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.

中文翻译：

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解开不良声誉：改变对淀粉样蛋白的认识

历史上，淀粉样蛋白被认为是与神经退行性疾病（包括阿尔茨海默氏病和帕金森氏病）相关的有毒/不可逆的蛋白质聚集体。最近的论文通过揭示生理淀粉样蛋白生成的广泛的细胞作用来挑战这种认识。这些发现表明，应将淀粉样蛋白折叠以及天然折叠和未折叠构型视为生理和可逆的蛋白质组织。