| scholarly article | Q13442814 |
| P2093 | author name string | Glockshuber R | |
| Huber-Wunderlich M | |||
| Jonda S | |||
| Mössner E | |||
| P2860 | cites work | A pathway for disulfide bond formation in vivo | Q24563594 |
| Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution | Q27671419 | ||
| Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy | Q27732861 | ||
| Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant | Q27747603 | ||
| Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization | Q27760300 | ||
| The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum | Q27936188 | ||
| Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum | Q27939552 | ||
| Thioredoxin--a fold for all reasons | Q29618984 | ||
| Oxidized redox state of glutathione in the endoplasmic reticulum | Q29619789 | ||
| Random circular permutation of DsbA reveals segments that are essential for protein folding and stability | Q30648508 | ||
| The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm | Q33551316 | ||
| The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo | Q33728264 | ||
| Pedigrees of some mutant strains of Escherichia coli K-12 | Q33851231 | ||
| Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA | Q33877973 | ||
| In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product | Q33972024 | ||
| 2 Thiol/disulfide exchange equilibria and disulfidebond stability | Q34303407 | ||
| The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. | Q34365141 | ||
| Molecular and cellular aspects of thiol-disulfide exchange. | Q34373608 | ||
| Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. | Q34444511 | ||
| Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria | Q34743720 | ||
| Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli | Q36087470 | ||
| Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells | Q36622135 | ||
| An in vivo pathway for disulfide bond isomerization in Escherichia coli | Q36687328 | ||
| Thioredoxin-catalyzed refolding of disulfide-containing proteins | Q37402702 | ||
| The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation | Q37631360 | ||
| Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine | Q38297474 | ||
| The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. | Q41065191 | ||
| Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure | Q41230313 | ||
| Making and breaking disulfide bonds | Q41620623 | ||
| Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases | Q42027032 | ||
| Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum | Q42151080 | ||
| Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli | Q42843291 | ||
| Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase | Q47628555 | ||
| The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli | Q47881156 | ||
| Homologous regions of the Salmonella enteritidis virulence plasmid and the chromosome of Salmonella typhi encode thiol: disulphide oxidoreductases belonging to the DsbA thioredoxin family | Q48051630 | ||
| Why is DsbA such an oxidizing disulfide catalyst? | Q48068494 | ||
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
| Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. | Q52393403 | ||
| Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties. | Q54559625 | ||
| Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds. | Q54588808 | ||
| Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. | Q54593983 | ||
| Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. | Q54598121 | ||
| Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli. | Q54599822 | ||
| Redox states of DsbA in the periplasm of Escherichia coli. | Q54612842 | ||
| Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. | Q54613834 | ||
| Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin. | Q54633635 | ||
| Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. | Q54646876 | ||
| Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli. | Q54750197 | ||
| The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules | Q57077650 | ||
| Production of Rat Protein Disulfide Isomerase in Saccharomyces cerevisiae | Q57961225 | ||
| Contributions of substrate binding to the catalytic activity of DsbC. | Q64974634 | ||
| Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin | Q70155193 | ||
| Thioredoxin and thioredoxin reductase | Q71521704 | ||
| Localization of thioredoxin from Escherichia coli in an osmotically sensitive compartment | Q71619969 | ||
| Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase | Q71715190 | ||
| DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA | Q71891832 | ||
| Protein disulfide-isomerase | Q71999770 | ||
| In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA) | Q72102596 | ||
| Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH | Q72551904 | ||
| Reconstitution of a protein disulfide catalytic system | Q74465528 | ||
| A single dipeptide sequence modulates the redox properties of a whole enzyme family | Q74486160 | ||
| Release of thioredoxin via the mechanosensitive channel MscL during osmotic downshock of Escherichia coli cells | Q77359794 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| P433 | issue | 12 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | protein folding | Q847556 |
| P304 | page(s) | 3271-3281 | |
| P577 | publication date | 1999-06-01 | |
| P1433 | published in | The EMBO Journal | Q1278554 |
| P1476 | title | 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 | |
| P478 | volume | 18 |
| Q34245202 | A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo |
| Q36747183 | Analysis of type II secretion of recombinant pneumococcal PspA and PspC in a Salmonella enterica serovar Typhimurium vaccine with regulated delayed antigen synthesis |
| Q34545621 | Catalysis of disulfide bond formation and isomerization in Escherichia coli |
| Q39275666 | Cloning of Soluble Human Stem Cell Factor in pET-26b(+) Vector |
| Q41456212 | Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. |
| Q43244316 | De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC. |
| Q57833448 | Determinants of Translocation and Folding of TreF, a Trehalase ofEscherichia coli |
| Q37083585 | Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm |
| Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
| Q54550138 | Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat. |
| Q73897313 | Disulfide bonds are generated by quinone reduction |
| Q22253168 | ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum |
| Q28243986 | ERp57 is a multifunctional thiol-disulfide oxidoreductase |
| Q30981412 | Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli |
| Q24644906 | Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm |
| Q33760255 | Electron avenue: pathways of disulfide bond formation and isomerization |
| Q35970728 | Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways |
| Q33840728 | Enzymes that catalyse the restructuring of proteins |
| Q40702083 | F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues |
| Q35236867 | Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA. |
| Q27666964 | Genetic selection designed to stabilize proteins uncovers a chaperone called Spy |
| Q37596401 | Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidase |
| Q37486247 | Human augmenter of liver regeneration: probing the catalytic mechanism of a flavin-dependent sulfhydryl oxidase |
| Q40447079 | Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms |
| Q78177288 | Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli |
| Q31613031 | Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA. |
| Q34269611 | Isolation and characterization of a novel human thioredoxin-like gene hTLP19 encoding a secretory protein. |
| Q46899985 | Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. |
| Q33342755 | Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control |
| Q28754640 | MTH1745, a protein disulfide isomerase-like protein from thermophilic archaea, Methanothermobacter thermoautotrophicum involving in stress response |
| Q35160295 | Mechanism of the electron transfer catalyst DsbB from Escherichia coli |
| 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 |
| Q34046362 | Native disulfide bond formation in proteins |
| Q33993677 | On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily |
| Q36195204 | Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA. |
| Q27653607 | Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue |
| Q38363552 | Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli |
| Q37433238 | Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC. |
| Q27635911 | Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein |
| Q33249034 | Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display |
| Q30377057 | Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. |
| Q54436865 | The CXXC motif is more than a redox rheostat. |
| Q39887818 | The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway |
| Q39714839 | Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. |
| Q42723141 | Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation |
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