De novo design of synthetic prion domains
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Summary
This work has developed a prion aggregation prediction algorithm (PAPA), specifically designed to predict prion propensity of Q/N-rich proteins, and shows not only that this algorithm is far more effective than traditional amyloid prediction algorithms at predicting prions propensity, but also that PAPA is capable of rationally designing protein domains that function as prions in vivo.
- Type
- article
- Published
- 2012-04-02
- Cited by
- 145
- References
- 45
- Access
- Open access
- OpenAlex
- https://openalex.org/W1977034658
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:17941850
Keywords
Fungal prion, Prion protein, Asparagine, Prion Proteins, Computational biology
References
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Cited by
- The natural history of yeast prions.
- Systematic mutagenesis of the mouse prion protein to identify critical regions for the efficient propagation of prions
- A bioinformatics method for identifying Q/N-rich prion-like domains in proteins.
- Amyloids or prions? That is the question
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- Life cycle of cytosolic prions
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- Heritable Remodeling of Yeast Multicellularity by an Environmentally Responsive Prion
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- Yeast Prions and Human Prion-like Proteins: Sequence Features and Prediction Methods
- Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains
- Interaction Networks of Prion, Prionogenic and Prion-Like Proteins in Budding Yeast, and Their Role in Gene Regulation
- Distinct Amino Acid Compositional Requirements for Formation and Maintenance of the [PSI+] Prion in Yeast
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- Prion proteins as memory molecules: an hypothesis.
- Prion-Like Characteristics of Polyglutamine-Containing Proteins