淀粉样蛋白形成蛋白/肽的相互陪伴Mutual chaperoning by amyloid forming proteins/peptides |
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课程网址: | http://videolectures.net/snc2015_zerovnik_mutual_chaperoning/ |
主讲教师: | Eva Žerovnik |
开课单位: | 约瑟夫·斯特凡研究所 |
开课时间: | 2015-10-01 |
课程语种: | 英语 |
中文简介: | 我们研究了淀粉样蛋白及其一些病理突变在细胞内形成的前纤维低聚物的蛋白质聚集和细胞毒性机制。公认的观点是,毒性最大的是6-30聚体范围内的可溶性低聚物,它们是寻找膜的,甚至会在膜上形成孔(1-2)。我将讨论改变淀粉样蛋白形成蛋白的淀粉样前构象可能作为相互伴侣,导致暂时抑制聚集和毒性的提议。将描述结晶蛋白、朊蛋白和stefin B的实例;淀粉样β(3)的所有粘合剂。还将讨论蛋白质聚集的小分子抑制剂。我们的主要模型蛋白来自胱蛋白酶抑制剂家族,stefin B将被更详细地描述。细胞对蛋白质错误折叠的反应可能会受到强烈的影响(4)。 |
课程简介: | We study the mechanisms of protein aggregation and cellular toxicity by the prefibrillar oligomers formed intracellularly by amyloidogenic proteins and some of their pathological mutants. It is an accepted view that the most toxic are soluble oligomers in range of 6 to 30 mers, that are membrane seeking and even make pores into membranes (1-2). I will discuss the proposal that changed pre-amyloidogenic conformations of amyloid forming proteins may act as mutual chaperones, leading to temporary inhibition of aggregation and toxicity. Examples will be described of crystallins, prion protein and stefin B; all binders of amyloid-beta (3). Small molecule inhibitors of protein aggregation will also be discussed. Our main model protein from the family of cystatins, stefin B will be described in more detail. It’s possible function in the cell’s response to protein mis-folding will be high-lighted (4). |
关 键 词: | 淀粉样蛋白; 蛋白质聚集; 可溶性低聚物 |
课程来源: | 视频讲座网 |
数据采集: | 2022-02-20:zkj |
最后编审: | 2022-02-23:liyy |
阅读次数: | 55 |