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

A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicity

19 Oct 2012

Abstract excerpt

Many neurodegenerative diseases including amyotrophic lateral sclerosis (ALS) are linked to the accumulation of specific protein aggregates in affected regions of the nervous system. SOD1, TDP-43, FUS and optineurin (OPTN) proteins were identified to form intraneuronal inclusions in ALS patients. In addition, mutations in OPTN are associated with both ALS and glaucoma. As the pathological role of OPTN in neuronal...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Amyotrophic Lateral Sclerosis Research
Share to Parkinson's Disease Mechanisms and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23078282
DOI: 10.1111/mmi.12075

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicityPMID 23078282Read ↗

A multi-omic analysis of optineurin proteinopathy in a yeast model suggests the involvement of lipid metabolism in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

Protein aggregation in amyotrophic lateral sclerosisSemantic proximity Read ↗

Optineurin deficiency disrupts phosphorylated tau proteostasis and clusterin expression in human neuronsSemantic proximity Read ↗

RNA-binding proteins with prion-like domains in ALS and FTLD-USemantic proximity Read ↗

Functional analysis of optineurin and some of its disease-associated mutants.Semantic proximity Read ↗

A novel amyotrophic lateral sclerosis mutation in OPTN induces ER stress and Golgi fragmentation in vitro.Semantic proximity Read ↗

Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregatesSemantic proximity Read ↗

Yeast reveals similar molecular mechanisms underlying alpha- and beta-synuclein toxicity.Semantic proximity Read ↗

Mistranslation and ageing unmask FUS and TDP-43 toxicity in yeast models of neurodegenerative diseasesSemantic proximity Read ↗

Fundamental roles of the Optineurin gene in the molecular pathology of Amyotrophic Lateral SclerosisSemantic proximity Read ↗

Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLSSemantic proximity Read ↗

Yeast as a Model to Unravel Mechanisms Behind FUS Toxicity in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

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