Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin.
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Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humansHaemophore functions revisitedUnique Heme-Iron Coordination by the Hemoglobin Receptor IsdB of Staphylococcus aureusStructural Basis for Hemoglobin Capture by Staphylococcus aureus Cell-surface Protein, IsdHStaphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its HemeThe Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from MethemoglobinDifferential Function of Lip Residues in the Mechanism and Biology of an Anthrax HemophoreStructure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture byStaphylococcus aureusSolution Structure and Molecular Determinants of Hemoglobin Binding of the First NEAT Domain of IsdB in Staphylococcus aureusThe structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocketMolecular and evolutionary analysis of NEAr-iron Transporter (NEAT) domainsMolecular mechanisms of bio-catalysis of heme extraction from hemoglobinHeme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis.Heme uptake in bacterial pathogensIsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus.A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdCThe 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.Molecular strategies of microbial iron assimilation: from high-affinity complexes to cofactor assembly systems.Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes.Utilization of host iron sources by Corynebacterium diphtheriae: multiple hemoglobin-binding proteins are essential for the use of iron from the hemoglobin-haptoglobin complex.IsdA and IsdB antibodies protect mice against Staphylococcus aureus abscess formation and lethal challengeNovel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaAThe five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC.The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Protective efficacy of the chimeric Staphylococcus aureus vaccine candidate IC in sepsis and pneumonia modelsBackbone 1H, 13C and 15N resonance assignments of the 39 kDa staphylococcal hemoglobin receptor IsdHAnalysis of novel iron-regulated, surface-anchored hemin-binding proteins in Corynebacterium diphtheriae¹H, ¹³C, ¹⁵N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureusMolecular mechanisms of Staphylococcus aureus iron acquisition.Subcellular localization of the Staphylococcus aureus heme iron transport components IsdA and IsdB.Axial ligand replacement mechanism in heme transfer from streptococcal heme-binding protein Shp to HtsA of the HtsABC transporterMechanisms of iron import in anthrax.Recent advances in bacterial heme protein biochemistry.The theft of host heme by Gram-positive pathogenic bacteria.Mechanisms of iron and haem transport by Listeria monocytogenes.Adhesion, invasion and evasion: the many functions of the surface proteins of Staphylococcus aureus.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Heme Synthesis and Acquisition in Bacterial Pathogens.The ClusPro web server for protein-protein docking.The Staphylococcus aureus Protein IsdH Inhibits Host Hemoglobin Scavenging to Promote Heme Acquisition by the Pathogen.
P2860
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P2860
Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin.
description
2008 nî lūn-bûn
@nan
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Functionally distinct NEAT (NE ...... tract heme from methemoglobin.
@ast
Functionally distinct NEAT (NE ...... tract heme from methemoglobin.
@en
type
label
Functionally distinct NEAT (NE ...... tract heme from methemoglobin.
@ast
Functionally distinct NEAT (NE ...... tract heme from methemoglobin.
@en
prefLabel
Functionally distinct NEAT (NE ...... tract heme from methemoglobin.
@ast
Functionally distinct NEAT (NE ...... tract heme from methemoglobin.
@en
P2093
P2860
P356
P1476
Functionally distinct NEAT (NE ...... tract heme from methemoglobin.
@en
P2093
Martin Phillips
Melissa L Wong
Robert T Clubb
Rosemarie M Pilpa
Scott A Robson
Valerie A Villareal
P2860
P304
P356
10.1074/JBC.M806007200
P407
P577
2008-11-03T00:00:00Z