Structural Variations in the Cross-β Core of Amyloid β Fibrils Revealed by Deep UV Resonance Raman Spectroscopy-Reference-Cited by-同舟云学术

Structural Variations in the Cross-β Core of Amyloid β Fibrils Revealed by Deep UV Resonance Raman Spectroscopy

Published:2010-04-20 Issue:18 Volume:132 Page:6324-6328
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Popova Ludmila A.¹,Kodali Ravindra¹,Wetzel Ronald¹,Lednev Igor K.¹

Affiliation:

1. Department of Chemistry University at Albany, SUNY, 1400 Washington Avenue, Albany, New York 12222, and Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15260

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja909074j

Reference37 articles.

1. Protein misfolding, evolution and disease

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4. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta -sheets in Alzheimer's beta -amyloid fibrils

5. Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling

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