NMR studies of amyloid interactions-Reference-Cited by-同舟云学术

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NMR studies of amyloid interactions

Published:2024-11 Issue: Volume:144-145 Page:63-96
ISSN:0079-6565
Container-title:Progress in Nuclear Magnetic Resonance Spectroscopy
language:en
Short-container-title:Progress in Nuclear Magnetic Resonance Spectroscopy

Author:

Middleton David A.^ORCID

Publisher

Elsevier BV

Reference254 articles.

1. The amyloid state and its association with protein misfolding diseases;Knowles;Nat. Rev. Mol. Cell Biol.,2014

2. Heat of supersaturation-limited amyloid burst directly monitored by isothermal titration calorimetry;Ikenoue;Proc. Natl. Acad. Sci. U. S. A.,2014

3. Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin;Davies;J. Biol. Chem.,2015

4. Structural insights into the polymorphism of amyloid-like fibrils formed by region 20–29 of amylin revealed by solid-state NMR and X-ray fiber diffraction;Madine;J. Am. Chem. Soc.,2008

5. General principles underpinning amyloid structure;Taylor;Front. Neurosci.,2022

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