Processing of heme and heme-containing proteins by bacteria.
about
Haem recognition by a Staphylococcus aureus NEAT domainHeme coordination by Staphylococcus aureus IsdEBis-methionyl Coordination in the Crystal Structure of the Heme-binding Domain of the Streptococcal Cell Surface Protein ShpStructural Basis for Multimeric Heme Complexation through a Specific Protein-Heme Interaction: THE CASE OF THE THIRD NEAT DOMAIN OF IsdH FROM STAPHYLOCOCCUS AUREUSRuffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureusStructure and heme binding properties ofEscherichia coliO157:H7 ChuXThe Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding PocketCrystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157Structures of Streptococcus pneumoniae PiaA and Its Complex with Ferrichrome Reveal Insights into the Substrate Binding and Release of High Affinity Iron TransportersResistance of neisseria meningitidis to the toxic effects of heme iron and other hydrophobic agents requires expression of ght.Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis.Genome-wide analysis reveals novel genes essential for heme homeostasis in Caenorhabditis elegansAnalysis of a DtxR-regulated iron transport and siderophore biosynthesis gene cluster in Corynebacterium diphtheriaeHaemin represses the haemolytic activity of Staphylococcus aureus in an Sae-dependent manner.The 2-Cys peroxiredoxin alkyl hydroperoxide reductase c binds heme and participates in its intracellular availability in Streptococcus agalactiae.Lack of heme synthesis in a free-living eukaryote.Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicityA Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdCAnalysis of a heme-dependent signal transduction system in Corynebacterium diphtheriae: deletion of the chrAS genes results in heme sensitivity and diminished heme-dependent activation of the hmuO promoter.The 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.Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus.Molecular strategies of microbial iron assimilation: from high-affinity complexes to cofactor assembly systems.Roles of iron acquisition systems in virulence of extraintestinal pathogenic Escherichia coli: salmochelin and aerobactin contribute more to virulence than heme in a chicken infection model.Characterization of a hemophore-like protein from Porphyromonas gingivalis.HutZ is required for efficient heme utilization in Vibrio choleraeMicrobial iron acquisition: marine and terrestrial siderophores.Haemophilus responses to nutritional immunity: epigenetic and morphological contribution to biofilm architecture, invasion, persistence and disease severity.The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins.Characterization of ferric and ferrous iron transport systems in Vibrio choleraeHeme utilization by nontypeable Haemophilus influenzae is essential and dependent on Sap transporter functionNovel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaADelineation of lipopolysaccharide (LPS)-binding sites on hemoglobin: from in silico predictions to biophysical characterization.A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compoundsRegulation of a glutamyl-tRNA synthetase by the heme status.Iron transport systems in Neisseria meningitidisThe Neisseria meningitidis ZnuD zinc receptor contributes to interactions with epithelial cells and supports heme utilization when expressed in Escherichia coli.Iron acquisition in the cystic fibrosis lung and potential for novel therapeutic strategies.Hal Is a Bacillus anthracis heme acquisition proteinHtaA 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.
P2860
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P2860
Processing of heme and heme-containing proteins by bacteria.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Processing of heme and heme-containing proteins by bacteria.
@ast
Processing of heme and heme-containing proteins by bacteria.
@en
Processing of heme and heme-containing proteins by bacteria.
@nl
type
label
Processing of heme and heme-containing proteins by bacteria.
@ast
Processing of heme and heme-containing proteins by bacteria.
@en
Processing of heme and heme-containing proteins by bacteria.
@nl
prefLabel
Processing of heme and heme-containing proteins by bacteria.
@ast
Processing of heme and heme-containing proteins by bacteria.
@en
Processing of heme and heme-containing proteins by bacteria.
@nl
P1433
P1476
Processing of heme and heme-containing proteins by bacteria.
@en
P2093
Donna Perkins-Balding
Igor Stojiljkovic
P304
P356
10.1089/104454902753759708
P577
2002-04-01T00:00:00Z