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- W2787658511 abstract "Amyloid fibrils are filamentous protein aggregates associated with the pathogenesis of a wide variety of human diseases. The formation of such aggregates typically follows nucleation-dependent kinetics, wherein the assembly and structural conversion of amyloidogenic proteins into oligomeric aggregates (nuclei) is the rate-limiting step of the overall reaction. In this study, we sought to gain structural insights into the oligomeric nuclei of the human prion protein (PrP) by preparing a series of deletion mutants lacking 14-44 of the C-terminal 107 residues of PrP and examined the kinetics and thermodynamics of these mutants in amyloid formation. An analysis of the experimental data using the concepts of the Φ-value analysis indicated that the helix 2 region (residues 168-196) acquires an amyloid-like β-sheet during nucleation, whereas the other regions preserves a relatively disordered structure in the nuclei. This finding suggests that the helix 2 region serves as the nucleation site for the assembly of amyloid fibrils.-Honda, R., Kuwata, K. Evidence for a central role of PrP helix 2 in the nucleation of amyloid fibrils." @default.
- W2787658511 created "2018-02-23" @default.
- W2787658511 creator A5016857780 @default.
- W2787658511 creator A5047328722 @default.
- W2787658511 date "2018-02-01" @default.
- W2787658511 modified "2023-09-24" @default.
- W2787658511 title "Evidence for a central role of PrP helix 2 in the nucleation of amyloid fibrils" @default.
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- W2787658511 doi "https://doi.org/10.1096/fj.201701183rr" @default.
- W2787658511 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29401635" @default.
- W2787658511 hasPublicationYear "2018" @default.
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