Structural and functional studies of a potassium ion channel that is opened and closed by different ligands have revealed a novel gating mechanism.

Long-lived intermediate states formed by glycoprotein catalysts are an essential part of the process used by influenza virus particles to infect cells.

Charybdotoxin, a toxin produced by scorpions, blocks a K⁺ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K⁺ mimic in the selectivity filter.

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.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

A modified form of Green Fluorescent Protein integrated into an ammonium transporter provides a sensor that can be used to monitor transport activity in vivo.

α-SNAP mediated rearrangement of Stim1 and Orai1 molecules within CRAC channel clusters is required for store-operated calcium entry.

The basal body of the type-III secretion system of Yersinia enterocolitica within bacterial membranes shows elasticity and is longer than related isolated systems.

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.

Efflux of xenobiotic fluoride from microorganisms occurs through a novel family of ion channels with stringent selectivity for fluoride ion and dual-topology molecular architecture.