Results 311 to 320 of about 1,112,203 (348)
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Synthesis and activity profiles of novel cyclic opioid peptide monomers and dimers.
Journal of Medicinal Chemistry, 1985A new family of cyclic opioid peptide analogues of the type H-Tyr-D-Xxx-Phe-Yyy-NH2 was obtained through amide bond formation between side chain amino and carboxyl groups of Orn (or Lys) and Asp (or Glu) residues substituted in positions 2 and 4 of the ...
P. Schiller+3 more
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New trends in the development of opioid peptide analogues as advanced remedies for pain relief.
Current Topics in Medicinal Chemistry, 2004The search for new peptides to be used as analgesics in place of morphine has been mainly directed to develop peptide analogues or peptidomimetics having higher biological stability and receptor selectivity.
L. Gentilucci
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Journal of Medicinal Chemistry, 1991
In an effort to determine the effect of side chain conformational restriction on opioid receptor selectivity, the cyclic phenylalanine analogues 2-aminoindan-2-carboxylic acid (Aic), 2-aminotetralin-2-carboxylic acid (Atc), and tetrahydroisoquinoline-3 ...
P. Schiller+6 more
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In an effort to determine the effect of side chain conformational restriction on opioid receptor selectivity, the cyclic phenylalanine analogues 2-aminoindan-2-carboxylic acid (Aic), 2-aminotetralin-2-carboxylic acid (Atc), and tetrahydroisoquinoline-3 ...
P. Schiller+6 more
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'Cross talk' between opioid peptide and adrenergic receptor signaling in isolated rat heart.
Circulation, 1997BACKGROUND Cardiac myocyte sarcolemma contains both catecholamine and opioid peptide receptors (OPRs). Opioid peptides are coreleased with catecholamines from nerve terminals in the heart. We investigated whether OPR stimulation influences the effects of
S. Pepe+4 more
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An all D-amino acid opioid peptide with central analgesic activity from a combinatorial library.
Science, 1994A synthetic combinatorial library containing 52,128,400 D-amino acid hexapeptides was used to identify a ligand for the mu opioid receptor. The peptide, Ac-rfwink-NH2, bears no resemblance to any known opioid peptide. Simulations using molecular dynamics,
C. Dooley+6 more
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Palatal myoclonus and opioid peptides
Acta Neurologica Scandinavica, 2009We report a patient who presented palatal myoclonus (PM) after anoxic brain damage that was completely abolished by the administration of opioid agonists. This suggests the involvement of peptide systems in the development of PM.
P. Martínez‐Lage Alvarez+3 more
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Opioid peptides and their receptors [PDF]
The endogenous opioid peptides belong to three groups: the endorphins, the enkephalins and the dynorphins. These three groups are clearly distinct chemical families derived from three different precursor peptides: pro-opiomelanocortin. proenkephalin and prodynorphin.
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Opioid Peptides and Vasopressin
1986During the past several years, several of the neuroscience disciplines have increasingly assumed both the character and methodologies of classical molecular biology. In large part, this inundation reflects our need to investigate and understand the “pretranslational” events governing the regulation of peptide hormone and receptor expression throughout ...
Henry Khachaturian+5 more
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Isolation of molluscan opioid peptides
Life Sciences, 1983An acid extract of neural tissues of the mollusc, Mytilus edulis, was fractionated by high-pressure chromatography. Peak fractions with retention times of that of Met-enkephalin, Leu-enkephalin and Met-enkephalin-Arg-Phe were subjected to competitive displacement assays in the same neural tissues.
George B. Stefano, Michael K. Leung
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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 +3 more sources