Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron.
about
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humansABC transporter FtsABCD of Streptococcus pyogenes mediates uptake of ferric ferrichrome.PerR confers phagocytic killing resistance and allows pharyngeal colonization by group A StreptococcusBis-methionyl Coordination in the Crystal Structure of the Heme-binding Domain of the Streptococcal Cell Surface Protein ShpStructural Basis for Hemoglobin Capture by Staphylococcus aureus Cell-surface Protein, IsdHIn vitro heme biotransformation by the HupZ enzyme from Group A streptococcusMolecular and evolutionary analysis of NEAr-iron Transporter (NEAT) domainsThe surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp.Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.Characterization of MtsR, a new metal regulator in group A streptococcus, involved in iron acquisition and virulence.Direct heme transfer reactions in the Group A Streptococcus heme acquisition pathway.Bacillus anthracis IsdG, a heme-degrading monooxygenaseDisease manifestations and pathogenic mechanisms of Group A Streptococcus.The crimson conundrum: heme toxicity and tolerance in GAS.Utilization of host iron sources by Corynebacterium diphtheriae: multiple hemoglobin-binding proteins are essential for the use of iron from the hemoglobin-haptoglobin complex.Defense from the Group A Streptococcus by active and passive vaccination with the streptococcal hemoprotein receptor.Differential regulation of iron- and manganese-specific MtsABC and heme-specific HtsABC transporters by the metalloregulator MtsR of group A Streptococcus.Non-heme-binding domains and segments of the Staphylococcus aureus IsdB protein critically contribute to the kinetics and equilibrium of heme acquisition from methemoglobin.Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization.Novel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaAPeroxide stimulon and role of PerR in group A Streptococcus.Phylogenetic approaches to microbial community classification.Mechanisms of group A Streptococcus resistance to reactive oxygen species.The GAS PefCD exporter is a MDR system that confers resistance to heme and structurally diverse compounds.Identification of iron-regulated genes of Bifidobacterium breve UCC2003 as a basis for controlled gene expression.CovRS-Regulated Transcriptome Analysis of a Hypervirulent M23 Strain of Group A Streptococcus pyogenes Provides New Insights into Virulence Determinants.The influence of iron availability on human salivary microbial community compositionIdentification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes.Induction of a quorum sensing pathway by environmental signals enhances group A streptococcal resistance to lysozymeStudy of streptococcal hemoprotein receptor (Shr) in iron acquisition and virulence of M1T1 group A streptococcus.Direct hemin transfer from IsdA to IsdC in the iron-regulated surface determinant (Isd) heme acquisition system of Staphylococcus aureus.The mechanism of direct heme transfer from the streptococcal cell surface protein Shp to HtsA of the HtsABC transporter.Structural Characterization of Heme Environmental Mutants of CgHmuT that Shuttles Heme Molecules to Heme TransportersAnalysis of the Corynebacterium diphtheriae DtxR regulon: identification of a putative siderophore synthesis and transport system that is similar to the Yersinia high-pathogenicity island-encoded yersiniabactin synthesis and uptake system.Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.HtaA is an iron-regulated hemin binding protein involved in the utilization of heme iron in Corynebacterium diphtheriae.Bacterial heme-transport proteins and their heme-coordination modes.The metal homeostasis protein, Lsp, of Streptococcus pyogenes is necessary for acquisition of zinc and virulenceSequestration and scavenging of iron in infection.Axial ligand replacement mechanism in heme transfer from streptococcal heme-binding protein Shp to HtsA of the HtsABC transporter
P2860
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P2860
Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Identification and characteriz ...... teins and acquisition of iron.
@ast
Identification and characteriz ...... teins and acquisition of iron.
@en
Identification and characteriz ...... teins and acquisition of iron.
@nl
type
label
Identification and characteriz ...... teins and acquisition of iron.
@ast
Identification and characteriz ...... teins and acquisition of iron.
@en
Identification and characteriz ...... teins and acquisition of iron.
@nl
prefLabel
Identification and characteriz ...... teins and acquisition of iron.
@ast
Identification and characteriz ...... teins and acquisition of iron.
@en
Identification and characteriz ...... teins and acquisition of iron.
@nl
P2093
P2860
P1476
Identification and characteriz ...... teins and acquisition of iron.
@en
P2093
Charles R Woods
Christopher S Bates
Griselle E Montañez
Rebecca M Vincent
Zehava Eichenbaum
P2860
P304
P356
10.1128/IAI.71.3.1042-1055.2003
P407
P577
2003-03-01T00:00:00Z