ArticleProceedings of the National Academy of Sciences of the United States of America2019
A bacteria-based genetic assay detects prion formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Detection system- and strain-dependent diversity of de novo [PSI+] prion generation and phenotypes in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2025Article
- Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025Review
- The Transformation Experiment of Frederick Griffith I: Its Narrowing and Potential for the Creation of Novel Microorganisms.Bioengineering (Basel, Switzerland) · 2025Review
- The emergence of bacterial prions.PLoS pathogens · 2024Review
- Systematic analysis of nonprogrammed frameshift suppression inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- A Story Between s and S: [Het-s] Prion of the FungusMycobiology · 2024Review
- Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023Review
- Measuring prion propagation in single bacteria elucidates a mechanism of loss.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Measuring prion propagation in single bacteria elucidates mechanism of loss.bioRxiv : the preprint server for biology · 2023Article
- Microfluidics for long-term single-cell time-lapse microscopy: Advances and applications.Frontiers in bioengineering and biotechnology · 2022Review
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- Generalizable Compositional Features Influencing the Proteostatic Fates of Polar Low-Complexity Domains.International journal of molecular sciences · 2021Article
- The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements.Molecular biology and evolution · 2021Article
- Phase separation by ssDNA binding protein controlled via protein-protein and protein-DNA interactions.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Development of a single-stranded DNA-binding protein fluorescent fusion toolbox.Nucleic acids research · 2020Article
- Protein assembly systems in natural and synthetic biology.BMC biology · 2020Review
- Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes.BMC genomics · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Prions are infectious, self-propagating protein aggregates that are notorious for causing devastating neurodegenerative diseases in mammals. Recent evidence supports the existence of prions in bacteria. However, the evaluation of candidate bacterial prion-forming proteins has been hampered by the lack of genetic assays for detecting their conversion to an aggregated prion conformation. Here we describe a bacteria
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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.