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

Persistent mRNA localization defects and cell death in ALS neurons caused by transient cellular stress.

Cell reports - 7 Sept 2021

Markmiller Sebastian, Sathe Shashank, Server Kari L, Nguyen Thai B, Fulzele Amit, Cody Neal, Javaherian Ashkan, Broski Sara, Finkbeiner Steven, Bennett Eric J, Lécuyer Eric, Yeo Gene W

Abstract excerpt

Persistent cytoplasmic aggregates containing RNA binding proteins (RBPs) are central to the pathogenesis of late-onset neurodegenerative disorders such as amyotrophic lateral sclerosis (ALS). These aggregates share components, molecular mechanisms, and cellular protein quality control pathways with stress-induced RNA granules (SGs). Here, we assess the impact of stress on the global mRNA localization landscape of...

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 Cell Death

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoplasmic Granules

Share to DNA-Binding Proteins

Share to Motor Neurons

Share to Mutation

Share to RNA-Binding Proteins

Share to RNA, Messenger

Source

Open in PubMed Open full text

Identifiers

PMID: 34496257
DOI: 10.1016/j.celrep.2021.109685
PMCID: PMC11341010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Persistent mRNA localization defects and cell death in ALS neurons caused by transient cellular stress.PMID 34496257Read ↗

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 ↗

Dr. Jekyll and Mr. Hyde? Physiology and Pathology of Neuronal Stress GranulesSemantic proximity Read ↗

Stress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrumSemantic proximity Read ↗

<i>LINC00205</i> acts as a multivalent scaffold promoting FUS <sup>P525L</sup> recruitment in Amyotrophic Lateral Sclerosis stress granulesSemantic proximity Read ↗

Regulation of physiological and pathological condensates by molecular chaperonesSemantic proximity Read ↗

Stress Granules and Neurodegenerative Disorders: A Scoping ReviewSemantic proximity Read ↗

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

RNA metabolism in ALS: When normal processes become pathologicalSemantic proximity Read ↗

The Nuclear SUMO-Targeted Ubiquitin Quality Control Network Regulates the Dynamics of Cytoplasmic Stress Granules.Semantic proximity Read ↗

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

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