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

Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae.

Eukaryotic cell - 1 Jul 2009

Choe Young-Jun, Ryu Yangkyun, Kim Hyun-Jin, Seok Yeong-Jae

Abstract excerpt

During propagation, yeast prions show a strict sequence preference that confers the specificity of prion assembly. Although propagations of [PSI(+)] and [RNQ(+)] are independent of each other, the appearance of [PSI(+)] is facilitated by the presence of [RNQ(+)]. To explain the [RNQ(+)] effect on the appearance of [PSI(+)], the cross-seeding model was suggested, in which Rnq1 aggregates act as imperfect templates...

Read the complete abstract on PubMed

Topics

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

Share to Fungal Proteins
Share to Gene Expression Regulation, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Macromolecular Substances

Share to Peptide Termination Factors

Share to Prions

Share to Protein Interaction Mapping

Share to Recombinant Fusion Proteins

Share to Up-Regulation

Source

Open in PubMed Open full text

Identifiers

PMID: 19411620
DOI: 10.1128/EC.00353-08
PMCID: PMC2708461

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

Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae.PMID 19411620Read ↗

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 ↗

Selfish prion of Rnq1 mutant in yeast.Semantic proximity Read ↗

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

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

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

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

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

The [ <i>RNQ</i> +] prion: A model of both functional and pathological amyloidSemantic proximity Read ↗

Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae.Semantic proximity Read ↗

The PNM2 mutation in the prion protein domain of SUP35 has distinct effects on different variants of the [PSI+] prion in yeast.Semantic proximity Read ↗

Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro- converted Sup35 protein.Semantic proximity Read ↗

The [PSI+] prion of yeast: a problem of inheritance.Semantic proximity Read ↗

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