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- W4306757331 endingPage "167859" @default.
- W4306757331 startingPage "167859" @default.
- W4306757331 abstract "Fibrillar aggregates of the α-synuclein (αS) protein are the hallmark of Parkinson's Disease and related neurodegenerative disorders. Characterization of the effects of mutations and post-translational modifications (PTMs) on the αS aggregation rate can provide insight into the mechanism of fibril formation, which remains elusive in spite of intense study. A comprehensive collection (375 examples) of mutant and PTM aggregation rate data measured using the fluorescent probe thioflavin T is presented, as well as a summary of the effects of fluorescent labeling on αS aggregation (20 examples). A curated set of 131 single mutant de novo aggregation experiments are normalized to wild type controls and analyzed in terms of structural data for the monomer and fibrillar forms of αS. These tabulated data serve as a resource to the community to help in interpretation of aggregation experiments and to potentially be used as inputs for computational models of aggregation." @default.
- W4306757331 created "2022-10-19" @default.
- W4306757331 creator A5001939171 @default.
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- W4306757331 creator A5028662408 @default.
- W4306757331 creator A5072512563 @default.
- W4306757331 date "2022-12-01" @default.
- W4306757331 modified "2023-10-09" @default.
- W4306757331 title "Effects of Mutations and Post-Translational Modifications on α-Synuclein In Vitro Aggregation" @default.
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