scholarly article | Q13442814 |
P50 | author | Kenji Inaba | Q62757053 |
P2093 | author name string | Koreaki Ito | |
P2860 | cites work | A pathway for disulfide bond formation in vivo | Q24563594 |
Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation | Q24568243 | ||
A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation | Q27940305 | ||
Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA | Q33877973 | ||
Biochemical basis of oxidative protein folding in the endoplasmic reticulum | Q33926107 | ||
Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade | Q33927908 | ||
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme | Q33937247 | ||
In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product | Q33972024 | ||
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. | Q34444511 | ||
Protein folding in the bacterial periplasm | Q35621918 | ||
Mitochondria can import artificial precursor proteins containing a branched polypeptide chain or a carboxy-terminal stilbene disulfonate | Q36220983 | ||
Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo | Q36450266 | ||
Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida. A new iron to subunit stoichiometry | Q36596004 | ||
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 | ||
Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli | Q37264681 | ||
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. | Q38289355 | ||
The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity | Q38316136 | ||
Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway | Q42668332 | ||
Identification of a segment of DsbB essential for its respiration-coupled oxidation | Q43512860 | ||
Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. | Q43792245 | ||
Why is DsbA such an oxidizing disulfide catalyst? | Q48068494 | ||
Identification of a protein required for disulfide bond formation in vivo | Q48201805 | ||
Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. | Q52524766 | ||
Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. | Q54154827 | ||
Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. | Q54593983 | ||
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 | ||
The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form. | Q54649633 | ||
DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA | Q71891832 | ||
Involvement of two sulfur atoms of protein disulfide isomerase and one sulfur atom of the DsbA/PpfA protein in the oxidation of mutant human lysozyme | Q72772847 | ||
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum | Q73151253 | ||
Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm | Q73537525 | ||
Disulfide bonds are generated by quinone reduction | Q73897313 | ||
Reconstitution of a protein disulfide catalytic system | Q74465528 | ||
A single dipeptide sequence modulates the redox properties of a whole enzyme family | Q74486160 | ||
Oxidative protein folding is driven by the electron transport system | Q78066764 | ||
P433 | issue | 11 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 2646-2654 | |
P577 | publication date | 2002-06-01 | |
P1433 | published in | The EMBO Journal | Q1278554 |
P1476 | title | Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade | |
P478 | volume | 21 |
Q28484215 | A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein |
Q27646618 | A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c |
Q47111875 | A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo |
Q39249324 | An Arabidopsis glutathione peroxidase functions as both a redox transducer and a scavenger in abscisic acid and drought stress responses |
Q30411815 | Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB |
Q33892804 | Assignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA. |
Q45044166 | Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli. |
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 |
Q26773784 | Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria |
Q44366662 | DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. |
Q92945212 | Entropy-Driven Mechanisms between Disulfide-Bond Formation Protein A (DsbA) and B (DsbB) in Escherichia coli |
Q36914442 | Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis |
Q34157680 | Formation and transfer of disulphide bonds in living cells |
Q36133918 | Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain |
Q55238554 | Functionalized Nano-adsorbent for Affinity Separation of Proteins. |
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 |
Q91903544 | Identification of Redox Partners of the Thiol-Disulfide Oxidoreductase SdbA in Streptococcus gordonii |
Q41714764 | Identification of two forms of Q{beta} replicase with different thermal stabilities but identical RNA replication activity. |
Q50706871 | Kinetic characterization of the disulfide bond-forming enzyme DsbB. |
Q47366634 | Mathematically combined half-cell reduction potentials of low-molecular-weight thiols as markers of seed ageing |
Q35160295 | Mechanism of the electron transfer catalyst DsbB from Escherichia coli |
Q38574431 | Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway |
Q27863341 | NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family |
Q90178754 | Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development |
Q38606615 | Protein disulfide bond generation in Escherichia coli DsbB-DsbA. |
Q46606780 | Reactivities of quinone-free DsbB from Escherichia coli |
Q42133067 | Real-time monitoring of intermediates reveals the reaction pathway in the thiol-disulfide exchange between disulfide bond formation protein A (DsbA) and B (DsbB) on a membrane-immobilized quartz crystal microbalance (QCM) system. |
Q44365527 | Reconstitution of membrane proteolysis by FtsH. |
Q35010550 | Solid-state NMR study of the charge-transfer complex between ubiquinone-8 and disulfide bond generating membrane protein DsbB |
Q27677973 | Structural and Functional Characterization of ScsC, a Periplasmic Thioredoxin-Like Protein from Salmonella enterica Serovar Typhimurium |
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Q27676407 | Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer |
Q41882010 | Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant |
Q27682316 | The 1.2 Å resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production |
Q36458569 | The CXXC motif at the N terminus of an alpha-helical peptide |
Q89830930 | The MsrAB reducing pathway of Streptococcus gordonii is needed for oxidative stress tolerance, biofilm formation, and oral colonization in mice |
Q27680786 | The Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide Isomerase |
Q63740805 | The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase |
Q41884481 | The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases |
Q35055321 | The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria. |
Q34476988 | Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme |
Q35192535 | TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance. |
Q41434914 | Ubiquinone and menaquinone electron carriers represent the yin and yang in the redox regulation of the ArcB sensor kinase. |
Q39860236 | YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA. |
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