Structure-activity relationships and structural conformation of a novel urotensin II-related peptide.

@article{Chatenet2004StructureactivityRA,
  title={Structure-activity relationships and structural conformation of a novel urotensin II-related peptide.},
  author={David Chatenet and Christophe Dubessy and J{\'e}r{\^o}me Leprince and C{\'e}dric Boularan and Ludovic Carlier and Isabelle S{\'e}galas-Milazzo and Laure Guilhaudis and Hassan Oulyadi and Daniel Davoust and Elizabeth Scalbert and Bruno Pfeiffer and Pierre Renard and M. Tonon and Isabelle Lihrmann and Pierre Pacaud and Hubert Vaudry},
  journal={Peptides},
  year={2004},
  volume={25 10},
  pages={1819-30}
}
Urotensin II (UII) has been described as the most potent vasoconstrictor peptide and recognized as the endogenous ligand of the orphan G protein-coupled receptor GPR14. Recently, a UII-related peptide (URP) has been isolated from the rat brain and its sequence has been established as H-Ala-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH. In order to study the structure-function relationships of URP, we have synthesized a series of URP analogs and measured their binding affinity on hGPR14-transfected cells and… CONTINUE READING

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