Alternative conformations of amyloidogenic proteins govern their behavior
Alternative conformations of amyloidogenic proteins govern their behavior
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DOI：
10.1016/s0959-440x(96)80089-3
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发表时间：
1996-02-01
影响因子：
6.8
通讯作者：
Kelly, JW
中科院分区：
文献类型：
--
作者：
Kelly, JW
最近的出版物强烈支持淀粉样蛋白构象改变导致淀粉样纤维形成并引起疾病的假设。对几种淀粉样蛋白的生物物理研究提供了对纤维形成所需的构象变化的见解。此外，新获得的中等到高分辨率的结构研究使我们更接近于了解淀粉样蛋白的结构。
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.