Discover Community Create You

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

Article

Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation.

The Journal of biological chemistry - 9 May 2008

Winton Matthew J, Igaz Lionel M, Wong Margaret M, Kwong Linda K, Trojanowski John Q, Lee Virginia M-Y

Abstract excerpt

TAR DNA-binding protein 43 (TDP-43) is the disease protein in frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U) and amyotrophic lateral sclerosis (ALS). Although normal TDP-43 is a nuclear protein, pathological TDP-43 is redistributed and sequestered as insoluble aggregates in neuronal nuclei, perikarya, and neurites. Here we recapitulate these pathological phenotypes in cultured cells...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Disease

Share to DNA-Binding Proteins

Share to Gene Expression Regulation

Share to Nuclear Localization Signals

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 18305110
DOI: 10.1074/jbc.M800342200
PMCID: PMC2442318

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation.PMID 18305110Read ↗

The role of TDP-43 mislocalization in amyotrophic lateral sclerosisSemantic proximity Read ↗

Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in miceSemantic proximity Read ↗

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

TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTDSemantic proximity Read ↗

The extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivoSemantic proximity Read ↗

Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43.Semantic proximity Read ↗

Molecular, functional, and pathological aspects of TDP-43 fragmentationSemantic proximity Read ↗

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

Nuclear import receptors are recruited by FG-nucleoporins to rescue hallmarks of TDP-43 proteinopathySemantic proximity Read ↗

Structural determinants of the cellular localization and shuttling of TDP-43Semantic proximity Read ↗

TDP-43—The key to understanding amyotrophic lateral sclerosisSemantic proximity Read ↗

The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative MechanismSemantic proximity Read ↗

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