Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
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ABC transporter FtsABCD of Streptococcus pyogenes mediates uptake of ferric ferrichrome.Heme coordination by Staphylococcus aureus IsdEBis-methionyl Coordination in the Crystal Structure of the Heme-binding Domain of the Streptococcal Cell Surface Protein ShpThe IsdC Protein from Staphylococcus aureus Uses a Flexible Binding Pocket to Capture HemeStaphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its HemeBenfang Lei's research on heme acquisition in Gram-positive pathogens and bacterial pathogenesisThe surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp.Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis.Direct heme transfer reactions in the Group A Streptococcus heme acquisition pathway.Identification of amino acid residues involved in heme binding and hemoprotein utilization in the Porphyromonas gingivalis heme receptor HmuR.The crimson conundrum: heme toxicity and tolerance in GAS.Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenesIdentification and characterization of the heme-binding proteins SeShp and SeHtsA of Streptococcus equi subspecies equi.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.Novel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaAThe GAS PefCD exporter is a MDR system that confers resistance to heme and structurally diverse compounds.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.Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporterHeme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.Lipid oxidation in trout muscle is strongly inhibited by a protein that specifically binds hemin released from hemoglobin.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.Regulation of intracellular heme trafficking revealed by subcellular reportersAxial ligand replacement mechanism in heme transfer from streptococcal heme-binding protein Shp to HtsA of the HtsABC transporterMechanisms of iron and haem transport by Listeria monocytogenes.Iron acquisition and regulation systems in Streptococcus species.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus.Spectroscopic identification of heme axial ligands in HtsA that are involved in heme acquisition by Streptococcus pyogenes.Streptococcal heme binding protein (Shp) promotes virulence and contributes to the pathogenesis of group A Streptococcus infection.Immunization with Streptococcal Heme Binding Protein (Shp) Protects Mice Against Group A Streptococcus Infection.Role for sagA and siaA in quorum sensing and iron regulation in Streptococcus pyogenes.Extracellular heme uptake and the challenges of bacterial cell membranes.Shr is a broad-spectrum surface receptor that contributes to adherence and virulence in group A streptococcus.Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin in Listeria monocytogenes.Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Cytochrome c biogenesis in Campylobacter jejuni requires cytochrome c6 (CccA; Cj1153) to maintain apocytochrome cysteine thiols in a reduced state for haem attachment.Proteomic analysis of putative heme-binding proteins in Streptococcus pyogenes.
P2860
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P2860
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
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
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
@ast
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
@en
type
label
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
@ast
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
@en
prefLabel
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
@ast
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
@en
P2860
P1476
Heme transfer from streptococcal cell surface protein Shp to HtsA of transporter HtsABC.
@en
P2093
Benfang Lei
Mengyao Liu
P2860
P304
P356
10.1128/IAI.73.8.5086-5092.2005
P407
P577
2005-08-01T00:00:00Z