Interactions between the Intrinsically Disordered Proteins β-Synuclein and α-Synuclein.
Interactions between the Intrinsically Disordered Proteins β-Synuclein and α-Synuclein.
复制标题
DOI：
10.1002/pmic.201800109
复制
发表时间：
2018-11
期刊：
影响因子：
3.4
通讯作者：
Baum J
中科院分区：
文献类型：
--
作者：
Williams JK;Yang X;Baum J
几种本质上无序的蛋白质（IDP）与神经退行性疾病中淀粉样原纤维的形成过程有关，开发抑制这些 IDP 聚集的方法对于建立针对疾病进展的有效疗法至关重要。 IDP α-突触核蛋白 (αS) 的聚集途径与多种称为突触核蛋白病的神经退行性疾病有关，并且已得到广泛表征。 β-突触核蛋白 (βS) 受到的关注较少，β-突触核蛋白 (βS) 是一种与 αS 共定位的同源 IDP，已知可以延迟 αS 原纤维的形成。在这篇综述中，我们重点关注 βS 以及 αS 和 βS 之间分子水平的相互作用，这是原纤维形成延迟的基础。我们重点介绍了开始在单体、低聚物和表面水平上定义 αS 和 βS 相互作用的研究，并表明 βS 在 αS 聚集的许多不同阶段的抑制调节中发挥作用。
Several intrinsically disordered proteins (IDPs) have been implicated in the process of amyloid fibril formation in neurodegenerative disease, and developing approaches to inhibit the aggregation of these IDPs is critical for establishing effective therapies against disease progression. The aggregation pathway of the IDP alpha-synuclein (αS), is implicated in several neurodegenerative diseases known as synucleinopathies and has been extensively characterized. Less attention has been leveraged on beta-synuclein (βS), a homologous IDP that co-localizes with αS and is known to delay αS fibril formation. In this review, we focus on βS and the molecular-level interactions between αS and βS that underlie the delay of fibril formation. We highlight studies that begin to define αS and βS interactions at the monomer, oligomer, and surface levels, and suggest that βS plays a role in regulation of inhibition at many different stages of αS aggregation.
登录
查看更多内容
影响因子：
2.9
作者：
Abeywardana, Tharindumala;Pratt, Matthew R.
通讯作者：
Pratt, Matthew R.
影响因子：
5.6
作者：
Ducas, Vanessa C.;Rhoades, Elizabeth
通讯作者：
Rhoades, Elizabeth
影响因子：
6.1
作者：
Collier, Timothy J.;Srivastava, Kinshuk R.;Paumier, Katrina L.
通讯作者：
Paumier, Katrina L.
DOI：
10.1073/pnas.1706197114
发表时间：
2017-09-26
影响因子：
11.1
作者：
Brady, Jacob P.;Farber, Patrick J.;Kay, Lewis E.
通讯作者：
Kay, Lewis E.
影响因子：
16.2
作者：
Bendor JT;Logan TP;Edwards RH
通讯作者：
Edwards RH