ArticleGenetics2003
Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.
Article in Genetics, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 61 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
61 citing papers in PubMed, 87 citations in OpenAlex.
- Transcriptomic analysis of Rnq1 loss and prionization reveals alterations in translation pathways and energy metabolism.Scientific reports · 2026Article
- Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.PLoS genetics · 2024Article
- Extracellular Vesicles-Encapsulated Yeast Prions and What They Can Tell Us about the Physical Nature of Propagons.International journal of molecular sciences · 2020Review
- Multi-scale 3D Cryo-Correlative Microscopy for Vitrified Cells.Structure (London, England : 1993) · 2020Article
- The actin cytoskeletal network plays a role in yeast prion transmission and contributes to prion stability.Molecular microbiology · 2020Article
- Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.Nature structural & molecular biology · 2020Article
- A unifying model for the propagation of prion proteins in yeast brings insight into the [PSI+] prion.PLoS computational biology · 2020Article
- Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.PloS one · 2020Article
- Article
- Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.Cell chemical biology · 2019Article
- Review
- Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Q-Rich Yeast Prion [Frontiers in molecular neuroscience · 2018Article
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
- More than just trash bins? Potential roles for extracellular vesicles in the vertical and horizontal transmission of yeast prions.Current genetics · 2016Review
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- The Yeast Prion [SWI(+)] Abolishes Multicellular Growth by Triggering Conformational Changes of Multiple Regulators Required for Flocculin Gene Expression.Cell reports · 2015Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
1 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The yeast Sup35 and Rnq1 proteins can exist in either the noninfectious soluble forms, [psi-] or [pin-], respectively, or the multiple infectious amyloid-like forms called [PSI+] or [PIN+] prion variants (or prion strains). It was previously shown that [PSI+] and [PIN+] prions enhance one another's de novo appearance. Here we show that specific prion variants of [PSI+] and [PIN+] disrupt each other's stable inheritance. Acquiring [PSI+] often impedes the inheritance of particular [PIN+] variants. Conversely, the presence of some [PIN+] variants impairs the inheritance of weak [PSI+] but not strong [PSI+] variants. These same [PIN+] variants generate a single-dot fluorescence pattern when a fusion of Rnq1 and green fluorescent protein is expressed. Another [PIN+] variant, which forms a distinctly different multiple-dot fluorescence pattern, does not impair [PSI+] inheritance. Thus, destabilization of prions by heterologous prions depends upon the variants involved. These findings may have implications for understanding interactions among other amyloid-forming proteins, including those associated with certain human diseases.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.