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

<i>C9orf72</i> repeat expansions cause neurodegeneration in <i>Drosophila</i> through arginine-rich proteins

8 Aug 2014

Abstract excerpt

An expanded GGGGCC repeat in C9orf72 is the most common genetic cause of frontotemporal dementia and amyotrophic lateral sclerosis. A fundamental question is whether toxicity is driven by the repeat RNA itself and/or by dipeptide repeat proteins generated by repeat-associated, non-ATG translation. To address this question, we developed in vitro and in vivo models to dissect repeat RNA and dipeptide repeat protein...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis Research
Share to Genetic Neurodegenerative Diseases
Share to Nerve injury and regeneration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25103406
DOI: 10.1126/science.1256800

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

<i>C9orf72</i> repeat expansions cause neurodegeneration in <i>Drosophila</i> through arginine-rich proteinsPMID 25103406Read ↗

Sense and antisense RNA are not toxic in Drosophila models of C9orf72-associated ALS/FTDSemantic proximity Read ↗

A <i>C. elegans</i> model of <i>C9orf72</i> -associated ALS/FTD uncovers a conserved role for eIF2D in RAN translationSemantic proximity Read ↗

C9orf72 arginine-rich dipeptide proteins interact with ribosomal proteins in vivo to induce a toxic translational arrest that is rescued by eIF1ASemantic proximity Read ↗

Emerging Perspectives on Dipeptide Repeat Proteins in C9ORF72 ALS/FTDSemantic proximity Read ↗

Drosophila melanogaster As a Model Organism to Study RNA Toxicity of Repeat Expansion-Associated Neurodegenerative and Neuromuscular DiseasesSemantic proximity Read ↗

Therapeutic reduction of GGGGCC repeat RNA levels by hnRNPA3 suppresses neurodegeneration in Drosophila models of C9orf72 -linked ALS/FTDSemantic proximity Read ↗

Co-expression of C9orf72 related dipeptide-repeats over 1000 repeat units reveals age- and combination-specific phenotypic profiles in Drosophila.Semantic proximity Read ↗

Glycine-alanine dipeptide repeat protein contributes to toxicity in a zebrafish model of C9orf72 associated neurodegenerationSemantic proximity Read ↗

CRISPR-Cas9 screens in human cells and primary neurons identify modifiers of <i>C9orf72</i> dipeptide repeat protein toxicitySemantic proximity Read ↗

Reactivation of nonsense-mediated mRNA decay protects against C9orf72 dipeptide-repeat neurotoxicitySemantic proximity Read ↗

The Role of Dipeptide Repeats in C9ORF72-Related ALS-FTDSemantic proximity Read ↗

CRISPR/Cas9-Mediated Excision of ALS/FTD-Causing Hexanucleotide Repeat Expansion in <i>C9ORF72</i> rescues major disease mechanisms <i>in vivo</i> and <i>in vitro</i>Semantic proximity Read ↗

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