摆脱不良声誉：改变对淀粉样蛋白的认知。
Disentangling a Bad Reputation: Changing Perceptions of Amyloids.
作者信息
Wang Miling, Audas Timothy E, Lee Stephen
机构信息
Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 31336, USA; Sylvester Comprehensive Cancer Center, Miller School of Medicine, University of Miami, Miami, FL 31336, USA.
Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC V5A 1S6, Canada.
出版信息
Trends Cell Biol. 2017 Jul;27(7):465-467. doi: 10.1016/j.tcb.2017.03.001. Epub 2017 Mar 27.
Abstract
Historically, amyloids were perceived as toxic/irreversible protein aggregates associated with neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Recent papers are challenging this perception by uncovering widespread cellular roles for physiological amyloidogenesis. These findings suggest that the amyloid-fold should be considered, alongside the native-fold and unfolded configurations, as a physiological and reversible protein organization.
摘要
从历史上看，淀粉样蛋白被视为与包括阿尔茨海默病和帕金森病在内的神经退行性疾病相关的有毒/不可逆蛋白质聚集体。最近的论文通过揭示生理性淀粉样蛋白生成的广泛细胞作用，对这一观念提出了挑战。这些发现表明，淀粉样折叠应与天然折叠和未折叠构象一起，被视为一种生理性且可逆的蛋白质组织形式。
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本文引用的文献
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