Gebhard F. X. Schertler

This paper resolves the mechanism of covalent bond formation in a LOV photoreceptor using time-resolved crystallography and spectroscopy, revealing a water-mediated proton transfer that accelerates the reaction by fourteen orders of magnitude.

This paper discovers NHAP, a fungal metabolite that selectively inhibits Gi-signaling, demonstrating functional blockade in cardiomyocytes without cytotoxicity.

This paper introduces optoDRD1, a photoswitchable optoGPCR that reversibly controls Gs signaling and arrestin recruitment using distinct wavelengths of light.

The paper develops cost-effective isotope labeling protocols in HEK293 cells for NMR studies of difficult-to-produce human proteins, enabling detailed structural and functional analysis.

This study identifies a novel chloride counterion mechanism in coral opsins that stabilizes the Schiff base proton, enabling light sensitivity without a traditional counterion residue.

This study presents active state structures of a bistable opsin, JSR1, bound to G proteins, revealing differences in activation mechanisms between monostable and bistable opsins.

This study shows that the all-trans 6.11 retinal analogue activates the invertebrate bistable opsin JSR1 and enables complex formation with downstream signaling partners.

This paper reports a method to capture the blue-light activated state of the Phot-LOV1 domain using time-resolved serial synchrotron crystallography and provides structural insights into its activation cascade.

This study determines the crystal structures of FR and YM bound to G11, revealing they stabilize Gq/11 heterotrimers by reinforcing the G and Gβ interface.

The paper analyzes variability in cryo-EM datasets of GPCR-G-protein complexes to identify common movements across different receptor-G-protein systems.

This study tests a dimeric prion protein ligand as a therapy for peripheral demyelination but finds it fails to rescue myelinopathy in PrP-deficient mice.