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Protein Folding in the Presence of Water‐Soluble Cyclic Diselenides with Novel Oxidoreductase and Isomerase Activities
Author(s) -
Arai Kenta,
Ueno Haruhito,
Asano Yuki,
Chakrabarty Gaurango,
Shimodaira Shingo,
Mugesh Govindasamy,
Iwaoka Michio
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700624
Subject(s) - protein disulfide isomerase , endoplasmic reticulum , protein folding , chemistry , foldase , unfolded protein response , folding (dsp implementation) , oxidative folding , disulfide bond , isomerase , biochemistry , chemical chaperone , biophysics , enzyme , biology , escherichia coli , groel , electrical engineering , gene , engineering
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.