ArticleScientific reports2017
Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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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.
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Who cites it
17 citing papers in PubMed.
- Combating ageing beyond the cell: Emerging roles of extracellular proteostasis.The FEBS journal · 2026Review
- Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity.Nature communications · 2025Article
- Investigating the Aggregation and Prionogenic Properties of Human Cancer-Related Proteins.Molecular and cellular biology · 2025Article
- Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.PLoS genetics · 2024Article
- Article
- Understanding the link between the actin cytoskeleton and prion biology.PLoS pathogens · 2023Article
- Article
- Article
- Biochemical Principles in Prion-Based Inheritance.Epigenomes · 2022Review
- Prions: Roles in Development and Adaptive Evolution.Journal of molecular evolution · 2020Review
- Prion Amyloid Polymorphs - The Tag Might Change It All.Frontiers in molecular biosciences · 2020Article
- The three faces of Sup35.Yeast (Chichester, England) · 2019Review
- A viral expression factor behaves as a prion.Nature communications · 2019Article
- Possible Role of Amyloid Cross-Seeding in Evolvability and Neurodegenerative Disease.Journal of Parkinson's disease · 2019Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Toxicity and infectivity: insights from de novo prion formation.Current genetics · 2018Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed. Cross-seeding, where one aggregated protein templates the misfolding of a heterologous protein, is one mechanism proposed to stimulate protein aggregation and facilitate disease pathogenesis. Here, we demonstrate the existence of cross-seeding as a crucial step in the formation of the yeast prion [PSI
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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.