Unzipping the mysteries of amyloid fiber formation

Andrew D. Miranker

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Unzipping the mysteries of amyloid fiber formation

机译：解开淀粉样纤维形成的奥秘

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Interest in the phenomenon of protein aggregation is as old as protein research. For example, changes in activity and covalent structure accompanying "coagulum" formation by insulin were important to the elucidation of the molecular origins of hormone action. In recent memory, the phenomenon of aggregation served only as an annoyance to the research biochemist and a serious economic consideration in the production and distribution of protein Pharmaceuticals. Now, however, one class of aggregate has drawn considerable interest from a range of disciplines. These aggregates are readily identified ultrastructurally by the presence of nonamorphous, filamentous structures, termed amyloid fibers.

机译：对蛋白质聚集现象的兴趣与蛋白质研究一样古老。例如，伴随着胰岛素“凝集”形成的活性和共价结构的变化对于阐明激素作用的分子起源很重要。在最近的记忆中，聚集现象仅使研究生物化学家感到烦恼，并且在蛋白质药物的生产和销售中引起了严重的经济考虑。但是，现在，一类合计已经引起了一系列学科的极大兴趣。这些聚集体很容易通过非淀粉状丝状结构（称为淀粉样纤维）的存在进行超微结构鉴定。

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《Proceedings of the National Academy of Sciences of the United States of America》 |2004年第13期|p.4335-4336|共2页
作者
Andrew D. Miranker;
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作者单位

Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, New Haven, CT 06520-8114;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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1. Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers [J] . NoorH., CaoP., RaleighD.P. Protein Science: A Publication of the Protein Society . 2012,第3期

机译：桑色素水合物抑制胰岛淀粉样蛋白多肽形成淀粉样蛋白并分解淀粉样蛋白纤维
2. pH-Controlled Formation of a Stable beta-Sheet and Amyloid-like Fibers from an Amphiphilic Peptide: The Importance of a Tailor-Made Binding Motif for Secondary Structure Formation [J] . Jana Poulami, Ehlers Martin, Zellermann Elio, Angewandte Chemie . 2016,第49期

机译：从两亲性肽的稳定的β-Sheet和淀粉样纤维的pH控制形成：量身定制的结合母题为二级结构形成的重要性。
3. pH-Controlled Formation of a Stable beta-Sheet and Amyloid-like Fibers from an Amphiphilic Peptide: The Importance of a Tailor-Made Binding Motif for Secondary Structure Formation [J] . Jana Poulami, Ehlers Martin, Zellermann Elio, Angewandte Chemie . 2016,第49期

机译：从两亲性肽的稳定的β-Sheet和淀粉样纤维的pH控制形成：量身定制的结合母题为二级结构形成的重要性。
4. Inhibition of islet amyloid polypeptide (IAPP) amyloid formation and cytotoxicity via structure-based,selective N-methylation of amide bonds of amyloid core sequences [C] . Aphrodite Kapurniotu, Anke Schmander, Konstantinos Tenidis European Peptide Symposium . 2002

机译：胰岛淀粉样蛋白形成和细胞毒性通过基于淀粉样芯序列的酰胺键的选择性N-甲基化抑制胰岛淀粉样蛋白多肽（IAPP）淀粉样蛋白形成和细胞毒性
5. Modification of amyloid fiber formation of α-synuclein and amyloid-β by small molecules [D] . Hayden, Eric Yale 2009

机译：小分子修饰α-突触核蛋白和淀粉样蛋白-β的淀粉样蛋白纤维形成
6. Unzipping the mysteries of amyloid fiber formation [O] . Andrew D. Miranker 2004

机译：解开淀粉样纤维形成的奥秘
7. Unzipping the mysteries of amyloid fiber formation [O] . Miranker, Andrew D. 2004

机译：解开淀粉样纤维形成的奥秘

Unzipping the mysteries of amyloid fiber formation

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