朊病毒和淀粉样蛋白的蛋白酶K抗性核心。

IF 1.9 3区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Vitaly V Kushnirov, Alexander A Dergalev, Alexander I Alexandrov
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引用次数: 29

摘要

淀粉样蛋白及其传染性亚群朊病毒是结构规则的原纤维聚集体。它们是由正常状态下可溶的蛋白质形成的。在淀粉样蛋白形式中,蛋白质的全部或部分多肽序列对蛋白酶K (PK)的处理具有抗性。淀粉样蛋白可以有结构变异,这可以通过它们被PK消化的模式来区分。在这篇综述中,我们描述并比较了来自不同生物的各种淀粉样蛋白的抗性核心的研究。这些数据提供了对淀粉样蛋白及其变体的精细结构的深入了解,同时也提出了一些有趣的问题,例如关于在体外和体外获得的淀粉样蛋白之间的差异,以及淀粉样蛋白一个区域的折叠可以影响其他区域的方式。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Proteinase K resistant cores of prions and amyloids.

Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant to treatment with proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained ex vivo and in vitro, as well as the manner in which folding of one region of the amyloid can affect other regions.

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来源期刊
Prion
Prion 生物-生化与分子生物学
CiteScore
5.20
自引率
4.30%
发文量
13
审稿时长
6-12 weeks
期刊介绍: Prion is the first international peer-reviewed open access journal to focus exclusively on protein folding and misfolding, protein assembly disorders, protein-based and structural inheritance. The goal is to foster communication and rapid exchange of information through timely publication of important results using traditional as well as electronic formats. The overriding criteria for publication in Prion are originality, scientific merit and general interest.
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