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Redox-mediated regulation of low complexity domain self-association
https://repo.qst.go.jp/records/84661
https://repo.qst.go.jp/records/846615c2f5e97-aa65-4fec-af32-695f682c3b27
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2021-11-12 | |||||
タイトル | ||||||
タイトル | Redox-mediated regulation of low complexity domain self-association | |||||
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 | |||||
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 |
Masato, Kato
× Masato, Kato× P Tu, Benjamin× L McKnight, Steven× Masato, Kato |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Eukaryotic cells express thousands of protein domains long believed to function in the absence of molecular order. These intrinsically disordered protein (IDP) domains are typified by gibberish-like repeats of only a limited number of amino acids that we refer to as domains of low sequence complexity. A decade ago, it was observed that these low complexity (LC) domains can undergo phase transition out of aqueous solution to form either liquid-like droplets or hydrogels. The self-associative interactions responsible for phase transition involve the formation of specific cross-β structures that are unusual in being labile to dissociation. Here we give evidence that the LC domains of two RNA binding proteins, ataxin-2 and TDP43, form cross-β interactions that specify biologically relevant redox sensors. | |||||
書誌情報 |
Current Opinion in Genetics & Development 巻 67, p. 111-118, 発行日 2021-04 |
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出版者 | ||||||
出版者 | Elsevier | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0959-437X | |||||
DOI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1016/j.gde.2020.12.006 | |||||
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識別子タイプ | URI | |||||
関連識別子 | https://www.sciencedirect.com/science/article/abs/pii/S0959437X20301702?via%3Dihub#! |