{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zheng X"],"funding":["Fundamental Research Funds for the Central Universities","Natural Science Foundation of Shaanxi Province","National Natural Science Foundation of China","Key Research and Development Plan of Shaanxi Province","Natural Science Foundation"],"pagination":["655-669"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11258413"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["83(8)"],"pubmed_abstract":["The RNA/DNA-binding protein TDP-43 plays a pivotal role in the ubiquitinated inclusions characteristic of TDP-43 proteinopathies, including most cases of frontotemporal lobar degeneration (FTLD-TDP) and Alzheimer disease (AD). To understand the mechanisms of pathological TDP-43 processing and identify potential biomarkers, we generated novel phosphorylation-independent monoclonal antibodies (MAbs) using bacteria-expressed human full-length recombinant TDP-43. Remarkably, we identified a distinctive MAb, No. 9, targeting an epitope in amino acid (aa) region 311-360 of the C-terminus. This antibody showed preferential reactivity for pathological TDP-43 inclusions, with only mild reactivity for normal nuclear TDP-43. MAb No. 9 revealed more pathology in FTLD-TDP type A and type B brains and i"],"journal":["Journal of neuropathology and experimental neurology"],"pubmed_title":["Production and characterization of novel monoclonal antibodies against pathological human TDP-43 proteins."],"pmcid":["PMC11258413"],"funding_grant_id":["2023-JC-YB-642","GK202107018","2018SF-106","81773265","GK202007023"],"pubmed_authors":["Wang M","Simayi D","Xia H","Zheng X","Mao Q","Ma X","Yang P","He Q","Chen S","Sun X","Zhao J"],"additional_accession":[]},"is_claimable":false,"name":"Production and characterization of novel monoclonal antibodies against pathological human TDP-43 proteins.","description":"The RNA/DNA-binding protein TDP-43 plays a pivotal role in the ubiquitinated inclusions characteristic of TDP-43 proteinopathies, including most cases of frontotemporal lobar degeneration (FTLD-TDP) and Alzheimer disease (AD). To understand the mechanisms of pathological TDP-43 processing and identify potential biomarkers, we generated novel phosphorylation-independent monoclonal antibodies (MAbs) using bacteria-expressed human full-length recombinant TDP-43. Remarkably, we identified a distinctive MAb, No. 9, targeting an epitope in amino acid (aa) region 311-360 of the C-terminus. This antibody showed preferential reactivity for pathological TDP-43 inclusions, with only mild reactivity for normal nuclear TDP-43. MAb No. 9 revealed more pathology in FTLD-TDP type A and type B brains and i","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2025-04-26T22:18:18.993Z","creation":"2025-04-06T17:12:27.765Z"},"accession":"S-EPMC11258413","cross_references":{"pubmed":["38728009"],"doi":["10.1093/jnen/nlae042"]}}