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- W2809533771 abstract "Significance Aggregation of amyloidogenic proteins is implicated in a number of debilitating human diseases. A mechanistic understanding of their aggregation behavior requires a quantitative description of the multistep equilibria involved in the self-assembly processes. Here we report the application of an integrative aggregation assay combining 19 F-NMR and turbidity measurements to reveal the kinetics and energetics of the human transthyretin aggregation pathway. A highly sensitive trifluoroacetyl probe enables direct observation and quantification of a weakly populated aggregation intermediate and reveals the importance of hydrophobic interactions for self-association. Extension of these studies to common pathogenic variants that are associated with early onset familial disease provides insights into the effect of the mutations on the kinetics and energetics of transthyretin aggregation." @default.
- W2809533771 created "2018-06-29" @default.
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- W2809533771 date "2018-06-18" @default.
- W2809533771 modified "2023-09-30" @default.
- W2809533771 title "Kinetic analysis of the multistep aggregation pathway of human transthyretin" @default.
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- W2809533771 doi "https://doi.org/10.1073/pnas.1807024115" @default.
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