ArticleFEBS letters2013
The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein.
Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Aggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils.International journal of molecular sciences · 2021Article
- The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning.International journal of molecular sciences · 2020Article
- Identification of a homology-independent linchpin domain controlling mouse and bank vole prion protein conversion.PLoS pathogens · 2020Article
- Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.Chemical science · 2019Article
- Direct Observation of Murine Prion Protein Replication in Vitro.Journal of the American Chemical Society · 2018Article
- Role of the Disulfide Bond in Prion Protein Amyloid Formation: A Thermodynamic and Kinetic Analysis.Biophysical journal · 2018Article
- Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.Scientific reports · 2015Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Recent studies revealed that elk-like S170N/N174T mutation in mouse prion protein (moPrP), which results in an increased rigidity of β2-α2 loop, leads to a prion disease in transgenic mice. Here we characterized the effect of this mutation on biophysical properties of moPrP. Despite similar thermodynamic stabilities of wild type and mutant proteins, the latter was found to have markedly higher propensity to form amyloid fibrils. Importantly, this effect was observed even under fully denaturing conditions, indicating that the increased conversion propensity of the mutant protein is not due to loop rigidity but rather results from greater amyloidogenic potential of the amino acid sequence within the loop region of S170N/N174T moPrP.
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Registered trials
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