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

The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity.

Nature communications - 29 Jan 2015

Li Quan, Yokoshi Moe, Okada Hitomi, Kawahara Yukio

Abstract excerpt

TAR DNA-binding protein of 43 kDa (TDP-43) and its C-terminal fragment of 25 kDa (CTF25) play critical roles in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Although the overexpression of TDP-43 in cultured cells and animals results in the production of CTF25, the cleavage...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Cell Death
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Peptides

Share to Protein Aggregates

Share to Proteolysis

Share to Solubility

Source

Identifiers

PMID: 25630387
DOI: 10.1038/ncomms7183

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25630387-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity.PMID 25630387Read ↗

Proteolytic processing of TAR DNA binding protein‐43 by caspases produces C‐terminal fragments with disease defining properties independent of progranulinSemantic proximity Read ↗

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

Truncation of the TAR DNA-binding protein 43 is not a prerequisite for cytoplasmic relocalization, and is suppressed by caspase inhibition and by introduction of the A90V sequence variant.Semantic proximity Read ↗

A novel mutation in the cleavage site N291 of TDP-43 protein in a familial case of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Asparaginyl endopeptidase cleaves TDP‐43 in brainSemantic 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 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: From pathomechanisms to therapeutic strategiesSemantic proximity Read ↗

TARDBP mutation analysis in TDP-43 proteinopathies and deciphering the toxicity of mutant TDP-43.Semantic proximity Read ↗

Tdp-25 Routing to Autophagy and Proteasome Ameliorates its Aggregation in Amyotrophic Lateral Sclerosis Target CellsSemantic proximity Read ↗

Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins.Semantic proximity Read ↗

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

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

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