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Suppression of amyloid fibrils using the GroEL apical domain

https://repository.lib.tottori-u.ac.jp/records/7369
https://repository.lib.tottori-u.ac.jp/records/7369
df4085a8-d959-4ab7-b100-c56b9a3ff342
名前 / ファイル ライセンス アクション
sr_srep31041.pdf sr_srep31041.pdf (5.7 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2022-06-30
タイトル
タイトル Suppression of amyloid fibrils using the GroEL apical domain
言語 en
言語
言語 eng
資源タイプ
資源タイプ journal article
著者 本郷, 邦広

× 本郷, 邦広

WEKO 779
e-Rad 80335504
研究者総覧鳥取大学 100000563

本郷, 邦広

ja-Kana ホンゴウ, クニヒロ

en Hongo, Kunihiro

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溝端, 知宏

× 溝端, 知宏

WEKO 2225
e-Rad 50263489
研究者総覧鳥取大学 100000572

溝端, 知宏

ja-Kana ミゾバタ, トモヒロ

en Mizobata, Tomohiro

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河田, 康志

× 河田, 康志

WEKO 1457
e-Rad 40177697
研究者総覧鳥取大学 100000496

河田, 康志

ja-Kana カワタ, ヤスシ

en Kawata, Yasushi

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Ojha, Bimlesh

× Ojha, Bimlesh

WEKO 27412

en Ojha, Bimlesh

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Fukui, Naoya

× Fukui, Naoya

WEKO 27413

en Fukui, Naoya

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著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University
著者所属(英)
言語 en
値 Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University
抄録
内容記述タイプ Other
内容記述 In E. coli cells, rescue of non-native proteins and promotion of native state structure is assisted by the chaperonin GroEL. An important key to this activity lies in the structure of the apical domain of GroEL (GroEL-AD) (residue 191–376), which recognizes and binds non-native protein molecules through hydrophobic interactions. In this study, we investigated the effects of GroEL-AD on the aggregation of various client proteins (α-Synuclein, Aβ42, and GroES) that lead to the formation of distinct protein fibrils in vitro. We found that GroEL-AD effectively inhibited the fibril formation of these three proteins when added at concentrations above a critical threshold; the specific ratio differed for each client protein, reflecting the relative affinities. The effect of GroEL-AD in all three cases was to decrease the concentration of aggregate-forming unfolded client protein or its early intermediates in solution, thereby preventing aggregation and fibrillation. Binding affinity assays revealed some differences in the binding mechanisms of GroEL-AD toward each client. Our findings suggest a possible applicability of this minimal functioning derivative of the chaperonins (the “minichaperones”) as protein fibrillation modulators and detectors.
書誌情報 Scientific Reports
en : Scientific Reports

巻 6, 発行日 2016-08-04
出版者
出版者 Springer Nature
ISSN
収録物識別子タイプ ISSN
収録物識別子 20452322
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 10.1038/srep31041
権利
権利情報 (C) The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in th
情報源
関連名称 Ojha Bimlesh, Fukui Naoya, Hongo Kunihiro, et al. Suppression of amyloid fibrils using the GroEL apical domain. Scientific Reports. 2016. 6. doi:10.1038/srep31041
関連サイト
識別子タイプ URI
関連識別子 https://www.nature.com/articles/srep31041
関連名称 https://www.nature.com/articles/srep31041
著者版フラグ
出版タイプ VoR
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