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An in vivo pathway for disulfide bond isomerization in Escherichia coli

An in vivo pathway for disulfide bond isomerization in Escherichia coli

http://www.wikidata.org/entity/Q36687328

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Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli Protein quality control in the bacterial periplasm Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria Many roles of the bacterial envelope reducing pathways Reducing systems protecting the bacterial cell envelope from oxidative damage The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar Typhimurium Monovalent antibody design and mechanism of action of onartuzumab, a MET antagonist with anti-tumor activity as a therapeutic agent Dissecting the Machinery That Introduces Disulfide Bonds in Pseudomonas aeruginosa The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly The Salmonella SPI1 type three secretion system responds to periplasmic disulfide bond status via the flagellar apparatus and the RcsCDB system Catalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule Mimics Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-domain open conformer Laboratory evolution of one disulfide isomerase to resemble another Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.Disulfide-dependent folding and export of Escherichia coli DsbC.DsbD-catalyzed transport of electrons across the membrane of 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.General mutagenesis of F plasmid TraI reveals its role in conjugative regulation 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 periplasm Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase.Disulfide bond formation in prokaryotes: history, diversity and design The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo.Expression and crystallization of SeDsbA, SeDsbL and SeSrgA from Salmonella enterica serovar Typhimurium.A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins.DsbC activation by the N-terminal domain of DsbD.Nonconsecutive disulfide bond formation in an essential integral outer membrane protein On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily Oxidative protein folding in bacteria.Formation and transfer of disulphide bonds in living cells.Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo.Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli.Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.

P2860

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P2860

An in vivo pathway for disulfide bond isomerization in Escherichia coli

http://www.wikidata.org/entity/Q36687328

description

1996 nî lūn-bûn

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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1996年论文

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1996年论文

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name

An in vivo pathway for disulfide bond isomerization in Escherichia coli

@ast

An in vivo pathway for disulfide bond isomerization in Escherichia coli

@en

type

label

An in vivo pathway for disulfide bond isomerization in Escherichia coli

@ast

An in vivo pathway for disulfide bond isomerization in Escherichia coli

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prefLabel

An in vivo pathway for disulfide bond isomerization in Escherichia coli

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An in vivo pathway for disulfide bond isomerization in Escherichia coli

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PNAS.93.23.13048

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An in vivo pathway for disulfide bond isomerization in Escherichia coli

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Beckwith J

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Belin D

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Martin N

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Rietsch A

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P2860

A pathway for disulfide bond formation in vivo

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli

The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library

Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA

Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.

Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH

Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids

Chromosomal transformation of Escherichia coli recD strains with linearized plasmids.

The ompA 5' untranslated RNA segment functions in Escherichia coli as a growth-rate-regulated mRNA stabilizer whose activity is unrelated to translational efficiency.

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13048-13053

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8917542

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Escherichia coli

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24044

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