Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
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Haemophore functions revisitedRapid Heme Transfer Reactions between NEAr Transporter Domains of Staphylococcus aureus: A Theoretical Study Using QM/MM and MD SimulationsThe Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from MethemoglobinSelective binding of antimicrobial porphyrins to the heme-receptor IsdH-NEAT3 ofStaphylococcus aureusDifferential 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) domainsMapping ultra-weak protein-protein interactions between heme transporters of Staphylococcus aureusIsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus.Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes.Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.The Heme Transport Capacity of LHR1 Determines the Extent of Virulence in Leishmania amazonensis.Staphylococcus aureus growth using human hemoglobin as an iron sourceHeme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Iron-regulated surface determinant (Isd) proteins of Staphylococcus lugdunensis.Spectroscopic Determination of Distinct Heme Ligands in Outer-Membrane Receptors PhuR and HasR of Pseudomonas aeruginosa.Extracellular heme uptake and the challenges of bacterial cell membranes.Insight into blocking heme transfer by exploiting molecular interactions in the core Isd heme transporters IsdA-NEAT, IsdC-NEAT, and IsdE of Staphylococcus aureus.Expression, immunogenicity and variation of iron-regulated surface protein A from bovine isolates of Staphylococcus aureus.Structural basis for binding and transfer of heme in bacterial heme-acquisition systems.
P2860
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P2860
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
description
2011 nî lūn-bûn
@nan
2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@ast
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@en
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@nl
type
label
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@ast
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@en
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@nl
prefLabel
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@ast
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@en
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@nl
P2093
P1476
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer
@en
P2093
Cherry X Mao
Jason C Grigg
Michael E P Murphy
P304
P356
10.1016/J.JMB.2011.08.047
P407
P577
2011-10-28T00:00:00Z