Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments

被引：280

作者：

Barghorn, S ^{[1
]}

Mandelkow, E ^{[1
]}

机构：

[1] Max Planck Unit Struct Mol Biol, D-22607 Hamburg, Germany

来源：

BIOCHEMISTRY | 2002年 / 41卷 / 50期

关键词：

D O I：

10.1021/bi026469j

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Alzheimer's disease is characterized by aggregates of tau protein. Attempts to study the conditions for aggregation in vitro have led to different experimental systems, some of which appear mutually exclusive (e.g., oxidative vs reductive conditions, induction by polyanions vs fatty acids). We show here that different approaches and pathways can be viewed in a common framework, and that apparent differences can be explained by variations in the kinetics of subreactions. A unified view of PHF aggregation should help to analyze the causes of PHF aggregation and devise methods to prevent it.

引用

页码：14885 / 14896

页数：12

共 57 条

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