{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cascella R"],"funding":["Fondazione Italiana di Ricerca per la Sclerosi Laterale Amiotrofica","Università di Firenze-Fondazione Cassa di Risparmio di Firenze","University of Genoa","University of Florence","Hitachi","Grant Heavy Equipment"],"pagination":["72-88"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9746631"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["55(1)"],"pubmed_abstract":["<b>Introduction:</b> Several neurodegenerative conditions are associated with a common histopathology within neurons of the central nervous system, consisting of the deposition of cytoplasmic inclusions of TAR DNA-binding protein 43 (TDP-43). Such inclusions have variably been described as morphologically and molecularly ordered aggregates having amyloid properties, as filaments without the cross-β-structure and dye binding specific for amyloid, or as amorphous aggregates with no defined structure and fibrillar morphology.<b>Aims and Methods:</b> Here we have expressed human full-length TDP-43 in neuroblastoma x spinal cord 34 (NSC-34) cells to investigate the morphological, structural, and tinctorial properties of TDP-43 inclusions <i>in situ</i>. We have used last-generation amyloid diag"],"journal":["Annals of medicine"],"pubmed_title":["An <i>in situ</i> and <i>in vitro</i> investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature."],"pmcid":["PMC9746631"],"funding_grant_id":["HT7800 120 kV","3404","TDP-43-STRUCT","TROTHERALS","TDP43SLA"],"pubmed_authors":["Natalello A","Ami D","Cascella R","Chiti F","Banchelli M","Staderini T","Cecchi C","Tampellini D","Matteini P","Adibi H","Abolghasem Ghadami S","Bigi A","Cortese K","Gagliani MC"],"additional_accession":[]},"is_claimable":false,"name":"An <i>in situ</i> and <i>in vitro</i> investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature.","description":"<b>Introduction:</b> Several neurodegenerative conditions are associated with a common histopathology within neurons of the central nervous system, consisting of the deposition of cytoplasmic inclusions of TAR DNA-binding protein 43 (TDP-43). Such inclusions have variably been described as morphologically and molecularly ordered aggregates having amyloid properties, as filaments without the cross-β-structure and dye binding specific for amyloid, or as amorphous aggregates with no defined structure and fibrillar morphology.<b>Aims and Methods:</b> Here we have expressed human full-length TDP-43 in neuroblastoma x spinal cord 34 (NSC-34) cells to investigate the morphological, structural, and tinctorial properties of TDP-43 inclusions <i>in situ</i>. We have used last-generation amyloid diag","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2026-06-04T09:48:18.425Z","creation":"2025-04-05T12:39:18.229Z"},"accession":"S-EPMC9746631","cross_references":{"pubmed":["36495262"],"doi":["10.1080/07853890.2022.2148734"]}}