The human protein disulphide isomerase family: substrate interactions and functional properties
about
The human protein disulfide isomerase gene familyERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptorERp29 induces breast cancer cell growth arrest and survival through modulation of activation of p38 and upregulation of ER stress protein p58IPKReductive activation of type 2 ribosome-inactivating proteins is promoted by transmembrane thioredoxin-related proteinPeroxidasin is secreted and incorporated into the extracellular matrix of myofibroblasts and fibrotic kidneyThe protein disulfide isomerase AGR2 is essential for production of intestinal mucusEpidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surfaceERp57 is essential for efficient folding of glycoproteins sharing common structural domainsActivins and activin antagonists in hepatocellular carcinomaEndoplasmic Reticulum Stress and Associated ROSThe Unfolded Protein Response and the Role of Protein Disulfide Isomerase in NeurodegenerationProtein folding and quality control in the ERN-linked sugar-regulated protein folding and quality control in the ERDisulfide bond formation in the mammalian endoplasmic reticulumMolecular mechanisms of prolactin and its receptorINS-gene mutations: from genetics and beta cell biology to clinical diseaseRedox regulation in amyotrophic lateral sclerosisA substrate-driven allosteric switch that enhances PDI catalytic activityCrystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tailThe Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible MoleculeInsights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase HeterodimerSolution structure of the bb' domains of human protein disulfide isomeraseCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDIThe Crystal Structure of the Protein-Disulfide Isomerase Family Member ERp27 Provides Insights into Its Substrate Binding CapabilitiesStructure of the Non-Catalytic Domain of the Protein Disulfide Isomerase-Related Protein (PDIR) Reveals Function in Protein BindingStructure of the third catalytic domain of the protein disulfide isomerase ERp46Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein foldingStructural insight into the dimerization of human protein disulfide isomeraseNMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway.N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding CycleERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57The branched-chain aminotransferase proteins: novel redox chaperones for protein disulfide isomerase--implications in Alzheimer's diseaseDisulfide bonds in ER protein folding and homeostasisER chaperones in mammalian development and human diseasesQuantitative Profiling of Protein S-Glutathionylation Reveals Redox-Dependent Regulation of Macrophage Function during Nanoparticle-Induced Oxidative StressCyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradationInteractome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperonesProgranulin, a glycoprotein deficient in frontotemporal dementia, is a novel substrate of several protein disulfide isomerase family proteins
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P2860
The human protein disulphide isomerase family: substrate interactions and functional properties
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The human protein disulphide i ...... ions and functional properties
@ast
The human protein disulphide i ...... ions and functional properties
@en
The human protein disulphide i ...... ions and functional properties
@nl
type
label
The human protein disulphide i ...... ions and functional properties
@ast
The human protein disulphide i ...... ions and functional properties
@en
The human protein disulphide i ...... ions and functional properties
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prefLabel
The human protein disulphide i ...... ions and functional properties
@ast
The human protein disulphide i ...... ions and functional properties
@en
The human protein disulphide i ...... ions and functional properties
@nl
P2860
P3181
P356
P1433
P1476
The human protein disulphide i ...... ions and functional properties
@en
P2093
Lloyd W Ruddock
P2860
P3181
P356
10.1038/SJ.EMBOR.7400311
P407
P577
2005-01-01T00:00:00Z