The small glycine residue in the Cav selectivity filter is an overlooked feature that determines Ca²⁺ selectivity and provides new insight into the Ca²⁺ selectivity mechanism conserved from prokaryotes to eukaryotes.

The transmembrane helices forming the pore determine the conductance of the selectivity filter through allosteric interactions.

The TRPV1, TRPV2 and TRPV3 channels are gated on the cytosolic side of the pore, whereas structural changes in the ion selectivity filter associated with activation don't control cation access.

Polyunsaturated fatty acids activate IKs channels by stabilizing a conductive state of the selectivity filter.

A chain of residues connecting the voltage sensing domain and the pore domain is responsible for a noncanonical communication between these domains.

Single-molecule measurement of conformational dynamics using a genetically encoded fluorescent probe suggests that the selectivity filter region of TRPV1 channels undergoes dynamic motion during agonist activation.

Invertebrate TRPM2 channels have stable pores but act as chanzymes that hydrolyze their activating ligand ADP ribose (ADPR), whereas vertebrate TRPM2 channels are catalytically dead but undergo pore inactivation.

Structural and functional analysis of a recently discovered non-canonical potassium channel family reveals a unique selectivity filter that is exposed to permeating ions only in the conductive state.

The conformation of an isoleucine gate located along the TM6 segment on the intracellular side below the selectivity filter is a critical component leading to a non-conductive state in the C-type inactivation process of K⁺ channels.

Sodium selectivity of acid-sensing ion channels is mediated by negatively charged side chains and not by a size-exclusion mechanism.