Results 151 to 160 of about 18,798 (210)
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Non-opioid actions of opioid peptides
Life Sciences, 2004Beside the well known actions of opioid peptides on mu-, delta- and kappa-opioid receptors, increasing amount of pharmacological and biochemical evidence has recently been published about non-opioid actions of various opioid peptides. These effects are not abolished by naloxone treatments.
Mária, Wollemann, Sándor, Benyhe
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Alcohol health and research world, 2005
Opioid peptides produced in the body act as neuromodulators that modify the actions of other neurotransmitters in the central nervous system. By altering the electrical properties of their target neurons, thereby making these neurons more difficult to excite, opioid peptides can influence the release of various neurotransmitters.
Daniel Daniel Tomé +2 more
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Opioid peptides produced in the body act as neuromodulators that modify the actions of other neurotransmitters in the central nervous system. By altering the electrical properties of their target neurons, thereby making these neurons more difficult to excite, opioid peptides can influence the release of various neurotransmitters.
Daniel Daniel Tomé +2 more
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Opioid and anti‐opioid peptides
Fundamental & Clinical Pharmacology, 1995Summary— The numerous endogenous opioid peptides (β‐endorphin, enkephalins, dynorphins…) and the exogenous opioids (such as morphine) exert their effects through the activation of receptors belonging to four main types: μ, Δ, k and ε. Opioidergic neurones and opioid receptors are largely distributed centrally and peripherally. It is thus not surprising
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Opioid receptors and endogenous opioid peptides
Medicinal Research Reviews, 1991The field to be reviewed is now 16 years old and is based on knowledge dating back centuries. It is therefore evident that an exhaustive review is impossible. The author plans to discuss areas likely to be of interest to the readers of this journal.
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Annual Review of Pharmacology and Toxicology, 1979
Opioid peptides are endogenous or synthetic peptides, with a spectrum of pharmacological activity similar to that of morphine and other narcotic agonist drugs. The designation opioid peptide can be made if (a) it produces morphine-like, naloxone reversible effects in several in vitro bioassay sys tems such as the guinea pig ileum (1), the cat ...
A, Beaumont, J, Hughes
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Opioid peptides are endogenous or synthetic peptides, with a spectrum of pharmacological activity similar to that of morphine and other narcotic agonist drugs. The designation opioid peptide can be made if (a) it produces morphine-like, naloxone reversible effects in several in vitro bioassay sys tems such as the guinea pig ileum (1), the cat ...
A, Beaumont, J, Hughes
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Cancer and Metastasis Reviews, 2004
Opioid and somatostatin systems are two main inhibitory systems in mammals implicated in a variety of processes from hormone secretion to the modulation of cell proliferation. Opioids and opioid receptors were found in a great diversity of primary human tumors and in various cancer cell lines.
Jakub, Fichna, Anna, Janecka
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Opioid and somatostatin systems are two main inhibitory systems in mammals implicated in a variety of processes from hormone secretion to the modulation of cell proliferation. Opioids and opioid receptors were found in a great diversity of primary human tumors and in various cancer cell lines.
Jakub, Fichna, Anna, Janecka
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Cyclization in Opioid Peptides
Current Drug Targets, 2013Endogenous opioid peptides have been studied extensively as potential therapeutics for the treatment of pain. The major problems of using natural opioid peptides as drug candidates are their poor receptor specificity, metabolic instability and inability to reach the brain after systemic administration.
Justyna, Piekielna +3 more
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Pigment Cell Research, 1996
Opioid peptides and other Tyr‐NH2‐terminal peptides are substrates in vitro for mushroom and sepia tyrosinase, giving rise to synthetic melanins retaining the peptide moiety (opiomelanins). The melanopeptides are characterized by a total solubility in hydrophylic solvents at neutral and basic pH. Opioid peptides (enkephalins, endorphins, and esorphins),
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Opioid peptides and other Tyr‐NH2‐terminal peptides are substrates in vitro for mushroom and sepia tyrosinase, giving rise to synthetic melanins retaining the peptide moiety (opiomelanins). The melanopeptides are characterized by a total solubility in hydrophylic solvents at neutral and basic pH. Opioid peptides (enkephalins, endorphins, and esorphins),
openaire +2 more sources