scholarly article | Q13442814 |
P50 | author | Shu Quan | Q57462325 |
P2093 | author name string | James C A Bardwell | |
Jonathan Pan | |||
Irmhild Schneider | |||
Annekathrin Von Hacht | |||
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Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate | Q42112518 | ||
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm | Q42271387 | ||
Redox state of cytoplasmic thioredoxin | Q43920319 | ||
Reconstitution of a disulfide isomerization system | Q43988793 | ||
DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. | Q44366662 | ||
Dimerization by domain hybridization bestows chaperone and isomerase activities | Q44559355 | ||
Structural and functional relations among thioredoxins of different species | Q44649576 | ||
Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae | Q44919472 | ||
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 intermediate | Q45307717 | ||
Protein folding activities of Escherichia coli protein disulfide isomerase | Q46312417 | ||
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 isomerase | Q47628555 | ||
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 vivo | Q48201805 | ||
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 | ||
P433 | issue | 39 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 28823-28833 | |
P577 | publication date | 2007-08-03 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | The CXXC motif is more than a redox rheostat | |
P478 | volume | 282 |
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