期刊
CHEMBIOCHEM
卷 19, 期 3, 页码 207-211出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201700624
关键词
diselenides; enzyme models; isomerases; protein folding; selenium
资金
- JSPS-DST Special Lecture Tour Program under the Japan-India Cooperative Science Program
- JST [SAKURA Exchange Program in Science] [E20150224001]
- JSPS [KAKENHI] [17K18123]
- PMAC for Private School of Japan [The Science Research Promotion Fund]
- SERB, New Delhi [J. C. Bose National Fellowship] [SB/S2/JCB-067/2015]
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.
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