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Staphylococcus 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 HemophoreIron and zinc exploitation during bacterial pathogenesisCharacterization of the sortase repertoire in Bacillus anthracisTwo-component system cross-regulation integrates Bacillus anthracis response to heme and cell envelope stressMolecular and evolutionary analysis of NEAr-iron Transporter (NEAT) domainsHeme uptake in bacterial pathogensNutritional immunity: transition metals at the pathogen-host interface.The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC.Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor.Characterization of heme ligation properties of Rv0203, a secreted heme binding protein involved in Mycobacterium tuberculosis heme uptake.Hal Is a Bacillus anthracis heme acquisition proteinHeme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.Insights on how the Mycobacterium tuberculosis heme uptake pathway can be used as a drug target.The roles of transition metals in the physiology and pathogenesis of Streptococcus pneumoniaeProgress toward the Development of a NEAT Protein Vaccine for Anthrax Disease.Dps biomineralizing proteins: multifunctional architects of nature.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Improvement of the respiration efficiency of Lactococcus lactis by decreasing the culture pH.The Corynebacterium diphtheriae iron-regulated surface protein HbpA is involved in the utilization of the Hemoglobin-Haptoglobin complex as an iron source.Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization.Heme sensing in Bacillus thuringiensis: a supplementary HssRS-regulated heme resistance system.
P2860
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P2860
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 22 January 2011
@en
vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Mechanisms of iron import in anthrax.
@en
Mechanisms of iron import in anthrax.
@nl
type
label
Mechanisms of iron import in anthrax.
@en
Mechanisms of iron import in anthrax.
@nl
prefLabel
Mechanisms of iron import in anthrax.
@en
Mechanisms of iron import in anthrax.
@nl
P2860
P1433
P1476
Mechanisms of iron import in anthrax.
@en
P2093
Anthony William Maresso
Erin Sarah Honsa
P2860
P2888
P304
P356
10.1007/S10534-011-9413-X
P577
2011-01-22T00:00:00Z