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Back Cover: An Amphiphilic Selenide Catalyst Behaves Like a Hybrid Mimic of Protein Disulfide Isomerase and Glutathione Peroxidase 7 (Chem. Asian J. 12/2014)
Author(s) -
Arai Kenta,
Moriai Kenji,
Ogawa Akinobu,
Iwaoka Michio
Publication year - 2014
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201490047
Subject(s) - protein disulfide isomerase , amphiphile , chemistry , foldase , protein folding , isomerase , selenide , endoplasmic reticulum , biochemistry , folding (dsp implementation) , oxidative folding , chaperone (clinical) , disulfide bond , glutathione , glutathione peroxidase , alkyl , enzyme , stereochemistry , selenium , organic chemistry , medicine , escherichia coli , groel , pathology , electrical engineering , gene , copolymer , engineering , polymer
Protein Folding Protein disulfide isomerase (PDI) and glutathione peroxidase 7 (GPx7) cooperatively promote the oxidative folding of disulfide (SS)‐containing proteins in the endoplasmic reticulum. PDI recognizes nascent proteins to convert them into the native folds by means of SS formation and SS isomerization and GPx7 catalyzes the reoxidation of reduced PDI with H 2 O 2 , respectively. In their Full Paper on page 3464 ff., featured on the Back Cover, Michio Iwaoka et al. report on the design of new amphiphilic selenides with a long‐chain alkyl group and their application to the refolding of reduced hen egg‐white lysozyme. Such a combination of a water‐soluble selenide and a long‐chain alkyl group may constitute a useful motif for designing medicines for protein‐misfolding diseases and for antioxidant therapy.