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功能性淀粉样蛋白——从细菌到人类

Functional amyloid--from bacteria to humans.

作者信息

Fowler Douglas M, Koulov Atanas V, Balch William E, Kelly Jeffery W

机构信息

Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

出版信息

Trends Biochem Sci. 2007 May;32(5):217-24. doi: 10.1016/j.tibs.2007.03.003. Epub 2007 Apr 6.

Abstract

Amyloid--a fibrillar, cross beta-sheet quaternary structure--was first discovered in the context of human disease and tissue damage, and was thought to always be detrimental to the host. Recent studies have identified amyloid fibers in bacteria, fungi, insects, invertebrates and humans that are functional. For example, human Pmel17 has important roles in the biosynthesis of the pigment melanin, and the factor XII protein of the hemostatic system is activated by amyloid. Functional amyloidogenesis in these systems requires tight regulation to avoid toxicity. A greater understanding of the diverse physiological applications of this fold has the potential to provide a fresh perspective for the treatment of amyloid diseases.

摘要

淀粉样蛋白——一种纤维状的交叉β-折叠四级结构——最初是在人类疾病和组织损伤的背景下被发现的,并且被认为总是对宿主有害。最近的研究已经在细菌、真菌、昆虫、无脊椎动物和人类中鉴定出了具有功能的淀粉样纤维。例如,人类的Pmel17在色素黑色素的生物合成中具有重要作用,并且止血系统中的因子XII蛋白会被淀粉样蛋白激活。这些系统中的功能性淀粉样蛋白生成需要严格调控以避免毒性。对这种折叠结构的多种生理应用有更深入的了解,有可能为淀粉样疾病的治疗提供新的视角。

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