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Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumTwo cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formationDisruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coliOxidative protein folding in eukaryotes: mechanisms and consequencesTargeting Bacterial Dsb Proteins for the Development of Anti-Virulence AgentsDisulfide-Bond-Forming Pathways in Gram-Positive BacteriaDisulfide bond formation in the bacterial periplasm: major achievements and challenges aheadMany roles of the bacterial envelope reducing pathwaysReducing systems protecting the bacterial cell envelope from oxidative damageOn the role of the cis-proline residue in the active site of DsbASolution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschiiThe disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductaseStaphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative foldingPreparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBDynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbBThe Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA EnzymesCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEStructure of a bacterial homologue of vitamin K epoxide reductaseStructural and functional characterization of three DsbA paralogues from Salmonella enterica serovar TyphimuriumStructure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid BilayerDissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosaThe 1.2 Å resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin productionThe Escherichia coli CcmG protein fulfils a specific role in cytochrome c assemblyThe Salmonella SPI1 type three secretion system responds to periplasmic disulfide bond status via the flagellar apparatus and the RcsCDB systemInsights into the structure and assembly of Escherichia coli outer membrane protein AThermodynamics of unfolding of an integral membrane protein in mixed micelles.Mutational analysis of the disulfide catalysts DsbA and DsbB.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbBCharacterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae.Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.DsbD-catalyzed transport of electrons across the membrane of Escherichia coli.Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli.Synthesis of the blood circulating C-terminal fragment of insulin-like growth factor (IGF)-binding protein-4 in its native conformation. Crystallization, heparin and IGF binding, and osteogenic activity.Proteome analysis of virulence factor regulated by autoinducer-2-like activity in Escherichia coli O157:H7.The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasmDisulfide bond formation involves a quinhydrone-type charge-transfer complex.Disulfide bond formation in prokaryotes: history, diversity and design
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
A pathway for disulfide bond formation in vivo
@ast
A pathway for disulfide bond formation in vivo
@en
A pathway for disulfide bond formation in vivo
@nl
type
label
A pathway for disulfide bond formation in vivo
@ast
A pathway for disulfide bond formation in vivo
@en
A pathway for disulfide bond formation in vivo
@nl
prefLabel
A pathway for disulfide bond formation in vivo
@ast
A pathway for disulfide bond formation in vivo
@en
A pathway for disulfide bond formation in vivo
@nl
P2093
P2860
P356
P1476
A pathway for disulfide bond formation in vivo
@en
P2093
P2860
P304
P356
10.1073/PNAS.90.3.1038
P407
P577
1993-02-01T00:00:00Z