR40","doi-asserted-by":"publisher","first-page":"e53877","DOI":"10.15252\/embr.202153877","volume":"22","author":"P De Rossi","year":"2021","unstructured":"De Rossi P, Scaber J, Paterson RW, Monteiro-Fernandes D, Loddo G, Oinas M et al (2021) FTLD-TDP assemblies seed neoaggregates with subtype-specific features via a prion-like cascade. EMBO Rep 22(12):e53877. https:\/\/doi.org\/10.15252\/embr.202153877","journal-title":"EMBO Rep"},{"key":"4770_CR41","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1016\/j.neulet.2017.12.037","volume":"666","author":"IF Harrison","year":"2018","unstructured":"Harrison IF, Smith AD, Dexter DT (2018) Pathological histone acetylation in Parkinson\u2019s disease: neuroprotection and inhibition of microglial activation through SIRT 2 inhibition. Neurosci Lett 666:48\u201357. https:\/\/doi.org\/10.1016\/j.neulet.2017.12.037","journal-title":"Neurosci Lett"},{"issue":"1","key":"4770_CR42","doi-asserted-by":"publisher","first-page":"1223","DOI":"10.1038\/s41467-022-28822-7","volume":"13","author":"J Garcia Morato","year":"2022","unstructured":"Garcia Morato J, Hans F, von Zweydorf F, Feederle R, Els\u00e4sser SJ, Skodras AA et al (2022) Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43. Nat Commun 13(1):1223. https:\/\/doi.org\/10.1038\/s41467-022-28822-7","journal-title":"Nat Commun"},{"issue":"5","key":"4770_CR43","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1016\/j.chembiol.2010.03.006","volume":"17","author":"EM Bowers","year":"2010","unstructured":"Bowers EM, Yan G, Mukherjee C, Orry A, Wang L, Holbert MA et al (2010) Virtual ligand screening of the p300\/CBP histone acetyltransferase: identification of a selective small molecule inhibitor. Chem Biol 17(5):471\u2013482. https:\/\/doi.org\/10.1016\/j.chembiol.2010.03.006","journal-title":"Chem Biol"},{"key":"4770_CR44","doi-asserted-by":"publisher","unstructured":"Luis M, Valor JV, Jose PLA, Angel B (2013) Lysine acetyltransferases CBP and p300 as therapeutic targets in cognitive and neurodegenerative disorders. Current Pharmaceutical Design. 19(28):5051\u20135064. https:\/\/doi.org\/10.2174\/13816128113199990382","DOI":"10.2174\/13816128113199990382"},{"key":"4770_CR45","doi-asserted-by":"publisher","unstructured":"Elizabeth EH, McKale RM, Kathryn JL (2016) HDAC inhibitors as epigenetic regulators of the immune system: impacts on cancer therapy and inflammatory diseases. BioMed Research International. 2016:8797206. https:\/\/doi.org\/10.1155\/2016\/8797206","DOI":"10.1155\/2016\/8797206"},{"key":"4770_CR46","doi-asserted-by":"publisher","unstructured":"Yvonne EK, Donya P, Ludo VDB (2021) Opportunities for histone deacetylase inhibition in amyotrophic lateral sclerosis. British Journal of Pharmacology. 178(6):1353\u20131372. https:\/\/doi.org\/10.1111\/bph.15217","DOI":"10.1111\/bph.15217"},{"key":"4770_CR47","doi-asserted-by":"publisher","unstructured":"Abdullah A, Ghallab A (2025) Epigenetic reprogramming as a therapeutic strategy for neurodegenerative diseases: A complex and novel approach. European Journal of Pharmacology. 1002:177853. https:\/\/doi.org\/10.1016\/j.ejphar.2025.177853","DOI":"10.1016\/j.ejphar.2025.177853"},{"issue":"7","key":"4770_CR48","doi-asserted-by":"publisher","first-page":"1147","DOI":"10.1007\/s10571-016-0452-2","volume":"37","author":"BL Tang","year":"2017","unstructured":"Tang BL (2017) Could sirtuin activities modify ALS onset and progression? Cell Mol Neurobiol 37(7):1147\u20131160. https:\/\/doi.org\/10.1007\/s10571-016-0452-2","journal-title":"Cell Mol Neurobiol"},{"key":"4770_CR49","doi-asserted-by":"publisher","first-page":"1025473","DOI":"10.3389\/fnagi.2022.1025473","volume":"14","author":"F Kabir","year":"2023","unstructured":"Kabir F, Atkinson R, Cook AL, Phipps AJ, King AE (2023) The role of altered protein acetylation in neurodegenerative disease. Front Aging Neurosci 14:1025473. https:\/\/doi.org\/10.3389\/fnagi.2022.1025473","journal-title":"Front Aging Neurosci"},{"key":"4770_CR50","doi-asserted-by":"publisher","first-page":"106645","DOI":"10.1016\/j.isci.2023.106645","volume":"26","author":"BA Evangelista","year":"2023","unstructured":"Evangelista BA, Cahalan SR, Ragusa JV et al (2023) Tandem detergent-extraction and immunoprecipitation of proteinopathy (TDiP): scalable enrichment of ALS-associated TDP-43 aggregates. iScience 26:106645. https:\/\/doi.org\/10.1016\/j.isci.2023.106645","journal-title":"iScience"},{"key":"4770_CR51","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1016\/j.clinms.2019.07.003","volume":"B","author":"TD Pobran","year":"2019","unstructured":"Pobran TD, Forgrave LM, Zheng YZ et al (2019) Detection and characterization of TDP-43 in human cells and tissues by multiple reaction monitoring mass spectrometry. Clin Mass Spectrom 14 Pt B:66\u201373. https:\/\/doi.org\/10.1016\/j.clinms.2019.07.003","journal-title":"Clin Mass Spectrom 14 Pt"},{"issue":"6","key":"4770_CR52","doi-asserted-by":"publisher","first-page":"645","DOI":"10.4155\/bio.13.19","volume":"5","author":"P Van Amsterdam","year":"2013","unstructured":"Van Amsterdam P, Companjen A, Brudny-Kloeppel M et al (2013) The European Bioanalysis Forum community\u2019s evaluation, interpretation and implementation of the European Medicines Agency guideline on Bioanalytical Method Validation. Bioanalysis 5(6):645\u2013659. https:\/\/doi.org\/10.4155\/bio.13.19","journal-title":"Bioanalysis"},{"issue":"5\u20136","key":"4770_CR53","doi-asserted-by":"publisher","first-page":"404","DOI":"10.3109\/21678421.2016.1167913","volume":"17","author":"P Oeckl","year":"2016","unstructured":"Oeckl P, Halbgebauer S, Anderl-Straub S et al (2016) Multicenter validation of CSF neurofilaments as diagnostic biomarkers for ALS. Amyotroph Lateral Scler Frontotemporal Degener 17(5\u20136):404\u2013413. https:\/\/doi.org\/10.3109\/21678421.2016.1167913","journal-title":"Amyotroph Lateral Scler Frontotemporal Degener"},{"issue":"1","key":"4770_CR54","doi-asserted-by":"publisher","first-page":"fcac029","DOI":"10.1093\/braincomms\/fcac029","volume":"4","author":"AG Thompson","year":"2022","unstructured":"Thompson AG, Gray E, Verber N et al (2022) Multicentre appraisal of amyotrophic lateral sclerosis biofluid biomarkers shows primacy of blood neurofilament light chain. Brain Commun 4(1):fcac029. https:\/\/doi.org\/10.1093\/braincomms\/fcac029","journal-title":"Brain Commun"},{"key":"4770_CR55","doi-asserted-by":"publisher","first-page":"919","DOI":"10.3389\/fneur.2020.00919","volume":"11","author":"Q Sun","year":"2020","unstructured":"Sun Q, Zhao X, Li S et al (2020) CSF neurofilament light chain elevation predicts ALS severity and progression. Front Neurol 11:919. https:\/\/doi.org\/10.3389\/fneur.2020.00919","journal-title":"Front Neurol"},{"issue":"6","key":"4770_CR56","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1002\/ana.26860","volume":"95","author":"M Benatar","year":"2024","unstructured":"Benatar M, Ostrow LW, Lewcock JW et al (2024) Biomarker qualification for neurofilament light chain in amyotrophic lateral sclerosis: theory and practice. Ann Neurol 95(6):833\u2013846. https:\/\/doi.org\/10.1002\/ana.26860","journal-title":"Ann Neurol"},{"issue":"6","key":"4770_CR57","doi-asserted-by":"publisher","first-page":"1771","DOI":"10.1038\/s41591-024-02937-4","volume":"30","author":"M Chatterjee","year":"2024","unstructured":"Chatterjee M, \u00d6zdemir S, Fritz C et al (2024) Plasma extracellular vesicle tau and TDP-43 as diagnostic biomarkers in FTD and ALS. Nat Med 30(6):1771\u20131783. https:\/\/doi.org\/10.1038\/s41591-024-02937-4","journal-title":"Nat Med"},{"issue":"1","key":"4770_CR58","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1186\/s13024-021-00470-3","volume":"16","author":"L Pasetto","year":"2021","unstructured":"Pasetto L, Callegaro S, Corbelli A et al (2021) Decoding distinctive features of plasma extracellular vesicles in amyotrophic lateral sclerosis. Mol Neurodegener 16(1):52. https:\/\/doi.org\/10.1186\/s13024-021-00470-3","journal-title":"Mol Neurodegener"},{"issue":"1","key":"4770_CR59","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1186\/s13024-025-00859-4","volume":"20","author":"ER Dellar","year":"2025","unstructured":"Dellar ER, Nikel L, Fowler S et al (2025) Extracellular vesicles in TDP-43 proteinopathies: pathogenesis and biomarker potential. Mol Neurodegener 20(1):68. https:\/\/doi.org\/10.1186\/s13024-025-00859-4","journal-title":"Mol Neurodegener"},{"issue":"1","key":"4770_CR60","doi-asserted-by":"publisher","first-page":"100071","DOI":"10.1016\/j.vesic.2025.100071","volume":"5","author":"Y Bi","year":"2025","unstructured":"Bi Y, Wang L, Li C (2025) Unveiling exosomal biomarkers in neurodegenerative diseases: LC-MS-based profiling. Extracell Vesicle 5(1):100071. https:\/\/doi.org\/10.1016\/j.vesic.2025.100071","journal-title":"Extracell Vesicle"},{"issue":"4","key":"4770_CR61","doi-asserted-by":"publisher","first-page":"597","DOI":"10.3390\/cells12040597","volume":"12","author":"I Cordts","year":"2023","unstructured":"Cordts I, Myszczynska MA, Roodveldt C, Allen SP, Van Den Bosch L, Vance C, Eggers C, Talbot K, Turner MR, Scotter EL, Otto M (2023) TDP-43 proteinopathy specific biomarker development. Cells 12(4):597. https:\/\/doi.org\/10.3390\/cells12040597","journal-title":"Cells"},{"key":"4770_CR62","doi-asserted-by":"publisher","first-page":"101336","DOI":"10.1016\/j.arr.2021.101336","volume":"68","author":"R Gupta","year":"2021","unstructured":"Gupta R, Sahu M, Srivastava D et al (2021) Post-translational modifications: regulators of neurodegenerative proteinopathies. Ageing Res Rev 68:101336. https:\/\/doi.org\/10.1016\/j.arr.2021.101336","journal-title":"Ageing Res Rev"},{"issue":"8","key":"4770_CR63","doi-asserted-by":"publisher","first-page":"100673","DOI":"10.1016\/j.medj.2025.100673","volume":"6","author":"BJ Murdock","year":"2025","unstructured":"Murdock BJ, Zhao B, Webber-Davis IF et al (2025) Early immune system changes in amyotrophic lateral sclerosis correlate with later disease progression. Med 6(8):100673. https:\/\/doi.org\/10.1016\/j.medj.2025.100673","journal-title":"Med"},{"issue":"6","key":"4770_CR64","doi-asserted-by":"publisher","first-page":"1353","DOI":"10.1111\/bph.15217","volume":"178","author":"YE Klingl","year":"2021","unstructured":"Klingl YE, Pakravan D, Van Den Bosch L (2021) Opportunities for histone deacetylase inhibition in amyotrophic lateral sclerosis. Br J Pharmacol 178(6):1353\u20131372. https:\/\/doi.org\/10.1111\/bph.15217","journal-title":"Br J Pharmacol"}],"container-title":["Neurochemical Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11064-026-04770-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11064-026-04770-2","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11064-026-04770-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T04:24:04Z","timestamp":1782707044000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11064-026-04770-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5,22]]},"references-count":64,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2026,6]]}},"alternative-id":["4770"],"URL":"https:\/\/doi.org\/10.1007\/s11064-026-04770-2","relation":{},"ISSN":["0364-3190","1573-6903"],"issn-type":[{"value":"0364-3190","type":"print"},{"value":"1573-6903","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,22]]},"assertion":[{"value":"21 January 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 April 2026","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 April 2026","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"22 May 2026","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}],"article-number":"169"}}