A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/22/8/453/4372006/gzp036.pdf
Reference64 articles.
1. The Role of His-18 in Amyloid Formation by Human Islet Amyloid Polypeptide
2. Characterization of the Heparin Binding Site in the N-Terminus of Human Pro-Islet Amyloid Polypeptide: Implications for Amyloid Formation
3. A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization Inhibitor
4. Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit
5. Structure of α-Helical Membrane-bound Human Islet Amyloid Polypeptide and Its Implications for Membrane-mediated Misfolding
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