Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli.
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Siderophore-based iron acquisition and pathogen controlThe v-myc-induced Q83 Lipocalin Is a SiderocalinA copper-activated two-component system interacts with zinc and imipenem resistance in Pseudomonas aeruginosaDifferential gene regulation in the Ag nanoparticle and Ag(+)-induced silver stress response in Escherichia coli: a full transcriptomic profile.Genome sequence of Synechococcus CC9311: Insights into adaptation to a coastal environmentCopper complexation screen reveals compounds with potent antibiotic properties against methicillin-resistant Staphylococcus aureus.The multi-copper-ion oxidase CueO of Salmonella enterica serovar Typhimurium is required for systemic virulence.Identification of a Salmonella ancillary copper detoxification mechanism by a comparative analysis of the genome-wide transcriptional response to copper and zinc excess.The copper-inducible ComR (YcfQ) repressor regulates expression of ComC (YcfR), which affects copper permeability of the outer membrane of Escherichia coli.Survival and growth in the presence of elevated copper: transcriptional profiling of copper-stressed Pseudomonas aeruginosa.Beyond iron: non-classical biological functions of bacterial siderophoresDraft Genome Sequence of Microbacterium profundi Shh49T, an Actinobacterium Isolated from Deep-Sea Sediment of a Polymetallic Nodule Environment.Microbial Copper-binding Siderophores at the Host-Pathogen InterfaceCopper homeostasis at the host-pathogen interfaceThe siderophore yersiniabactin binds copper to protect pathogens during infection.Methanobactin and the Link between Copper and Bacterial Methane OxidationTrade-off between iron uptake and protection against oxidative stress: deletion of cueO promotes uropathogenic Escherichia coli virulence in a mouse model of urinary tract infectionA multicopper oxidase is required for copper resistance in Mycobacterium tuberculosisShotgun proteomic analysis of Yersinia ruckeri strains under normal and iron-limited conditionsIron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence.Cuprous oxidase activity of CueO from Escherichia coli.Copper toxicity and the origin of bacterial resistance--new insights and applications.Dps biomineralizing proteins: multifunctional architects of nature.Pathogenic adaptations to host-derived antibacterial copper.Copper tolerance and virulence in bacteria.Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium Aurantimonas sp. strain SI85-9A1.Genetic basis and importance of metal resistant genes in bacteria for bioremediation of contaminated environments with toxic metal pollutants.Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis.Catecholate siderophore esterases Fes, IroD and IroE are required for salmochelins secretion following utilization, but only IroD contributes to virulence of extra-intestinal pathogenic Escherichia coli.A multicopper oxidase contributes to the copper tolerance of Brucella melitensis 16M.Transcriptional and posttranscriptional events control copper-responsive expression of a Rhodobacter capsulatus multicopper oxidase.Four-electron reduction of dioxygen by a multicopper oxidase, CueO, and roles of Asp112 and Glu506 located adjacent to the trinuclear copper center.Engineering Klebsiella sp. 601 multicopper oxidase enhances the catalytic efficiency towards phenolic substrates.TolC is involved in enterobactin efflux across the outer membrane of Escherichia coli.Role of the extracytoplasmic function protein family sigma factor RpoE in metal resistance of Escherichia coliDifferential expression of the three multicopper oxidases from Myxococcus xanthus.Engineering of a psychrophilic bacterium for the bioremediation of aromatic compounds.Direct identification of a bacterial manganese(II) oxidase, the multicopper oxidase MnxG, from spores of several different marine Bacillus species.A versatile and efficient markerless gene disruption system for Acidithiobacillus thiooxidans: application for characterizing a copper tolerance related multicopper oxidase gene.A new approach to studying ion uptake by actinomycetes.
P2860
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P2860
Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Linkage between catecholate si ...... dase CueO in Escherichia coli.
@en
type
label
Linkage between catecholate si ...... dase CueO in Escherichia coli.
@en
prefLabel
Linkage between catecholate si ...... dase CueO in Escherichia coli.
@en
P2093
P2860
P1476
Linkage between catecholate si ...... dase CueO in Escherichia coli.
@en
P2093
Christopher Rensing
Daniel Thieme
Gregor Grass
Günter F Wildner
Keshari Thakali
Phillip E Klebba
P2860
P304
P356
10.1128/JB.186.17.5826-5833.2004
P50
P577
2004-09-01T00:00:00Z