Structure and function of amyloid in Alzheimer's disease

被引：124

作者：

Morgan, C

Colombres, M

Nuñez, MT

Inestrosa, NC

机构：

[1] Pontificia Univ Catolica Chile, Fac Ciencias Biol, Ctr FONDAP Regulac Celular & Patol Joaquin V Luco, Santiago, Chile

[2] Univ Chile, Inst Nutr & Tecnol Alimentos, Lab Bioinformat & Expres Gen, Santiago, Chile

[3] Univ Chile, Fac Ciencias, Inst Milenio CBB, Dept Biol,Lab Hierro & Biol Envejecimiento, Santiago, Chile

来源：

PROGRESS IN NEUROBIOLOGY | 2004年 / 74卷 / 06期

关键词：

D O I：

10.1016/j.pneurobio.2004.10.004

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

This review is focused on the structure and function of Alzheimer's amyloid deposits. Amyloid formation is a process in which normal well-folded cellular proteins undergo a self-assembly process that leads to the formation of large and ordered protein structures. Amyloid deposition, oligomerization, and higher order polymerization, and the structure adopted by these assemblies. as well as their functional relationship with cell biology are underscored. Numerous efforts have been directed to elucidate these issues and their relation with senile dementia. Significant advances made in the last decade in amyloid structure, dynamics and cell biology are summarized and discussed. The mechanism of amyloid neurotoxicity is discussed with emphasis on the Wnt signaling pathway. This review is focused on Alzheimer's amyloid fibrils in general and has been divided into two parts dealing with the structure and function of amyloid. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：323 / 349

页数：27

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