ReviewFEMS yeast research2010
Prion amyloid structure explains templating: how proteins can be genes.
Review in FEMS yeast research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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
37 citing papers in PubMed, 67 citations in OpenAlex.
- Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- Origin of life: β-sheet amyloid conformers as the primordial functional polymers on the early Earth and their role in the emergence of complex dynamic networks.FEBS letters · 2025Review
- Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023Review
- Review
- Review
- Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.Molecular and cellular biology · 2020Article
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.Cellular and molecular life sciences : CMLS · 2018Article
- Article
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype.Journal of virology · 2015Article
- Review
- Physical and structural basis for polymorphism in amyloid fibrils.Protein science : a publication of the Protein Society · 2014Review
- Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.The Journal of biological chemistry · 2014Article
- Yeast prions help identify and define chaperone interaction networks.Current pharmaceutical biotechnology · 2014Review
- Molecular structures of amyloid and prion fibrils: consensus versus controversy.Accounts of chemical research · 2013Review
- Amyloids and yeast prion biology.Biochemistry · 2013Article
- Septin-containing barriers control the differential inheritance of cytoplasmic elements.Cell reports · 2013Article
- Viruses and prions of Saccharomyces cerevisiae.Advances in virus research · 2013Review
- Sex, prions, and plasmids in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The yeast and fungal prions determine heritable and infectious traits, and are thus genes composed of protein. Most prions are inactive forms of a normal protein as it forms a self-propagating filamentous β-sheet-rich polymer structure called amyloid. Remarkably, a single prion protein sequence can form two or more faithfully inherited prion variants, in effect alleles of these genes. What protein structure explains this protein-based inheritance? Using solid-state nuclear magnetic resonance, we showed that the infectious amyloids of the prion domains of Ure2p, Sup35p and Rnq1p have an in-register parallel architecture. This structure explains how the amyloid filament ends can template the structure of a new protein as it joins the filament. The yeast prions [PSI(+)] and [URE3] are not found in wild strains, indicating that they are a disadvantage to the cell. Moreover, the prion domains of Ure2p and Sup35p have functions unrelated to prion formation, indicating that these domains are not present for the purpose of forming prions. Indeed, prion-forming ability is not conserved, even within Saccharomyces cerevisiae, suggesting that the rare formation of prions is a disease. The prion domain sequences generally vary more rapidly in evolution than does the remainder of the molecule, producing a barrier to prion transmission, perhaps selected in evolution by this protection.
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.