Characterization of Ca²⁺ selectivity and non-conductance mechanism induced by pore mutation N617D in the skeletal muscle DHPR.

A peptide derived from BK and JC polyomavirus protein VP2/3 inhibits viral infection by targeting a binding site in the pore of polyomavirus VP1 pentamers, enabling future VP1-targeted therapeutic strategies.

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.

Studies of EMRE, one of the four essential protein subunits in the mitochondrial calcium uniporter complex that regulates calcium ion levels in mitochondria, reveal new details about the physical interactions between the subunits.

Arc-shaped PFO oligomers consisting of at least four subunits can insert into the membrane in a kinetically controlled process opening a transmembrane pore, whereby post-insertion growth may ultimately lead to formation of a complete ring.

Genetic, proteomic, and structural analyses provide insight into the role of Brl1 during nuclear pore complex biogenesis, suggesting a function in the fusion of outer and inner nuclear membranes.

Efficiency measures the fundamental link between agonist binding and protein conformational change, and in nicotinic receptors has 5 values that calibrate energy changes in the induced fit that triggers activation.

Gating currents analysis at different Ca²⁺ concentrations of BK channels reveals a strong allosteric coupling between Ca²⁺- and voltage-sensing modules via equivalent contributions exerted by the RCK1 and RCK2 Ca²⁺-sites.

The centipede peptide toxin SpTx1 blocks the pore of ATP-sensitive potassium channels in pancreatic β cells to markedly enhance insulin secretion and mitigate hyperglycemia in diabetic mice insensitive to the anti-diabetic sulfonylurea glibenclamide.

Ligand-induced two-fold symmetric arrangement in TRPV2 is observed in the native-like nanodisc-reconstituted condition using cryo-electron microscopy.