| scholarly article | Q13442814 |
| P2093 | author name string | J Qiu | |
| J C Bardwell | |||
| G Georgiou | |||
| J R Swartz | |||
| P H Bessette | |||
| P2860 | cites work | Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli | Q78177288 |
| A pathway for disulfide bond formation in vivo | Q24563594 | ||
| Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm | Q24644906 | ||
| Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter | Q27860697 | ||
| Random circular permutation of DsbA reveals segments that are essential for protein folding and stability | Q30648508 | ||
| An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins | Q33557662 | ||
| On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily | Q33993677 | ||
| The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. | Q34365141 | ||
| Determinants of membrane protein topology | Q34372343 | ||
| Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. | Q34444511 | ||
| A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery | Q35692775 | ||
| In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT. | Q36157575 | ||
| Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator | Q36423135 | ||
| An in vivo pathway for disulfide bond isomerization in Escherichia coli | Q36687328 | ||
| Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity | Q37631345 | ||
| Use of the rep technique for allele replacement to construct new Escherichia coli hosts for maintenance of R6K gamma origin plasmids at different copy numbers | Q38311874 | ||
| Expression of active human tissue-type plasminogen activator in Escherichia coli. | Q39479612 | ||
| Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA. | Q39840357 | ||
| The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. | Q41065191 | ||
| Making and breaking disulfide bonds | Q41620623 | ||
| Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases | Q42027032 | ||
| 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 properties of protein disulfide isomerase (DsbA) from Escherichia coli | Q42843291 | ||
| In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. | Q46203577 | ||
| Protein folding activities of Escherichia coli protein disulfide isomerase | Q46312417 | ||
| Why is DsbA such an oxidizing disulfide catalyst? | Q48068494 | ||
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
| The CXXC motif: a rheostat in the active site. | Q52267222 | ||
| Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds. | Q54588808 | ||
| Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. | Q54613834 | ||
| The folding of bovine pancreatic trypsin inhibitor in the Escherichia coli periplasm. | Q54628637 | ||
| Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin. | Q54633635 | ||
| A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease | Q54679075 | ||
| A plasmid expression vector that permits stabilization of both mRNAs and proteins encoded by the cloned genes. | Q54787854 | ||
| Mutagenic studies on human protein disulfide isomerase by complementation of Escherichia coli dsbA and dsbC mutants | Q63363483 | ||
| Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and φ80 transducing phages | Q66900225 | ||
| Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin | Q70155193 | ||
| Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH | Q72551904 | ||
| Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase | Q73236000 | ||
| A single dipeptide sequence modulates the redox properties of a whole enzyme family | Q74486160 | ||
| In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG | Q74602402 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Escherichia coli | Q25419 |
| protein folding | Q847556 | ||
| P304 | page(s) | 980-988 | |
| P577 | publication date | 2001-02-01 | |
| P1433 | published in | Journal of Bacteriology | Q478419 |
| P1476 | title | Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli | |
| P478 | volume | 183 |
| Q47111875 | A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo |
| Q44980469 | Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome |
| Q35074321 | Analysis of the isomerase and chaperone-like activities of an amebic PDI (EhPDI). |
| Q90592392 | C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning |
| Q47635000 | Cell-free metabolic engineering promotes high-level production of bioactive Gaussia princeps luciferase |
| Q30277068 | Components of the type six secretion system are substrates of Francisella tularensis Schu S4 DsbA-like FipB protein |
| Q41456212 | Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. |
| Q30746401 | Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding |
| Q80877153 | Disulfide bond isomerization in prokaryotes |
| Q26773784 | Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |
| Q44260052 | DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo |
| Q35970728 | Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways |
| Q39479612 | Expression of active human tissue-type plasminogen activator in Escherichia coli. |
| Q40702083 | F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues |
| Q30406080 | FipB, an essential virulence factor of Francisella tularensis subsp. tularensis, has dual roles in disulfide bond formation |
| Q42594830 | Functional similarities of a thermostable protein-disulfide oxidoreductase identified in the archaeon Pyrococcus horikoshii to bacterial DsbA enzymes |
| Q40469171 | Genetic analysis of disulfide isomerization in Escherichia coli: expression of DsbC is modulated by RNase E-dependent mRNA processing |
| Q42150654 | Improved detection of domoic acid using covalently immobilised antibody fragments |
| Q46899985 | Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. |
| Q30350105 | Mutational analysis of the disulfide catalysts DsbA and DsbB. |
| Q29248355 | Origin of anti-tumor activity of the cysteine-containing GO peptides and further optimization of their cytotoxic properties |
| Q34598013 | Recombinant protein expression for therapeutic applications |
| Q27680167 | Rv2969c, essential for optimal growth inMycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases |
| Q36478560 | SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm |
| Q27683945 | Structure of the Acinetobacter baumannii Dithiol Oxidase DsbA Bound to Elongation Factor EF-Tu Reveals a Novel Protein Interaction Site |
| Q54436865 | The CXXC motif is more than a redox rheostat. |
| Q27680786 | The Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide Isomerase |
| Q27639655 | The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex |
| Q36909442 | The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis. |
| Q42150785 | Transcriptional regulation of the Escherichia coli gene rraB, encoding a protein inhibitor of RNase E. |
| Q40718297 | Twin-arginine translocation of active human tissue plasminogen activator in Escherichia coli |
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