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

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

Molecular cell - 19 Nov 2020

Rhine Kevin, Makurath Monika A, Liu James, Skanchy Sophie, Lopez Christian, Catalan Kevin F, Ma Ye, Fare Charlotte M, Shorter James, Ha Taekjip, Chemla Yann R, Myong Sua

Abstract excerpt

The RNA-binding protein fused in sarcoma (FUS) can form pathogenic inclusions in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD). Over 70 mutations in Fus are linked to ALS/FTLD. In patients, all Fus mutations are heterozygous, indicating that the mutant drives disease progression despite the presence of wild-type (WT) FUS. Here, we demonstrate that...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis
Share to Frontotemporal Dementia

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycine

Share to Inclusion Bodies

Share to Neuroblastoma

Share to RNA-Binding Protein FUS

Share to Tumor Cells, Cultured

Source

Open in PubMed Open full text

Identifiers

PMID: 33159856
DOI: 10.1016/j.molcel.2020.10.014
PMCID: PMC7688085

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

ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS.PMID 33159856Read ↗

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

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

ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function.Semantic proximity Read ↗

FUS-ALS mutants alter FMRP phase separation equilibrium and impair protein translation.Semantic 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 ↗

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

ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules.Semantic proximity Read ↗

Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative DiseasesSemantic proximity Read ↗

FUS-ALS mutants alter FMRP phase separation equilibrium and impair protein translationSemantic proximity Read ↗

ALS-causing hPFN1 mutants differentially disrupt LLPS of FUS prion-like domain.Semantic proximity Read ↗

Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation.Semantic proximity Read ↗

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain.Semantic proximity Read ↗

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