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

FUS ALS neurons activate major stress pathways and reduce translation as an early protective mechanism against neurodegeneration.

Cell reports - 28 Feb 2023

Szewczyk Barbara, Günther René, Japtok Julia, Frech Moritz J, Naumann Marcel, Lee Hyun O, Hermann Andreas

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder causing progressive loss of motor neurons. Mutations in Fused in sarcoma (FUS) leading to its cytoplasmic mislocalization cause a subset of ALS. Under stress, mutant FUS localizes to stress granules (SGs)-cytoplasmic condensates composed of RNA and various proteins. Aberrant dynamics of SGs is linked to the pathology of ALS. Here, using motor...

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 Cytoplasm

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Induced Pluripotent Stem Cells

Share to Motor Neurons

Share to Mutation

Share to RNA-Binding Protein FUS

Source

Identifiers

PMID: 36696267
DOI: 10.1016/j.celrep.2023.112025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

FUS ALS neurons activate major stress pathways and reduce translation as an early protective mechanism against neurodegeneration.PMID 36696267Read ↗

ALS-associated FUS mutation reshapes the RNA and protein composition of stress granules.Semantic proximity Read ↗

ALS-associated FUS mutation reshapes the RNA and protein composition of Stress GranulesSemantic proximity Read ↗

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

Compositional analysis of ALS-linked stress granule-like structures reveals factors and cellular pathways dysregulated by mutant FUS under stressSemantic proximity Read ↗

Stress-Specific Spatiotemporal Responses of RNA-Binding Proteins in Human Stem-Cell-Derived Motor Neurons.Semantic proximity Read ↗

ALS-linked cytoplasmic FUS assemblies are compositionally different from physiological stress granules and sequester hnRNPA3, a novel modifier of FUS toxicity.Semantic proximity Read ↗

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

ALS mutant FUS proteins are recruited into stress granules in induced Pluripotent Stem Cells (iPSCs) derived motoneuronsSemantic proximity Read ↗

Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?Semantic proximity Read ↗

Establishment of In Vitro FUS-Associated Familial Amyotrophic Lateral Sclerosis Model Using Human Induced Pluripotent Stem CellsSemantic proximity Read ↗

Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons.Semantic proximity Read ↗

FUS Mislocalization and Vulnerability to DNA Damage in ALS Patients Derived hiPSCs and Aging MotoneuronsSemantic proximity Read ↗

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