{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Otte CG"],"funding":["Robert Packard Center for ALS at Johns Hopkins","NIA NIH HHS","ALS Association","University of Pittsburgh Center for Protein Conformational Diseases","NINDS NIH HHS","National Institutes of Health","LiveLikeLou Center for ALS Research at the University of Pittsburgh Brain Institute","Muscular Dystrophy Association"],"pagination":["105078"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9040199"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["146"],"pubmed_abstract":["TDP-43 is a predominantly nuclear DNA/RNA binding protein that is often mislocalized into insoluble cytoplasmic inclusions in post-mortem patient tissue in a variety of neurodegenerative disorders including Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal dementia (FTD). The underlying causes of TDP-43 proteinopathies remain unclear, but recent studies indicate the formation of these protein assemblies is driven by aberrant phase transitions of RNA deficient TDP-43. Technical limitations have prevented our ability to understand how TDP-43 proteinopathy relates to disease pathogenesis. Current animal models of TDP-43 proteinopathy often rely on overexpression of wild-type TDP-43 to non-physiological levels that may initiate neurotoxicity through nuclear gain of function mechanisms, or"],"journal":["Neurobiology of disease"],"pubmed_title":["Optogenetic TDP-43 nucleation induces persistent insoluble species and progressive motor dysfunction in vivo."],"pmcid":["PMC9040199"],"funding_grant_id":["R01NS081303","R01NS105756","R21 AG064940","R21 NS100055","R01 NS105756","R21NS111768","R01 NS081303","R21NS101661","R21 NS111768","R21 NS101661","R21AG064940","R21NS100055"],"pubmed_authors":["Otte CG","Mann JR","Donnelly CJ","Pyles NJ","Gleixner AM","Ramesh N","Fortuna TR","Pandey UB"],"additional_accession":[]},"is_claimable":false,"name":"Optogenetic TDP-43 nucleation induces persistent insoluble species and progressive motor dysfunction in vivo.","description":"TDP-43 is a predominantly nuclear DNA/RNA binding protein that is often mislocalized into insoluble cytoplasmic inclusions in post-mortem patient tissue in a variety of neurodegenerative disorders including Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal dementia (FTD). The underlying causes of TDP-43 proteinopathies remain unclear, but recent studies indicate the formation of these protein assemblies is driven by aberrant phase transitions of RNA deficient TDP-43. Technical limitations have prevented our ability to understand how TDP-43 proteinopathy relates to disease pathogenesis. Current animal models of TDP-43 proteinopathy often rely on overexpression of wild-type TDP-43 to non-physiological levels that may initiate neurotoxicity through nuclear gain of function mechanisms, or","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Dec","modification":"2025-04-04T07:44:03.055Z","creation":"2025-04-04T07:44:03.055Z"},"accession":"S-EPMC9040199","cross_references":{"pubmed":["32927062"],"doi":["10.1016/j.nbd.2020.105078"]}}