Molecular basis for agonist selectivity and activation of the orphan bombesin receptor subtype 3 receptor. (scientific article published on 15 November 2007)

International Union of Pharmacology. LXVIII. Mammalian bombesin receptors: nomenclature, distribution, pharmacology, signaling, and functions in normal and disease states

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Rational design of a peptide agonist that interacts selectively with the orphan receptor, bombesin receptor subtype 3.

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The fifth transmembrane segment of the neuromedin B receptor is critical for high affinity neuromedin B binding

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Discovery of a high affinity radioligand for the human orphan receptor, bombesin receptor subtype 3, which demonstrates that it has a unique pharmacology compared with other mammalian bombesin receptors

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Ability of various bombesin receptor agonists and antagonists to alter intracellular signaling of the human orphan receptor BRS-3.

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The design of a new potent and selective ligand for the orphan bombesin receptor subtype 3 (BRS3).

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An aspartate residue at the extracellular boundary of TMII and an arginine residue in TMVII of the gastrin-releasing peptide receptor interact to facilitate heterotrimeric G protein coupling

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Identification of Four Amino Acids in the Gastrin-releasing Peptide Receptor That Are Required for High Affinity Agonist Binding

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Development of bombesin analogs with conformationally restricted amino acid substitutions with enhanced selectivity for the orphan receptor human bombesin receptor subtype 3.

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Identification of a unique ligand which has high affinity for all four bombesin receptor subtypes

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P433

issue

P407

language of work or name

English

Q1860

P304

page(s)

463-474