ReviewPrion
Prion proteostasis: Hsp104 meets its supporting cast.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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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
37 citing papers in PubMed, 49 citations in OpenAlex.
- Heat Shock Protein 104 (Genes · 2025Article
- Design principles to tailor Hsp104 therapeutics.Cell reports · 2024Article
- Decoding chaperone complexes: Insights from NMR spectroscopy.Biophysics reviews · 2024Review
- What Can Be Learned from the Partitioning Behavior of Proteins in Aqueous Two-Phase Systems?International journal of molecular sciences · 2024Review
- Design principles to tailor Hsp104 therapeutics.bioRxiv : the preprint server for biology · 2024Article
- Prion-Like Proteins in Phase Separation and Their Link to Disease.Biomolecules · 2021Review
- Protein aggregation and the evolution of stress resistance in clinical yeast.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
- Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.PloS one · 2020Article
- AAA+ Protein-Based Technologies to Counter Neurodegenerative Disease.Biophysical journal · 2019Review
- Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain.FEMS yeast research · 2018Article
- RNA-binding proteins with prion-like domains in health and disease.The Biochemical journal · 2017Review
- Protein-Remodeling Factors As Potential Therapeutics for Neurodegenerative Disease.Frontiers in neuroscience · 2017Review
- Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease.Brain research · 2016Review
- Mechanistic Insights into Hsp104 Potentiation.The Journal of biological chemistry · 2016Article
- Repurposing Hsp104 to Antagonize Seminal Amyloid and Counter HIV Infection.Chemistry & biology · 2015Article
- Review
- Review
- Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.PloS one · 2014Article
- Reversing deleterious protein aggregation with re-engineered protein disaggregases.Cell cycle (Georgetown, Tex.) · 2014Article
- A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions.MicrobiologyOpen · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Infectious amyloid forms of the release factor, Sup35, comprise the yeast prion [PSI+]. This protein-based unit of inheritance is an evolutionary capacitor able to release cryptic genetic variation during environmental stress and generate potentially beneficial phenotypes. Genetic data have uncovered a sophisticated proteostasis network that tightly regulates [PSI+] formation, propagation and elimination. Central to this network, is the AAA+ ATPase and protein disaggregase, Hsp104. Shifting the balance of the cytosolic Hsp70:Hsp40 chaperone machinery and associated nucleotide exchange factors also influences the [PSI+] prion cycle. Yet, a precise understanding of how these systems co-operate to directly modulate the protein folding events required for sustainable Sup35 prionogenesis has remained elusive. Here, we spotlight recent advances that begin to clarify this issue. We suggest that the Hsp70:Hsp40 chaperone machinery functions collectively as a rheostat that adjusts Hsp104's basic prion-remodeling activities.
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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.