C-terminal frameshift variant of TDP-43 with pronounced aggregation-propensity causes rimmed vacuole myopathy but not ALS/FTD.

doi:10.1007/s00401-023-02565-1

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Community

Back to search

Article

C-terminal frameshift variant of TDP-43 with pronounced aggregation-propensity causes rimmed vacuole myopathy but not ALS/FTD.

Acta neuropathologica - 1 Jun 2023

Ervilha Pereira Pedro, Schuermans Nika, Meylemans Antoon, LeBlanc Pontus, Versluys Lauren, Copley Katie E, Rubien Jack D, Altheimer Christopher, Peetermans Myra, Debackere Elke, Vanakker Olivier, Janssens Sandra, Baets Jonathan, Verhoeven Kristof, Lammens Martin, Symoens Sofie, De Paepe Boel, Barmada Sami J, Shorter James, De Bleecker Jan L, Bogaert Elke, Dermaut Bart

Abstract excerpt

Neuronal TDP-43-positive inclusions are neuropathological hallmark lesions in frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). Pathogenic missense variants in TARDBP, the gene encoding TDP-43, can cause ALS and cluster in the C-terminal prion-like domain (PrLD), where they modulate the liquid condensation and aggregation properties of the protein. TDP-43-positive inclusions are also found in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Distal Myopathies

Share to DNA-Binding Proteins

Share to Frameshift Mutation

Share to Frontotemporal Dementia

Share to Mutation

Share to Pick Disease of the Brain

Share to Rats

Source

Open in PubMed Open full text

Identifiers

PMID: 37000196
DOI: 10.1007/s00401-023-02565-1
PMCID: PMC10175433

Genes

TARDBP
NEB
TTN

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

C-terminal frameshift variant of TDP-43 with pronounced aggregation-propensity causes rimmed vacuole myopathy but not ALS/FTD.PMID 37000196Read ↗

The new missense G376V-TDP-43 variant induces late-onset distal myopathy but not amyotrophic lateral sclerosisSemantic proximity Read ↗

Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLDSemantic proximity Read ↗

RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathySemantic proximity Read ↗

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

Phase to Phase with TDP-43.Semantic proximity Read ↗

A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicitySemantic proximity Read ↗

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.Semantic proximity Read ↗

Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.Semantic proximity Read ↗

Cell environment shapes TDP-43 function with implications in neuronal and muscle diseaseSemantic proximity Read ↗

Amyotrophic lateral sclerosis caused by TARDBP mutations: from genetics to TDP-43 proteinopathy.Semantic proximity Read ↗

Role and therapeutic potential of liquid-liquid phase separation in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Role of RNA Binding Proteins with prion-like domains in muscle and neuromuscular diseasesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.