<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Cascella R</submitter><funding>Fondazione Italiana di Ricerca per la Sclerosi Laterale Amiotrofica</funding><funding>Università di Firenze-Fondazione Cassa di Risparmio di Firenze</funding><funding>University of Genoa</funding><funding>University of Florence</funding><funding>Hitachi</funding><funding>Grant Heavy Equipment</funding><pagination>72-88</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9746631</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>55(1)</volume><pubmed_abstract>&lt;b>Introduction:&lt;/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.&lt;b>Aims and Methods:&lt;/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 &lt;i>in situ&lt;/i>. We have used last-generation amyloid diag</pubmed_abstract><journal>Annals of medicine</journal><pubmed_title>An &lt;i>in situ&lt;/i> and &lt;i>in vitro&lt;/i> investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature.</pubmed_title><pmcid>PMC9746631</pmcid><funding_grant_id>HT7800 120 kV</funding_grant_id><funding_grant_id>3404</funding_grant_id><funding_grant_id>TDP-43-STRUCT</funding_grant_id><funding_grant_id>TROTHERALS</funding_grant_id><funding_grant_id>TDP43SLA</funding_grant_id><pubmed_authors>Natalello A</pubmed_authors><pubmed_authors>Ami D</pubmed_authors><pubmed_authors>Cascella R</pubmed_authors><pubmed_authors>Chiti F</pubmed_authors><pubmed_authors>Banchelli M</pubmed_authors><pubmed_authors>Staderini T</pubmed_authors><pubmed_authors>Cecchi C</pubmed_authors><pubmed_authors>Tampellini D</pubmed_authors><pubmed_authors>Matteini P</pubmed_authors><pubmed_authors>Adibi H</pubmed_authors><pubmed_authors>Abolghasem Ghadami S</pubmed_authors><pubmed_authors>Bigi A</pubmed_authors><pubmed_authors>Cortese K</pubmed_authors><pubmed_authors>Gagliani MC</pubmed_authors></additional><is_claimable>false</is_claimable><name>An &lt;i>in situ&lt;/i> and &lt;i>in vitro&lt;/i> investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature.</name><description>&lt;b>Introduction:&lt;/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.&lt;b>Aims and Methods:&lt;/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 &lt;i>in situ&lt;/i>. We have used last-generation amyloid diag</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Dec</publication><modification>2026-06-04T09:48:18.425Z</modification><creation>2025-04-05T12:39:18.229Z</creation></dates><accession>S-EPMC9746631</accession><cross_references><pubmed>36495262</pubmed><doi>10.1080/07853890.2022.2148734</doi></cross_references></HashMap>