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Title: Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement.
Authors: Yamaguchi, Takahiro
Matsuzaki, Katsumi  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-0182-1690 (unconfirmed)
Hoshino, Masaru  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0003-4099-0232 (unconfirmed)
Author's alias: 星野, 大
Keywords: Nuclear magnetic resonance
Paramagnetic relaxation enhancement
Cross seeding
Amyloid fibril
Dock-Lock model
Issue Date: 18-Mar-2013
Publisher: Elsevier B.V.
Journal title: FEBS letters
Volume: 587
Issue: 6
Start page: 620
End page: 624
Abstract: 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).
Rights: © 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(Published Version): 10.1016/j.febslet.2013.02.008
PubMed ID: 23416305
Appears in Collections:Journal Articles

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