Published in J Biol Chem on January 22, 2015
Dual-seq transcriptomics reveals the battle for iron during Pseudomonas aeruginosa acute murine pneumonia. Sci Rep (2016) 0.99
Heme Synthesis and Acquisition in Bacterial Pathogens. J Mol Biol (2016) 0.85
Regulation of Pseudomonas aeruginosa Virulence by Distinct Iron Sources. Genes (Basel) (2016) 0.76
Metabolite-driven Regulation of Heme Uptake by the Biliverdin IXβ/δ-Selective Heme Oxygenase (HemO) of Pseudomonas aeruginosa. J Biol Chem (2016) 0.76
Use of a Multiplex Transcript Method for Analysis of Pseudomonas aeruginosa Gene Expression Profiles in the Cystic Fibrosis Lung. Infect Immun (2016) 0.76
Ligand-induced allostery in the interaction of the Pseudomonas aeruginosa heme binding protein with heme oxygenase. Proc Natl Acad Sci U S A (2017) 0.75
Spectroscopic Determination of Distinct Heme Ligands in Outer-Membrane Receptors PhuR and HasR of Pseudomonas aeruginosa. Biochemistry (2015) 0.75
A Small Protein, HemP, is a Transcriptional Activator for Hemin Uptake Operon in Burkholderia multivorans ATCC 17616. Appl Environ Microbiol (2017) 0.75
Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons. Methods Enzymol (1994) 9.16
Cleavage of the haem-protein link by acid methylethylketone. Biochim Biophys Acta (1959) 5.69
Gene repression by the ferric uptake regulator in Pseudomonas aeruginosa: cycle selection of iron-regulated genes. Proc Natl Acad Sci U S A (1996) 2.71
The Neisseria meningitidis haemoglobin receptor: its role in iron utilization and virulence. Mol Microbiol (1995) 2.52
Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: sequence of the gene, regulation of expression, and homology to the family of TonB-dependent proteins. J Bacteriol (1994) 2.27
Genetics and regulation of two distinct haem-uptake systems, phu and has, in Pseudomonas aeruginosa. Microbiology (2000) 2.16
A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli. J Bacteriol (1997) 2.02
Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme. J Am Chem Soc (2002) 1.98
Heme and virulence: how bacterial pathogens regulate, transport and utilize heme. Nat Prod Rep (2007) 1.78
Heme acquisition by hemophores. Biometals (2007) 1.72
Crystal structure of the heme-IsdC complex, the central conduit of the Isd iron/heme uptake system in Staphylococcus aureus. J Biol Chem (2007) 1.69
Iron uptake and metabolism in pseudomonads. Appl Microbiol Biotechnol (2010) 1.62
Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa. J Bacteriol (2001) 1.55
Use of heme-protein complexes by the Yersinia enterocolitica HemR receptor: histidine residues are essential for receptor function. J Bacteriol (1999) 1.54
Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex. Proc Natl Acad Sci U S A (2009) 1.53
Protein secretion in gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding. EMBO J (1996) 1.44
Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa. Biochemistry (2004) 1.36
The heme oxygenase(s)-phytochrome system of Pseudomonas aeruginosa. J Biol Chem (2004) 1.35
Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae. Biochemistry (2005) 1.31
Thermodynamics of heme binding to the HasA(SM) hemophore: effect of mutations at three key residues for heme uptake. Biochemistry (2003) 1.30
Iron and pathogenesis of Shigella: iron acquisition in the intracellular environment. Biometals (2006) 1.26
The heme transfer from the soluble HasA hemophore to its membrane-bound receptor HasR is driven by protein-protein interaction from a high to a lower affinity binding site. J Biol Chem (2006) 1.26
Haemophore-mediated signal transduction across the bacterial cell envelope in Serratia marcescens: the inducer and the transported substrate are different molecules. Mol Microbiol (2003) 1.23
Characterization of the outer membrane receptor ShuA from the heme uptake system of Shigella dysenteriae. Substrate specificity and identification of the heme protein ligands. J Biol Chem (2007) 1.20
Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins. J Biol Chem (2007) 1.18
Within-host evolution of Pseudomonas aeruginosa reveals adaptation toward iron acquisition from hemoglobin. MBio (2014) 1.18
The cytoplasmic heme-binding protein (PhuS) from the heme uptake system of Pseudomonas aeruginosa is an intracellular heme-trafficking protein to the delta-regioselective heme oxygenase. J Biol Chem (2006) 1.17
Identification and characterization of the hemophore-dependent heme acquisition system of Yersinia pestis. Infect Immun (2001) 1.17
Unique heme-iron coordination by the hemoglobin receptor IsdB of Staphylococcus aureus. Biochemistry (2011) 1.16
Free and hemophore-bound heme acquisitions through the outer membrane receptor HasR have different requirements for the TonB-ExbB-ExbD complex. J Bacteriol (2004) 1.12
Kinetic and spectroscopic studies of hemin acquisition in the hemophore HasAp from Pseudomonas aeruginosa. Biochemistry (2010) 1.05
Pseudomonas aeruginosa adapts its iron uptake strategies in function of the type of infections. Front Cell Infect Microbiol (2013) 1.04
Identification of two heme-binding sites in the cytoplasmic heme-trafficking protein PhuS from Pseudomonas aeruginosa and their relevance to function. Biochemistry (2007) 1.04
Haemophore-mediated signalling in Serratia marcescens: a new mode of regulation for an extra cytoplasmic function (ECF) sigma factor involved in haem acquisition. Mol Microbiol (2004) 1.03
Adaptation of iron homeostasis pathways by a Pseudomonas aeruginosa pyoverdine mutant in the cystic fibrosis lung. J Bacteriol (2014) 1.02
Biosynthetic preparation of isotopically labeled heme. Anal Biochem (1995) 0.99
Iron-coordinating tyrosine is a key determinant of NEAT domain heme transfer. J Mol Biol (2011) 0.98
Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: heme binding by an induced fit mechanism. Proteins (2010) 0.97
Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO). Proc Natl Acad Sci U S A (2012) 0.93
Structural, NMR spectroscopic, and computational investigation of hemin loading in the hemophore HasAp from Pseudomonas aeruginosa. J Am Chem Soc (2010) 0.93
Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO). J Biol Chem (2012) 0.92
The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand. J Mol Biol (2006) 0.92
Heme uptake in bacterial pathogens. Curr Opin Chem Biol (2014) 0.89
The P. aeruginosa heme binding protein PhuS is a heme oxygenase titratable regulator of heme uptake. ACS Chem Biol (2013) 0.88
Expression of the phytochrome operon in Pseudomonas aeruginosa is dependent on the alternative sigma factor RpoS. FEMS Microbiol Lett (2008) 0.83
Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor. Biochim Biophys Acta (2014) 0.79
The Hem and Has haem uptake systems in Serratia marcescens. Microbiology (2010) 0.79