Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
about
NMR structures of membrane proteins in phospholipid bilayersProperties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid ResidueDynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbBStructure of a bacterial homologue of vitamin K epoxide reductaseHigh-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental dataStructure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid BilayerRv2969c, 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 oxidasesComparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct ClassesCrystal Structure of the Dithiol Oxidase DsbA Enzyme from Proteus Mirabilis Bound Non-covalently to an Active Site Peptide LigandVirtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbAStructures of membrane proteins.The Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053.Disulfide bond formation in prokaryotes: history, diversity and designAssignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA.Food Reformulation, Responsive Regulation, and "Regulatory Scaffolding": Strengthening Performance of Salt Reduction Programs in Australia and the United KingdomThioredoxin-like proteins in F and other plasmid systemsDisulfide bond formation system in Escherichia coli.Mechanisms of oxidative protein folding in the bacterial cell envelope.Phylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family.A new on-axis multimode spectrometer for the macromolecular crystallography beamlines of the Swiss Light Source.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.
P2860
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P2860
Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@ast
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@en
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@nl
type
label
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@ast
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@en
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@nl
prefLabel
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@ast
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@en
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@nl
P2093
P2860
P1433
P1476
Preparation and structure of t ...... nsmembrane redox catalyst DsbB
@en
P2093
Goran Malojcić
John P A Grimshaw
Robin L Owen
P2860
P304
P356
10.1016/J.FEBSLET.2008.07.063
P407
P577
2008-10-15T00:00:00Z