نتایج جستجو برای: protein disulfide isomerase

تعداد نتایج: 1249610  

2017
Emily J Furlong Alvin W Lo Fabian Kurth Lakshmanane Premkumar Makrina Totsika Maud E S Achard Maria A Halili Begoña Heras Andrew E Whitten Hassanul G Choudhury Mark A Schembri Jennifer L Martin

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...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2009
Yayoi Onda Toshihiro Kumamaru Yasushi Kawagoe

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...

Journal: :Pharmaceutical and biomedical research 2023

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...

Journal: :Cell 2006
Tim Elliott Jacques Neefjes

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.

Journal: :The Biochemical journal 2011
Lei Wang Li Zhu Chih-chen Wang

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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