ArticleProceedings of the National Academy of Sciences of the United States of America2024
Exposed Hsp70-binding site impacts yeast Sup35 prion disaggregation and propagation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed.
- Deletion Analysis of Phase Separation, Amyloid Formation and Prion Propagation by the Intrinsically Disordered Region of Yeast Sup35 Protein.International journal of molecular sciences · 2026Article
- Coiled-coil homo-oligomerization and disaggregase Hsp104 act in parallel to stabilize orphan septins.bioRxiv : the preprint server for biology · 2026Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypes.Research square · 2025Article
- Structural polymorphism of α-synuclein fibrils alters the pathway of Hsc70-mediated disaggregation.The EMBO journal · 2025Article
- Phase Separation-Regulated Fungal Growth, Sexual Development, Adaptation and Synthetic Biology Applications.Journal of fungi (Basel, Switzerland) · 2025Review
- Cross-species rescue reveals sequence requirements for a rapidly evolving intrinsically disordered region.PLoS biology · 2025Article
- Prion-Dependent Lethality ofInternational journal of molecular sciences · 2025Article
- On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins.International journal of molecular sciences · 2025Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The dynamic balance between formation and disaggregation of amyloid fibrils is associated with many neurodegenerative diseases. Multiple chaperones interact with and disaggregate amyloid fibrils, which impacts amyloid propagation and cellular phenotypes. However, it remains poorly understood whether and how site-specific binding of chaperones to amyloids facilitates the concerted disaggregation process and modulates physiological consequences in vivo. Here, we identified binding sites of Ssa1, Sis1, and Hsp104 chaperones for Sup35, the protein determinant of yeast prion [
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Registered trials
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