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| ファイル | 記述 | サイズ | フォーマット | |
|---|---|---|---|---|
| ijms18112271.pdf | 2.19 MB | Adobe PDF | 見る/開く |
完全メタデータレコード
| DCフィールド | 値 | 言語 |
|---|---|---|
| dc.contributor.author | Iwakawa, Naoto | en |
| dc.contributor.author | Morimoto, Daichi | en |
| dc.contributor.author | Walinda, Erik | en |
| dc.contributor.author | Kawata, Yasushi | en |
| dc.contributor.author | Shirakawa, Masahiro | en |
| dc.contributor.author | Sugase, Kenji | en |
| dc.contributor.alternative | 岩川, 直都 | ja |
| dc.contributor.alternative | 森本, 大智 | ja |
| dc.contributor.alternative | 白川, 昌宏 | ja |
| dc.contributor.alternative | 菅瀬, 謙治 | ja |
| dc.date.accessioned | 2018-08-21T04:47:04Z | - |
| dc.date.available | 2018-08-21T04:47:04Z | - |
| dc.date.issued | 2017-10-28 | - |
| dc.identifier.issn | 1661-6596 | - |
| dc.identifier.uri | http://hdl.handle.net/2433/233929 | - |
| dc.description.abstract | Amyloid fibril formation is associated with numerous neurodegenerative diseases. To elucidate the mechanism of fibril formation, the thioflavin T (ThT) fluorescence assay is widely used. ThT is a fluorescent dye that selectively binds to amyloid fibrils and exhibits fluorescence enhancement, which enables quantitative analysis of the fibril formation process. However, the detailed binding mechanism has remained unclear. Here we acquire real-time profiles of fibril formation of superoxide dismutase 1 (SOD1) using high-sensitivity Rheo-NMR spectroscopy and detect weak and strong interactions between ThT and SOD1 fibrils in a time-dependent manner. Real-time information on the interaction between ThT and fibrils will contribute to the understanding of the binding mechanism of ThT to fibrils. In addition, our method provides an alternative way to analyze fibril formation. | en |
| dc.format.mimetype | application/pdf | - |
| dc.language.iso | eng | - |
| dc.publisher | MDPI AG | en |
| dc.rights | © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0). | en |
| dc.subject | amyloid fibrils | en |
| dc.subject | thioflavin T | en |
| dc.subject | molecular interactions | en |
| dc.subject | Rheo-NMR | en |
| dc.subject | real-time observation | en |
| dc.subject | SOD1 | en |
| dc.title | Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR | en |
| dc.type | journal article | - |
| dc.type.niitype | Journal Article | - |
| dc.identifier.jtitle | International Journal of Molecular Sciences | en |
| dc.identifier.volume | 18 | - |
| dc.identifier.issue | 11 | - |
| dc.relation.doi | 10.3390/ijms18112271 | - |
| dc.textversion | publisher | - |
| dc.identifier.artnum | 2271 | - |
| dc.address | Department of Molecular Engineering, Graduate School of Engineering, Kyoto University | en |
| dc.address | Department of Molecular Engineering, Graduate School of Engineering, Kyoto University | en |
| dc.address | Department of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University | en |
| dc.address | Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University | en |
| dc.address | Department of Molecular Engineering, Graduate School of Engineering, Kyoto University | en |
| dc.address | Department of Molecular Engineering, Graduate School of Engineering, Kyoto University | en |
| dc.identifier.pmid | 29143789 | - |
| dcterms.accessRights | open access | - |
| dc.identifier.pissn | 1661-7827 | - |
| dc.identifier.eissn | 1660-4601 | - |
| 出現コレクション: | 学術雑誌掲載論文等 | |
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