ArticleNature communications2014
Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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.
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.
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Who cites it
32 citing papers in PubMed.
- Study of blood linear RNA nominates CD55 and DLD as early-stage biomarkers for Parkinson's disease.Brain : a journal of neurology · 2026Article
- Size of Biomolecular Condensates Dictates Fate in Liquid-Solid Phase Transitions through Amorphous-Amyloid Competition.Journal of the American Chemical Society · 2026Article
- Biofilm-Associated Amyloid Proteins Linked with the Progression of Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- The middle domain of Hsp104 can ensure substrates are functional after processing.PLoS genetics · 2024Article
- Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024Article
- Concentration and time-dependent amyloidogenic characteristics of intrinsically disordered N-terminal region ofFrontiers in microbiology · 2023Article
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Article
- Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.Genetics · 2021Article
- Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets.iScience · 2021Article
- Review
- The Amphipathic GM1 Molecule Stabilizes Amyloid Aggregates, Preventing their Cytotoxicity.Biophysical journal · 2020Article
- Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.Nature structural & molecular biology · 2020Article
- Nonsense Mutations in the YeastInternational journal of molecular sciences · 2020Article
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
- 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
- The three faces of Sup35.Yeast (Chichester, England) · 2019Review
- Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants.International journal of molecular sciences · 2019Article
- NAA10-related syndrome.Experimental & molecular medicine · 2018Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The self-assembly of alternative conformations of normal proteins into amyloid aggregates has been implicated in both the acquisition of new functions and in the appearance and progression of disease. However, while these amyloidogenic pathways are linked to the emergence of new phenotypes, numerous studies have uncoupled the accumulation of aggregates from their biological consequences, revealing currently underappreciated complexity in the determination of these traits. Here, to explore the molecular basis of protein-only phenotypes, we focused on the Saccharomyces cerevisiae Sup35/[PSI(+)] prion, which confers a translation termination defect and expression level-dependent toxicity in its amyloid form. Our studies reveal that aggregated Sup35 retains its normal function as a translation release factor. However, fluctuations in the composition and size of these complexes specifically alter the level of this aggregate-associated activity and thereby the severity and toxicity of the amyloid state. Thus, amyloid heterogeneity is a crucial contributor to protein-only phenotypes.
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