Address and message sequences for the nociceptin receptor: a structure-activity study of nociceptin-(1-13)-peptide amide.

@article{Guerrini1997AddressAM,
  title={Address and message sequences for the nociceptin receptor: a structure-activity study of nociceptin-(1-13)-peptide amide.},
  author={R. Guerrini and G. Calo and A. Rizzi and C. Bianchi and L. Lazarus and S. Salvadori and P. Temussi and D. Regoli},
  journal={Journal of medicinal chemistry},
  year={1997},
  volume={40 12},
  pages={
          1789-93
        }
}
Nociceptin (NC) and some of its fragments as well as nociceptin-(1-13)-peptide amide [NC- (1-13)-NH2] and a series of its analogues were prepared and tested in the mouse vas deferens in an attempt to identify the sequences involved in the activation (message) and in the binding (address) of nociceptin to its receptor. The NC receptor that inhibits the electrically evoked twitches of the mouse vas deferens was demonstrated to be distinct from the delta opioid receptor, since naloxone and Dmt-Tic… Expand
Characterization of [Nphe1]nociceptin(1‐13)NH2, a new selective nociceptin receptor antagonist
Structure activity studies of nociceptin/orphanin FQ(1-13)-NH2 derivatives modified in position 5.
Helix-constrained nociceptin peptides are potent agonists and antagonists of ORL-1 and nociception.
Pronociceptive effects of nociceptin/orphanin FQ (13-17) at peripheral and spinal level in mice.
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