Item type |
文献 / Documents(1) |
公開日 |
2020-12-17 |
アクセス権 |
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アクセス権 |
open access |
資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
出版社版DOI |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.7554/eLife.43302 |
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言語 |
ja |
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関連名称 |
10.7554/eLife.43302 |
出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
タイトル |
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タイトル |
Cell-based HTS identifies a chemical chaperone for preventing ER protein aggregation and proteotoxicity |
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言語 |
en |
著者 |
キタカゼ, ケイスケ
タニウチ, シュウスケ
カワノ, エリ
濱田, 良真
三宅, 雅人
親泊, 美帆
コジマ, ヒロタツ
小迫, 英尊
クリバラ, トモコ
ヨシダ, スグル
ホソヤ, タカミツ
親泊, 政一
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抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
The endoplasmic reticulum (ER) is responsible for folding secretory and membrane proteins, but disturbed ER proteostasis may lead to protein aggregation and subsequent cellular and clinical pathologies. Chemical chaperones have recently emerged as a potential therapeutic approach for ER stress-related diseases. Here, we identified 2-phenylimidazo[2,1-b]benzothiazole derivatives (IBTs) as chemical chaperones in a cell-based high-throughput screen. Biochemical and chemical biology approaches revealed that IBT21 directly binds to unfolded or misfolded proteins and inhibits protein aggregation. Finally, IBT21 prevented cell death caused by chemically induced ER stress and by a proteotoxin, an aggression-prone prion protein. Taken together, our data show the promise of IBTs as potent chemical chaperones that can ameliorate diseases resulting from protein aggregation under ER stress. |
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言語 |
en |
書誌情報 |
en : eLife
巻 8,
p. e43302,
発行日 2019-12-17
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収録物ID |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
2050084X |
出版者 |
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出版者 |
eLife Sciences Publications |
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言語 |
en |
権利情報 |
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言語 |
en |
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権利情報 |
This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. |
EID |
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識別子 |
363645 |
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識別子タイプ |
URI |
言語 |
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言語 |
eng |