Research into light-gated ion channels called channelrhodospins laid the foundations for the development of optogenetics, a technique that has gone on to revolutionize neuroscience.

In Drosophila, the loss of Frataxin causes iron accumulation in the nervous system, which in turn enhances sphingolipid synthesis and activation of PDK1 and Mef2, which leads to neurodegeneration.

Efflux of xenobiotic fluoride from microorganisms occurs through a novel family of ion channels with stringent selectivity for fluoride ion and dual-topology molecular architecture.

Two newly identified assembly factors for the ribosome-associated iron-sulfur protein Rli1 reveal a general mechanism for how the cytosolic iron-sulfur protein assembly (CIA) machinery recruits apoproteins.

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.

TMEM16F shifts its ion selectivity in response to change of intracellular Ca²⁺, membrane potential and ionic strength.

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.

An unbiased genome-wide human forward genetic screen identifies the vacuolar ATPase complex and assembly factors as regulators of HIF stability through their actions on intracellular iron metabolism.

Structures of OSCA1.2, a member of a newly characterized family of mechanically activated ion channels, provide insights into mechanism of channel gating by membrane tension.