Alternative conformations of amyloidogenic proteins govern their behavior

被引：556

作者：

Kelly, JW

机构：

[1] Department of Chemistry, Texas A and M University, College Station

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1996年 / 6卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(96)80089-3

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：

Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis. In addition, newly available moderate to high resolution structural studies are bringing us closer to understanding the structure of amyloid.

引用

页码：11 / 17

页数：7

共 44 条

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