Observation of β-Amyloid Peptide Oligomerization by Pressure-Jump NMR Spectroscopy
Author:
Affiliation:
1. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, United States
Funder
National Institute of Diabetes and Digestive and Kidney Diseases
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.9b06970
Reference29 articles.
1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
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4. Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils
5. Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
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