Drug design for G-protein-coupled receptors by a ligand-based NMR method.
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Christian Griesinger | Teresa Carlomagno | K Ulrich Wendt | T. Klabunde | C. Griesinger | T. Carlomagno | S. Bartoschek | Ingo Focken | Stefan Bartoschek | Thomas Klabunde | S. Stengelin | Ingo Focken | K. Wendt | Elisabeth Defossa | Viktoria Dietrich | Siegfried Stengelin | E. Defossa | Viktoria Dietrich | Stefan Bartoschek
[1] Jens Meiler,et al. The INPHARMA method: protein-mediated interligand NOEs for pharmacophore mapping. , 2005, Angewandte Chemie.
[2] M. Nilges,et al. Re‐Face Stereospecificity of Methylenetetrahydromethanopterin and Methylenetetrahydrofolate Dehydrogenases is Predetermined by Intrinsic Properties of the Substrate , 2001, Chembiochem : a European journal of chemical biology.
[3] H. Shapiro,et al. Role of GPR40 in fatty acid action on the β cell line INS-1E , 2005 .
[4] Gebhard F. X. Schertler,et al. Structure of a β1-adrenergic G-protein-coupled receptor , 2008, Nature.
[5] Bernd Meyer,et al. Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy. , 1999, Angewandte Chemie.
[6] K. Akasaka. Intermolecular spin diffusion as a method for studying macromolecule-ligand interactions , 1979 .
[7] Masataka Harada,et al. Free fatty acids regulate insulin secretion from pancreatic β cells through GPR40 , 2003, Nature.
[8] B. Meyer,et al. Charakterisierung von Ligandenbindung durch Sättigungstransfer‐Differenz‐NMR‐Spektroskopie , 1999 .
[9] J. Drews. Drug discovery: a historical perspective. , 2000, Science.
[10] B. Meyer,et al. Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin alpha(IIb)beta3 in native platelets than in liposomes. , 2005, Journal of the American Chemical Society.
[11] J. Chambers,et al. Neuromedin U Is a Potent Agonist at the Orphan G Protein-coupled Receptor FM3* , 2000, The Journal of Biological Chemistry.
[12] R. Stevens,et al. The 2.6 Angstrom Crystal Structure of a Human A2A Adenosine Receptor Bound to an Antagonist , 2008, Science.
[13] J. Sanders,et al. Nuclear magnetic double resonance; the use of difference spectroscopy , 1982 .
[14] C. Griesinger,et al. Specific methyl group protonation for the measurement of pharmacophore-specific interligand NOE interactions. , 2008, Chemistry.
[15] R. MacKinnon. Potassium channels and the atomic basis of selective ion conduction (Nobel Lecture). , 2004 .
[16] Peter Monecke,et al. Crystallography-independent determination of ligand binding modes. , 2008, Angewandte Chemie.
[17] M. Mortrud,et al. The G protein-coupled receptor repertoires of human and mouse , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[18] Roderick MacKinnon. Kaliumkanäle und die atomare Basis der selektiven Ionenleitung (Nobel-Vortrag)† , 2004 .
[19] B. Meyer,et al. Determination of the binding specificity of an integral membrane protein by saturation transfer difference NMR: RGD peptide ligands binding to integrin alphaIIbbeta3. , 2001, Journal of medicinal chemistry.