In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG

scientific article published on 01 March 1999

In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.274.12.7784
P698PubMed publication ID10075670

P2093author name stringG Georgiou
H F Gilbert
P H Bessette
J J Cotto
P2860cites workGapped BLAST and PSI-BLAST: a new generation of protein database search programsQ24545170
The complete genome sequence of Escherichia coli K-12Q27860542
Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox bufferQ34019971
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.Q34365141
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Q34444511
Protein folding in the bacterial periplasmQ35621918
Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulationQ35970767
In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT.Q36157575
Chromosomal transformation of Escherichia coli recD strains with linearized plasmids.Q36177080
Mutation of conserved residues in Escherichia coli thioredoxin: Effects on stability and functionQ36277627
Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cellsQ36622135
An in vivo pathway for disulfide bond isomerization in Escherichia coliQ36687328
A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteinsQ36893186
Leaderless polypeptides efficiently extracted from whole cells by osmotic shockQ39846925
Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperatureQ39948895
Protein folding in the periplasm of Escherichia coliQ40683971
Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structureQ41230313
Protein misfolding in the cell envelope of Escherichia coli: new signaling pathwaysQ41361800
Making and breaking disulfide bondsQ41620623
Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomeraseQ42156942
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coliQ42843291
Kinetic analysis of the folding and unfolding of a mutant form of bovine pancreatic trypsin inhibitor lacking the cysteine-14 and -38 thiolsQ44379877
In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.Q46203577
Protein folding activities of Escherichia coli protein disulfide isomeraseQ46312417
Paracoccus denitrificans CcmG is a periplasmic protein-disulphide oxidoreductase required for c- and aa3-type cytochrome biogenesis; evidence for a reductase role in vivoQ48049000
Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds.Q52524766
Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds.Q54588808
Redox states of DsbA in the periplasm of Escherichia coli.Q54612842
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.Q54613834
A plasmid expression vector that permits stabilization of both mRNAs and proteins encoded by the cloned genes.Q54787854
Protein foldingQ68539600
Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromesQ73039144
Disulfide bond catalysts in Escherichia coliQ74420339
Reconstitution of a protein disulfide catalytic systemQ74465528
P433issue12
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)7784-7792
P577publication date1999-03-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleIn vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
P478volume274

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cites work (P2860)
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