Defining pathways for amyloid assembly could impact therapeutic strategies for as many as 50 disease states. Here we show that amyloid assembly is subject to different forces regulating nucleation and propagation steps and provide evidence that the more global β-sheet/β-sheet facial complementarity is a critical determinant for amyloid nucleation and structural selection.

中文翻译：

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淀粉样蛋白组装中的多步构象选择

定义淀粉样蛋白组装途径可能会影响多达50种疾病状态的治疗策略。在这里，我们显示淀粉样蛋白组装受到不同的力调节成核和传播步骤，并提供证据表明，更全面的β-sheet/β-sheet面部互补性是淀粉样蛋白成核和结构选择的关键决定因素。