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

Drosha-dependent microRNAs modulate FUS-mediated neurodegeneration in vivo.

Nucleic acids research - 10 Nov 2023

Kour Sukhleen, Fortuna Tyler, Anderson Eric N, Mawrie Darilang, Bilstein Jessica, Sivasubramanian Ramakrishnan, Ward Caroline, Roy Rishit, Rajasundaram Dhivyaa, Sterneckert Jared, Pandey Udai Bhan

Abstract excerpt

Mutations in the Fused in Sarcoma (FUS) gene cause the familial and progressive form of amyotrophic lateral sclerosis (ALS). FUS is a nuclear RNA-binding protein involved in RNA processing and the biogenesis of a specific set of microRNAs. Here we report that Drosha and two previously uncharacterized Drosha-dependent miRNAs are strong modulators of FUS expression and prevent the cytoplasmic segregation 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 Drosophila

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drosophila Proteins

Share to MicroRNAs

Share to Neurodegenerative Diseases

Share to Neurons

Share to Ribonuclease III

Share to RNA-Binding Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 37791873
DOI: 10.1093/nar/gkad774
PMCID: PMC10639082

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

Drosha-dependent microRNAs modulate FUS-mediated neurodegeneration in vivo.PMID 37791873Read ↗

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

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

RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutationsSemantic 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 ↗

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

Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms.Semantic proximity Read ↗

FUS is sequestered in nuclear aggregates in ALS patient fibroblastsSemantic proximity Read ↗

FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination.Semantic proximity Read ↗

Expression of human FUS protein in Drosophila leads to progressive neurodegeneration.Semantic proximity Read ↗

Antiviral Immune Response as a Trigger of FUS Proteinopathy in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

ALS-linked FUS mutants affect the localization of U7 snRNP and replication-dependent histone gene expression in human cells.Semantic proximity Read ↗

Loss of fused in sarcoma (FUS) promotes pathological Tau splicing.Semantic proximity Read ↗

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