ArticleProtein science : a publication of the Protein Society2021
Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Electrostatic Interactions Guide the Detrimental Effect of Oleic Acid on Monoclonal Antibody Stability.Pharmaceutical research · 2026Article
- Cosolutes Modulate Polyubiquitin Fibrillation.ACS omega · 2026Article
- A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
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Abstract
The prion protein (PrP) misfolds and oligomerizes at pH 4 in the presence of physiological salt concentrations. Low pH and salt cause structural perturbations in the monomeric prion protein that lead to misfolding and oligomerization. However, the changes in stability within different regions of the PrP prior to oligomerization are poorly understood. In this study, we have characterized the local stability in PrP at high resolution using amide temperature coefficients (T
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