Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.

scientific article published on June 2002

Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1093/EMBOJ/21.11.2646
P932PMC publication ID126043
P698PubMed publication ID12032077
P5875ResearchGate publication ID11340593

P50authorKenji InabaQ62757053
P2093author name stringKoreaki Ito
P2860cites workA pathway for disulfide bond formation in vivoQ24563594
Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formationQ24568243
A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formationQ27940305
Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbAQ33877973
Biochemical basis of oxidative protein folding in the endoplasmic reticulumQ33926107
Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascadeQ33927908
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzymeQ33937247
In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene productQ33972024
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Q34444511
Protein folding in the bacterial periplasmQ35621918
Mitochondria can import artificial precursor proteins containing a branched polypeptide chain or a carboxy-terminal stilbene disulfonateQ36220983
Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivoQ36450266
Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida. A new iron to subunit stoichiometryQ36596004
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
Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coliQ37264681
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.Q38289355
The essential function of yeast protein disulfide isomerase does not reside in its isomerase activityQ38316136
Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathwayQ42668332
Identification of a segment of DsbB essential for its respiration-coupled oxidationQ43512860
Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B.Q43792245
Why is DsbA such an oxidizing disulfide catalyst?Q48068494
Identification of a protein required for disulfide bond formation in vivoQ48201805
Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds.Q52524766
Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli.Q54154827
Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli.Q54593983
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
Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.Q54633635
The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form.Q54649633
DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbAQ71891832
Involvement of two sulfur atoms of protein disulfide isomerase and one sulfur atom of the DsbA/PpfA protein in the oxidation of mutant human lysozymeQ72772847
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulumQ73151253
Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasmQ73537525
Disulfide bonds are generated by quinone reductionQ73897313
Reconstitution of a protein disulfide catalytic systemQ74465528
A single dipeptide sequence modulates the redox properties of a whole enzyme familyQ74486160
Oxidative protein folding is driven by the electron transport systemQ78066764
P433issue11
P407language of work or nameEnglishQ1860
P304page(s)2646-2654
P577publication date2002-06-01
P1433published inThe EMBO JournalQ1278554
P1476titleParadoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade
P478volume21

Reverse relations

cites work (P2860)
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