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Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy
http://hdl.handle.net/2297/25776
http://hdl.handle.net/2297/25776caeac462-3971-4100-84f9-48db6be8b1ee
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
SC-PR-ANDO-T-13240.pdf (408.7 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-10-03 | |||||
| タイトル | ||||||
| タイトル | Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
Milhiet, Pierre-Emmanuel
× Milhiet, Pierre-Emmanuel× Yamamoto, Daisuke× Berthoumieu, Olivia× Dosset, Patrice× Grimellec, Christian Le× Verdier, Jean-Michel× Marchal, Stéphane× Ando, Toshio |
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| 提供者所属 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 金沢大学理工研究域数物科学系 | |||||
| 書誌情報 |
PLoS ONE 巻 5, 号 10, p. e13240, 発行日 2010-01-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 1932-6203 | |||||
| DOI | ||||||
| 関連タイプ | isIdenticalTo | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1371/journal.pone.0013240 | |||||
| 出版者 | ||||||
| 出版者 | Public Library of Science | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Formation of fibrillar structures of proteins that deposit into aggregates has been suggested to play a key role in various neurodegenerative diseases. However mechanisms and dynamics of fibrillization remains to be elucidated. We have previously established that lithostathine, a protein overexpressed in the pre-clinical stages of Alzheimer's disease and present in the pathognomonic lesions associated with this disease, form fibrillar aggregates after its N-terminal truncation. In this paper we visualized, using high-speed atomic force microscopy (HS-AFM), growth and assembly of lithostathine protofibrils under physiological conditions with a time resolution of one image/s. Real-time imaging highlighted a very high velocity of elongation. Formation of fibrils via protofibril lateral association and stacking was also monitored revealing a zipper-like mechanism of association. We also demonstrate that, like other amyloid ß peptides, two lithostathine protofibrils can associate to form helical fibrils. Another striking finding is the propensity of the end of a growing protofibril or fibril to associate with the edge of a second fibril, forming false branching point. Taken together this study provides new clues about fibrillization mechanism of amyloid proteins. © 2010 Milhiet et al. | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
