Vanilloid sensitivity has been introduced into the TRPV2 channel, revealing that the gating and permeation properties of this enigmatic TRP channel are remarkably similar to the capsaicin receptor.

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

Activation of TRPV4 induced increases in Ca²⁺ influx, activated CaMKII, enhanced pro-inflammatory NFκB-NLRP3 signaling, and promoted inflammation response, thus contributing to pathological cardiac remodeling.

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.

Targeting senescent cells in human intervertebral discs, using senotherapeutics, provides a potential therapeutic strategy to prevent or reduce disc degeneration and pain.

Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.

Eugenol has the potential as a novel exercise mimetic, and TRPV1 may represent a promising target for the development of exercise mimetics.

Novel capsaicin analogs with conserved chemistry but varying sizes were used as molecular rulers to investigate energetics of conformational changes in the ligand-binding pocket and mechanisms of TRPV1 ligand-gating.

Allosteric gating in a transient receptor potential channel is modulated by external sodium ions and a tarantula toxin.

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