| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M505453200 |
| P698 | PubMed publication ID | 16280324 |
| P2093 | author name string | George Georgiou | |
| Hiroshi Kadokura | |||
| Jon Beckwith | |||
| Laura Segatori | |||
| Lori Murphy | |||
| Hiram Gilbert | |||
| Silvia Arredondo | |||
| P2860 | cites work | Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli | Q27621623 |
| The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex | Q27639655 | ||
| Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter | Q27860697 | ||
| Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli | Q30981412 | ||
| On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily | Q33993677 | ||
| Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer | Q34019971 | ||
| Oxidative protein folding in bacteria | Q34124799 | ||
| Protein disulfide bond formation in prokaryotes | Q34169951 | ||
| The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. | Q34365141 | ||
| Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. | Q34828345 | ||
| Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm | Q35951953 | ||
| Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways | Q35970728 | ||
| Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli | Q37264681 | ||
| Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli | Q38363552 | ||
| Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. | Q39714839 | ||
| Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. | Q40788115 | ||
| 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 | ||
| Snapshots of DsbA in action: detection of proteins in the process of oxidative folding | Q44739250 | ||
| An engineered pathway for the formation of protein disulfide bonds | Q44771731 | ||
| In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. | Q46203577 | ||
| The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. | Q51555815 | ||
| Structure of DsbC from Haemophilus influenzae. | Q54500765 | ||
| P433 | issue | 8 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 4911-4919 | |
| P577 | publication date | 2005-11-09 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. | |
| P478 | volume | 281 |
| Q90592392 | C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning |
| Q48153150 | Conformational dynamics of Peb4 exhibit "mother's arms" chain model: a molecular dynamics study. |
| Q43244316 | De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC. |
| Q36353781 | Disulfide bond formation and ToxR activity in Vibrio cholerae |
| Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
| Q80877153 | Disulfide bond isomerization in prokaryotes |
| Q43637583 | Helicobacter pylori proteins response to nitric oxide stress |
| Q47387477 | How Are Proteins Reduced in the Endoplasmic Reticulum? |
| Q27649041 | Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase |
| Q30362756 | Laboratory evolution of one disulfide isomerase to resemble another |
| Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
| Q38574431 | Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway |
| Q36195204 | Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA. |
| Q36943800 | Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies |
| Q37433238 | Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC. |
| Q27677973 | Structural and Functional Characterization of ScsC, a Periplasmic Thioredoxin-Like Protein from Salmonella enterica Serovar Typhimurium |
| Q27680786 | The Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide Isomerase |
| Q36606739 | The origami of thioredoxin-like folds |
| Q35192535 | TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance. |
Search more.