当前位置: X-MOL 学术Protein J. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Structure and Function of Alzheimer's Amyloid βeta Proteins from Monomer to Fibrils: A Mini Review.
The Protein Journal ( IF 3 ) Pub Date : 2019-07-19 , DOI: 10.1007/s10930-019-09854-3
Nikhil Agrawal 1 , Adam A Skelton 1, 2
Affiliation  

Alzheimer’s disease is the most common form of dementia, that affects millions of people worldwide. According to the widely accepted amyloid cascade hypothesis, misfolding and aggregation of Aβ peptides is the principal cause of Alzheimer’s disease. In the present mini-review, we have discussed the different structures of Aβ protein from monomer to fibrils and their arrangement in different symmetries. We have highlighted the critical amino acid residue that plays a crucial role in the early stage misfolding of Aβ monomers, Aβ fibrils arrangement in different symmetries, the elongation process and Aβ protein interaction with the membrane. We have further discussed the antibodies that are currently in clinical trial phase III for Alzheimer’s disease.

中文翻译:

从单体到原纤维的阿尔茨海默氏症淀粉样β蛋白的结构和功能:迷你综述。

阿尔茨海默氏病是痴呆症的最常见形式,它影响着全球数百万人。根据广泛接受的淀粉样蛋白级联假说,Aβ肽的错误折叠和聚集是阿尔茨海默氏病的主要原因。在本篇微型综述中,我们讨论了Aβ蛋白从单体到原纤维的不同结构及其在不同对称性中的排列。我们已经强调了关键氨基酸残基,该残基在Aβ单体的早期错误折叠,不同对称性的Aβ原纤维排列,延伸过程以及Aβ蛋白与膜的相互作用中起关键作用。我们进一步讨论了目前处于针对阿尔茨海默氏病的临床试验III期的抗体。
更新日期:2019-07-19
down
wechat
bug