Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme - Wikidata - wikimedia - TriplyDB

Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme

Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme

http://www.wikidata.org/entity/Q27675004

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Rapid Heme Transfer Reactions between NEAr Transporter Domains of Staphylococcus aureus: A Theoretical Study Using QM/MM and MD Simulations Selective binding of antimicrobial porphyrins to the heme-receptor IsdH-NEAT3 ofStaphylococcus aureus Structure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture byStaphylococcus aureus Solution Structure and Molecular Determinants of Hemoglobin Binding of the First NEAT Domain of IsdB in Staphylococcus aureus The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket Iron and zinc exploitation during bacterial pathogenesis Heme uptake in bacterial pathogens IsdB-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.Non-heme-binding domains and segments of the Staphylococcus aureus IsdB protein critically contribute to the kinetics and equilibrium of heme acquisition from methemoglobin.The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Native top-down mass spectrometry for the structural characterization of human hemoglobin.Integrating Native Mass Spectrometry and Top-Down MS for Defining Protein Interactions Important in Biology and Medicine Axial ligand replacement mechanism in heme transfer from streptococcal heme-binding protein Shp to HtsA of the HtsABC transporter Structural Characterization of a Thrombin-Aptamer Complex by High Resolution Native Top-Down Mass Spectrometry.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.The Staphylococcus aureus Protein IsdH Inhibits Host Hemoglobin Scavenging to Promote Heme Acquisition by the Pathogen.The Corynebacterium diphtheriae iron-regulated surface protein HbpA is involved in the utilization of the Hemoglobin-Haptoglobin complex as an iron source.Energetics underlying hemin extraction from human hemoglobin by Staphylococcus aureus.

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Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme

http://www.wikidata.org/entity/Q27675004

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2013 nî lūn-bûn

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2013 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2013 թվականի հունվարին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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JBC.M112.419119

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Journal of Biological Chemistry

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Staphylococcus aureus Uses a N ...... Hemoglobin and Steal Its Heme

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Benfang Lei

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Claire F Dickson

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G Reza Malmirchegini

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Jiang Zhang

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Joseph A Loo

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Kaavya Krishna Kumar

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Megan Sjodt

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Mengyao Liu

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Robert T Clubb

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Scott A Robson

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P2860

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

NEAT: a domain duplicated in genes near the components of a putative Fe3+ siderophore transporter from Gram-positive pathogenic bacteria.

Three-dimensional solution structure of the B domain of staphylococcal protein A: comparisons of the solution and crystal structures

Haem recognition by a Staphylococcus aureus NEAT domain

Heme coordination by Staphylococcus aureus IsdE

Structural Basis for Multimeric Heme Complexation through a Specific Protein-Heme Interaction: THE CASE OF THE THIRD NEAT DOMAIN OF IsdH FROM STAPHYLOCOCCUS AUREUS

The IsdC Protein from Staphylococcus aureus Uses a Flexible Binding Pocket to Capture Heme

Structure of the dimerization domain of DiGeorge Critical Region 8

Unique Heme-Iron Coordination by the Hemoglobin Receptor IsdB of Staphylococcus aureus

Molecular basis of recognition of antibacterial porphyrins by heme-transporter IsdH-NEAT3 of Staphylococcus aureus

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