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

Mislocated FUS is sufficient for gain-of-toxic-function amyotrophic lateral sclerosis phenotypes in mice.

Brain : a journal of neurology - 1 Sept 2016

Shiihashi Gen, Ito Daisuke, Yagi Takuya, Nihei Yoshihiro, Ebine Taeko, Suzuki Norihiro

Abstract excerpt

Mutations in RNA-binding proteins, including fused in sarcoma (FUS) and TAR DNA-binding protein 43 (TDP-43, encoded by TARDBP), are associated with sporadic and familial amyotrophic lateral sclerosis. A major question is whether neuronal loss is caused by toxic gain-of-function cytoplasmic aggregates or loss of nuclear RNA-binding protein function. We generated a transgenic mouse overexpressing exogenous FUS...

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 Behavior, Animal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disease Progression

Share to Mice, Inbred C57BL

Share to Mice, Transgenic

Share to Motor Activity

Share to Nuclear Localization Signals

Share to RNA-Binding Protein FUS

Source

Identifiers

PMID: 27368346
DOI: 10.1093/brain/aww161

Genes

FUS
TARDBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mislocated FUS is sufficient for gain-of-toxic-function amyotrophic lateral sclerosis phenotypes in mice.PMID 27368346Read ↗

Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice.Semantic proximity Read ↗

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

Toxic gain of function from mutant FUS protein is crucial to trigger cell autonomous motor neuron loss.Semantic proximity Read ↗

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

FUS/TLS deficiency causes behavioral and pathological abnormalities distinct from amyotrophic lateral sclerosis.Semantic proximity Read ↗

Extensive splicing changes in an ALS/FTD transgenic mouse model overexpressing cytoplasmic fused in sarcoma.Semantic proximity Read ↗

Importance of Functional Loss of FUS in FTLD/ALSSemantic proximity Read ↗

Pathogenesis of FUS-associated ALS and FTD: insights from rodent modelsSemantic proximity Read ↗

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

Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashionSemantic proximity Read ↗

Expression of Fused in sarcoma mutations in mice recapitulates the neuropathology of FUS proteinopathies and provides insight into disease pathogenesis.Semantic proximity Read ↗

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

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