The near-atomic cryoEM pore complex structure of pneumolysin, the main virulence factor of Streptococcus pneumoniae, shows how the individual domains rearrange during the pore formation.

The HCN1 channel gates thanks to a coupling mechanism involving the reorganization of the interfaces between the voltage-sensor domains and pore helices, subtly shifting the balance between hydrophobic and hydrophilic interactions in a 'domino effect'.

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.

Cationic cell-penetrating peptides (CPPs) enter cells through ~2 (–5)-nm-wide water pores induced by the strong negative plasma membrane potential that CPPs and the activity of potassium channels generate.

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.

Proline/glycine kink in the helical peptides affects the peptide ability to form membrane pores by stabilising toroidal pore structures but disrupting barrel-stave pore structures.

The molecular mechanism that candidalysin uses to perforate membranes is unraveled, which opens the door to the rational design of inhibitors against candidiasis.

The proteins Bax and Bak, which increase the permeability of the mitochondrial membrane during apoptosis, are also crucial for generating a mitochondrial membrane pore that is specifically involved in necrosis.

Functional reconstitution of a mammalian P2X7 receptor uncovers an intrinsic and lipid-dependent dye-permeable membrane pore.

During neurotransmitter release, calcium-induced membrane insertion of the C2B domain of Synaptotagmin re-orients the bound SNARE complex which dilates the fusion pore in a mechanical lever action.