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Preserving protein function through reversible aggregation.
Nature Cell Biology ( IF 17.3 ) Pub Date : 2017-Sep-29 , DOI: 10.1038/ncb3620
Jörg Höhfeld

It is generally accepted that protein function depends on a defined 3D structure, with unfolding and aggregation dealing a final blow to functionality. A study now shows that the regulated exposure of an unstructured region in yeast pyruvate kinase triggers reversible aggregation to preserve protein function under stress.

中文翻译:

通过可逆的聚集来保持蛋白质功能。

人们普遍认为蛋白质功能取决于定义的3D结构,其展开和聚集会对功能造成最后的打击。现在的一项研究表明,酵母丙酮酸激酶中非结构化区域的受调控暴露会触发可逆聚集,从而在压力下保持蛋白质功能。
更新日期:2017-09-30
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