▪ Abstract The ability of pathogens to obtain iron from transferrins, ferritin, hemoglobin, and
other iron-containing proteins of their host is central to whether they live or die. To combat …

Iron enters dividing cells of higher eukaryotes via the transferrin receptor. Once inside the
cell, the iron may be considered to be in 1 of 3 pools, although overlap and interchange …

Controlling iron/oxygen chemistry in biology depends on multiple genes, regulatory
messenger RNA (mRNA) structures, signaling pathways and protein catalysts. Ferritin, a …

Iron is a critical nutrient for the growth and survival of most bacterial species. Accordingly,
much attention has been paid to the mechanisms by which host organisms sequester iron …

Cobalt is toxic for cells, but mechanisms of this toxicity are largely unknown. The
biochemical and genetic experiments reported here demonstrate that iron-sulfur proteins are …

The iroN gene of Salmonella enterica and uropathogenic Escherichia coli encodes the outer
membrane receptor of Fe3+‐bound salmochelin, a siderophore tailored to evade capture by …

Escherichia coli contains at least two iron storage proteins, a ferritin (FtnA) and a
bacterioferritin (Bfr). To investigate their specific functions, the corresponding genes (ftnA …

The Fur protein is a primary regulator that monitors and controls cytoplasmic iron levels. We
now report the identification of a regulatory pathway mediated by the Salmonella response …

Iron is required by almost all bacteria, but concentrations above physiological levels are
toxic. In bacteria, intracellular iron is regulated mostly by the ferric uptake regulator, Fur, or a …

Covering: 2000–2006 The ability of bacterial pathogens to obtain iron is essential for their
survival, and the expression of such virulence factors is (in part) essential for establishing …