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

Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.

Cold Spring Harbor perspectives in medicine - 1 Sept 2017

Guo Lin, Shorter James

Abstract excerpt

Cytoplasmic TDP-43 mislocalization and aggregation is a pathological hallmark of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 is an RNA-binding protein (RBP) with a prion-like domain (PrLD) that promotes TDP-43 misfolding. PrLDs possess compositional similarity to canonical prion domains of various yeast proteins, including Sup35. Strikingly, disease-causing TDP-43 mutations reside...

Read the complete abstract on PubMed

Topics

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

Share to DNA-Binding Proteins
Share to EWSR1 gene
Share to FUS gene

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to RNA-Binding Proteins

Share to TDP-43 Proteinopathies

Source

Open in PubMed Open full text

Identifiers

PMID: 27920024
DOI: 10.1101/cshperspect.a024554
PMCID: PMC5580514

Genes

EWSR1
FUS
TAF15

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

Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.PMID 27920024Read ↗

RNA-binding proteins with prion-like domains in health and disease.Semantic proximity Read ↗

RNA-binding proteins in ALS and FTD: from pathogenic mechanisms to therapeutic insightsSemantic proximity Read ↗

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

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

RNA-binding proteins with prion-like domains in ALS and FTLD-USemantic proximity Read ↗

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

Connecting RNA-Modifying Similarities of TDP-43, FUS, and SOD1 with MicroRNA Dysregulation Amidst A Renewed Network Perspective of Amyotrophic Lateral Sclerosis Proteinopathy.Semantic proximity Read ↗

Decoding TDP-43: the molecular chameleon of neurodegenerative diseasesSemantic proximity Read ↗

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 ↗

Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseSemantic proximity Read ↗

Mutations in human prion-like domains: pathogenic but not always amyloidogenic.Semantic proximity Read ↗

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