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Stable Expression of the Human Kinin B1 Receptor in Chinese Hamster Ovary Cells
TLDR
The B1, unlike the B2, receptor does not desensitize (as demonstrated by continuous phosphoinositide hydrolysis), enhancing the potential role of this receptor during inflammatory events.
Antinociceptive profile of the pseudopeptide B2 bradykinin receptor antagonist NPC 18688 in mice
TLDR
The action of NPC 18688 was quite selective for the B2 receptor, and like Hoe 140, it caused graded inhibition of bradykinin (BK, 3 mol/paw)‐induced increase in mouse paw volume, with mean ID50S and MI of 6 and 9 nmol kg−1 and 56±7 and 62±6%, respectively.
Roles of μ-Opioid Receptors and Nociceptin/Orphanin FQ Peptide Receptors in Buprenorphine-Induced Physiological Responses in Primates
TLDR
Functional evidence that the activation of NOP receptors did not attenuate buprenorphine-induced antinociception in primates is provided and the therapeutic potential of mixed MOP/NOP agonists as innovative analgesics is strongly supported.
Oral antinociception and oedema inhibition produced by NPC 18884, a non-peptidic bradykinin B2 receptor antagonist
TLDR
The novel non-peptide BK B2 receptor antagonist NPC 18884 produces rapid onset, potent and relatively long-lasting oral antinociceptive and oedema inhibition properties.
The N Terminus of Bradykinin When Bound to the Human Bradykinin B2 Receptor Is Adjacent to Extracellular Cys20 and Cys277 in the Receptor*
TLDR
Results show that Cys103 and Cys184 are both required for expression of high affinity agonist and antagonist binding sites in the human B2 receptor, while Cys20 and CYS277 are not required.
NMR and computational evidence that high-affinity bradykinin receptor antagonists adopt C-terminal beta-turns.
TLDR
The results presented support the hypothesis that high-affinity bradykinin receptor antagonists must adopt C-terminal beta-turn conformations.
Pharmacological profile of NPC 12626, a novel, competitive N-methyl-D-aspartate receptor antagonist.
TLDR
The results of the current study indicate that NPC 12626 is a novel, systemically active and competitive NMDA receptor antagonist.
Novel, potent ORL-1 receptor agonist peptides containing alpha-Helix-promoting conformational constraints.
TLDR
The data support a hypothesis that the receptor-bound form of NC might adopt an amphipathic helix in the "address" segment of the sequence, which is implicated in a wide variety of physiological and pathophysiological processes.
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