Suppr超能文献

绘制朊病毒蛋白和 Sho 相互作用位点的图谱。

Mapping the interaction site of prion protein and Sho.

机构信息

Institute of Military Veterinary, Academy of Military Medical Sciences, 1068 Qinglong Road, Changchun, 130062 China.

出版信息

Mol Biol Rep. 2010 Jun;37(5):2295-300. doi: 10.1007/s11033-009-9722-0. Epub 2009 Aug 15.

Abstract

The cellular prion protein (PrP(C)) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP(C) remains unclear. Sho (Shadoo, shadow of prion protein) and PrP(C) have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61-77 and PrP(C) 108-126 domains. This indicates that Sho may play a role in the physiological function of PrP(C) and prion pathogenesis.

摘要

细胞朊病毒蛋白 (PrP(C)) 在哺乳动物中高度保守,被认为具有重要的细胞功能。然而,尽管经过了几十年的深入研究,PrP(C) 的生理功能仍然不清楚。Sho(Shadoo,朊病毒蛋白的阴影)和 PrP(C) 具有相似的 N 端,这表明这两种蛋白质具有相似的生物学功能。使用两种蛋白质的截断突变体和酵母双杂交分析,并通过共免疫沉淀和表面等离子体共振 (SPR) 进行验证,我们鉴定出 Sho 61-77 与 PrP(C) 108-126 结构域之间存在相互作用。这表明 Sho 可能在 PrP(C) 的生理功能和朊病毒发病机制中发挥作用。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验