Sébastien Granier

This study identifies distinct determinants of ACKR1 recognition by bacterial toxins, revealing a two-step mechanism involving sulfotyrosine binding and extracellular vestibule interaction.

This paper develops an electrophysiological method to study pore formation by bi-component staphylococcal leukotoxins in real-time using Xenopus oocytes, revealing receptor-dependent kinetics and a hybrid model of subunit oligomerization.

This study identifies Ephrin B1 as a key mediator of CXCR4 tumorigenic signaling by promoting its intracellular localization and inhibiting surface expression and signaling.

This study shows deltaviruses use helper virus particles as Trojan Horses for cell entry, revealing a new mode of viral transmission.

This study uses inverse agonistic nanobodies to reveal constitutive activity of ACKR3, showing it drives non-canonical signaling and basal cell motility, suggesting therapeutic potential.

The paper solves cryo-EM structures of the V2R bound to Tolvaptan and Mambaquaretin toxin, revealing distinct antagonist binding modes and inactive conformations.

This study investigates the conformational dynamics of ACKR3 activation using HDX-MS and molecular dynamics simulations, revealing key structural changes and ligand binding mechanisms.

The paper investigates how opioid ligands selectively activate G protein over β-arrestin pathways in the μ-opioid receptor using a combination of experimental and computational methods.