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Characterization of the Intrinsically Disordered Region of FUS-LC protein involved in fibril formation with molecular dynamics simulations
https://repo.qst.go.jp/records/84330
https://repo.qst.go.jp/records/843302bda0e5e-b1c2-477b-8ff7-fc6abda26ca8
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2021-11-02 | |||||
| タイトル | ||||||
| タイトル | Characterization of the Intrinsically Disordered Region of FUS-LC protein involved in fibril formation with molecular dynamics simulations | |||||
| 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 |
Chan Yao Chong, Maud
× Chan Yao Chong, Maud× Soon Chan, Wai× Kumar, Amarjeet× Shun, Sakuraba× Hidetoshi, Kono× Chan Yao Chong, Maud× Soon Chan, Wai× Kumar, Amarjeet× Shun, Sakuraba× Hidetoshi, Kono |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | In the cell nucleus, liquid-liquid phase separation (LLPS) caused by proteins is thought to be the key mechanism that produces non-membrane compartments which segregate sets of DNA and proteins. In some diseases such as amyotrophic lateral sclerosis (ALS) and Alzheimer, it is observed that proteins that separate into LLPS can aggregate and form insoluble fibrils. In ALS patients, mutations have been found in the low-complexity (LC) regions of the FUS protein. LC domains, do not have a stable conformation, are classified as Intrinsically Disordered Proteins and could self-aggregate and form fibrils. Using all-atom molecular dynamics simulations, we study the fibril structures of FUS-LC domain and the impact of the mutations to understand the aggregation mechanism. |
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| 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 59th Annual Meeting of the Biophysical Society of Japan | |||||
| 発表年月日 | ||||||
| 日付 | 2021-11-26 | |||||
| 日付タイプ | Issued | |||||
