Masha Y. Niv

The paper uses molecular dynamics simulations to study how ligand binding at two sites of TAS2R14 affects receptor dynamics and chloride ion behavior.

The paper evaluates the Boltz-2 co-folding framework to predict ligand binding pockets in TAS2R GPCRs and identifies sequence features that determine pocket preference.

The paper examines how three pharmaceutical drugs activate TAS2R14 through different binding modes and efficacy, using cell-based assays and receptor mutations.

The paper investigates the inhibitory mechanisms of TAS2R14 antagonists by analyzing mutations and computational models, revealing distinct binding sites and potencies.

The paper reveals the cryo-EM structure of hTAS2R14 bound to FFA and gustducin, showing dual binding pockets and supporting a dual binding mode for FFA.

The paper discovers new ligands for the promiscuous TAS2R14 bitter taste receptor using a mixed experimental and computational approach, identifying 10 antagonists and 200 agonists.

The paper shows D2O activates T1R3 subunits in a transmembrane domain-dependent manner, with mutations impairing this activation.