Oxidation State-dependent Protein-Protein Interactions in Disulfide Cascades

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Oxidation State-dependent Protein-Protein Interactions in Disulfide Cascades is …
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P356DOI10.1074/JBC.M111.236141
P932PMC publication ID3137068
P698PubMed publication ID21543317

P50authorChristina RedfieldQ40991351
Alan D GoddardQ57165145
Paraskevi KritsiligkouQ58232639
Despoina A.I. MavridouQ61143134
Stuart J FergusonQ93073354
Julie M StevensQ123478217
P2093author name stringEmmanuel Saridakis
Despoina A I Mavridou
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Structural basis of Redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA.Q47871496
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High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study.Q53546796
Overproduction of CcmABCDEFGH restores cytochrome c maturation in a DsbD deletion strain of E. coli: another route for reductant?Q53633026
Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy.Q54440365
Kinetics of the intramolecular disulfide exchange between the periplasmic domains of DsbD.Q54446674
Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.Q54451866
Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal beta-sheet and the fingerprint region.Q54454409
Nitrite and ammonia assimilation by anaerobic continuous cultures of Escherichia coliQ70054581
Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxinQ70155193
Generation of a Membrane Potential by One of Two Independent Pathways for Nitrite Reduction by Escherichia coliQ72933077
Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to functionQ73665019
Disulfide bond isomerization in prokaryotesQ80877153
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Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbDQ27639041
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Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serineQ27640398
Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)Q27641276
Solution structure and dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidisQ27651317
Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbBQ27653763
The Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA EnzymesQ27655136
Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar TyphimuriumQ27660252
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Protein production by auto-induction in high density shaking culturesQ27860514
Satisfying hydrogen bonding potential in proteinsQ27860940
Refinement of macromolecular structures by the maximum-likelihood methodQ27861011
Novel Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromesQ30832647
Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascadeQ33927908
Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coliQ33936557
Protein disulfide bond formation in prokaryotesQ34169951
Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturationQ34446362
The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductasesQ35893668
Pathways of disulfide bond formation in Escherichia coliQ36381634
nDsbD: a redox interaction hub in the Escherichia coli periplasmQ36512199
The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domainQ36688584
The name's bond......disulfide bondQ36969452
Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine.Q37033153
Thioredoxins and glutaredoxins as facilitators of protein folding.Q37106759
The disulfide bond formation (Dsb) systemQ37136271
The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisitedQ37142505
DSB proteins and bacterial pathogenicity.Q37386934
Disulfide formation in the ER and mitochondria: two solutions to a common process.Q37508527
Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathwayQ38574431
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.Q40788115
P433issue28
P407language of work or nameEnglishQ1860
P921main subjectcell biologyQ7141
protein-protein interactionQ896177
P304page(s)24943-56
P577publication date2011-07-15
P1433published inJournal of Biological ChemistryQ867727
P1476titleOxidation State-dependent Protein-Protein Interactions in Disulfide Cascades
P478volume286