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

Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases

24 Apr 2019

Abstract excerpt

Fused in sarcoma (FUS) is a DNA/RNA binding protein that is involved in RNA metabolism and DNA repair. Numerous reports have demonstrated by pathological and genetic analysis that FUS is associated with a variety of neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD), and polyglutamine diseases. Traditionally, the fibrillar aggregation of FUS was...

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 Prion Diseases and Protein Misfolding
Share to RNA Research and Splicing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 31022909
DOI: 10.3390/molecules24081622

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative DiseasesPMID 31022909Read ↗

Breaking β-sheets in FUS prion-like domain preserves phase separation and function but prevents aggregation and toxicitySemantic proximity Read ↗

The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.Semantic proximity Read ↗

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.Semantic proximity Read ↗

Modelling FUSopathies: focus on protein aggregationSemantic proximity Read ↗

The Low Complexity Domain of the FUS RNA Binding Protein Self-assembles via the Mutually Exclusive Use of Two Distinct Cross-β CoresSemantic proximity Read ↗

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

Self-assembly of FUS through its low-complexity domain contributes to neurodegeneration.Semantic proximity Read ↗

The prion-like domain of Fused in Sarcoma is phosphorylated by multiple kinases affecting liquid- and solid-phase transitions.Semantic proximity Read ↗

The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localizationSemantic proximity Read ↗

Multi-scale in silico analysis of the phase separation behavior of FUS mutants.Semantic proximity Read ↗

ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS.Semantic proximity Read ↗

Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms.Semantic proximity Read ↗

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