Exploiting virus-encoded ion channels as drug targets drove a multi-faceted approach to deriving potent small molecules targeting HCV p7, simultaneously providing new insights into its fundamental biology.

MD-simulations reveal low- to high-affinity conformational shift of orthosteric site in the nicotinic acetylcholine receptor, offering insight into agonist roles in activation dynamics, and highlighting the utility of agonist efficiency.

During viral assembly, ESCRTIII and VPS4 are recruited after most of the HIV-1 membrane is bent but disappear prior to scission of the virion from the cell.

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.

Introduction of single photoswitchable unnatural amino acid into a neuronal receptor provides reversible, rapid and robust control of its activity by light, representing an important contribution to the fast expanding field of optopharmacology.

CryoEM reveals the structure of a two-component archaeal S-layer, which sheds new light on archaeal cell biology.

Biochemical analysis on hetero-mutated c₁₀ subunits ring and molecular dynamics simulations demonstrate the cooperation among c-subunits of F_oF₁-ATP synthase in rotation-coupled proton translocation.

Benzene mapping simulations of envelope protein rafts from six different flaviviruses reveal a conserved cryptic site whose cluster of ionisable residues is likely responsible for orchestrating pH-dependent conformational changes during fusion, thereby representing an attractive target for antiviral development.

Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.