ReviewPrion
Prion-prion interactions.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 51 citations in OpenAlex.
- An adenine model of inborn metabolism errors alters TDP-43 aggregation and reduces its toxicity in yeast revealing insights into protein misfolding diseases.Microbial cell (Graz, Austria) · 2025Article
- Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation.PLoS genetics · 2024Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Calcium-responsive transactivator (CREST) toxicity is rescued by loss of PBP1/ATXN2 function in a novel yeast proteinopathy model and in transgenic flies.PLoS genetics · 2019Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.Scientific reports · 2017Article
- Prion-based memory of heat stress in yeast.Prion · 2017Article
- Article
- Interaction of Prions Causes Heritable Traits in Saccharomyces cerevisiae.PLoS genetics · 2016Article
- Article
- Heterologous aggregates promote de novo prion appearance via more than one mechanism.PLoS genetics · 2015Article
- Functional role of Tia1/Pub1 and Sup35 prion domains: directing protein synthesis machinery to the tubulin cytoskeleton.Molecular cell · 2014Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Article
- Review
- A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions.MicrobiologyOpen · 2013Article
- Variant-specific prion interactions: Complicating factors.Cellular logistics · 2013Article
- Prions in yeast.Genetics · 2012Review
- Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.Prion · 2012Review
- Environmental regulation of prions in yeast.PLoS pathogens · 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
2 authors at 1 institution in 1 country.
Funding
Abstract
The term prion has been used to describe self-replicating protein conformations that can convert other protein molecules of the same primary structure into its prion conformation. Several different proteins have now been found to exist as prions in Saccharomyces cerevisiae. Surprisingly, these heterologous prion proteins have a strong influence on each others' appearance and propagation, which may result from structural similarity between the prions. Both positive and negative effects of a prion on the de novo appearance of a heterologous prion have been observed in genetic studies. Other examples of reported interactions include mutual or unilateral inhibition and destabilization when two prions are present together in a single cell. In vitro work showing that one purified prion stimulates the conversion of a purified heterologous protein into a prion form, suggests that facilitation of de novo prion formation by heterologous prions in vivo is a result of a direct interaction between the prion proteins (a cross-seeding mechanism) and does not require other cellular components. However, other cellular structures, e.g., the cytoskeleton, may provide a scaffold for these interactions in vivo and chaperones can further facilitate or inhibit this process. Some negative prion-prion interactions may also occur via a direct interaction between the prion proteins. Another explanation is a competition between the prions for cellular factors involved in prion propagation or differential effects of chaperones stimulated by one prion on the heterologous prions.
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.