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• W2080049180 abstract "The cloning of over 100 members of the superfamily of G-protein coupled receptors has resulted in the identification and characterization of novel targets for therapeutic intervention. In addition, mutagenesis studies aimed at understanding the nature of the molecular interactions of these receptors with peptides and small molecules have led to advancements in the ability to synthesize novel therapeutic agents with high affinity and specificity for these receptors. These experiments have shown that there is a common binding site for small molecules within the transmembrane domain of G-protein coupled receptors regardless of the nature of the endogenous, physiologically relevant receptor agonist. Finally, the demonstration that the binding sites for peptide agonists and nonpeptide competitive antagonists are not necessarily identical has provided insights regarding the mechanism of competitive antagonism in these receptors." @default.
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• W2080049180 date "1995-08-01" @default.
• W2080049180 modified "2023-10-17" @default.
• W2080049180 title "Molecular characterization of a common binding site for small molecules within the transmembrane domain of G-protein coupled receptors" @default.
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• W2080049180 doi "https://doi.org/10.1016/1056-8719(95)00002-y" @default.
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