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タイトル: | Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement. |
著者: | Yamaguchi, Takahiro Matsuzaki, Katsumi https://orcid.org/0000-0002-0182-1690 (unconfirmed) Hoshino, Masaru https://orcid.org/0000-0003-4099-0232 (unconfirmed) |
著者名の別形: | 星野, 大 |
キーワード: | Nuclear magnetic resonance Paramagnetic relaxation enhancement Cross seeding Amyloid fibril Dock-Lock model |
発行日: | 18-Mar-2013 |
出版者: | Elsevier BV |
誌名: | FEBS letters |
巻: | 587 |
号: | 6 |
開始ページ: | 620 |
終了ページ: | 624 |
抄録: | The most common isoforms of amyloid-β (Aβ) proteins are composed of 40 or 42 amino acid residues. While Aβ-(1-40) is the predominant species, Aβ-(1-42) is more fibrillogenic and neurotoxic, suggesting that Aβ-(1-42) plays a critical role in the initiation of amyloid fibril formation. We investigated the mechanisms by which soluble Aβ-(1-40) associates with preformed Aβ-(1-42) seeds. A paramagnetic relaxation enhancement analysis showed that the Aβ-(1-40) monomer and Aβ-(1-42) seed interact via their C-terminal region in a parallel fashion, and the N-terminal part does not to contribute to the interaction. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: A beta-(1-40) and A beta-(1-42)bind by fluorescence technology (View interaction) A beta-(1-42) and A beta-(1-40)bind by nuclear magnetic resonance (View interaction). |
著作権等: | © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
URI: | http://hdl.handle.net/2433/173120 |
DOI(出版社版): | 10.1016/j.febslet.2013.02.008 |
PubMed ID: | 23416305 |
出現コレクション: | 学術雑誌掲載論文等 |
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