The tarantula toxins psalmotoxin and guangxitoxin have a similar concave surface for interacting with α-helices in voltage-gated and acid-sensing ion channels.

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.

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

Mapping the locations of hypertrophic cardiomyopathy gene variants onto the three-dimensional structures of contractile proteins revealed that these disrupt protein interactions are critical for normal cardiac relaxation and efficient energy usage.

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.

Integrative analysis of a Drosophila model of hypertrophic cardiomyopathy demonstrates that prolonged binding of the myosin cross-bridge to actin is a root cause of the disorder.

A mutation that causes heart disease in humans increases the number of active myosin heads during contraction in the muscles of fruit flies, leading to the progressive dysfunction of the flight muscles and heart tube.

X-ray crystallography reveals new conceptual insights into the location of the β2-subunit in the Na_v channel signaling complex.

Three residues work together as a valve-like mechanism to control desensitization from pre-open and open states in the ion channels ASIC1a, ASIC2a, and ASIC3.