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

Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI+] yeast.

The Journal of biological chemistry - 6 Jul 2012

Zhao Xiaohong, Park Yang-Nim, Todor Horia, Moomau Christine, Masison Daniel, Eisenberg Evan, Greene Lois E

Abstract excerpt

Expression of huntingtin fragments with 103 glutamines (HttQ103) is toxic in yeast containing either the [PIN(+)] prion, which is the amyloid form of Rnq1, or [PSI(+)] prion, which is the amyloid form of Sup35. We find that HttQP103, which has a polyproline region at the C-terminal end of the polyQ repeat region, is significantly more toxic in [PSI(+)] yeast than in [PIN(+)], even though HttQP103 formed multiple...

Read the complete abstract on PubMed

Topics

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

Share to Glutamine
Share to Huntingtin Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Confocal

Share to Peptide Fragments

Share to Peptide Termination Factors

Share to Prions

Share to Transformation, Genetic

Share to Trinucleotide Repeat Expansion

Source

Open in PubMed Open full text

Identifiers

PMID: 22573320
DOI: 10.1074/jbc.M111.287748
PMCID: PMC3390612

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

Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI+] yeast.PMID 22573320Read ↗

[PSI(+)] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast.Semantic proximity Read ↗

Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP.Semantic proximity Read ↗

Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1.Semantic proximity Read ↗

The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants.Semantic proximity Read ↗

Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.Semantic proximity Read ↗

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

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

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

The Sup35 domains required for maintenance of weak, strong or undifferentiated yeast [PSI+] prions.Semantic proximity Read ↗

Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.Semantic proximity Read ↗

Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.Semantic proximity Read ↗

Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model.Semantic proximity Read ↗

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