D. B. Veprintsev

This study investigates the kinetic selectivity of drugs targeting the β1-adrenoceptor, finding that hydrophobic interactions dominate ligand binding kinetics over combined polar and hydrophobic interactions.

This study identifies chemotype-specific biased signaling in cannabinoid receptors by analyzing ligand-induced signaling cascades.

ThermoBRET quantifies GPCR thermostability using BRET without labelled ligands, revealing ligand effects on protein unfolding in non-purified samples.

This paper demonstrates the functional solubilisation of the β2-adrenoceptor using DIBMA, showing improved thermal stability compared to detergent-based methods.

The paper describes a compound that covalently labels a GPCR with a fluorescent tag without blocking its binding site, enabling study of native GPCR function and localization.

This paper optimizes the production and purification of recombinant human Hsp90β in E. coli to yield a stable, pure, and well-folded protein.