Kinetics of the Interactions between Copper and Amyloid‐β with FAD Mutations and Phosphorylation at the N terminus

Abstract

Mutations and post-translational modifications of amyloid-β (Aβ) peptide in its N terminus have been shown to increase fibril formation, yet the molecular mechanism is not clear. Here we investigated the kinetics of the interactions of copper with two Aβ peptides containing Familial Alzheimer's disease (FAD) mutations (English (H6R) and Tottori (D7N)), as… (More)
DOI: 10.1002/cbic.201600255

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@inproceedings{Girvan2016KineticsOT, title={Kinetics of the Interactions between Copper and Amyloid‐β with FAD Mutations and Phosphorylation at the N terminus}, author={Paul Girvan and Toru Miyake and Xiangyu Teng and Thomas Branch and Liming Ying}, booktitle={Chembiochem : a European journal of chemical biology}, year={2016} }