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Your search keyword '"Mathiesen, Jesper Mosolff"' showing total 18 results

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18 results on '"Mathiesen, Jesper Mosolff"'

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1. Glycine: a long-sought novel ligand for GPR158.

2. Negative allosteric modulation of the glucagon receptor by RAMP2.

3. Glepaglutide, a novel glucagon-like peptide-2 agonist, has anti-inflammatory and mucosal regenerative effects in an experimental model of inflammatory bowel disease in rats.

4. Structural insights into differences in G protein activation by family A and family B GPCRs.

5. Probing the Existence of a Metastable Binding Site at the β 2 -Adrenergic Receptor with Homobivalent Bitopic Ligands.

6. G s protein peptidomimetics as allosteric modulators of the β 2 -adrenergic receptor.

7. A cAMP Biosensor-Based High-Throughput Screening Assay for Identification of Gs-Coupled GPCR Ligands and Phosphodiesterase Inhibitors.

8. Real-time trafficking and signaling of the glucagon-like peptide-1 receptor.

9. cAMP biosensors applied in molecular pharmacological studies of G protein-coupled receptors.

10. A new metabotropic glutamate receptor agonist with in vivo anti-allodynic activity.

11. The C-terminal tail of CRTH2 is a key molecular determinant that constrains Galphai and downstream signaling cascade activation.

12. Antagonism of the prostaglandin D2 receptor CRTH2 attenuates asthma pathology in mouse eosinophilic airway inflammation.

13. Novel selective orally active CRTH2 antagonists for allergic inflammation developed from in silico derived hits.

14. The metabotropic glutamate receptor 4 is internalized and desensitized upon protein kinase C activation.

15. On the mechanism of interaction of potent surmountable and insurmountable antagonists with the prostaglandin D2 receptor CRTH2.

16. Molecular pharmacology and therapeutic prospects of metabotropic glutamate receptor allosteric modulators.

17. Identification of indole derivatives exclusively interfering with a G protein-independent signaling pathway of the prostaglandin D2 receptor CRTH2.

18. Positive allosteric modulation of the human metabotropic glutamate receptor 4 (hmGluR4) by SIB-1893 and MPEP.

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