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

Autophagy protects against de novo formation of the [PSI+] prion in yeast.

Molecular biology of the cell - 15 Dec 2015

Speldewinde Shaun H, Doronina Victoria A, Grant Chris M

Abstract excerpt

Prions are self-propagating, infectious proteins that underlie several neurodegenerative diseases. The molecular basis underlying their sporadic formation is poorly understood. We show that autophagy protects against de novo formation of [PSI(+)], which is the prion form of the yeast Sup35 translation termination factor. Autophagy is a cellular degradation system, and preventing autophagy by mutating its core...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy
Share to Gene Expression Regulation, Fungal
Share to Neurodegenerative Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Peptide Termination Factors

Share to Prions

Share to Saccharomyces cerevisiae Proteins

Share to Spermidine

Source

Open in PubMed Open full text

Identifiers

PMID: 26490118
DOI: 10.1091/mbc.E15-08-0548
PMCID: PMC4678013

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

Autophagy protects against de novo formation of the [PSI+] prion in yeast.PMID 26490118Read ↗

A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast.Semantic proximity Read ↗

Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.Semantic proximity Read ↗

Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Semantic proximity Read ↗

Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Semantic proximity Read ↗

Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant.Semantic proximity Read ↗

Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation.Semantic proximity Read ↗

Spreading of a Prion Domain from Cell-to-Cell by Vesicular Transport in Caenorhabditis elegansSemantic proximity Read ↗

Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion.Semantic proximity Read ↗

Biochemical and genetic methods for characterization of [PIN+] prions in yeast.Semantic proximity Read ↗

Prions affect the appearance of other prions: the story of [PIN(+)].Semantic proximity Read ↗

Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion.Semantic proximity Read ↗

Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast.Semantic proximity Read ↗

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