The N-Terminal Domain of Aβ40-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis
Author:
Affiliation:
1. The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900 Israel
2. Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, United States
Funder
United States-Israel Binational Science Foundation
Israel Science Foundation
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.1c10131
Reference40 articles.
1. Amyloid peptides and proteins in review
2. Seeded growth of -amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
3. Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy
4. Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
5. Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
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