Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes

scientific journal article

Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes is …
instance of (P31):
scholarly articleQ13442814
review articleQ7318358

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P356DOI10.1016/S0003-9861(02)00337-5
P698PubMed publication ID12176051

P2093author name stringColin Thorpe
Donald L. Coppock
George K. Turi
Joan Burnside
Karen L. Hoober
Nicole M. Glynn
Sonali Raje
P2860cites workRegulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29Q22253311
Manipulation of oxidative protein folding and PDI redox state in mammalian cellsQ24291898
The CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaQ24599012
Divergence time estimates for the early history of animal phyla and the origin of plants, animals and fungiQ24672301
Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysisQ27631180
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2pQ27636724
Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidaseQ27930591
Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein familyQ27933986
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulumQ27936188
An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteinsQ27938563
Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulumQ27939552
A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formationQ27940305
Highly divergent amino termini of the homologous human ALR and yeast scERV1 gene products define species specific differences in cellular localizationQ28138322
Intracrine hepatopoietin potentiates AP-1 activity through JAB1 independent of MAPK pathwayQ28205362
Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeastQ28291894
Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidaseQ28583331
Physiological functions of thioredoxin and thioredoxin reductaseQ29615600
Oxidized redox state of glutathione in the endoplasmic reticulumQ29619789
Rat seminal vesicle FAD-dependent sulfhydryl oxidase. Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family.Q30643454
Identification and expression of a new sulfhydryl oxidase SOx-3 during the cell cycle and the estrus cycle in uterine cellsQ30713545
Glutathione and its role in cellular functionsQ33777917
Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidasesQ33878493
Biochemical basis of oxidative protein folding in the endoplasmic reticulumQ33926107
Circulating thioredoxin suppresses lipopolysaccharide-induced neutrophil chemotaxisQ33952980
A hydrogen peroxide-forming NADH oxidase that functions as an alkyl hydroperoxide reductase in Amphibacillus xylanusQ33994572
Antigen-presenting dendritic cells provide the reducing extracellular microenvironment required for T lymphocyte activationQ34009906
Native disulfide bond formation in proteinsQ34046362
Thioredoxin reductase two modes of catalysis have evolvedQ34049898
Dehydroascorbate reductionQ34059231
Complete pathway for protein disulfide bond formation encoded by poxvirusesQ34067229
Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assemblyQ34358464
Redox regulation of cellular activationQ34425412
The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1.Q34486132
Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulumQ34589237
A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formationQ35377030
Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: expression of biologically active recombinant ALR and demonstration of tissue distributionQ35684766
Thioredoxin, a redox enzyme released in infection and inflammation, is a unique chemoattractant for neutrophils, monocytes, and T cellsQ36368272
Molecular mechanisms of augmenter of liver regeneration as immunoregulator: its effect on interferon-gamma expression in rat liverQ38308545
Vaccinia virus E10R protein is associated with the membranes of intracellular mature virions and has a role in morphogenesisQ40838212
Making and breaking disulfide bondsQ41620623
Protein disulfide isomerase and assisted protein foldingQ41641785
A flavoprotein responsible for the intense sulfhydryl oxidase activity of rat seminal vesicle secretionQ41667953
Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomeraseQ42156942
Characterization of the membrane-associated thiol oxidase activity of rat small-intestinal epitheliumQ42459851
Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomeraseQ42792635
Protein-disulfide isomerase- and protein thiol-dependent dehydroascorbate reduction and ascorbate accumulation in the lumen of the endoplasmic reticulumQ43514942
Aspergillus niger sulfhydryl oxidaseQ46162649
Skin sulfhydryl oxidase purification and some propertiesQ53783411
Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion.Q55063147
A sulfhydryl oxidase from chicken egg white.Q55066797
Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide IsomeraseQ61718588
Sulfhydryl oxidase from egg white. A facile catalyst for disulfide bond formation in proteins and peptides.Q64991284
Epididymal sulfhydryl oxidase: a sperm-protective enzyme from the male reproductive tractQ67272226
Distribution of sulfhydryl oxidase activity in the rat and hamster male reproductive tractQ67351257
Unequivocal evidence in support of the nonenzymatic redox coupling between glutathione/glutathione disulfide and ascorbic acid/dehydroascorbic acidQ67571098
Microsomal mixed-function oxidase-dependent renaturation of reduced ribonucleaseQ67707927
The augmenter of liver regeneration induces mitochondrial gene expression in rat liver and enhances oxidative phosphorylation capacity of liver mitochondriaQ73139600
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulumQ73151253
Properties and biological activities of thioredoxinsQ74150080
Egg white sulfhydryl oxidase: kinetic mechanism of the catalysis of disulfide bond formationQ74599280
Thioredoxin reductase-thioredoxin fusion enzyme from Mycobacterium leprae: comparison with the separately expressed thioredoxin reductaseQ77569638
Flavin-dependent sulfhydryl oxidases in protein disulfide bond formationQ77745544
The genetics of disulfide bond metabolismQ77936221
Oxidative protein folding is driven by the electron transport systemQ78066764
Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombinQ78108804
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectQuiescin Q6 sulfhydryl oxidase 1Q21986343
Quiescin sulfhydryl oxidase 1 Dmel_CG4670Q29809611
Quiescin sulfhydryl oxidase 2 Dmel_CG17843Q29810306
P304page(s)1–12
P577publication date2002-09-01
P1433published inArchives of Biochemistry and BiophysicsQ635818
P1476titleSulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes
P478volume405

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