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malfunction
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functional inhibition of protein disulfide isomerase by S-nitrosylation may contribute to pathophysiology in both mutant superoxide dismutase 1-linked disease and sporadic amyotrophic lateral sclerosis
malfunction
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mice lacking AGR2 are viable but are highly susceptible to colitis, indicating a critical role for AGR2 in protection from disease
malfunction
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PDI inhibition or silencing increases apoptosis and inhibits migration and adhesion of endothelial cells, overview
malfunction
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the anomalous behavior of PDI during a key step in oxidative regeneration may contribute to misfolding in the endoplasmic reticulum, aggregation, and neurodegenerative disease
malfunction
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inhibition of cell surface PDI induces a marked increase in tissue factor procoagulant function
malfunction
PDIL2-3 knockdown causes aberrant accumulation of prolamins in endoplasmic reticulum-derived type-I protein bodies whereas the oxidative folding of vacuole-targeted proteins, such as proglutelins and alpha-globulin, is hardly affected. PDIL2-3 knockdown inhibits the accumulation of Cys-rich 10-kD prolamin in the core of type-I protein bodies
malfunction
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enzyme silencing decreases Nox1 expression and reactive oxygen species production as well as platelet-derived growth factor-induced Rac1 and RhoA activities
malfunction
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enzyme silencing prevents Nox responses to angiotensin II and inhibits Akt phosphorylation in vascular cells and parasite phagocytosis in macrophages
malfunction
PDIA6-deficient cells hyperrespond to endoplasmic reticulum stress with sustained autophosphorylation of inositol-requiring enzyme 1alpha and splicing of XBP1 mRNA, resulting in exaggerated upregulation of UPR target genes and increased apoptosis. In vivo, PDIA6-deficient Caenorhabditis elegans exhibits constitutive unfolded protein response and fails to complete larval development
malfunction
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enzyme inhibition results ina 25% loss of vessel caliber post-injury. This is accompanied by decreased hydrogen peroxide formation and changes in collagen organization, resulting in increased arterial stiffness
malfunction
deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
malfunction
TXNDC5 knockdown in lung cancer cells inhibits cell proliferation and represses anchorage-independent colony formation and migration, but increases cell invasion and activation of mitogen-activated protein kinases. Knockdown of TXNDC5 sensitizes human lung cancer cells to endoplasmic reticulum (ER) stress-induced cell death. Knockdown of TXNDC5 enhances EGF-induced MAPK activation in human lung cancer cells, which may contribute to the increased invasiveness of these cells
malfunction
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deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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malfunction
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deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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malfunction
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deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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malfunction
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deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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malfunction
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deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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malfunction
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deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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metabolism
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the close interdependence between Mnl1p and PDI suggests that these two proteins form a functional unit in the ER-associated degradation, ERAD, pathway
metabolism
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isoform PDI2 interacts with proteins in both the endoplasmic reticulum (ER) and nucleus, including ER-resident protein folding chaperone, BiP1, and nuclear embryo transcription factor, MEE8
metabolism
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enzyme-mediated disulfide bond exchange plays a pivotal role in the post-ligation phase of integrin alphaIIbbeta3-mediated adhesion to fibrinogen
metabolism
isoform PDIL1;1 plays primary roles in both disulfide bond formation and disulfide bond reduction, which allow for redox control of protein quality and packaging
metabolism
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the enzyme is a catalyst of oxidative protein folding
metabolism
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the enzyme is responsible for the oxidation (formation), reduction (break down) and isomerization (rearrangement) of protein disulfide bonds via disulfide interchange activity. The enzyme also has general chaperone activity
metabolism
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the enzyme participates in many important cellular events including the oxidative protein folding, the endoplasmic reticulum associated degradation, the retrieval of unassembled proteins in the early secretory pathway, and the regulation of unfolded protein response pathways
metabolism
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
metabolism
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the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
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metabolism
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the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
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metabolism
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the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
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metabolism
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the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
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metabolism
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the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
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metabolism
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the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
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physiological function
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endoplasmic reticulum stress is important in the formation of mutant superoxide dismutase 1 inclusions, and protein disulfide isomerase has an important function in ameliorating mutant superoxide dismutase 1 aggregation and toxicity
physiological function
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FXIII-PDI activity may have a role in platelet function
physiological function
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PDI and other PDI family proteins are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum
physiological function
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PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
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PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
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PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
PDI is a multifunctional protein for catalyzing the formation, isomerization, and reduction of disulfide bonds
physiological function
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PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
physiological function
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PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
physiological function
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PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
physiological function
PDIA3 is an endoplasmic reticulum stress protein. It is induced by oxidative stress and plays a role in relation to stress regulation
physiological function
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PDIp may function as a protein-folding catalyst for secretory digestive enzymes
physiological function
physiological roles of PDIA3 and PDI-P5 in sperm maturation and fertilization, overview
physiological function
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the enzyme is involved in myocardial angiogenesis, overview
physiological function
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the enzyme is involved in myocardial angiogenesis. Protein disulfide isomerase is highly upregulated in hypoxic myocardial capillary endothelial cells, chronic hypoxia increases the survival rate and reduces the infarct size in myocardial ischemia, overview
physiological function
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the enzyme is required for infection by Chlamydia species
physiological function
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the enzyme plays a role in the formation of disulfide bonds in immunoglobulins, it is also involved in disulfide bond formation of the IgG4 subclass of antibody, but catalysis of disulfide bond formation is not rate limiting for IgG4 production
physiological function
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the enzyme plays a role in the formation of disulfide bonds in immunoglobulins, it is also involved in disulfide bond formation of the IgG4 subclass of antibody, but catalysis of disulfide bond formation is not rate limiting for IgG4 production
physiological function
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the protein disulfide isomerase AGR2 is essential for production of intestinal mucin MUC2, a large, cysteine-rich glycoprotein that forms the protective mucus gel lining the intestine
physiological function
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the substrate binding, but not catalytic, activity of PDI is essential for the degradation of MHC class I HC by human cytomegalovirus glycoprotein US2, but not by US11, since oxidative folding of US2 is required for US2 function in inducing degradation of MHC class I molecules, PDI catalyses the release of MHC class I molecules from US2, function for PDI in SPP-mediated ERAD pathway, overview
physiological function
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extracellular protein disulfide isomerase negatively regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure
physiological function
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PDI is required for cholera toxin intoxication but not for cholera toxin subunit A1 translocation
physiological function
PDIL2-3 does not facilitate the oxidative folding of proglutelins
physiological function
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protein disulfide isomerase blocks transcription factor C/EBP-alpha translation but not transcription
physiological function
the a and a' domains of PDIL1-1 are both functional in the oxidative folding of proglutelins
physiological function
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the DsbA coexpressed as whole cell bioconversion system can more efficiently detoxify high concentration of organophosphates than cells expressing methyl parathion hydrolase only. Overexpression of protein disulfide isomerase DsbA enhances detectability in the environment following degradation of pesticide residues
physiological function
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enzyme overexpression spontaneously enhances Nox activation and expression. In neutrophils, enzyme redox-dependently associates with p47phox and supports the respiratory burst
physiological function
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extracellular protein disulfide isomerase (PDI) regulates ligand-binding activity of alphaMbeta2 integrin and neutrophil recruitment during vascular inflammation. Neutrophil PDI is required for neutrophil adhesion and crawling during tumor necrosis factor-alpha-induced vascular inflammation in vivo
physiological function
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extracellular protein disulfide isomerase (PDI) regulates ligand-binding activity of alphaMbeta2 integrin and neutrophil recruitment during vascular inflammation. Neutrophil PDI is required for neutrophil adhesion and crawling during tumor necrosis factor-alpha-induced vascular inflammation in vivo
physiological function
isoform PDIA6 limits the duration of inositol-requiring enzyme 1alpha (IRE1alpha) activity by direct binding to cysteine 148 in the lumenal domain of the sensor, which is oxidized when IRE1 is activated
physiological function
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protein disulfide isomerase directly interacts with beta-actin Cys374 during cell adhesion and spreading and regulates cytoskeleton reorganization
physiological function
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protein disulfide isomerase interacts with tau protein and physiologically inhibits its fibrillization mainly through ist thioredoxin-like catalytic domain a, forming a 1:1 complex and preventing Tau misfolding. Protein disulfide isomerase is both an enzyme and a chaperone, and implicated in neuroprotection against Alzheimer disease
physiological function
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protein disulfide isomerase is required for platelet-derived growth factor-induced vascular smooth muscle cell migration, Nox1 NADPH oxidase expression, and Rho-GTPase activation
physiological function
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protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and prion protein mutant-induced cytotoxicity. The enzyme functions as a pleiotropic regulator in the processes of different misfolded prion proteins and at different stages during prion infection. The enzyme is involved in mitochondrial dysfunction induced by misfolded prion
physiological function
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the enzyme is associated with the reproductive development and enriched in adult females
physiological function
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the enzyme is responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum
physiological function
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the enzyme isoform PDI2 is involved in circadian rhythm regulation. Isoform PDI2 is a redox-active protein and has refolding activity. Overexpression of the ioform PDI2 causes a shift in acrophase of the circadian rhythm of phototaxis
physiological function
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the enzyme plays a key role in assisting Leishmania protein folding via its capacity to catalyze formation, breakage, and rearrangement of disulfide bonds in nascent polypeptides. The enzyme displays a chaperone-like activity
physiological function
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the surface-associated enzyme is an important regulator of coagulation factor ligation to thrombin-stimulated platelets and of subsequent feedback activation of platelet thrombin generation. Extracellular enzyme regulates thrombin generation on thrombin-stimulated platelets
physiological function
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enzyme overexpression has a negative impact on the initiation of chlorophyll degradation and proteolysis within chloroplasts. Enzyme overexpression in leaves induces a stay-green phenotype during darkness, where oxidative conditions favor catabolism
physiological function
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isoform PDI8 functions in the oxidation of cysteines to produce disulfide bonds. It likely plays a role in folding newly-synthesized secretory proteins as they translocate across the endoplasmic reticulum membrane into the lumen
physiological function
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isoform PDIA1 is required for agonist-triggered Nox NADPH oxidase activation and cell migration in vascular cells and macrophages. The enzyme also plays role in cytoskeleton organization
physiological function
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PDI1 is a virulence factor of Phytophthora parasitica and contributes to plant infection
physiological function
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the enzyme affects the redox homeostasis and unfolded protein response-related genes. The enzyme is involved in all major developmental processes, such as the formation of sclerotia, conidial anastomosis tubes and infection cushions, is involved in oxidative and osmotic stress resistance, and needed for full virulence
physiological function
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the enzyme is a regulatorof vessel architecture and circumference that prevents inward remodeling without effects on wall thickness or neointima formation
physiological function
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the enzyme is required for plants to survive under reducing conditions. Isoform PDI11 is involved in protein oxidative refolding
physiological function
enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
physiological function
the redox regulator sulfiredoxin (Srx) forms a complex with thioredoxin domain-containing 5 protein in response to endoplasmic reticulum (ER) stress, but not to oxidative stress, in lung cancer cells. Increased association of Srx with TXNDC5 facilitates the retention of normally cytosolic Srx in the ER. TXNDC5 directly interacts with Srx through its thioredoxin-like domains
physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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physiological function
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the enzyme plays a key role in assisting Leishmania protein folding via its capacity to catalyze formation, breakage, and rearrangement of disulfide bonds in nascent polypeptides. The enzyme displays a chaperone-like activity
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physiological function
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enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
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additional information
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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additional information
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the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
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