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

Reducing TDP-43 aggregation does not prevent its cytotoxicity.

Acta neuropathologica communications - 9 Aug 2013

Liu Rui, Yang Guang, Nonaka Takashi, Arai Tetsuaki, Jia William, Cynader Max S

Abstract excerpt

BACKGROUND: TAR DNA-binding protein 43 (TDP-43) is a protein that is involved in the pathology of Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Lobar Degeneration (FTLD). In patients with these neurodegenerative diseases, TDP-43 does not remain in its normal nuclear location, but instead forms insoluble aggregates in both the nucleus and cytoplasm of affected neurons. RESULTS: We used high density...

Read the complete abstract on PubMed

Topics

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

Share to Arsenites
Share to Cell Death
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Survival

Share to Fluorescent Antibody Technique

Share to HeLa Cells

Share to Immunoblotting

Share to In Situ Nick-End Labeling

Source

Open in PubMed Open full text

Identifiers

PMID: 24252504
DOI: 10.1186/2051-5960-1-49
PMCID: PMC3893365

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reducing TDP-43 aggregation does not prevent its cytotoxicity.PMID 24252504Read ↗

TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domainSemantic proximity Read ↗

Cellular Model of TAR DNA-binding Protein 43 (TDP-43) Aggregation Based on Its C-terminal Gln/Asn-rich RegionSemantic proximity Read ↗

Inhibition of TDP-43 aggregation by nucleic acid binding.Semantic proximity Read ↗

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

Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathySemantic proximity Read ↗

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

[TDP-43 proteinopathies, toward understanding of the molecular pathogenesis].Semantic proximity Read ↗

TDP‐43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degenerationSemantic proximity Read ↗

Overexpression of ALS-associated p.M337V human TDP-43 in mice worsens disease features compared to wild-type human TDP-43 mice.Semantic proximity Read ↗

An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity.Semantic proximity Read ↗

TDP-43 dysfunction results in R-loop accumulation and DNA replication defectsSemantic proximity Read ↗

Rational Generation of Monoclonal Antibodies and Intrabodies Selective for Pathogenic TDP-43Semantic proximity Read ↗

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