ArticleThe Journal of biological chemistry2015
Prion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- Life at the interface: Byron Caughey's search for prion disease inhibitors through chemistry, structure, and cell physiology.Acta neuropathologica · 2026Review
- PolyProline Predictor: A web server for empirical sequence-based prediction of polyproline II helices.Protein science : a publication of the Protein Society · 2026Article
- Breaking β-sheets in FUS prion-like domain preserves phase separation and function but prevents aggregation and toxicity.bioRxiv : the preprint server for biology · 2026Article
- Refinement of the Fusion Tag PagP for Effective Formation of Inclusion Bodies in Escherichia coli.Microbiology spectrum · 2023Article
- Seed amplification and RT-QuIC assays to investigate protein seed structures and strains.Cell and tissue research · 2023Review
- Cryo-EM of prion strains from the same genotype of host identifies conformational determinants.PLoS pathogens · 2022Article
- Review
- A single amino acid residue in bank vole prion protein drives permissiveness to Nor98/atypical scrapie and the emergence of multiple strain variants.PLoS pathogens · 2022Article
- Defining the Protein Seeds of Neurodegeneration using Real-Time Quaking-Induced Conversion Assays.Biomolecules · 2020Review
- Challenges and Advances in Antemortem Diagnosis of Human Transmissible Spongiform Encephalopathies.Frontiers in bioengineering and biotechnology · 2020Review
- Review
- Characterization of mutations inNeuropsychiatric disease and treatment · 2018Review
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- PrP P102L and Nearby Lysine Mutations Promote SpontaneousJournal of virology · 2017Article
- Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.PLoS pathogens · 2017Article
- A family with hereditary cerebellar ataxia finally confirmed as Gerstmann-Straussler-Scheinker syndrome with P102L mutation in PRNP gene.Neurosciences (Riyadh, Saudi Arabia) · 2017Article
- Inactivation of Prions and Amyloid Seeds with Hypochlorous Acid.PLoS pathogens · 2016Article
- Article
- Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.Prion · 2016Article
- Quantitative, functional MRI and neurophysiological markers in a case of Gerstmann-Sträussler-Scheinker syndrome.Functional neurologyArticle
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Human prion diseases can have acquired, sporadic, or genetic origins, each of which results in the conversion of prion protein (PrP) to transmissible, pathological forms. The genetic prion disease Gerstmann-Straussler-Scheinker syndrome can arise from point mutations of prolines 102 or 105. However, the structural effects of these two prolines, and mutations thereof, on PrP misfolding are not well understood. Here, we provide evidence that individual mutations of Pro-102 or Pro-105 to noncyclic aliphatic residues such as the Gerstmann-Straussler-Scheinker-linked leucines can promote the in vitro formation of PrP amyloid with extended protease-resistant cores reminiscent of infectious prions. This effect was enhanced by additional charge-neutralizing mutations of four nearby lysine residues comprising the so-called central lysine cluster. Substitution of these proline and lysine residues accelerated PrP conversion such that spontaneous amyloid formation was no longer slower than scrapie-seeded amyloid formation. Thus, Pro-102 and Pro-105, as well as the lysines in the central lysine cluster, impede amyloid formation by PrP, implicating these residues as key structural modulators in the conversion of PrP to disease-associated types of amyloid.
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