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Observation of Liquid-Liquid Phase Separation of FUS-LC using VUV-CD Spectroscopy
https://repo.qst.go.jp/records/85211
https://repo.qst.go.jp/records/85211d615f0c2-7bf8-44da-875c-c30a436e5d3b
Item type | 会議発表用資料 / Presentation(1) | |||||
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公開日 | 2022-03-14 | |||||
タイトル | ||||||
タイトル | Observation of Liquid-Liquid Phase Separation of FUS-LC using VUV-CD Spectroscopy | |||||
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_c94f | |||||
資源タイプ | conference object | |||||
アクセス権 | ||||||
アクセス権 | metadata only access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
著者 |
Kentaro, Fujii
× Kentaro, Fujii× Nobuo, Maita× Masato, Kato× Koichi, Matsuo(Hiroshima Univ.)× Kentaro, Fujii× Nobuo, Maita× Masato, Kato |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Aggregation of the RNA-binding protein FUS (Fused in Sarcoma) has been implicated in the neurodegenerative diseases such as ALS (amyotrophic lateral sclerosis) and FTD (frontotemporal dementia) [1]. The low-complexity domain of the FUS (FUS-LC) mediated liquid-liquid phase separation (LLPS) [2], but the structural mechanism is not known in detail. To address the revealing the mechanism, several structural analyses such as NMR or x-ray crystallography were examined [2, 3]. Reentry, Murakami and co-authors were performed Raman microscopy to analyze LLPS local structure [4]. They revealed that the FUS LC have extremely high concentrations which could not achieved in vitro experiments. In order to reveal the process to form LLPS such a high concentration, we examined the spectroscopic study using VUV-CD measurement, which can analyze the secondary structure of the proteins. | |||||
会議概要(会議名, 開催地, 会期, 主催者等) | ||||||
内容記述タイプ | Other | |||||
内容記述 | The 26th Hiroshima International Symposium on Synchrotron Radiation | |||||
発表年月日 | ||||||
日付 | 2022-03-10 | |||||
日付タイプ | Issued |