Alternative Pathways of Human Islet Amyloid Polypeptide Aggregation Distinguished by 19F Nuclear Magnetic Resonance-Detected Kinetics of Monomer Consumption
Author:
Affiliation:
1. Department of Chemistry, ‡Department of Biological Chemistry, and §Department of Biophysics, University of Michigan, Ann Arbor, Michigan 48109, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi3012548
Reference80 articles.
1. Protein Misfolding, Functional Amyloid, and Human Disease
2. Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR
3. Recent atomic models of amyloid fibril structure
4. Solid-State NMR Studies of Amyloid Fibril Structure
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