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

Tdp-25 Routing to Autophagy and Proteasome Ameliorates its Aggregation in Amyotrophic Lateral Sclerosis Target Cells

13 Aug 2018

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease that primarily affects motoneurons, while non-neuronal cells may contribute to disease onset and progression. Most ALS cases are characterized by the mislocalization and aggregation of the TAR DNA binding protein 43 (TDP-43) in affected cells. TDP-43 aggregates contain C-terminal TDP-43 fragments of 35 kDa (TDP-35) and 25 kDa (TDP-25) and...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis Research
Share to Parkinson's Disease Mechanisms and Treatments
Share to Prion Diseases and Protein Misfolding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 30120266
DOI: 10.1038/s41598-018-29658-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tdp-25 Routing to Autophagy and Proteasome Ameliorates its Aggregation in Amyotrophic Lateral Sclerosis Target CellsPMID 30120266Read ↗

TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: From pathomechanisms to therapeutic strategiesSemantic proximity Read ↗

Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective ResponsesSemantic proximity Read ↗

Molecular Mechanisms of TDP-43 Misfolding and Pathology in 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 ↗

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

Motor neuron-specific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis.Semantic proximity Read ↗

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

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

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

Multi-phaseted problems of TDP-43 in selective neuronal vulnerability in ALSSemantic proximity Read ↗

TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets.Semantic proximity Read ↗

Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders.Semantic proximity Read ↗

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