scholarly article | Q13442814 |
P50 | author | Mamoru Suzuki | Q42293247 |
Satoshi Murakami | Q42779584 | ||
Atsushi Nakagawa | Q47163973 | ||
Kenji Inaba | Q62757053 | ||
P2093 | author name string | Koreaki Ito | |
Hiroka Iida | |||
Mai Kinjo | |||
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 | ||
Improved methods for building protein models in electron density maps and the location of errors in these models | Q26776980 | ||
Processing of X-ray diffraction data collected in oscillation mode | Q26778468 | ||
Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB | Q27652023 | ||
NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation | Q27652518 | ||
Conformational transition of Sec machinery inferred from bacterial SecYE structures | Q27652527 | ||
Coot: model-building tools for molecular graphics | Q27860505 | ||
The CCP4 suite: programs for protein crystallography | Q27861090 | ||
Formation and transfer of disulphide bonds in living cells | Q34157680 | ||
Protein disulfide bond formation in prokaryotes | Q34169951 | ||
Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB. | Q34246180 | ||
Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility | Q35941498 | ||
Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells | Q36622135 | ||
The name's bond......disulfide bond | Q36969452 | ||
Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine. | Q37033153 | ||
The disulfide bond formation (Dsb) system | Q37136271 | ||
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 | ||
Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway | Q38574431 | ||
Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway | Q42668332 | ||
DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. | Q44366662 | ||
Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli. | Q45044166 | ||
Reactivities of quinone-free DsbB from Escherichia coli | Q46606780 | ||
Why is DsbA such an oxidizing disulfide catalyst? | Q48068494 | ||
Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria | Q48156777 | ||
Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex. | Q53618251 | ||
Environment of the active site region of RseP, an Escherichia coli regulated intramembrane proteolysis protease, assessed by site-directed cysteine alkylation | Q54450004 | ||
Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation | Q54451866 | ||
Partial (13)C and (15)N chemical-shift assignments of the disulfide-bond-forming enzyme DsbB by 3D magic-angle spinning NMR spectroscopy | Q57098944 | ||
Disulfide bonds are generated by quinone reduction | Q73897313 | ||
P433 | issue | 6 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | crystal structure | Q895901 |
P304 | page(s) | 779-91 | |
P577 | publication date | 2009-03-18 | |
P1433 | published in | The EMBO Journal | Q1278554 |
P1476 | title | Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB | |
P478 | volume | 28 |
Q36479175 | A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis. |
Q33892804 | Assignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA. |
Q39665863 | Campylobacter protein oxidation influences epithelial cell invasion or intracellular survival as well as intestinal tract colonization in chickens. |
Q48139731 | Chemistry and Enzymology of Disulfide Cross-Linking in Proteins. |
Q27680624 | Comparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct Classes |
Q47433501 | Comparison of NMR and crystal structures of membrane proteins and computational refinement to improve model quality |
Q27683799 | Crystal Structure of the Dithiol Oxidase DsbA Enzyme from Proteus Mirabilis Bound Non-covalently to an Active Site Peptide Ligand |
Q30406181 | Crystallization chaperone strategies for membrane proteins |
Q34323819 | Cytochrome c assembly. |
Q27679294 | Disarming Burkholderia pseudomallei : Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In Vivo |
Q49788752 | Disulfide bond formation in prokaryotes |
Q33723782 | Disulfide bond formation in prokaryotes: history, diversity and design |
Q38001127 | Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals. |
Q37536471 | Disulfide bond formation system in Escherichia coli. |
Q92945212 | Entropy-Driven Mechanisms between Disulfide-Bond Formation Protein A (DsbA) and B (DsbB) in Escherichia coli |
Q34991338 | Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases |
Q27666760 | Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy |
Q35894964 | Food Reformulation, Responsive Regulation, and "Regulatory Scaffolding": Strengthening Performance of Salt Reduction Programs in Australia and the United Kingdom |
Q37596401 | Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidase |
Q37281453 | Helical membrane protein conformations and their environment |
Q38979654 | Heterogeneous dielectric generalized Born model with a van der Waals term provides improved association energetics of membrane-embedded transmembrane helices |
Q27674386 | High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data |
Q90577503 | Inhibition of Pseudomonas aeruginosa and Mycobacterium tuberculosis disulfide bond forming enzymes |
Q36289066 | Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions |
Q47610685 | Intramembrane Thiol Oxidoreductases: Evolutionary Convergence and Structural Controversy. |
Q33743375 | Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes |
Q37724253 | Mechanisms of oxidative protein folding in the bacterial cell envelope |
Q27006900 | NMR structures of membrane proteins in phospholipid bilayers |
Q38098314 | New concepts and aids to facilitate crystallization |
Q27667688 | Oxidation State-dependent Protein-Protein Interactions in Disulfide Cascades |
Q38472604 | Oxidative folding: recent developments |
Q40673326 | Phylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family |
Q34056994 | Reversible Covalent Chemistries Compatible with the Principles of Constitutional Dynamic Chemistry: New Reactions to Create More Diversity |
Q35010550 | Solid-state NMR study of the charge-transfer complex between ubiquinone-8 and disulfide bond generating membrane protein DsbB |
Q27659264 | Structure of a bacterial homologue of vitamin K epoxide reductase |
Q27676407 | Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer |
Q27681521 | Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer |
Q30391943 | Structures of membrane proteins |
Q30396232 | Systematic evaluation of CS-Rosetta for membrane protein structure prediction with sparse NOE restraints |
Q41767891 | The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli |
Q35055321 | The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria. |
Q28546904 | Virtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbA |
Q47287209 | Vitamin K epoxide reductase and its paralogous enzyme have different structures and functions |
Search more.