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. 2018 Jul 20;293(36):13910–13920. doi: 10.1074/jbc.RA118.001862

Figure 7.

Figure 7.

Schematic representation of the effect of truncation on prion-like properties of αS. The N-terminal truncation of human αS changes the structure of the fibrils to a form similar to that of WT mouse αS fibrils. Furthermore, the N-terminally 10- or 30-residue–truncated human αS fibrils have lower conformational stability than WT human αS fibrils. As a result, these fibrils propagate effectively in WT mice. The C-terminally 20-residue–truncated fibrils show enhanced seeding activity in vitro, but reduced seeding activity in cell model and mouse model. There is no direct correlation between in vitro and in vivo propagation activities.