Alexander Zürn

TL;DR: The results suggest that GPCRs are present on the cell surface in a dynamic equilibrium, with constant formation and dissociation of new receptor complexes that can be targeted, in a ligand-regulated manner, to different cell-surface microdomains.

TL;DR: A generally applicable labeling procedure that can be applied to proteins with expression below 1 pmol mg−1 of protein, such as G protein–coupled receptors, and it can be used to study the intracellular localization of proteins as well as functional interactions in fluorescence resonance energy transfer experiments.

TL;DR: Data suggests that partial agonism is linked to distinct conformational changes within a G-protein-coupled receptor and agrees with X-ray receptor structures indicating larger agonist-induced movements at the cytoplasmic ends of transmembrane domain VI than V.

TL;DR: Recent progress in biophysical approaches that have led to the current understanding of conformational changes that occur during GPCR activation are summarized.

TL;DR: This work reports site-specific, orthogonal labeling of two cellular proteins in intact cells with two small fluorescent dyes: fluorescein arsenical hairpin binder, FlAsH, and its red analogue, Re asH, which bind to tetracysteine motifs.