G. Skiniotis

This study uses time-resolved cryo-EM to visualize the conformational changes in a GPCR-G protein complex during activation, revealing the structural pathway of G protein dissociation.

This study investigates how endocannabinoids modulate CB1 receptor signaling by comparing their activation of Gi1 with synthetic cannabinoids and revealing structural differences in ligand binding.

The paper reports cryoEM structures of the μ-opioid receptor bound to biased agonists PZM21 and FH210, revealing structural basis for reduced β-arrestin recruitment and guiding development of safer analgesics.

The paper develops and validates OPLS-AA/M force field parameters for simulating GPCRs and other membrane proteins, showing reliable behavior compared to quantum mechanics and experimental data.

This study compares the structural and signaling differences between two μOR agonists, lofentanil and mitragynine pseudoindoxyl, revealing how their distinct binding modes lead to different G protein and β-arrestin activation profiles.

The paper presents cryo-EM structures of SSTR2 with ligands and Gi protein, revealing ligand recognition mechanisms and subtype selectivity.

This paper uses nanobodies to determine cryo-EM structures of inactive-state GPCRs, achieving resolutions comparable to X-ray crystallography and providing insights into ligand binding.

The paper reports a cryoEM structure of the PDE6 complex with GTP-bound transducin, revealing its catalytic mechanism and conformational dynamics.

The paper shows that Dvl and Axin oligomerization dynamics regulate Wnt/β-catenin signaling efficiency by controlling β-catenin phosphorylation inhibition.

GemSpot models ligand poses into cryoEM maps using computational chemistry methods, achieving accurate interactions and map agreement in validated cases.

This paper introduces DRRAFTER, a method to model RNA-protein complexes from cryoEM maps, showing it can build accurate RNA coordinates in real-world scenarios.