Articles dans des revues avec comité de lecture (48)
  1. 24. Langlet, C., Nachtergael, I., Robberecht, P., & Langer, I. (2006). Mutation of the phosphorylatable residue Thr429 in Glu of the human VPAC1 led to a constitutively desensitized receptor. Peptides, 27(7), 1865-1870. doi:10.1016/j.peptides.2006.01.010
  2. 25. Tikhonova, I. G., Boulègue, C., Langer, I., & Fourmy, D. (2006). Modeled structure of the whole regulator G-protein signaling-2. Biochemical and biophysical research communications, 341(3), 715-720. doi:10.1016/j.bbrc.2005.12.221
  3. 26. Foucaud, M., Tikhonova, I. G., Langer, I., Escrieut, C., Dufresne, M., Seva, C., Maigret, B., & Fourmy, D. (2006). Partial agonism, neutral antagonism, and inverse agonism at the human wild-type and constitutively active cholecystokinin-2 receptors. Molecular pharmacology, 69(3), 680-690. doi:10.1124/mol.105.019992
  4. 27. Langlet, C., Langer, I., Vertongen, P., Gaspard, N., Vanderwinden, J.-M., & Robberecht, P. (2005). Contribution of the carboxyl terminus of the VPAC1 receptor to agonist-induced receptor phosphorylation, internalization, and recycling. The Journal of biological chemistry, 280(30), 28034-28043. doi:10.1074/jbc.M500449200
  5. 28. Langer, I., Tikhonova, I. G., Travers, M.-A., Archer-Lahlou, E., Escrieut, C., Maigret, B., & Fourmy, D. (2005). Evidence that interspecies polymorphism in the human and rat cholecystokinin receptor-2 affects structure of the binding site for the endogenous agonist cholecystokinin. The Journal of biological chemistry, 280(23), 22198-22204. doi:10.1074/jbc.M501786200
  6. 29. Langer, I., Langlet, C., & Robberecht, P. (2005). Effect of inactivating mutations on phosphorylation and internalization of the human VPAC2 receptor. Journal of molecular endocrinology, 34(2), 405-414. doi:10.1677/jme.1.01717
  7. 30. Langer, I., & Robberecht, P. (2005). Mutations in the carboxy-terminus of the third intracellular loop of the human recombinant VPAC1 receptor impair VIP-stimulated [Ca2+]i increase but not adenylate cyclase stimulation. Cellular signalling, 17(1), 17-24. doi:10.1016/j.cellsig.2004.05.009
  8. 31. Langlet, C., Gaspard, N., Nachtergael, I., Robberecht, P., & Langer, I. (2004). Comparative efficacy of VIP and analogs on activation and internalization of the recombinant VPAC2 receptor expressed in CHO cells. Peptides, 25(12), 2079-2086. doi:10.1016/j.peptides.2004.08.017
  9. 32. Vertongen, P., Langlet, C., Langer, I., Gaspard, N., & Robberecht, P. (2004). Ac His1 [D-Phe2, K15, R16, L27] VIP (3-7)/GRF (8-27)--a VPAC1 receptor antagonist--is an inverse agonist on two constitutively active truncated VPAC1 receptors. Peptides, 25(11), 1943-1949. doi:10.1016/j.peptides.2004.06.001
  10. 33. Langer, I., Grégoire, F., Nachtergael, I., De Neef, P., Vertongen, P., & Robberecht, P. (2004). Hexanoylation of a VPAC2 receptor-preferring ligand markedly increased its selectivity and potency. Peptides, 25(2), 275-278. doi:10.1016/j.peptides.2003.12.013
  11. 34. Nachtergael, I., Vertongen, P., Langer, I., Perret, J., Robberecht, P., & Waelbroeck, M. (2003). Evidence for a direct interaction between the Thr11 residue of vasoactive intestinal polypeptide and Tyr184 located in the first extracellular loop of the VPAC2 receptor. Biochemical journal, 370(Pt 3), 1003-1009. doi:10.1042/BJ20020811
  12. 35. Langer, I., Vertongen, P., Perret, J., Waelbroeck, M., & Robberecht, P. (2003). Lysine 195 and aspartate 196 in the first extracellular loop of the VPAC1 receptor are essential for high affinity binding of agonists but not of antagonists. Neuropharmacology, 44(1), 125-131.
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