ライフサイエンスコーパス: NMB-R

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1 tivating squid Galphaq more effectively, and NMB-R also showed slight preference for squid Galphaq.

2 GRP-R and NMB-R catalyzed GTPgammaS binding to both squid and mous

3 te these qualitative similarities, GRP-R and NMB-R had distinct kinetic properties in receptor-G prot

4 ved in all species variants of the GRP-R and NMB-R which bind bombesin with high affinity, but they a

5 red to the other two BN receptors, GRP-R and NMB-R, and a natural ligand for BRS-3 is currently unkno

6 Like GRP-R and NMB-R, BRS-3 did not catalyze GTPgammaS binding to Galph

7 A binds with nanomolar affinity to GRP-R and NMB-R, has low retention of radioactivity in kidney, dem

8 The GRP-R- and NMB-R-catalyzed activations of Galphaq were dependent up

9 ld be conserved among all homologues of bb4, NMB-R, and GRP-R; conversely, at least one of these amin

10 RS-3 protein and 53% identity with the mouse NMB-R protein.

11 the present study we explored the ability of NMB-R activation to cause tyrosine phosphorylation of fo

12 These results demonstrate that activation of NMB-R can cause rapid tyrosine phosphorylation of p125(F

13 Only NMB-R-null mice accumulated fewer lung mast cells after

14 Cells expressing GRP-R or NMB-R catalyzed the activation of squid retinal Galphaq

15 the conserved amino acids in either GRP-R or NMB-R increased the affinity of the mutated BRS-3 (4Delt

16 site for the recently described non-peptide NMB-R antagonist PD168368.

17 All species homologues of GRP-R, NMB-R, and bb4 bind bombesin with dissociation constants

18 .8 nmol/L) and to the neuromedin B receptor (NMB-R) (0.9 nmol/L), with no affinity for the bb3 recept

19 h bombesin receptors (neuromedin B receptor (NMB-R) and gastrin-releasing peptide receptor (GRP-R)).

20 receptor (GRP-R), the neuromedin B receptor (NMB-R), and bombesin receptor subtype 3 (BRS-3).

21 ide receptor (GRP-R), neuromedin B receptor (NMB-R), and bombesin receptor subtype 3 (BRS-3).

22 receptor (GRP-R), the neuromedin B receptor (NMB-R), bombesin receptor subtype 3 (BRS-3), and bombesi

23 eceptor subtype 3 and neuromedin-B receptor (NMB-R), but not gastrin-releasing peptide receptor.

24 istinct receptor, the neuromedin B receptor (NMB-R), of which little is known about its cellular basi

25 ptor (GRP-R, or bb2), neuromedin B receptor (NMB-R, or bb1), and the bombesin receptor subtype 3 (BRS

26 ritical for high affinity NMB binding to the NMB-R.

27 y that is close to the affinity of wild-type NMB-R for NMB.

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