Free and hemophore-bound heme acquisitions through the outer membrane receptor HasR have different requirements for the TonB-ExbB-ExbD complex.
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Haemophore functions revisitedHeme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complexThe Structure of HasB Reveals a New Class of TonB Protein FoldMolecular and evolutionary analysis of NEAr-iron Transporter (NEAT) domainsNagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus.Activities of the Serratia marcescens heme receptor HasR and isolated plug and beta-barrel domains: the beta-barrel forms a heme-specific channelMetal limitation and toxicity at the interface between host and pathogenHeme utilization in Campylobacter jejuni.Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.Gene expression changes in Porphyromonas gingivalis W83 after inoculation in rat oral cavityHasB, the Serratia marcescens TonB paralog, is specific to HasR.Bacterial heme-transport proteins and their heme-coordination modes.Regulation of iron transport systems in Enterobacteriaceae in response to oxygen and iron availability.Mechanisms of iron import in anthrax.Cell-surface signaling in Pseudomonas: stress responses, iron transport, and pathogenicity.Gallium-Protoporphyrin IX Inhibits Pseudomonas aeruginosa Growth by Targeting Cytochromes.Small molecule antivirulents targeting the iron-regulated heme oxygenase (HemO) of P. aeruginosa.Metabolite-driven Regulation of Heme Uptake by the Biliverdin IXβ/δ-Selective Heme Oxygenase (HemO) of Pseudomonas aeruginosa.Spectroscopic Determination of Distinct Heme Ligands in Outer-Membrane Receptors PhuR and HasR of Pseudomonas aeruginosa.Structural basis for haem piracy from host haemopexin by Haemophilus influenzae.Heme and a five-amino-acid hemophore region form the bipartite stimulus triggering the has signaling cascade.Mutagenesis and molecular modeling reveal three key extracellular loops of the membrane receptor HasR that are involved in hemophore HasA binding.Purification, crystallization and preliminary X-ray analysis of the outer membrane complex HasA-HasR from Serratia marcescens.Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR.Binding of iron-free siderophore, a common feature of siderophore outer membrane transporters of Escherichia coli and Pseudomonas aeruginosa.Iron uptake is essential for Escherichia coli survival in drinking water.Haem release from haemopexin by HxuA allows Haemophilus influenzae to escape host nutritional immunity.
P2860
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P2860
Free and hemophore-bound heme acquisitions through the outer membrane receptor HasR have different requirements for the TonB-ExbB-ExbD complex.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Free and hemophore-bound heme ...... or the TonB-ExbB-ExbD complex.
@en
type
label
Free and hemophore-bound heme ...... or the TonB-ExbB-ExbD complex.
@en
prefLabel
Free and hemophore-bound heme ...... or the TonB-ExbB-ExbD complex.
@en
P2093
P2860
P1476
Free and hemophore-bound heme ...... or the TonB-ExbB-ExbD complex.
@en
P2093
Cécile Wandersman
Philippe Delepelaire
Sylvie Létoffé
P2860
P304
P356
10.1128/JB.186.13.4067-4074.2004
P577
2004-07-01T00:00:00Z