Claire Weill

TL;DR: A compact architecture for the muscarinic M1 receptor amino‐terminal domain is suggested which may fold in a manner similar to that of rhodopsin, and this fluorescence‐based assay allows reliable detection of unlabelled competitors.

TL;DR: Efficient protein delivery with a non-peptide based reagent is demonstrated, in human epithelial carcinoma HeLa cells and primary human skin fibroblasts and a step-by-step method to optimize conditions for successful intracellular protein delivery is presented.

TL;DR: The ability to introduce antibodies to live cells opens new insights to a wide range of applications, such as protein intracellular trafficking studies, protein interference studies with blocking antibodies, and live immunolabeling or protein phosphorylation states studies.

TL;DR: Four recombinant human M1 (hM1) muscarinic acetylcholine receptors (mAChRs) combining several modifications were designed and overexpressed in HEK293 cells, demonstrating that these EGFP‐ and epitope‐fused hM1 receptors are valuable tools for further functional, biochemical, and structural studies ofMuscarinic receptors.

TL;DR: Ligand binding properties of--and activation of the calcium release response by--the fusion proteins are almost identical to those of the wild-type muscarinic receptor, indicating that such fluorescently-labelled receptors are valuable model systems for further functional, biochemical and structural studies.