Distinct microscopic mechanisms for the accelerated aggregation of pathogenic Tau mutants revealed by kinetic analysis.

Abstract excerpt

The self-assembly of Tau protein into amyloid structures is associated with Alzheimer's disease and other tauopathies. Dominant familial mutations in the Tau gene, such as P301L and P301S, increase the propensity of the Tau protein to aggregate abnormally into filaments. A quantitative description of the fibrillization process of Tau will facilitate the understanding of the cytotoxicity of Tau aggregates and...

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