Carsten Hoffmann

This study shows that hormone oscillations maintain cellular responsiveness and coordination across cell types by allowing receptor resensitization and buffering kinetic variation.

This study shows ACKR3 is released on extracellular vesicles under both basal and ligand-induced conditions, sequestering chemokines and opioid peptides and modulating their signaling.

This study uses dynamic pharmacophores to analyze binding mode ensembles of M2 receptor partial agonists and shows correlations between ligand efficacy and spatial distribution of lipophilic contacts.

The paper challenges the conventional view of GPCR internalization by showing multiple pathways regulate receptor internalization, with specific findings on the GLP-1R's mechanism.

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.

This study identifies non-canonical internalization mechanisms for mGlu receptors, showing some require neither GRKs nor beta-arrestins for agonist-induced internalization.

This study shows that the C-terminal tail of LPHN2 modulates G protein and arrestin-3 signaling bias through alternative splicing and GRK interactions.

This study uses NMR to show GRK1 and GRK2 produce distinct phosphorylation patterns on C-terminal peptides of GPCRs, revealing time-dependent phosphorylation barcodes that may influence arrestin interactions during desensitization.

The paper investigates how GPCR domains influence β-arrestin functions and conformational changes, revealing domain-specific effects on signaling outcomes.

The paper identifies microbial bile salt conjugates that activate TGR5 and FXR receptors in human systems and quantifies their presence in blood and bile.

The paper evaluates GRK antibodies for western blot specificity and introduces a method to compare protein abundance using suitable antibodies.