ArticleChemistry & biology2012
Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)].
Article in Chemistry & biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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
33 citing papers in PubMed, 44 citations in OpenAlex.
- Design principles to tailor Hsp104 therapeutics.Cell reports · 2024Article
- The middle domain of Hsp104 can ensure substrates are functional after processing.PLoS genetics · 2024Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system.Nature chemical biology · 2022Article
- The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021Review
- Article
- RNA-binding and prion domains: the Yin and Yang of phase separation.Nucleic acids research · 2020Article
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019Review
- Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma.The Journal of biological chemistry · 2019Article
- Entropic constraints on the steady-state fitness of competing self-replicators.The Journal of chemical physics · 2018Article
- Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance.Molecular and cellular biology · 2018Article
- Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain.FEMS yeast research · 2018Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Amyloid assembly and disassembly.Journal of cell science · 2018Review
- Designer protein disaggregases to counter neurodegenerative disease.Current opinion in genetics & development · 2017Review
- RNA-binding proteins with prion-like domains in health and disease.The Biochemical journal · 2017Review
- Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Journal of molecular biology · 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
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Structurally distinct, self-templating prion "strains" can encode distinct phenotypes and amplify at different rates depending upon the environment. Indeed, prion strain ensembles can evolve in response to environmental challenges, which makes them highly challenging drug targets. It is not understood how the proteostasis network amplifies one prion strain at the expense of another. Here, we demonstrate that Hsp104 remodels the distinct intermolecular contacts of different synthetic Sup35 prion strains in a way that selectively amplifies prions encoding strong [PSI(+)] and simultaneously eliminates prions encoding weak [PSI(+)]. Hsp104 has reduced ability to fragment prions encoding weak [PSI(+)], but readily converts them to nontemplating forms. By contrast, Hsp104 readily fragments prions encoding strong [PSI(+)], but has reduced ability to eliminate their infectivity. Thus, we illuminate direct mechanisms underpinning how the proteostasis network can drive prion strain selection.
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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.