Maoqing Dong
Department of Molecular Pharmacology and Experimental Therapeutics
Mayo Clinic
13400 East Shea Boulevard
Scottsdale
USA
Name/email consistency: high
- Site of action of a pentapeptide agonist at the glucagon-like peptide-1 receptor. Insight into a small molecule agonist-binding pocket. Dong, M., Pinon, D.I., Miller, L.J. Bioorg. Med. Chem. Lett. (2012)
- Juxtamembranous region of the amino terminus of the family B G protein-coupled calcitonin receptor plays a critical role in small-molecule agonist action. Dong, M., Cox, R.F., Miller, L.J. J. Biol. Chem. (2009)
- Exploration of the endogenous agonist mechanism for activation of secretin and VPAC1 receptors using synthetic glycosylated peptides. Dong, M., Pinon, D.I., Miller, L.J. J. Mol. Neurosci. (2008)
- Insights into the structural basis of endogenous agonist activation of family B G protein-coupled receptors. Dong, M., Gao, F., Pinon, D.I., Miller, L.J. Mol. Endocrinol. (2008)
- Molecular approximation between residue 10 of secretin and its receptor demonstrated by photoaffinity labeling. Dong, M., Miller, L.J. Ann. N. Y. Acad. Sci. (2006)
- Importance of the amino terminus in secretin family G protein-coupled receptors. Intrinsic photoaffinity labeling establishes initial docking constraints for the calcitonin receptor. Dong, M., Pinon, D.I., Cox, R.F., Miller, L.J. J. Biol. Chem. (2004)
- Molecular approximation between a residue in the amino-terminal region of calcitonin and the third extracellular loop of the class B G protein-coupled calcitonin receptor. Dong, M., Pinon, D.I., Cox, R.F., Miller, L.J. J. Biol. Chem. (2004)
