The Organization of Aromatic Side Groups in an Amyloid Fibril Probed by Solid-State 2H and 19F NMR Spectroscopy-Reference-Cited by-同舟云学术

The Organization of Aromatic Side Groups in an Amyloid Fibril Probed by Solid-State 2H and 19F NMR Spectroscopy

Published:2006-06-01 Issue:25 Volume:128 Page:8098-8099
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Jack Edward¹,Newsome Matthew¹,Stockley Peter G.¹,Radford Sheena E.¹,Middleton David A.¹

Affiliation:

1. Faculty of Life Sciences, University of Manchester, P.O. Box 88, Manchester M60 1QD, United Kingdom, and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT United Kingdom

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0581898

Reference13 articles.

1. Mechanisms of amyloid fibril self-assembly and inhibition

2. Structure of the cross-β spine of amyloid-like fibrils

3. Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide

4. Role of Aromatic Interactions in Amyloid Formation by Peptides Derived from Human Amylin

5. A structural model for Alzheimer's -amyloid fibrils based on experimental constraints from solid state NMR

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