ReviewPrion2015
Structure-based view on [PSI(+)] prion properties.
Review in Prion, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
11 citing papers in PubMed.
- Prion-Dependent Lethality ofInternational journal of molecular sciences · 2025Article
- Identification of New FG-Repeat Nucleoporins with Amyloid Properties.International journal of molecular sciences · 2023Article
- NOS1AP Interacts with α-Synuclein and Aggregates in Yeast and Mammalian Cells.International journal of molecular sciences · 2022Article
- The Human NUP58 Nucleoporin Can Form Amyloids In Vitro and In Vivo.Biomedicines · 2021Article
- Bioinformatics methods for identification of amyloidogenic peptides show robustness to misannotated training data.Scientific reports · 2021Article
- Design of a New [Frontiers in molecular neuroscience · 2019Article
- Article
- Quantifying Nucleation In Vivo Reveals the Physical Basis of Prion-like Phase Behavior.Molecular cell · 2018Article
- Overproduction of Sch9 leads to its aggregation and cell elongation in Saccharomyces cerevisiae.PloS one · 2018Article
- Epigenetic inheritance, prions and evolution.Journal of genetics · 2017Review
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yeast [PSI(+)] prion is one of the most suitable and well characterized system for the investigation of the prion phenomenon. However, until recently, the lack of data on the 3D arrangement of Sup35p prion fibrils hindered progress in this area. The recent arrival in this field of new experimental techniques led to the parallel and in-register superpleated β-structure as a consensus model for Sup35p fibrils. Here, we analyzed the effect of amino acid substitutions of the Sup35 protein through the prism of this structural model. Application of a newly developed computational approach, called ArchCandy, gives us a better understanding of the effect caused by mutations on the fibril forming potential of Sup35 protein. This bioinformatics tool can be used for the design of new mutations with desired modification of prion properties. Thus, we provide examples of how today, having progress toward elucidation of the structural arrangement of Sup35p fibrils, researchers can advance more efficiently to a better understanding of prion [PSI(+)] stability and propagation.
Indexed as
Identifiers
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.