INT41652

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Context Info
Confidence 0.16
First Reported 1982
Last Reported 1983
Negated 1
Speculated 0
Reported most in Abstract
Documents 3
Total Number 4
Disease Relevance 0
Pain Relevance 1.57

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

signal transducer activity (Oprl1) cell-cell signaling (Pomc) cytoplasm (Pomc)
extracellular space (Pomc) generation of precursor metabolites and energy (Pomc) signal transduction (Pomc)
Anatomy Link Frequency
neurons 1
Pomc (Rattus norvegicus)
Oprl1 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
opiate 21 100.00 Very High Very High Very High
Potency 4 93.68 High High

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Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Thus, at physiological levels it seems unlikely that the des-Tyr1 fragment of gamma-endorphin will exhibit any significant interaction with the opiate receptor.
gamma-endorphin Binding (interaction) of opiate receptor associated with opiate
1) Confidence 0.16 Published 1982 Journal Peptides Section Abstract Doc Link 6176977 Disease Relevance 0 Pain Relevance 0.34
Because N-acetyl-beta-endorphin is nonanalgesic and does not bind to the opiate receptor (Smyth, D.G., Massey, D.E., Zakarian, S., and Finnie, M.D. (1979) Nature (Lond.) 279, 252-254), it appears that the physiological significance of beta-endorphin acetyltransferase is that it can modulate the activity of endorphin secreted from opiomelanotropinergic cells and neurons.
endorphin Neg (not) Binding (bind) of opiate receptor in neurons associated with opiate
2) Confidence 0.15 Published 1983 Journal J. Biol. Chem. Section Abstract Doc Link 6296134 Disease Relevance 0 Pain Relevance 0.10
With regard to opiate receptor binding, peptide 4 was twice as potent as beta-endorphin in mu-receptor assays but half as potent in delta-receptor assays.
beta-endorphin Binding (potent) of opiate receptor associated with opiate
3) Confidence 0.09 Published 1983 Journal J. Biol. Chem. Section Abstract Doc Link 6305980 Disease Relevance 0 Pain Relevance 0.42
A comparison of these results with those of previous model peptides provides further evidence for the importance of an amphiphilic helical structure in beta-endorphin residues 13-31, which determines the resistance to proteolysis of the natural molecule and contributes to the delta- and mu-opiate receptor interaction.
beta-endorphin Binding (interaction) of mu-opiate receptor associated with opiate
4) Confidence 0.09 Published 1983 Journal J. Biol. Chem. Section Abstract Doc Link 6305980 Disease Relevance 0 Pain Relevance 0.70

General Comments

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