Article

ADAR2-Mediated RNA Editing Promotes TDP-43 Nuclear Export and Alters RNA Binding

2026-06-25

Abstract excerpt

<h4>ABSTRACT</h4> <h4>BACKGROUND</h4> TAR DNA binding protein - 43 (TDP-43) nuclear loss is a pathological hallmark of amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and related neurodegenerative disorders. While the consequences of TDP-43 dysfunction have been well-characterized, the mechanisms driving TDP-43 mislocalization remain poorly understood. Previous observations of altered localiz...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: f50e022f-62f9-5aef-a6e1-be7c2247e57b
DOI: 10.64898/2026.06.22.730622

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

ADAR2-Mediated RNA Editing Promotes TDP-43 Nuclear Export and Alters RNA BindingDOI 10.64898/2026.06.22.730622Read

TDP-43 dysregulation of polyadenylation site selection is a defining feature of RNA misprocessing in ALS/FTD and related disordersSemantic proximity Read

TDP-43 dysregulation of polyadenylation site selection is a defining feature of RNA misprocessing in amyotrophic lateral sclerosis and frontotemporal dementiaSemantic proximity Read

TDP-43 directly inhibits RNA accumulation in neurites through modulation of RNA stabilitySemantic proximity Read

RNA methylation influences TDP43 binding and disease pathogenesis in models of amyotrophic lateral sclerosis and frontotemporal dementiaSemantic proximity Read

Familial ALS/FTD-associated RNA-Binding deficient TDP-43 mutants cause neuronal and synaptic transcript dysregulation <i>in vitro</i>Semantic proximity Read

Novel and known transcriptional targets of ALS/FTD protein TDP-43: Meta-analysis and interactive graphical databasesSemantic proximity Read

Familial ALS/FTD-associated RNA-binding deficient TDP-43 mutants cause neuronal and synaptic transcript dysregulation in vitroSemantic proximity Read

Comparison of parallel high-throughput RNA sequencing between knockout of TDP-43 and its overexpression reveals primarily nonreciprocal and nonoverlapping gene expression changes in the central nervous system of Drosophila.Semantic proximity Read

Major hnRNP proteins act as general TDP-43 functional modifiers both in Drosophila and human neuronal cellsSemantic proximity Read

TDP-43 nuclear loss in FTD/ALS causes widespread alternative polyadenylation changesSemantic proximity Read

Aberrant splicing in Huntington’s disease via disrupted TDP-43 activity accompanied by altered m6A RNA modificationSemantic proximity Read

TDP-43 loss induces extensive cryptic polyadenylation in ALS/FTDSemantic proximity Read