The interactions that shape amyloid fibrils in disease

被引：0
|
作者：
Joachimiak, Lukasz A. [1 ]
机构：
[1] Univ Texas Southwestern Med Ctr, Peter ODonnell Jr Brain Inst, Dept Biochem, Ctr Alzheimers & Neurodegenerat Dis, Dallas, TX 75390 USA
来源：
STRUCTURE | 2022年 / 30卷 / 08期
关键词：
D O I：
10.1016/j.str.2022.07.003
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：
In this issue of Structure, van der Kant and colleagues use a computational approach to uncover what dictates assembly of proteins into amyloid fibrils. Structurally distinct amyloids have about 30% of their residues predisposed to cross-beta conformation, while less favorable regions may be the source of polymorphism by interacting with stabilizing cofactors.
引用
收藏
页码：1045 / 1047
页数：4
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