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.

Channel activity is a novel regulatory mechanism for channel mobility in the plasma membrane.

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.

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.

The structure of a bivalent double-knot tarantula toxin bound to the outer pore of the capsaicin receptor reveals a novel mode of toxin-channel recognition that has important implications for thermosensation.

TrpV1 receptor activation rescues cognition-relevant network dynamics in mouse hippocampus in an acute Alzheimer disease model providing a novel therapeutic target.

Globotriaosylcermide directly impacts neuronal integrity and ion channel function as potential mechanism underlying small fiber pathology in Fabry disease.

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 molecular identity of the temperature-sensitive ion channel of human sperm that ensures depolarization is TRPV4.

Electrophysiological experiments, Ca²⁺ imaging, and behavioral studies in mice identify the TRPM3 ion channel as a novel target of G-protein βγ subunits.