ArticleBiochemistry2013
Amyloids and yeast prion biology.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 57 citations in OpenAlex.
- Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025Review
- Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023Review
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Mechanisms and therapeutic potential of interactions between human amyloids and viruses.Cellular and molecular life sciences : CMLS · 2021Review
- Elucidating the regulatory mechanism of Swi1 prion in global transcription and stress responses.Scientific reports · 2020Article
- The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species.The EMBO journal · 2020Article
- Prions: Roles in Development and Adaptive Evolution.Journal of molecular evolution · 2020Review
- Anti-prion systems in yeast.The Journal of biological chemistry · 2019Review
- Tau Biology, Tauopathy, Traumatic Brain Injury, and Diagnostic Challenges.Journal of Alzheimer's disease : JAD · 2019Review
- The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.International journal of molecular sciences · 2018Review
- Mammalian amyloidogenic proteins promote prion nucleation in yeast.The Journal of biological chemistry · 2018Article
- Aβ seeds and prions: How close the fit?Prion · 2017Article
- Hsp104 disaggregase at normal levels cures many [Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation.Scientific reports · 2016Article
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Article
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- Article
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue Targeting.Frontiers in molecular biosciences · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The prions (infectious proteins) of Saccharomyces cerevisiae are proteins acting as genes, by templating their conformation from one molecule to another in analogy to DNA templating its sequence. Most yeast prions are amyloid forms of normally soluble proteins, and a single protein sequence can have any of several self-propagating forms (called prion strains or variants), analogous to the different possible alleles of a DNA gene. A central issue in prion biology is the structural basis of this conformational templating process. The in-register parallel β sheet structure found for several infectious yeast prion amyloids naturally suggests an explanation for this conformational templating. While most prions are plainly diseases, the [Het-s] prion of Podospora anserina may be a functional amyloid, with important structural implications. Yeast prions are important models for human amyloid diseases in general, particularly because new evidence is showing infectious aspects of several human amyloidoses not previously classified as prions. We also review studies of the roles of chaperones, aggregate-collecting proteins, and other cellular components using yeast that have led the way in improving the understanding of similar processes that must be operating in many human amyloidoses.
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.