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

关键词：

D O I：

暂无

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

共 50 条

[41] Late endocytic dysfunction as a putative cause of amyloid fibril formation in Alzheimer's disease
Yuyama, Kohei
Yanagisawa, Katsuhiko
JOURNAL OF NEUROCHEMISTRY, 2009, 109 (05) : 1250 - 1260
[42] Mechanism of interaction of Alzheimer's disease drugs with aggregates of β- amyloid peptide (Aβ 1-42)
Ramakrishnan, Latha
Bhattarai, Nirjal
Henning, Phillip P.
Rajbhandari, Labchan
Thapa, Rajan B.
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2009, 237 : 421 - 421
[43] Potential pathogenic role of β-amyloid1-42-aluminum complex in Alzheimer's disease
Drago, Denise
Bettella, Mikol
Bolognin, Silvia
Cendron, Laura
Scancar, Janez
Milacic, Radmila
Ricchelli, Fernanda
Casini, Angela
Messori, Luigi
Tognon, Giuseppe
Zatta, Paolo
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2008, 40 (04): : 731 - 746
[44] Cerebrospinal fluid β-amyloid1–42 correlates with rate of progression in Alzheimer’s disease
George S. Vlachos
George P. Paraskevas
Dimitris Naoumis
Elizabeth Kapaki
Journal of Neural Transmission, 2012, 119 : 799 - 804
[45] Plasma Levels of Amyloid β1-42 Are Independent of Neuronal Function in Alzheimer's Disease
Sedaghat, Fereshteh
Dedousi, Eleni
Costa, Vasiliki
Dimitriadis, Athanasios S.
Baloyannis, Stavros J.
JOURNAL OF ALZHEIMERS DISEASE, 2009, 17 (02) : 343 - 348
[46] Surface plasmon resonance for the analysis of β-amyloid interactions and fibril formation in 1Alzheimer's disease research
Aguilar, MI
Small, DH
NEUROTOXICITY RESEARCH, 2005, 7 (1-2) : 17 - 27
[47] Cerebrospinal fluid β-amyloid1-42 correlates with rate of progression in Alzheimer's disease
Vlachos, George S.
Paraskevas, George P.
Naoumis, Dimitris
Kapaki, Elizabeth
JOURNAL OF NEURAL TRANSMISSION, 2012, 119 (07) : 799 - 804
[48] High-resolution NMR spectroscopy of the β-amyloid(1-28) fibril typical for Alzheimer's disease
Mikros, E
Benaki, D
Humpfer, E
Spraul, M
Loukas, S
Stassinopoulou, CI
Pelecanou, M
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2001, 40 (19) : 3603 - +
[49] Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
Harper, JD
Lieber, CM
Lansbury, PT
CHEMISTRY & BIOLOGY, 1997, 4 (12): : 951 - 959
[50] Influence of Hyperglycemic Conditions on Self-Association of the Alzheimer's Amyloid β (Aβ1-42) Peptide
Menon, Sneha
Sengupta, Neelanjana
ACS OMEGA, 2017, 2 (05): : 2134 - 2147

← 1 2 3 4 5 →