The CXXC motif is more than a redox rheostat.

scientific article published on 3 August 2007

The CXXC motif is more than a redox rheostat. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M705291200
P698PubMed publication ID17675287
P5875ResearchGate publication ID6164681

P50authorShu QuanQ57462325
P2093author name stringJames C A Bardwell
Jonathan Pan
Irmhild Schneider
Annekathrin Von Hacht
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Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coliQ30981412
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The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.Q34365141
Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibriaQ34743720
Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coliQ36087470
Similarities and differences in the thioredoxin superfamilyQ36228435
The CXXC motif at the N terminus of an alpha-helical peptideQ36458569
The origami of thioredoxin-like foldsQ36606739
Thioredoxin-catalyzed refolding of disulfide-containing proteinsQ37402702
Dipoles localized at helix termini of proteins stabilize chargesQ37423541
Efficient catalysis of disulfide formation during protein folding with a single active-site cysteineQ38297474
Insertional inactivation of dsbA produces sensitivity to cadmium and zinc in Escherichia coliQ39845433
Biochemical effects of mercury, cadmium, and leadQ39924500
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.Q40788115
Disruption of the intracellular sulfhydryl homeostasis by cadmium-induced oxidative stress leads to protein thiolation and ubiquitination in neuronal cellsQ41040434
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.Q41846532
Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductasesQ42027032
Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrateQ42112518
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasmQ42271387
Redox state of cytoplasmic thioredoxinQ43920319
Reconstitution of a disulfide isomerization systemQ43988793
DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.Q44366662
Dimerization by domain hybridization bestows chaperone and isomerase activitiesQ44559355
Structural and functional relations among thioredoxins of different speciesQ44649576
Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiaeQ44919472
Steady-state and transient kinetic analyses of taurine/alpha-ketoglutarate dioxygenase: effects of oxygen concentration, alternative sulfonates, and active-site variants on the FeIV-oxo intermediateQ45307717
Protein folding activities of Escherichia coli protein disulfide isomeraseQ46312417
Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC.Q46640858
Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomeraseQ47628555
Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family.Q47630691
Different types of interactions involving cysteine sulfhydryl group in proteins.Q47821445
Why is DsbA such an oxidizing disulfide catalyst?Q48068494
Identification of a protein required for disulfide bond formation in vivoQ48201805
Kinetic characterization of the disulfide bond-forming enzyme DsbB.Q50706871
The CXXC motif: a rheostat in the active site.Q52267222
Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis.Q52539607
Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+.Q54096984
The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.Q54563918
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.Q54613834
P433issue39
P407language of work or nameEnglishQ1860
P304page(s)28823-28833
P577publication date2007-08-03
P1433published inJournal of Biological ChemistryQ867727
P1476titleThe CXXC motif is more than a redox rheostat
P478volume282

Reverse relations

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