A high-resolution structure reveals how the RhopH complex traffics within Plasmodium-infected human erythrocytes to serve divergent, essential functions.

Compressive force spectroscopy of single molecules reveals that intra-protein forces underlie the long-distance coordination of structural changes within a cytotoxin during pore formation.

Electron and atomic force microscopy show how bacterial toxins bind to a host membrane and assemble into arcs and rings, before undergoing a dramatic, concerted conformational change to insert into the membrane.

Perforin-2 deficiency is lethal upon infection with pathogenic bacteria despite the presence of other bactericidal effectors.

Cryo-EM and X-ray structures of α-xenorhabdolysin in soluble and pore form of Xenorhabdus nematophila give novel insights into the mechanism of action of bi-component α-pore-forming toxins.

The structural relationship between TMC and TMEM16 proteins provides insight into the structure and functional mechanisms of the mechanotransduction channel complex in hair cells.

The structure, function and mechanism of the malaria vaccine candidate CelTOS reveal a unique pore-forming and membrane-disrupting protein with specificity for the inner leaflet of host and vector cells.

The structure of a pannexin 1 uncovers the extracellular loops of pannexin 1 as important structural motifs for ion selectivity and channel inhibition.

Biochemical analysis reveals molecular mechanisms underlying the activation of the mitochondrial Ca²⁺ uniporter by intracellular Ca²⁺ signals.

Genetic and electrophysiological experiments reveal that a gene called MCU encodes the ion channel pore that allows calcium ions to cross the inner mitochondrial membrane.