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A transient receptor channel in Toxoplasma gondii that conducts calcium represents the first molecular element that initiates upstream calcium signals that activate parasite pathogenic pathways.

Highly temperature-sensitive behavior of voltage-gated potassium channels provides a mechanistic model for how heat-activated TRP channels serve as temperature and pain sensors.

C-terminal domain of thermoTRPV channels regulates channel gating at the cytoplasmic interface through a switch-like process.

Disease-associated mutants of the TRPM3 ion channel are overactive, and they are inhibited by the antiepileptic medication primidone, offering a potential therapeutic intervention to treat this channelopathy.

The cooling agent pocket in TRPM8 is conserved in a subset of other TRPM channels and the cooling agent icilin can regulate opening of TRPM4 channels in response to calcium and voltage.

PKD2 (polycystin-2) channels are a major component of a flow-sensing signaling mechanism in endothelial cells that stimulates vasodilation and reduces blood pressure.

Arterial myocyte PKD2 channels are activated by vasoconstrictor stimuli, which increases blood pressure, are upregulated during hypertension and cell-specific knockout in vivo reduces both physiological blood pressure and hypertension.

TRPV channels share general mechanisms of activation while exhibiting subtype-specific features along the activation pathway that can determine their apparent sensitivity to stimuli.

Pro-nociceptive and pro-inflammatory TRPM3 (transient receptor potential melastatin 3) channels, expressed in somatosensory neurons, are inhibited by activation of Gαi-coupled receptors, such as µ-opioid receptors, in vitro and in vivo.

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