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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D O I：

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中图分类号：

学科分类号：

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.

引用

页码：499 / 505

页数：6

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