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.

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.

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

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.

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.

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

A chemical probe was characterized for potency, selectivity, and ability to alter CARM1-dependent epigenetic plasticity against cancer cell invasion.

Adapting to rapid or slow finger tapping selectively biases the apparent numerosity of sequences or arrays of visual stimuli.

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.

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.