scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.274.32.22147 |
P698 | PubMed publication ID | 10428777 |
P2093 | author name string | C Thorpe | |
H F Gilbert | |||
K L Hoober | |||
S L Sheasley | |||
P2860 | cites work | Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum | Q24673769 |
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum | Q27936188 | ||
Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum | Q27939552 | ||
Oxidized redox state of glutathione in the endoplasmic reticulum | Q29619789 | ||
Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer | Q34019971 | ||
Cotranslational folding and calnexin binding during glycoprotein synthesis | Q34108450 | ||
Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine | Q38361723 | ||
The renal thiol (glutathione) oxidase subcellular localization and properties | Q40179433 | ||
The bonds that tie: catalyzed disulfide bond formation | Q40848083 | ||
Making and breaking disulfide bonds | Q41620623 | ||
Protein disulfide isomerase and assisted protein folding | Q41641785 | ||
The eS-Sence of -SH in the ER. | Q41698034 | ||
Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase | Q42792635 | ||
The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase | Q42859987 | ||
Purification and properties of sulfhydryl oxidase from bovine pancreas | Q44860926 | ||
Sulfhydryl oxidase-catalyzed formation of disulfide bonds in reduced ribonuclease | Q44861992 | ||
Aspergillus niger sulfhydryl oxidase | Q46162649 | ||
Protein folding: a missing redox link in the endoplasmic reticulum | Q47890004 | ||
Skin sulfhydryl oxidase purification and some properties | Q53783411 | ||
Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion. | Q55063147 | ||
A sulfhydryl oxidase from chicken egg white. | Q55066797 | ||
Sulfhydryl oxidase from rat skin | Q69405702 | ||
Resolution of renal sulfhydryl oxidase from gamma-glutamyltransferase by covalent chromatography on cysteinylsuccinamidopropyl-glass | Q72536285 | ||
Protein disulfide isomerase | Q74420336 | ||
Egg white sulfhydryl oxidase: kinetic mechanism of the catalysis of disulfide bond formation | Q74599280 | ||
The endoplasmic reticulum as a protein-folding compartment | Q75292619 | ||
The genetics of disulfide bond metabolism | Q77936221 | ||
P433 | issue | 32 | |
P407 | language of work or name | English | Q1860 |
P1104 | number of pages | 4 | |
P304 | page(s) | 22147-22150 | |
P577 | publication date | 1999-08-01 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Sulfhydryl oxidase from egg white. A facile catalyst for disulfide bond formation in proteins and peptides. | |
P478 | volume | 274 |
Q44118932 | A continuous fluorescence assay for sulfhydryl oxidase |
Q24642673 | A flavin-dependent sulfhydryl oxidase in bovine milk |
Q28477571 | A novel disulfide-rich protein motif from avian eggshell membranes |
Q28189332 | An initiator and its flanking elements function as a core promoter driving transcription of the Hepatopoietin gene |
Q33968624 | Arsenic(III) species inhibit oxidative protein folding in vitro |
Q48139731 | Chemistry and Enzymology of Disulfide Cross-Linking in Proteins. |
Q26829235 | Disulfide bond formation in the mammalian endoplasmic reticulum |
Q38368689 | Disulfide bond generation in mammalian blood serum: detection and purification of quiescin-sulfhydryl oxidase |
Q36890086 | Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats in Drosophila melanogaster |
Q27930591 | Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase |
Q41863637 | Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase |
Q34387555 | Exploring the smallest active fragment of HsQSOX1b and finding a highly efficient oxidative engine |
Q42460946 | FAD-linked sulfhydryl oxidase QSOX: topographic, cellular, and subcellular immunolocalization in adult rat central nervous system |
Q77745544 | Flavin-dependent sulfhydryl oxidases in protein disulfide bond formation |
Q34157680 | Formation and transfer of disulphide bonds in living cells |
Q88478736 | Gaussia princeps luciferase: a bioluminescent substrate for oxidative protein folding |
Q36642894 | Generating disulfides with the Quiescin-sulfhydryl oxidases |
Q33777917 | Glutathione and its role in cellular functions |
Q37596401 | Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidase |
Q33739290 | High expression of QSOX1 reduces tumorogenesis, and is associated with a better outcome for breast cancer patients |
Q24317717 | Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis |
Q24298577 | Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1 |
Q40069757 | Involvement of sulfhydryl oxidase QSOX1 in the protection of cells against oxidative stress-induced apoptosis |
Q24291898 | Manipulation of oxidative protein folding and PDI redox state in mammalian cells |
Q40899371 | Mia40 is a facile oxidant of unfolded reduced proteins but shows minimal isomerase activity |
Q34046362 | Native disulfide bond formation in proteins |
Q46382252 | Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain |
Q34222636 | Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins |
Q33941860 | Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase |
Q38236912 | Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum |
Q46324255 | Partial oxidation and oxidative polymerization of metallothionein |
Q42473743 | Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins |
Q35980820 | Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family |
Q56806409 | Protein–protein crosslinking in food: methods, consequences, applications |
Q39146688 | Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst. |
Q33699199 | Quiescin sulfhydryl oxidase from Trypanosoma brucei: catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain. |
Q24306165 | Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum |
Q22253311 | Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29 |
Q77745550 | Sulfhydryl oxidases as factors for mitochondrial biogenesis |
Q28512421 | Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes |
Q39659701 | The conserved CXXC motif of hepatic stimulator substance is essential for its role in mitochondrial protection in H2O2‐induced cell apoptosis |
Q36571987 | The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase |
Q33828308 | The emerging role of QSOX1 in cancer |
Q77199396 | The expanding world of oxidative protein folding |
Q79074416 | The potentiation role of hepatopoietin on activator protein-1 is dependent on its sulfhydryl oxidase activity |
Q51971504 | Tissue distribution of quiescin Q6/sulfhydryl oxidase (QSOX) in developing mouse. |
Q37343919 | Two phases of disulfide bond formation have differing requirements for oxygen. |
Q42181768 | Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum |
Search more.