Results 141 to 150 of about 4,036 (179)
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Characterization of bombesin receptors using a novel, potent, radiolabeled antagonist that distinguishes bombesin receptor subtypes.

Molecular Pharmacology, 1993
Bombesin (Bn)-related peptides affect numerous cell functions; however, receptor characterization by radiolabeled ligands is limited because only radiolabeled agonists exist. In the present study we demonstrate that [D-Tyr6]Bn(6-13)methyl ester [[D-Tyr6]Bn(6-13)ME] functions as a Bn receptor antagonist with high affinity.
S, Mantey   +3 more
openaire   +2 more sources

Regulation of bombesin receptors on pancreatic acini by cholecystokinin

American Journal of Physiology-Gastrointestinal and Liver Physiology, 1989
When guinea pig pancreatic acini are first incubated with the COOH-terminal octapeptide of cholecystokinin (CCK-8), washed, and then reincubated with 125I-[Tyr4]bombesin (125I-[Tyr4]BN) there is a significant decrease in binding of 125I-[Tyr4]BN compared with that observed with pancreatic acini that have been first incubated with no additions. The CCK-
M, Younes   +4 more
openaire   +2 more sources

Bombesin Receptor Subtype-3 in Human Diseases

Archives of Medical Research, 2019
This review summarizes the recent findings of the roles of bombesin receptor subtype-3 (BRS-3) in various patho-physiological conditions. Studies have demonstrated that two mammalians bombesin-like peptides, GRP and NMB, exhibit a large range of functions by binding to three receptors.
Mei, Li   +7 more
openaire   +2 more sources

Progress in the development of potent bombesin receptor antagonists

Trends in Pharmacological Sciences, 1991
Bombesin and the mammalian-related peptides gastrin-releasing peptide (GRP), GRP and neuromedin B have been shown to have numerous actions in the CNS, gastrointestinal tract and on growth. However, the role of the peptides in various physiological processes has remained unclear because of the lack of potent antagonists.
R T, Jensen, D H, Coy
openaire   +2 more sources

Bombesin Receptor Antagonists Block the Effects of Exogenous Bombesin but Not of Nutrients on Food Intake

Physiology & Behavior, 1997
The endogenous, meal-contingent release of bombesin (BN)-like peptides is thought to contribute to the termination of a meal. In the following experiments the potency of BN receptor antagonists to attenuate the ability of nutrients to suppress food intake was tested.
openaire   +2 more sources

Bombesin receptor antagonists

Critical Reviews in Oncology/Hematology, 1996
R, de Castiglione, L, Gozzini
openaire   +2 more sources

Mammalian bombesin receptors

Medicinal Research Reviews, 1995
G S, Kroog, R T, Jensen, J F, Battey
openaire   +2 more sources

Bombesin receptor antagonists

Drugs of the Future, 1998
null Moody, T.W., null Jensen, R.T.
openaire   +1 more source

Bombesin Receptors

2007
S.J. Enna, David B. Bylund
openaire   +1 more source

Interaction between bombesin receptor activated protein and bombesin receptor subtype 3

Regulatory Peptides, 2012
Y. Liu   +8 more
openaire   +1 more source

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