Detecting hidden sequence propensity for amyloid fibril formation
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Reference41 articles.
1. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid;Balbirnie;Proc. Natl. Acad. Sci.,2001
2. β2-Microglobulin amyloidosis: Insights from conservation analysis and fibril modeling by protein docking techniques;Benyamini;J. Mol. Biol.,2003
3. Convervation and amyloid formation: A study of the gelsolin-like family;Benyamini;Proteins,2003
4. Van der Waals locks: Loop-n-lock structure of globular proteins;Berezovsky;J. Mol. Biol.,2001
5. Identification of the region of non-Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity;Bodles;J. Neurochem.,2001
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