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Int. J. Mol. Sci. 2018, 19(8), 2449;

Implications of Metal Binding and Asparagine Deamidation for Amyloid Formation

Graduate School of Pharmaceutical Sciences, Suzuka University of Medical Science, Suzuka 513-8670, Japan
Department of Bio-Analytical Chemistry, Faculty of Pharmacy, Musashino University, 1-1-20 Shinmachi, Nishitokyo, Tokyo 202-8585, Japan
Author to whom correspondence should be addressed.
Received: 20 July 2018 / Revised: 10 August 2018 / Accepted: 14 August 2018 / Published: 19 August 2018
(This article belongs to the Special Issue Amyloid Fibrils and Methods for Their Study)
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Increasing evidence suggests that amyloid formation, i.e., self-assembly of proteins and the resulting conformational changes, is linked with the pathogenesis of various neurodegenerative disorders such as Alzheimer’s disease, prion diseases, and Lewy body diseases. Among the factors that accelerate or inhibit oligomerization, we focus here on two non-genetic and common characteristics of many amyloidogenic proteins: metal binding and asparagine deamidation. Both reflect the aging process and occur in most amyloidogenic proteins. All of the amyloidogenic proteins, such as Alzheimer’s β-amyloid protein, prion protein, and α-synuclein, are metal-binding proteins and are involved in the regulation of metal homeostasis. It is widely accepted that these proteins are susceptible to non-enzymatic posttranslational modifications, and many asparagine residues of these proteins are deamidated. Moreover, these two factors can combine because asparagine residues can bind metals. We review the current understanding of these two common properties and their implications in the pathogenesis of these neurodegenerative diseases. View Full-Text
Keywords: Alzheimer’s disease; oligomerization; conformation; prion disease; iron Alzheimer’s disease; oligomerization; conformation; prion disease; iron

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Sadakane, Y.; Kawahara, M. Implications of Metal Binding and Asparagine Deamidation for Amyloid Formation. Int. J. Mol. Sci. 2018, 19, 2449.

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