Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation-Reference-Cited by-同舟云学术

Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation

Published:2004-01-29 Issue:7 Volume:126 Page:1992-2005
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hou Liming¹,Shao Haiyan¹,Zhang Yongbo¹,Li Hua¹,Menon Nanda K.¹,Neuhaus Elizabeth B.¹,Brewer John M.¹,Byeon In-Ja L.¹,Ray Dale G.¹,Vitek Michael P.¹,Iwashita Takashi¹,Makula Ronald A.¹,Przybyla Alan B.¹,Zagorski Michael G.¹

Affiliation:

1. Contribution from the Department of Chemistry, Case Western Reserve University, Cleveland, Ohio 44106-7078, Department of Biochemistry, University of Georgia, Athens, Georgia 30602, Department of Chemistry, Chemical Instrumentation Center, The Ohio State University, Columbus, Ohio 43210, Department of Neurology, Duke University Medical Center, Durham, North Carolina 27710, and Suntory Institute of Bioorganic Research, Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 618, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja036813f

Reference80 articles.

1. Emerging β-Amyloid Therapies for the Treatment of Alzheimers Disease

2. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

3. Two-Dimensional Structure of β-Amyloid(10−35) Fibrils

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

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