Structural Polymorphs Suggest Competing Pathways for the Formation of Amyloid Fibrils That Diverge from a Common Intermediate Species
Author:
Affiliation:
1. Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1396, United States
2. Department of Chemistry, University of California-Irvine, Irvine, California 92697-2025, United States
Funder
Division of Chemistry
National Institute of Diabetes and Digestive and Kidney Diseases
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00997
Reference80 articles.
1. Amyloid Fiber Formation and Membrane Disruption are Separate Processes Localized in Two Distinct Regions of IAPP, the Type-2-Diabetes-Related Peptide
2. Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective
3. Protein Misfolding, Functional Amyloid, and Human Disease
4. Effect of Different Salt Ions on the Propensity of Aggregation and on the Structure of Alzheimer’s Aβ(1-40) Amyloid Fibrils
5. Aβ(1–40) Forms Five Distinct Amyloid Structures whose β-Sheet Contents and Fibril Stabilities Are Correlated
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