ReviewPrion
The [RNQ+] prion: a model of both functional and pathological amyloid.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington's Disease.Angewandte Chemie (International ed. in English) · 2024Article
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
- fLPS: Fast discovery of compositional biases for the protein universe.BMC bioinformatics · 2017Article
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
- Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Molecular microbiology · 2014Article
- Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Molecular microbiology · 2014Article
- Prion strains and amyloid polymorphism influence phenotypic variation.PLoS pathogens · 2014Review
- Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.The Journal of biological chemistry · 2014Article
- Article
- Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.PLoS genetics · 2014Article
- Extracellular environment modulates the formation and propagation of particular amyloid structures.Molecular microbiology · 2014Article
- Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.Molecular microbiology · 2014Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteins.PloS one · 2013Article
- Prions in yeast.Genetics · 2012Review
- A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.The Journal of biological chemistry · 2012Article
- Article
- Microbial manipulation of the amyloid fold.Research in microbiologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
The formation of fibrillar amyloid is most often associated with protein conformational disorders such as prion diseases, Alzheimer disease and Huntington disease. Interestingly, however, an increasing number of studies suggest that amyloid structures can sometimes play a functional role in normal biology. Several proteins form self-propagating amyloids called prions in the budding yeast Saccharomyces cerevisiae. These unique elements operate by creating a reversible, epigenetic change in phenotype. While the function of the non-prion conformation of the Rnq1 protein is unclear, the prion form, [RNQ+], acts to facilitate the de novo formation of other prions to influence cellular phenotypes. The [RNQ+] prion itself does not adversely affect the growth of yeast, but the overexpression of Rnq1p can form toxic aggregated structures that are not necessarily prions. The [RNQ+] prion is also involved in dictating the aggregation and toxicity of polyglutamine proteins ectopically expressed in yeast. Thus, the [RNQ+] prion provides a tractable model that has the potential to reveal significant insight into the factors that dictate how amyloid structures are initiated and propagated in both physiological and pathological contexts.
Indexed as
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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.