The protein disulphide-isomerase family: unravelling a string of folds.
about
The human protein disulfide isomerase gene familyERp16, an endoplasmic reticulum-resident thiol-disulfide oxidoreductase: biochemical properties and role in apoptosis induced by endoplasmic reticulum stressERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stressERp57 is essential for efficient folding of glycoproteins sharing common structural domainsA novel function of tissue-type transglutaminase: protein disulphide isomeraseTROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.The human protein disulphide isomerase family: substrate interactions and functional propertiesThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaMultiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in NeurodegenerationOxidative protein folding: selective pressure for prolamin evolution in riceThe P5 disulfide switch: taming the aging unfolded protein responseMechanisms and models of endoplasmic reticulum stress in chondrodysplasiaRedox regulation in amyotrophic lateral sclerosisFunctional Role of the Disulfide Isomerase ERp57 in Axonal RegenerationAcid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry.Interactions and Oligomerization of Hantavirus GlycoproteinsCrystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related proteinSaccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferasesFunctional differences in yeast protein disulfide isomerases.Oxidative stress, unfolded protein response, and apoptosis in developmental toxicityERp57 is a multifunctional thiol-disulfide oxidoreductaseERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57Orthologs in Arabidopsis thaliana of the Hsp70 interacting protein HipFunctional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein foldingCharacterization of the estradiol-binding site structure of human protein disulfide isomerase (PDI)ERp29 deficiency affects sensitivity to apoptosis via impairment of the ATF6-CHOP pathway of stress responseAntarctic krill 454 pyrosequencing reveals chaperone and stress transcriptome.MTH1745, a protein disulfide isomerase-like protein from thermophilic archaea, Methanothermobacter thermoautotrophicum involving in stress responseStrategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.From structure to redox: The diverse functional roles of disulfides and implications in disease.Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion.Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding.Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: thioredoxin inhibits protein kinase C-mediated phosphorylation of histoneCharacterization of two protein disulfide isomerases from the endocytic pathway of bloodstream forms of Trypanosoma brucei.Disulfide-dependent folding and export of Escherichia coli DsbC.Approaches for the identification of potential excreted/secreted proteins of Leishmania major parasites.Proteomic identification of secreted proteins as surrogate markers for signal transduction inhibitor activityIn vivo selection for metastasis promoting genes in the mouseStress genes and proteins in the archaea.
P2860
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P2860
The protein disulphide-isomerase family: unravelling a string of folds.
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The protein disulphide-isomerase family: unravelling a string of folds.
@ast
The protein disulphide-isomerase family: unravelling a string of folds.
@en
The protein disulphide-isomerase family: unravelling a string of folds.
@nl
type
label
The protein disulphide-isomerase family: unravelling a string of folds.
@ast
The protein disulphide-isomerase family: unravelling a string of folds.
@en
The protein disulphide-isomerase family: unravelling a string of folds.
@nl
prefLabel
The protein disulphide-isomerase family: unravelling a string of folds.
@ast
The protein disulphide-isomerase family: unravelling a string of folds.
@en
The protein disulphide-isomerase family: unravelling a string of folds.
@nl
P2860
P1433
P1476
The protein disulphide-isomerase family: unravelling a string of folds.
@en
P2093
P2860
P356
10.1042/0264-6021:3390001
P407
P478
339 ( Pt 1)
P577
1999-04-01T00:00:00Z