Combined simulations and electrophysiological experiments show that the CLC channels and exchangers form physically distinct and evolutionarily conserved pathways through which Cl^- and H⁺ ions move when crossing biological membranes.

Crystallography together with electron-resonance spectroscopy, molecular-dynamics simulations, and transport measurements reveal the molecular details of protein conformational change, and how this change contributes to function in a CLC-type chloride/proton exchanger.

Ano1 deletion disrupts Ca²⁺ waves within Kölliker’s organ, reduces burst-firing activity and frequency selectivity of auditory brainstem neurons in the medial nucleus of the trapezoid body, and impairs the functional refinement of its projections to the lateral superior olive.

A cryo-electron microscopy study of the human CLC-1 chloride ion channel reveals the structural basis of why some CLC proteins function as passive chloride channels whereas others function as an active proton-chloride antiporters.

Single-particle cryo-EM and electrophysiology studies of the chloride channel TMEM16A reveals the structural basis for anion conduction and uncover its relationship to lipid scramblases of the same family.

Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.

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

A combination of high-resolution structure determination, electrophysiology, and MD simulations reveal fundamental insight into the molecular function of voltage-gated chloride channels.

Through interactions with viral RNA and NS5, Zika virus changes the composition of the IGF2BP2-containing ribonucleoprotein complex for the benefit of the viral RNA amplification step of its life cycle.

Genetic and cellular studies in rodents found branched-chain amino acids are critical nutrients that are transported and oxidized in the mitochondria through their carrier MBC for optimal febrile responses.