Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity
about
Structure and heme binding properties ofEscherichia coliO157:H7 ChuXCrystal structure of the Pseudomonas aeruginosa cytoplasmic heme binding protein, Apo-PhuSHeme degrading protein HemS is involved in oxidative stress response of Bartonella henselaeMetabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO)Transcriptional and posttranscriptional regulation of Shigella shuT in response to host-associated iron availability and temperatureRNA-mediated thermoregulation of iron-acquisition genes in Shigella dysenteriae and pathogenic Escherichia coli.The ABC transporter HrtAB confers resistance to hemin toxicity and is regulated in a hemin-dependent manner by the ChrAS two-component system in Corynebacterium diphtheriae.Bacillus anthracis IsdG, a heme-degrading monooxygenaseOvercoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.Pseudomonas aeruginosa adapts its iron uptake strategies in function of the type of infectionsThe crimson conundrum: heme toxicity and tolerance in GAS.Temporal signaling and differential expression of Bordetella iron transport systems: the role of ferrimones and positive regulators.Genetics and environmental regulation of Shigella iron transport systems.Staphylococcus aureus haem oxygenases are differentially regulated by iron and haem.The P. aeruginosa heme binding protein PhuS is a heme oxygenase titratable regulator of heme uptakeBacterial heme-transport proteins and their heme-coordination modes.Role and regulation of heme iron acquisition in gram-negative pathogens.Sequestration and scavenging of iron in infection.Iron, 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.Mechanisms of iron import in anthrax.Iron homeostasis and management of oxidative stress response in bacteria.Heme Synthesis and Acquisition in Bacterial Pathogens.Functional characterization of the Shigella dysenteriae heme ABC transporter.Non-heme induction of heme oxygenase-1 does not alter cellular iron metabolism.Characterization of the outer membrane receptor ShuA from the heme uptake system of Shigella dysenteriae. Substrate specificity and identification of the heme protein ligands.Plesiomonas shigelloides hugZ encodes an iron-regulated heme binding protein required for heme iron utilization.Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193.
P2860
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P2860
Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Shigella dysenteriae ShuS prom ...... protects against heme toxicity
@ast
Shigella dysenteriae ShuS prom ...... protects against heme toxicity
@en
type
label
Shigella dysenteriae ShuS prom ...... protects against heme toxicity
@ast
Shigella dysenteriae ShuS prom ...... protects against heme toxicity
@en
prefLabel
Shigella dysenteriae ShuS prom ...... protects against heme toxicity
@ast
Shigella dysenteriae ShuS prom ...... protects against heme toxicity
@en
P2093
P2860
P1476
Shigella dysenteriae ShuS prom ...... protects against heme toxicity
@en
P2093
Elizabeth E Wyckoff
Gregory F Lopreato
Kimberly A Tipton
Shelley M Payne
P2860
P304
P356
10.1128/JB.187.16.5658-5664.2005
P407
P577
2005-08-01T00:00:00Z