We are analyzing https://link.springer.com/article/10.1007/s11302-008-9106-2.

Title:
Development of selective agonists and antagonists of P2Y receptors | Purinergic Signalling
Description:
Although elucidation of the medicinal chemistry of agonists and antagonists of the P2Y receptors has lagged behind that of many other members of group A G protein-coupled receptors, detailed qualitative and quantitative structure–activity relationships (SARs) were recently constructed for several of the subtypes. Agonists selective for P2Y1, P2Y2, and P2Y6 receptors and nucleotide antagonists selective for P2Y1 and P2Y12 receptors are now known. Selective nonnucleotide antagonists were reported for P2Y1, P2Y2, P2Y6, P2Y11, P2Y12, and P2Y13 receptors. At the P2Y1 and P2Y12 receptors, nucleotide agonists (5′-diphosphate derivatives) were converted into antagonists of nanomolar affinity by altering the phosphate moieties, with a focus particularly on the ribose conformation and substitution pattern. Nucleotide analogues with conformationally constrained ribose-like rings were introduced as selective receptor probes for P2Y1 and P2Y6 receptors. Screening chemically diverse compound libraries has begun to yield new lead compounds for the development of P2Y receptor antagonists, such as competitive P2Y12 receptor antagonists with antithrombotic activity. Selective agonists for the P2Y4, P2Y11, and P2Y13 receptors and selective antagonists for P2Y4 and P2Y14 receptors have not yet been identified. The P2Y14 receptor appears to be the most restrictive of the class with respect to modification of the nucleobase, ribose, and phosphate moieties. The continuing process of ligand design for the P2Y receptors will aid in the identification of new clinical targets.
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Keywords {🔍}

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Topics {✒️}

article download pdf protein-coupled nucleotide receptors sonia de castro preferentially gq-coupled receptors n3-epsilon-adenine nucleoside sp-utp-α-s- analogue c-nucleotide-based antagonist 28 5′-bisphosphate c-nucleotide analogues cloned human p2u-purinoreceptor 1h-tetrazol-5-yl group uncharged nucleoside-based antagonist adenine-derived nucleotide agonists modifications yields 2′-amino-2-thio-utp uracil nucleotide-responsive subtypes 2-thio-utp 63a preserve van der giet receptor-binding site surrounds combining receptor-based modeling γ-imido group leads orally active direct-acting full size table protein-coupled receptors suramin-derived compound library quantitative structure–activity relationships terminally thiophosphate-substituted analogues selective p2y-purinoceptor agonists parent compound 4-thio-udp rhodopsin-based homology modeling [32p]2-iodo-n6-methyl 1321n1 astrocytoma cells suitable radioligand-binding methods 5′-triphosphate derivatives ar-c67085 privacy choices/manage cookies methanocarba-constrained carbocyclic ring author information authors inhibit p2y11 receptors protein-dependent facilitation van galen pjm 2′-amino-2′-deoxy-2-thio-utp c-nucleoside pyrazolo[1 moderate antagonist activity α-thio amp derivatives protein signaling intracellularly ecto-nucleotide pyrophosphatase potent p2y-purinoceptor agonists adp-responsive receptors structure activity relationship extracellular β-nad+ appears sp-2-mes-atp-α purinergic receptor acting

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         headline:Development of selective agonists and antagonists of P2Y receptors
         description:Although elucidation of the medicinal chemistry of agonists and antagonists of the P2Y receptors has lagged behind that of many other members of group A G protein-coupled receptors, detailed qualitative and quantitative structure–activity relationships (SARs) were recently constructed for several of the subtypes. Agonists selective for P2Y1, P2Y2, and P2Y6 receptors and nucleotide antagonists selective for P2Y1 and P2Y12 receptors are now known. Selective nonnucleotide antagonists were reported for P2Y1, P2Y2, P2Y6, P2Y11, P2Y12, and P2Y13 receptors. At the P2Y1 and P2Y12 receptors, nucleotide agonists (5′-diphosphate derivatives) were converted into antagonists of nanomolar affinity by altering the phosphate moieties, with a focus particularly on the ribose conformation and substitution pattern. Nucleotide analogues with conformationally constrained ribose-like rings were introduced as selective receptor probes for P2Y1 and P2Y6 receptors. Screening chemically diverse compound libraries has begun to yield new lead compounds for the development of P2Y receptor antagonists, such as competitive P2Y12 receptor antagonists with antithrombotic activity. Selective agonists for the P2Y4, P2Y11, and P2Y13 receptors and selective antagonists for P2Y4 and P2Y14 receptors have not yet been identified. The P2Y14 receptor appears to be the most restrictive of the class with respect to modification of the nucleobase, ribose, and phosphate moieties. The continuing process of ligand design for the P2Y receptors will aid in the identification of new clinical targets.
         datePublished:2008-07-04T00:00:00Z
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            Cancer Research
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      headline:Development of selective agonists and antagonists of P2Y receptors
      description:Although elucidation of the medicinal chemistry of agonists and antagonists of the P2Y receptors has lagged behind that of many other members of group A G protein-coupled receptors, detailed qualitative and quantitative structure–activity relationships (SARs) were recently constructed for several of the subtypes. Agonists selective for P2Y1, P2Y2, and P2Y6 receptors and nucleotide antagonists selective for P2Y1 and P2Y12 receptors are now known. Selective nonnucleotide antagonists were reported for P2Y1, P2Y2, P2Y6, P2Y11, P2Y12, and P2Y13 receptors. At the P2Y1 and P2Y12 receptors, nucleotide agonists (5′-diphosphate derivatives) were converted into antagonists of nanomolar affinity by altering the phosphate moieties, with a focus particularly on the ribose conformation and substitution pattern. Nucleotide analogues with conformationally constrained ribose-like rings were introduced as selective receptor probes for P2Y1 and P2Y6 receptors. Screening chemically diverse compound libraries has begun to yield new lead compounds for the development of P2Y receptor antagonists, such as competitive P2Y12 receptor antagonists with antithrombotic activity. Selective agonists for the P2Y4, P2Y11, and P2Y13 receptors and selective antagonists for P2Y4 and P2Y14 receptors have not yet been identified. The P2Y14 receptor appears to be the most restrictive of the class with respect to modification of the nucleobase, ribose, and phosphate moieties. The continuing process of ligand design for the P2Y receptors will aid in the identification of new clinical targets.
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         Nucleotide
         Purine
         Pyrimidine
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         Structure activity relationship
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         general
         Pharmacology/Toxicology
         Human Physiology
         Neurosciences
         Cancer Research
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            address:
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            address:
               name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
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            name:University of North Carolina School of Medicine
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               type:PostalAddress
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      affiliation:
            name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
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      name:Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, USA
      name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA

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