{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T19:58:42Z","timestamp":1792526322992,"version":"4.5.0"},"reference-count":114,"publisher":"Elsevier BV","issue":"15","license":[{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,4,30]],"date-time":"2025-04-30T00:00:00Z","timestamp":1745971200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["R01 NS114289"],"award-info":[{"award-number":["R01 NS114289"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"German Research Foundation","doi-asserted-by":"publisher","award":["369799452"],"award-info":[{"award-number":["369799452"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004076","name":"K\u00f6rber Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004076","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","award":["725836"],"award-info":[{"award-number":["725836"]}],"id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009076","name":"University of Science and Technology of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100009076","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008483","name":"NOMIS Stiftung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008483","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000090","name":"Congressionally Directed Medical Research Programs","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000090","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004189","name":"Max Planck Society","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004189","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000005","name":"US Department of Defense","doi-asserted-by":"publisher","award":["W81XWH-20-1-0241"],"award-info":[{"award-number":["W81XWH-20-1-0241"]}],"id":[{"id":"10.13039\/100000005","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell"],"published-print":{"date-parts":[[2025,7]]},"DOI":"10.1016\/j.cell.2025.04.039","type":"journal-article","created":{"date-parts":[[2025,5,23]],"date-time":"2025-05-23T10:35:06Z","timestamp":1747996506000},"page":"4123-4140.e18","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":147,"title":["Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates"],"prefix":"10.1016","volume":"188","author":[{"given":"Xiao","family":"Yan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Kuster","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Priyesh","family":"Mohanty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jik","family":"Nijssen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karina","family":"Pombo-Garc\u00eda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge","family":"Garcia Morato","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Azamat","family":"Rizuan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Titus M.","family":"Franzmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aleksandra","family":"Sergeeva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anh M.","family":"Ly","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Feilin","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia M.","family":"Passos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leah","family":"George","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Szu-Huan","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jayakrishna","family":"Shenoy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helen L.","family":"Danielson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Busra","family":"Ozguney","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alf","family":"Honigmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuna M.","family":"Ayala","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicolas L.","family":"Fawzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dennis W.","family":"Dickson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wilfried","family":"Rossoll","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeetain","family":"Mittal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4017-6505","authenticated-orcid":false,"given":"Simon","family":"Alberti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony A.","family":"Hyman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cell.2025.04.039_bib1","doi-asserted-by":"crossref","first-page":"656","DOI":"10.2174\/156720510793611592","article-title":"Tau in Alzheimer disease and related tauopathies","volume":"7","author":"Iqbal","year":"2010","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.cell.2025.04.039_bib2","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature10324","article-title":"\u03b1-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation","volume":"477","author":"Bartels","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.04.039_bib3","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1016\/j.celrep.2013.09.043","article-title":"Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins","volume":"5","author":"Ciryam","year":"2013","journal-title":"Cell Rep."},{"key":"10.1016\/j.cell.2025.04.039_bib4","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-13311-5","article-title":"Human TAUP301L overexpression results in TAU hyperphosphorylation without neurofibrillary tangles in adult zebrafish brain","volume":"7","author":"Cosacak","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.cell.2025.04.039_bib5","doi-asserted-by":"crossref","first-page":"13175","DOI":"10.1074\/jbc.M115.712083","article-title":"The Dynamics and Turnover of Tau Aggregates in Cultured Cells: INSIGHTS INTO THERAPIES FOR TAUOPATHIES","volume":"291","author":"Guo","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib6","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1002\/jnr.24092","article-title":"Overexpression of \u03b1-synuclein in an astrocyte cell line promotes autophagy inhibition and apoptosis","volume":"96","author":"Erustes","year":"2018","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.cell.2025.04.039_bib7","article-title":"Microglia-specific overexpression of \u03b1-synuclein leads to severe dopaminergic neurodegeneration by phagocytic exhaustion and oxidative toxicity","volume":"12","author":"Bido","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.04.039_bib8","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-021-27221-8","article-title":"Axonal TDP-43 condensates drive neuromuscular junction disruption through inhibition of local synthesis of nuclear encoded mitochondrial proteins","volume":"12","author":"Altman","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.04.039_bib9","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":"10.1016\/j.cell.2025.04.039_bib10","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":"10.1016\/j.cell.2025.04.039_bib11","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/nn.2779","article-title":"Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43","volume":"14","author":"Polymenidou","year":"2011","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.cell.2025.04.039_bib12","doi-asserted-by":"crossref","first-page":"3778","DOI":"10.1242\/jcs.038950","article-title":"Structural determinants of the cellular localization and shuttling of TDP-43","volume":"121","author":"Ayala","year":"2008","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.cell.2025.04.039_bib13","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/s41583-021-00431-1","article-title":"Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation","volume":"22","author":"Tziortzouda","year":"2021","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.cell.2025.04.039_bib14","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-018-25008-4","article-title":"Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization","volume":"8","author":"Pinarbasi","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.cell.2025.04.039_bib15","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.cell.2025.04.039_bib16","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.cell.2025.04.039_bib17","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.cell.2025.04.039_bib18","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1007\/s00401-013-1211-9","article-title":"Staging TDP-43 pathology in Alzheimer\u2019s disease","volume":"127","author":"Josephs","year":"2014","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.cell.2025.04.039_bib19","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1093\/brain\/awz099","article-title":"Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report","volume":"142","author":"Nelson","year":"2019","journal-title":"Brain"},{"key":"10.1016\/j.cell.2025.04.039_bib20","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1021\/acs.biochem.6b01088","article-title":"Phase to Phase with TDP-43","volume":"56","author":"Sun","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.cell.2025.04.039_bib21","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1186\/s13287-018-1048-1","article-title":"Modeling hallmark pathology using motor neurons derived from the family and sporadic amyotrophic lateral sclerosis patient-specific iPS cells","volume":"9","author":"Sun","year":"2018","journal-title":"Stem Cell Res. Ther."},{"key":"10.1016\/j.cell.2025.04.039_bib22","doi-asserted-by":"crossref","first-page":"19437","DOI":"10.1074\/jbc.M116.737726","article-title":"Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies","volume":"291","author":"Cascella","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib23","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1146\/annurev-biochem-061516-044518","article-title":"Protein Misfolding Diseases","volume":"86","author":"Hartl","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.cell.2025.04.039_bib24","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":"10.1016\/j.cell.2025.04.039_bib25","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1038\/s41586-023-06405-w","article-title":"TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP","volume":"620","author":"Arseni","year":"2023","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.04.039_bib26","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1038\/s41594-019-0248-4","article-title":"Cryo-EM structures of four polymorphic TDP-43 amyloid cores","volume":"26","author":"Cao","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.cell.2025.04.039_bib27","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":"10.1016\/j.cell.2025.04.039_bib28","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1038\/emboj.2011.471","article-title":"Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking","volume":"31","author":"Cohen","year":"2012","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2025.04.039_bib29","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1038\/s41580-020-00326-6","article-title":"Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing","volume":"22","author":"Alberti","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.cell.2025.04.039_bib30","doi-asserted-by":"crossref","first-page":"2841","DOI":"10.1038\/emboj.2010.143","article-title":"ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import","volume":"29","author":"Dormann","year":"2010","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2025.04.039_bib31","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":"10.1016\/j.cell.2025.04.039_bib32","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/s41582-019-0157-5","article-title":"Bridging biophysics and neurology: aberrant phase transitions in neurodegenerative disease","volume":"15","author":"Nedelsky","year":"2019","journal-title":"Nat. Rev. Neurol."},{"key":"10.1016\/j.cell.2025.04.039_bib33","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.cell.2025.04.039_bib34","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.cell.2020.03.049","article-title":"RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation","volume":"181","author":"Guill\u00e9n-Boixet","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.04.039_bib35","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/j.cell.2020.03.050","article-title":"Competing Protein-RNA Interaction Networks Control Multiphase Intracellular Organization","volume":"181","author":"Sanders","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.04.039_bib36","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.cell.2020.03.046","article-title":"G3BP1 Is a Tunable Switch that Triggers Phase Separation to Assemble Stress Granules","volume":"181","author":"Yang","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.04.039_bib37","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0013250","article-title":"Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue","volume":"5","author":"Liu-Yesucevitz","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.cell.2025.04.039_bib38","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":"10.1016\/j.cell.2025.04.039_bib39","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1097\/NEN.0000000000000102","article-title":"Poly-A binding protein-1 localization to a subset of TDP-43 inclusions in amyotrophic lateral sclerosis occurs more frequently in patients harboring an expansion in C9orf72","volume":"73","author":"McGurk","year":"2014","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.cell.2025.04.039_bib40","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":"10.1016\/j.cell.2025.04.039_bib41","doi-asserted-by":"crossref","DOI":"10.1111\/bpa.13215","article-title":"Colocalization of TDP-43 and stress granules at the early stage of TDP-43 aggregation in amyotrophic lateral sclerosis","volume":"34","author":"Mori","year":"2024","journal-title":"Brain Pathol."},{"key":"10.1016\/j.cell.2025.04.039_bib42","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.molcel.2018.07.002","article-title":"Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization","volume":"71","author":"McGurk","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.cell.2025.04.039_bib43","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1074\/jbc.RA118.006351","article-title":"Aggregation of the nucleic acid-binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation","volume":"294","author":"Chen","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib44","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-022-32939-0","article-title":"Stress induced TDP-43 mobility loss independent of stress granules","volume":"13","author":"Streit","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.04.039_bib45","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":"10.1016\/j.cell.2025.04.039_bib46","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/S0021-9258(17)49926-1","article-title":"Multiple distinct pathways lead to hyperubiquitylated insoluble TDP-43 protein independent of its translocation into stress granules","volume":"295","author":"Hans","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib47","doi-asserted-by":"crossref","first-page":"1378","DOI":"10.1038\/s41556-022-00988-8","article-title":"Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition","volume":"24","author":"Lu","year":"2022","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.cell.2025.04.039_bib48","doi-asserted-by":"crossref","first-page":"13302","DOI":"10.1074\/jbc.M800342200","article-title":"Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation","volume":"283","author":"Winton","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib49","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nmeth.2834","article-title":"Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells","volume":"11","author":"Kulak","year":"2014","journal-title":"Nat. Methods"},{"key":"10.1016\/j.cell.2025.04.039_bib50","article-title":"Quantitative phase microscopy enables precise and efficient determination of biomolecular condensate composition","author":"McCall","year":"2020","journal-title":"bioRxiv"},{"key":"10.1016\/j.cell.2025.04.039_bib51","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1097\/01.jnen.0000248554.45456.58","article-title":"TDP-43-positive white matter pathology in frontotemporal lobar degeneration with ubiquitin-positive inclusions","volume":"66","author":"Neumann","year":"2007","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.cell.2025.04.039_bib52","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1002\/ana.21425","article-title":"Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"64","author":"Hasegawa","year":"2008","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.cell.2025.04.039_bib53","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":"10.1016\/j.cell.2025.04.039_bib54","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1126\/science.abb8032","article-title":"Beyond aggregation: Pathological phase transitions in neurodegenerative disease","volume":"370","author":"Mathieu","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.cell.2025.04.039_bib55","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nature20413","article-title":"Decoding ALS: from genes to mechanism","volume":"539","author":"Taylor","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.04.039_bib56","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1083\/jcb.201508028","article-title":"G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits","volume":"212","author":"Kedersha","year":"2016","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.cell.2025.04.039_bib57","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.18413","article-title":"Distinct stages in stress granule assembly and disassembly","volume":"5","author":"Wheeler","year":"2016","journal-title":"eLife"},{"key":"10.1016\/j.cell.2025.04.039_bib58","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202009079","article-title":"High-fidelity reconstitution of stress granules and nucleoli in mammalian cellular lysate","volume":"220","author":"Freibaum","year":"2021","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.cell.2025.04.039_bib59","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1080\/109374000436355","article-title":"Molecular aspects of arsenic stress","volume":"3","author":"Bernstam","year":"2000","journal-title":"J. Toxicol. Environ. Health B Crit. Rev."},{"key":"10.1016\/j.cell.2025.04.039_bib60","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1080\/14728222.2018.1439923","article-title":"TDP-43 post-translational modifications in health and disease","volume":"22","author":"Buratti","year":"2018","journal-title":"Expert Opin. Ther. Targets"},{"key":"10.1016\/j.cell.2025.04.039_bib61","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3389\/fnmol.2017.00005","article-title":"Cysteine Modifications in the Pathogenesis of ALS","volume":"10","author":"Valle","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.cell.2025.04.039_bib62","article-title":"Methods to Classify Cytoplasmic Foci as Mammalian Stress Granules","volume":"123","author":"Aulas","year":"2017","journal-title":"J. Vis. Exp."},{"key":"10.1016\/j.cell.2025.04.039_bib63","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/s41586-021-03905-5","article-title":"Nucleation landscape of biomolecular condensates","volume":"599","author":"Shimobayashi","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.04.039_bib64","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/j.str.2016.07.007","article-title":"ALS Mutations Disrupt Phase Separation Mediated by \u03b1-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain","volume":"24","author":"Conicella","year":"2016","journal-title":"Structure"},{"key":"10.1016\/j.cell.2025.04.039_bib65","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1002338","article-title":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43","volume":"14","author":"Lim","year":"2016","journal-title":"PLoS Biol."},{"key":"10.1016\/j.cell.2025.04.039_bib66","doi-asserted-by":"crossref","first-page":"19614","DOI":"10.1074\/jbc.M113.463828","article-title":"Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion","volume":"288","author":"Jiang","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib67","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2305625120","article-title":"A synergy between site-specific and transient interactions drives the phase separation of a disordered, low-complexity domain","volume":"120","author":"Mohanty","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2025.04.039_bib68","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":"10.1016\/j.cell.2025.04.039_bib69","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.62718","article-title":"Multiple pathways of toxicity induced by C9orf72 dipeptide repeat aggregates and G4C2 RNA in a cellular model","volume":"10","author":"Frottin","year":"2021","journal-title":"eLife"},{"key":"10.1016\/j.cell.2025.04.039_bib70","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":"10.1016\/j.cell.2025.04.039_bib71","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1038\/s41593-017-0047-3","article-title":"TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS\/FTD","volume":"21","author":"Chou","year":"2018","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.cell.2025.04.039_bib72","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1007\/s00401-017-1698-6","article-title":"Mutant TDP-43 within motor neurons drives disease onset but not progression in amyotrophic lateral sclerosis","volume":"133","author":"Ditsworth","year":"2017","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.cell.2025.04.039_bib73","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":"10.1016\/j.cell.2025.04.039_bib74","doi-asserted-by":"crossref","first-page":"23079","DOI":"10.1074\/jbc.M111.328757","article-title":"Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43)","volume":"287","author":"Bentmann","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib75","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.abb3774","article-title":"C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy","volume":"12","author":"Cook","year":"2020","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.cell.2025.04.039_bib76","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s13024-019-0310-z","article-title":"Aberrant deposition of stress granule-resident proteins linked to C9orf72-associated TDP-43 proteinopathy","volume":"14","author":"Chew","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.cell.2025.04.039_bib77","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1186\/s40478-020-01055-9","article-title":"Intracellular dynamics of Ataxin-2 in the human brains with normal and frontotemporal lobar degeneration with TDP-43 inclusions","volume":"8","author":"Watanabe","year":"2020","journal-title":"Acta Neuropathol. Commun."},{"key":"10.1016\/j.cell.2025.04.039_bib78","article-title":"Proteomic analysis of the TDP-43-associated insoluble fraction from NEFH-TDP-43 mouse brain suggests sustained stress granule formation, CLUH granule recruitment and impaired mitochondrial metabolism","author":"Dunlop","year":"2024","journal-title":"bioRxiv"},{"key":"10.1016\/j.cell.2025.04.039_bib79","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1007\/s00401-014-1380-1","article-title":"Frontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine","volume":"129","author":"Irwin","year":"2015","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.cell.2025.04.039_bib80","doi-asserted-by":"crossref","first-page":"4680","DOI":"10.1016\/j.cell.2021.07.018","article-title":"TDP-43 condensation properties specify its RNA-binding and regulatory repertoire","volume":"184","author":"Hallegger","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.04.039_bib81","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4891","article-title":"A complex network of interdomain interactions underlies the conformational ensemble of monomeric TDP-43 and modulates its phase behavior","volume":"33","author":"Mohanty","year":"2024","journal-title":"Protein Sci."},{"key":"10.1016\/j.cell.2025.04.039_bib82","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1038\/nrd1330","article-title":"Neurodegenerative diseases and oxidative stress","volume":"3","author":"Barnham","year":"2004","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.cell.2025.04.039_bib83","doi-asserted-by":"crossref","first-page":"5883","DOI":"10.1073\/pnas.1912055117","article-title":"TDP-43 \u03b1-helical structure tunes liquid-liquid phase separation and function","volume":"117","author":"Conicella","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2025.04.039_bib84","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1038\/s41586-021-04199-3","article-title":"Structure of pathological TDP-43 filaments from ALS with FTLD","volume":"601","author":"Arseni","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.cell.2025.04.039_bib86","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.cell.2018.06.006","article-title":"A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins","volume":"174","author":"Wang","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.cell.2025.04.039_bib98","doi-asserted-by":"crossref","first-page":"4712","DOI":"10.1093\/nar\/gkt1407","article-title":"The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids","volume":"42","author":"Kuo","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.cell.2025.04.039_bib91","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":"10.1016\/j.cell.2025.04.039_bib99","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-017-00062-0","article-title":"Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation","volume":"8","author":"Afroz","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.cell.2025.04.039_bib92","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/s12104-018-09870-x","article-title":"1H, 15N and 13C backbone assignment of apo TDP-43 RNA recognition motifs","volume":"13","author":"Scott","year":"2019","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.cell.2025.04.039_bib85","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.15252\/embj.201695957","article-title":"An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function","volume":"36","author":"Mateju","year":"2017","journal-title":"EMBO J."},{"key":"10.1016\/j.cell.2025.04.039_bib112","doi-asserted-by":"crossref","DOI":"10.1016\/j.commatsci.2019.109363","article-title":"HOOMD-blue: A Python package for high-performance molecular dynamics and hard particle Monte Carlo simulations","volume":"173","author":"Anderson","year":"2020","journal-title":"Comput. Mater. Sci."},{"key":"10.1016\/j.cell.2025.04.039_bib87","doi-asserted-by":"crossref","DOI":"10.15252\/embr.202153632","article-title":"Specific RNA interactions promote TDP-43 multivalent phase separation and maintain liquid properties","volume":"22","author":"Grese","year":"2021","journal-title":"EMBO Rep."},{"key":"10.1016\/j.cell.2025.04.039_bib88","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1038\/nbt.3049","article-title":"Combinatorial analysis of developmental cues efficiently converts human pluripotent stem cells into multiple neuronal subtypes","volume":"33","author":"Maury","year":"2015","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.cell.2025.04.039_bib89","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1038\/nprot.2017.039","article-title":"FISH-Flow, a protocol for the concurrent detection of mRNA and protein in single cells using fluorescence in situ hybridization and flow cytometry","volume":"12","author":"Arrigucci","year":"2017","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.cell.2025.04.039_bib90","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2022.818655","article-title":"TDP-43 Oligomerization and Phase Separation Properties Are Necessary for Autoregulation","volume":"16","author":"Koehler","year":"2022","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.cell.2025.04.039_bib93","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s10858-016-0060-y","article-title":"CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysis","volume":"66","author":"Skinner","year":"2016","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.cell.2025.04.039_bib94","doi-asserted-by":"crossref","first-page":"5113","DOI":"10.1021\/ct500569b","article-title":"Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association","volume":"10","author":"Best","year":"2014","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.cell.2025.04.039_bib95","doi-asserted-by":"crossref","first-page":"9505","DOI":"10.1021\/acs.jpcb.0c07545","article-title":"Refining All-Atom Protein Force Fields for Polar-Rich, Prion-like, Low-Complexity Intrinsically Disordered Proteins","volume":"124","author":"Tang","year":"2020","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.cell.2025.04.039_bib96","doi-asserted-by":"crossref","DOI":"10.1063\/1.2121687","article-title":"A general purpose model for the condensed phases of water: TIP4P\/2005","volume":"123","author":"Abascal","year":"2005","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.cell.2025.04.039_bib97","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1021\/jz900079w","article-title":"Simulation of Osmotic Pressure in Concentrated Aqueous Salt Solutions","volume":"1","author":"Luo","year":"2010","journal-title":"J. Phys. Chem. Lett."},{"key":"10.1016\/j.cell.2025.04.039_bib100","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1002\/bmb.65","article-title":"Molecular modeling of estrogen receptor using molecular operating environment","volume":"35","author":"Roy","year":"2007","journal-title":"Biochem. Mol. Biol. Educ."},{"key":"10.1016\/j.cell.2025.04.039_bib101","doi-asserted-by":"crossref","first-page":"11671","DOI":"10.1021\/acs.jpcb.0c10489","article-title":"Molecular Details of Protein Condensates Probed by Microsecond Long Atomistic Simulations","volume":"124","author":"Zheng","year":"2020","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.cell.2025.04.039_bib102","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1002\/pro.4094","article-title":"Improved coarse-grained model for studying sequence dependent phase separation of disordered proteins","volume":"30","author":"Regy","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.cell.2025.04.039_bib103","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/S1574-1400(09)00503-9","article-title":"Methods for Monte Carlo simulations of biomacromolecules","volume":"5","author":"Vitalis","year":"2009","journal-title":"Annu. Rep. Comput. Chem."},{"key":"10.1016\/j.cell.2025.04.039_bib104","doi-asserted-by":"crossref","DOI":"10.1063\/5.0018516","article-title":"Heterogeneous parallelization and acceleration of molecular dynamics simulations in GROMACS","volume":"153","author":"P\u00e1ll","year":"2020","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.cell.2025.04.039_bib105","doi-asserted-by":"crossref","first-page":"4069","DOI":"10.1063\/1.449071","article-title":"The Nose\u2013Hoover thermostat","volume":"83","author":"Evans","year":"1985","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.cell.2025.04.039_bib106","doi-asserted-by":"crossref","first-page":"3684","DOI":"10.1063\/1.448118","article-title":"Molecular dynamics with coupling to an external bath","volume":"81","author":"Berendsen","year":"1984","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.cell.2025.04.039_bib107","article-title":"). Nonasymptotic estimates for Stochastic Gradient Langevin Dynamics under local conditions in nonconvex optimization","author":"Zhang","year":"2019","journal-title":"arXiv"},{"key":"10.1016\/j.cell.2025.04.039_bib108","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1005659","article-title":"OpenMM 7: Rapid development of high performance algorithms for molecular dynamics","volume":"13","author":"Eastman","year":"2017","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.cell.2025.04.039_bib109","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: An N log( N ) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.cell.2025.04.039_bib110","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0021-9991(77)90098-5","article-title":"Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes","volume":"23","author":"Ryckaert","year":"1977","journal-title":"J. Comput. Phys."},{"key":"10.1016\/j.cell.2025.04.039_bib111","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.cell.2025.04.039_bib113","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2109967118","article-title":"Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants","volume":"118","author":"Kelley","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cell.2025.04.039_bib114","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1005941","article-title":"Sequence determinants of protein phase behavior from a coarse-grained model","volume":"14","author":"Dignon","year":"2018","journal-title":"PLoS Comput. Biol."}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867425005094?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867425005094?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T12:54:36Z","timestamp":1782478476000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867425005094"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7]]},"references-count":114,"journal-issue":{"issue":"15","published-print":{"date-parts":[[2025,7]]}},"alternative-id":["S0092867425005094"],"URL":"https:\/\/doi.org\/10.1016\/j.cell.2025.04.039","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2024.01.23.576837","asserted-by":"object"}]},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[2025,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates","name":"articletitle","label":"Article Title"},{"value":"Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cell.2025.04.039","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Author(s). Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}