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MARESSO, ANTHONY

One or more keywords matched the following items that are connected to MARESSO, ANTHONY

Item Type	Name
Academic Article	The near-iron transporter (NEAT) domains of the anthrax hemophore IsdX2 require a critical glutamine to extract heme from methemoglobin.
Academic Article	Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin.
Academic Article	Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis.
Academic Article	A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC.
Academic Article	The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC.
Academic Article	Hal Is a Bacillus anthracis heme acquisition protein.
Academic Article	Surface protein IsdC and Sortase B are required for heme-iron scavenging of Bacillus anthracis.
Academic Article	The theft of host heme by Gram-positive pathogenic bacteria.
Academic Article	Differential function of lip residues in the mechanism and biology of an anthrax hemophore.
Concept	Heme
Academic Article	A product of heme catabolism modulates bacterial function and survival.
Academic Article	Bacillus anthracis Overcomes an Amino Acid Auxotrophy by Cleaving Host Serum Proteins.
Academic Article	A dual component heme biosensor that integrates heme transport and synthesis in bacteria.
Grant	Targeting Heme Transporters for Improved Vaccines against Anthrax
Grant	Bacterial Heme Transport by non-Isd NEAT Proteins
Grant	Next-stage Development of Heme Transporters as a Vaccine for Anthrax
Grant	Characterization of Heme Acquisition in B. anthracis
Grant	Optical Imaging to Monitor Heme Acquisition during Bacterial Infection
Grant	The Importance and Function of Heme Degrading Enzymes during Anthrax Disease
Grant	Characterization of Heme Acquisition in Bacillus Anthracis
Academic Article	Heme catabolism in the causative agent of anthrax.
Academic Article	NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.

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Heme