Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

被引：0
|
作者：
Yiling Xiao
Buyong Ma
Dan McElheny
Sudhakar Parthasarathy
Fei Long
Minako Hoshi
Ruth Nussinov
Yoshitaka Ishii
机构：
[1] University of Illinois at Chicago,Department of Chemistry
[2] Cancer and Inflammation Program,Department of Anatomy and Developmental Biology
[3] Leidos Biomedical Research,Department of Human Genetics and Molecular Medicine
[4] National Cancer Institute at Frederick,undefined
[5] Institute of Biomedical Research and Innovation,undefined
[6] Graduate School of Medicine,undefined
[7] Kyoto University,undefined
[8] Sackler Institute of Molecular Medicine,undefined
[9] Sackler School of Medicine,undefined
[10] Tel Aviv University,undefined
[11] Center for Structural Biology,undefined
[12] University of Illinois at Chicago,undefined
来源：
Nature Structural & Molecular Biology | 2015年 / 22卷
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摘要：
Aβ(1–42) is the most pathogenic amyloid-β species in Alzheimer's disease (AD). The solid-state NMR–based atomic model of an Aβ(1–42) fibril elucidates the mechanism of fibril formation and propagation in AD and other amyloid diseases.
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页码：499 / 505
页数：6
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