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

Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations.

Nucleic acids research - 1 Apr 2011

Kino Yoshihiro, Washizu Chika, Aquilanti Elisa, Okuno Misako, Kurosawa Masaru, Yamada Mizuki, Doi Hiroshi, Nukina Nobuyuki

Abstract excerpt

TLS (translocated in liposarcoma), also known as FUS (fused in sarcoma), is an RNA/DNA-binding protein that plays regulatory roles in transcription, pre-mRNA splicing and mRNA transport. Mutations in TLS are responsible for familial amyotrophic lateral sclerosis (ALS) type 6. Furthermore, TLS-containing intracellular inclusions are found in polyglutamine diseases, sporadic ALS, non-SOD1 familial ALS and a subset...

Read the complete abstract on PubMed

Topics

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

Share to Adenovirus E1A Proteins
Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Line

Share to Cytoplasmic Granules

Share to Green Fluorescent Proteins

Share to Recombinant Fusion Proteins

Share to RNA-Binding Protein FUS

Share to RNA Splicing

Source

Open in PubMed Open full text

Identifiers

PMID: 21109527
DOI: 10.1093/nar/gkq1162
PMCID: PMC3074126

Genes

FUS
SOD1

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

Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations.PMID 21109527Read ↗

Nuclear transport impairment of amyotrophic lateral sclerosis‐linked mutations in FUS/TLSSemantic proximity Read ↗

Functions of FUS/TLS From DNA Repair to Stress Response: Implications for ALSSemantic proximity Read ↗

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

Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations.Semantic proximity Read ↗

[FUS/TLS as a polyglutamine aggregate interacting protein].Semantic proximity Read ↗

A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43.Semantic proximity Read ↗

Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis.Semantic proximity Read ↗

ALS-associated mutations in FUS disrupt the axonal distribution and function of SMN.Semantic proximity Read ↗

Subcellular localization and RNAs determine FUS architecture in different cellular compartments.Semantic proximity Read ↗

Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granulesSemantic proximity Read ↗

"STRESSED OUT": The role of FUS and TDP-43 in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Autosomal dominant inheritance of rapidly progressive amyotrophic lateral sclerosis due to a truncation mutation in the fused in sarcoma (FUS) gene.Semantic proximity Read ↗

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