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淀粉样蛋白的不同构象决定了它们的行为。

Alternative conformations of amyloidogenic proteins govern their behavior.

作者信息

Kelly J W

机构信息

Department of Chemistry, Texas A&M University, College Station 77843-3255, USA.

出版信息

Curr Opin Struct Biol. 1996 Feb;6(1):11-7. doi: 10.1016/s0959-440x(96)80089-3.

DOI:10.1016/s0959-440x(96)80089-3
PMID:8696966
Abstract

Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis. In addition, newly available moderate to high resolution structural studies are bringing us closer to understanding the structure of amyloid.

摘要

近期的出版物有力地支持了这样一种假说，即淀粉样蛋白的构象变化会导致淀粉样纤维的形成并引发疾病。对几种淀粉样蛋白的生物物理研究为纤维形成所需的构象变化提供了见解。此外，新获得的中等至高分辨率结构研究使我们更接近了解淀粉样蛋白的结构。

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Alternative conformations of amyloidogenic proteins govern their behavior.淀粉样蛋白的不同构象决定了它们的行为。
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