Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa. - Wikidata - awgldk - TriplyDB

Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.

Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.

http://www.wikidata.org/entity/Q35199426

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Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein Regulation of Pseudomonas aeruginosa Virulence by Distinct Iron Sources Dual-seq transcriptomics reveals the battle for iron during Pseudomonas aeruginosa acute murine pneumonia.Use of a Multiplex Transcript Method for Analysis of Pseudomonas aeruginosa Gene Expression Profiles in the Cystic Fibrosis Lung Heme Synthesis and Acquisition in Bacterial Pathogens.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.Ligand-induced allostery in the interaction of the Pseudomonas aeruginosa heme binding protein with heme oxygenase.The Small Protein HemP Is a Transcriptional Activator for the Hemin Uptake Operon in Burkholderia multivorans ATCC 17616.

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P2860

Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.

http://www.wikidata.org/entity/Q35199426

description

2015 nî lūn-bûn

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2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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Aaron D Smith

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Angela Wilks

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P2860

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex

Structural, NMR Spectroscopic, and Computational Investigation of Hemin Loading in the Hemophore HasAp from Pseudomonas aeruginosa

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

Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer

Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO)

Genetics and regulation of two distinct haem-uptake systems, phu and has, in Pseudomonas aeruginosa

Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: cycle selection of iron-regulated genes

A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants

Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: heme binding by an induced fit mechanism.

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