نتایج جستجو برای: protein disulfide isomerase
تعداد نتایج: 1249610 فیلتر نتایج به سال:
Copper resistance is a key virulence trait of the uropathogen Proteus mirabilis. Here we show that P. mirabilis ScsC (PmScsC) contributes to this defence mechanism by enabling swarming in the presence of copper. We also demonstrate that PmScsC is a thioredoxin-like disulfide isomerase but, unlike other characterized proteins in this family, it is trimeric. PmScsC trimerization and its active si...
The developing endosperm of rice (Oryza sativa, Os) synthesizes a large amount of storage proteins on the rough (r)ER. The major storage proteins, glutelins and prolamins, contain either intra or intermolecular disulfide bonds, and oxidative protein folding is necessary for the sorting of the proteins to the protein bodies. Here, we investigated an electron transfer pathway for the formation of...
Background: Cyclophosphamide is widely prescribed as an anti-cancer drug and used immunosuppressant. Hemorrhagic cystitis one of the common complications cyclophosphamide intake. We hypothesized that endoplasmic reticulum stress-related proteins could be altered in urothelium treated with cyclophosphamide. Objectives: checked effect on expression various Vero cells. Methods: cells varying doses...
The loading of peptides into the groove of MHC class I molecules prior to antigen presentation is a complex process. In this issue of Cell, Park et al. (2006) show that peptide loading gets a helping hand from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidoreductase activity.
In eukaryotes, disulfide bonds are formed in the endoplasmic reticulum, facilitated by the Ero1 (endoplasmic reticulum oxidoreductin 1) oxidase/PDI (protein disulfide-isomerase) system. Mammals have two ERO1 genes, encoding Ero1α and Ero1β proteins. Ero1β is constitutively expressed in professional secretory tissues and induced during the unfolded protein response. In the present work, we show ...
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