Drosophila ZIP13 (Slc39a13), a presumed zinc importer, is responsible for iron delivery to the secretory pathway.

The diffusional barrier formed between phagocyte integrin and fungal glucans preserves the microbiostatic phagocytic environment generated during the frustrated phagocytosis of Candida albicans hypha.

Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.

The structural and mechanistic characterization of competitive inhibition of human DMT1 offers a promising route for the development of compounds for the treatment of iron overload disorders.

The structural and functional characterization of EleNRMT defines the basis for the distinct ion selectivity of a clade of the SLC11/NRAMP family which, instead of transporting transition metal ions, have evolved as uncoupled transporters of Mg²⁺.

Manganese drives the activation of the ‘target of rapamycin complex 1’ and uncouples sensing and response to nutrient availability.

The structure of the human iron exporter ferroportin in complex with its inhibitor vamifeport, which is currently in clinical development against β-thalassemia and sickle cell disease, provides insight into pharmacological mechanisms.

The structure of an NRAMP-related Al³⁺ transporter illustrates the evolution of a branch of a conserved protein family of metal ion transporters in plants to combat Al³⁺ toxicity in acidic soil.

Structures of a transition metal transporter spanning the entire Mn²⁺ transport cycle reveal distinct coordination geometries and dynamic polar networks that enable Mn²⁺ import, and a Cd²⁺-bound structure helps explain how Cd²⁺ behaves differently as a substrate.