ArticlePloS one2014
Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- Homopeptide and homocodon levels across fungi are coupled to GC/AT-bias and intrinsic disorder, with unique behaviours for some amino acids.Scientific reports · 2021Article
- RNA as the stone guest of protein aggregation.Nucleic acids research · 2020Review
- Protein assembly systems in natural and synthetic biology.BMC biology · 2020Review
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- The pathophysiology of neurodegenerative disease: Disturbing the balance between phase separation and irreversible aggregation.Progress in molecular biology and translational science · 2020Review
- Evolutionary behaviour of bacterial prion-like proteins.PloS one · 2019Article
- Conservation of Prion-Like Composition and Sequence in Prion-Formers and Prion-Like Proteins ofFrontiers in molecular biosciences · 2019Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Regulation of sub-compartmental targeting and folding properties of the Prion-like protein Shadoo.Scientific reports · 2017Article
- The evolutionary scope and neurological disease linkage of yeast-prion-like proteins in humans.Biology direct · 2016Article
- Prions, amyloids, and RNA: Pieces of a puzzle.Prion · 2016Review
- Emergence and evolution of yeast prion and prion-like proteins.BMC evolutionary biology · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast. Other 'prionogenic' proteins are likely prions that have been determined experimentally to form amyloid in vivo, and to have prion-like domains that are able to propagate heritable states. Furthermore, there are over 300 additional 'prion-like' yeast proteins that have similar amino-acid composition to prions (primarily a bias for asparagines and glutamines). Here, we examine the protein functional and interaction networks that involve prion, prionogenic and prion-like proteins. Set against a marked overall preference for N/Q-rich prion-like proteins not to interact with each other, we observe a significant tendency of prion/prionogenic proteins to interact with other, N/Q-rich prion-like proteins. This tendency is mostly due to a small number of networks involving the proteins NUP100p, LSM4p and PUB1p. In general, different data analyses of functional and interaction networks converge to indicate a strong linkage of prionogenic and prion-like proteins, to stress-granule assembly and related biological processes. These results further elucidate how prions may impact gene regulation, and reveal a broader horizon for the functional relevance of N/Q-rich prion-like domains.
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