2018年2月2日
Protein Folding in the Presence of Water-Soluble Cyclic Diselenides with Novel Oxidoreductase and Isomerase Activities
ChemBioChem
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- 巻
- 19
- 号
- 3
- 開始ページ
- 207
- 終了ページ
- 211
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/cbic.201700624
- 出版者・発行元
- Wiley-VCH Verlag
The protein disulfide isomerase (PDI) family, found in the endoplasmic reticulum (ER) of the eukaryotic cell, catalyzes the formation and cleavage of disulfide bonds and thereby helps in protein folding. A decrease in PDI activity under ER stress conditions leads to protein misfolding, which is responsible for the progression of various human diseases, such as Alzheimer's, Parkinson's, diabetes mellitus, and atherosclerosis. Here we report that water-soluble cyclic diselenides mimic the multifunctional activity of the PDI family by facilitating oxidative folding, disulfide formation/reduction, and repair of the scrambled disulfide bonds in misfolded proteins.
- リンク情報
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- DOI
- https://doi.org/10.1002/cbic.201700624
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/29197144
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000424105700003&DestApp=WOS_CPL
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85039546464&origin=inward 本文へのリンクあり
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85039546464&origin=inward
- ID情報
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- DOI : 10.1002/cbic.201700624
- ISSN : 1439-7633
- ISSN : 1439-4227
- eISSN : 1439-7633
- PubMed ID : 29197144
- SCOPUS ID : 85039546464
- Web of Science ID : WOS:000424105700003