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Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar TyphimuriumRv2969c, 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 oxidasesThe Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide IsomeraseCellular disulfide bond formation in bioactive peptides and proteinsRedox regulation by reversible protein S-thiolation in bacteriaThioredoxin-like protein TlpA from Bradyrhizobium japonicum is a reductant for the copper metallochaperone ScoIFunctional conservation of coenzyme Q biosynthetic genes among yeasts, plants, and humansVirtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbACharacterization of Francisella tularensis Schu S4 defined mutants as live-attenuated vaccine candidatesc-type cytochrome assembly in Saccharomyces cerevisiae: a key residue for apocytochrome c1/lyase interaction.Protein folding in the cell: challenges and progress.The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria.Resveratrol and para-coumarate serve as ring precursors for coenzyme Q biosynthesis.Modulation of biofilm-formation in Salmonella enterica serovar Typhimurium by the periplasmic DsbA/DsbB oxidoreductase system requires the GGDEF-EAL domain protein STM3615Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.Novel roles for protein disulphide isomerase in disease states: a double edged sword?Flocculation of Escherichia coli Cells in Association with Enhanced Production of Outer Membrane Vesicles.OspC is potent plasminogen receptor on surface of Borrelia burgdorferi.Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A.Microcin PDI regulation and proteolytic cleavage are unique among known microcins.Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Biosynthesis of coenzyme Q in eukaryotes.Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidases.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulumCysteine-rich low molecular weight antimicrobial peptides from Brevibacillus and related genera for biotechnological applications.Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.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.Functional and structural characterization of protein disulfide oxidoreductase from Thermus thermophilus HB27.The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of the Francisella tularensis dsbA Deletion Mutant.Development of a generic β-lactamase screening system for improved signal peptides for periplasmic targeting of recombinant proteins in Escherichia coli.Soluble expression of active recombinant human tissue plasminogen activator derivative (K2S) in Escherichia coli.Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories: production of human alpha-galactosidase A.Co-expression of Dsb proteins enables soluble expression of a single-chain variable fragment (scFv) against human type 1 insulin-like growth factor receptor (IGF-1R) in E. coli.Solid-Phase Organic Synthesis and Catalysis: Some Recent Strategies Using Alumina, Silica, and Polyionic Resins
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 29 June 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Disulfide bond formation system in Escherichia coli.
@en
Disulfide bond formation system in Escherichia coli.
@nl
type
label
Disulfide bond formation system in Escherichia coli.
@en
Disulfide bond formation system in Escherichia coli.
@nl
prefLabel
Disulfide bond formation system in Escherichia coli.
@en
Disulfide bond formation system in Escherichia coli.
@nl
P2860
P356
P1476
Disulfide bond formation system in Escherichia coli
@en
P2093
Kenji Inaba
P2860
P304
P356
10.1093/JB/MVP102
P50
P577
2009-06-29T00:00:00Z