| scholarly article | Q13442814 |
| P2093 | author name string | G Jander | |
| J Beckwith | |||
| N L Martin | |||
| P2860 | cites work | The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds | Q70403083 |
| Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds | Q71368922 | ||
| A pathway for disulfide bond formation in vivo | Q24563594 | ||
| Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 | Q25938983 | ||
| Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule | Q29616679 | ||
| Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase | Q30369923 | ||
| Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae | Q33613621 | ||
| Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme | Q33937247 | ||
| The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself | Q33960682 | ||
| Positively charged amino acid residues can act as topogenic determinants in membrane proteins | Q34323545 | ||
| Evolutionary conservation among biotin enzymes. | Q34560204 | ||
| Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions | Q35966566 | ||
| Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli | Q36087470 | ||
| Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo | Q36450266 | ||
| A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd | Q37273291 | ||
| TnphoA: a transposon probe for protein export signals | Q37557281 | ||
| Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins | Q38274381 | ||
| The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity | Q38316136 | ||
| Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides | Q39665725 | ||
| Experimental studies of protein folding and unfolding | Q39772419 | ||
| Simple, rapid, and quantitative release of periplasmic proteins by chloroform | Q39969842 | ||
| The bonds that tie: catalyzed disulfide bond formation | Q40848083 | ||
| The topological analysis of integral cytoplasmic membrane proteins | Q40890215 | ||
| A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae | Q42599846 | ||
| Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
| Nucleotide sequence of a regulatory region controlling alginate synthesis in Pseudomonas aeruginosa: characterization of the algR2 gene | Q48281135 | ||
| The prediction of transmembrane protein sequences and their conformation: an evaluation. | Q52493577 | ||
| Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme | Q54607526 | ||
| A genetic approach to analyzing membrane protein topology. | Q54775339 | ||
| Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and φ80 transducing phages | Q66900225 | ||
| Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins | Q67298135 | ||
| Catalysis of thiol/disulfide exchange: single-turnover reduction of protein disulfide-isomerase by glutathione and catalysis of peptide disulfide reduction | Q69804770 | ||
| P433 | issue | 21 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | membrane protein | Q423042 |
| P304 | page(s) | 5121-7 | |
| P577 | publication date | 1994-11-01 | |
| P1433 | published in | The EMBO Journal | Q1278554 |
| P1476 | title | Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation | |
| P478 | volume | 13 |
| Q36479175 | A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis. |
| Q47111875 | A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo |
| Q30411815 | Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB |
| Q90592392 | C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning |
| Q34067229 | Complete pathway for protein disulfide bond formation encoded by poxviruses |
| Q34246180 | Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB. |
| Q33712972 | Disulfide bond formation involves a quinhydrone-type charge–transfer complex |
| Q80877153 | Disulfide bond isomerization in prokaryotes |
| Q33932871 | DsbC activation by the N-terminal domain of DsbD. |
| Q27653763 | Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB |
| Q92945212 | Entropy-Driven Mechanisms between Disulfide-Bond Formation Protein A (DsbA) and B (DsbB) in Escherichia coli |
| Q33877973 | Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA |
| Q40702083 | F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues |
| Q38289355 | Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. |
| Q92180501 | Four thiol-oxidoreductases involved in the formation of disulphide bonds in the Streptomyces lividans TK21 secretory proteins |
| Q37638014 | Identification of Extracellular Segments by Mass Spectrometry Improves Topology Prediction of Transmembrane Proteins. |
| Q48065316 | Intron position as an evolutionary marker of thioredoxins and thioredoxin domains |
| Q35160295 | Mechanism of the electron transfer catalyst DsbB from Escherichia coli |
| Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
| Q34700221 | Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase |
| Q38574431 | Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway |
| Q40943090 | Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily |
| Q30350105 | Mutational analysis of the disulfide catalysts DsbA and DsbB. |
| Q39678300 | Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells |
| Q35635177 | Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells |
| Q35970767 | Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation |
| Q90178754 | Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development |
| Q39647375 | Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. |
| Q35621918 | Protein folding in the bacterial periplasm |
| Q36622135 | Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells |
| Q42668332 | Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway |
| Q37264681 | Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli |
| Q30377057 | Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli. |
| Q39826392 | The dsbB gene product is required for protease production by Burkholderia cepacia |
| Q41884481 | The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases |
| Q41883518 | The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding |
| Q35942715 | Transcriptional regulation of the assT-dsbL-dsbI gene cluster in Salmonella enterica serovar Typhi IMSS-1 depends on LeuO, H-NS, and specific growth conditions. |
| Q24550637 | Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum |
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