{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(1)"],"submitter":["Chevalier E"],"pubmed_abstract":["Abnormal cytoplasmic localization and accumulation of pathological transactive response DNA binding protein of 43 kDa (TDP-43) underlies several devastating diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 pathology (FTLD-TDP). A key element is the correlation between disease progression and spatio-temporal propagation of TDP-43-mediated pathology in the central nervous system. Several lines of evidence support the concept of templated aggregation and cell to cell spreading of pathological TDP-43. To further investigate this mechanism in vivo, we explored the efficacy of capturing and masking the seeding-competent region of extracellular TDP-43 species. For this, we generated a novel monoclonal antibody (mAb), ACI-6677, that targets the"],"journal":["Acta neuropathologica communications"],"pagination":["156"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11448013"],"repository":["biostudies-literature"],"pubmed_title":["Targeting the TDP-43 low complexity domain blocks spreading of pathology in a mouse model of ALS/FTD."],"pmcid":["PMC11448013"],"pubmed_authors":["Chevalier E","Afroz T","Pfeifer A","Piorkowska K","Audrain M","Ratnam M","Ollier R","Seredenina T","Kosco-Vilbois M","Fuchs A"],"additional_accession":[]},"is_claimable":false,"name":"Targeting the TDP-43 low complexity domain blocks spreading of pathology in a mouse model of ALS/FTD.","description":"Abnormal cytoplasmic localization and accumulation of pathological transactive response DNA binding protein of 43 kDa (TDP-43) underlies several devastating diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 pathology (FTLD-TDP). A key element is the correlation between disease progression and spatio-temporal propagation of TDP-43-mediated pathology in the central nervous system. Several lines of evidence support the concept of templated aggregation and cell to cell spreading of pathological TDP-43. To further investigate this mechanism in vivo, we explored the efficacy of capturing and masking the seeding-competent region of extracellular TDP-43 species. For this, we generated a novel monoclonal antibody (mAb), ACI-6677, that targets the","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2025-04-04T02:00:01.11Z","creation":"2025-04-04T02:00:01.11Z"},"accession":"S-EPMC11448013","cross_references":{"pubmed":["39363348"],"doi":["10.1186/s40478-024-01867-z"]}}