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We began analyzing https://link.springer.com/article/10.1007/s11302-008-9106-2, but it redirected us to https://link.springer.com/article/10.1007/s11302-008-9106-2. The analysis below is for the second page.

Title[redir]:
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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🏙️ Massive Traffic: 50M - 100M visitors per month


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Keywords {🔍}

receptor, receptors, google, scholar, article, cas, pubmed, antagonists, potent, derivatives, human, atp, agonists, potency, jacobson, chem, agonist, selective, nucleotide, cells, analogues, med, harden, antagonist, fig, phosphate, ribose, adenosine, pharmacol, subtypes, activity, adenine, triphosphate, udp, utp, derivative, boyer, moiety, nucleotides, adp, group, modification, identification, ligands, inactive, uracil, modeling, activate, ring, mrs,

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

Schema {🗺️}

WebPage:
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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
         dateModified:2008-07-04T00:00:00Z
         pageStart:75
         pageEnd:89
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            Purine
            Pyrimidine
            G protein-coupled receptor
            Structure activity relationship
            Biomedicine
            general
            Pharmacology/Toxicology
            Human Physiology
            Neurosciences
            Cancer Research
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                     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: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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      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
      dateModified:2008-07-04T00:00:00Z
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         Nucleotide
         Purine
         Pyrimidine
         G protein-coupled receptor
         Structure activity relationship
         Biomedicine
         general
         Pharmacology/Toxicology
         Human Physiology
         Neurosciences
         Cancer Research
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            name:Sonia de Castro
            affiliation:
                  name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
                  address:
                     name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
                     type:PostalAddress
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            type:Person
            name:T. Kendall Harden
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                  name:University of North Carolina School of Medicine
                  address:
                     name:Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, USA
                     type:PostalAddress
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            type:Person
            name:Hyojin Ko
            affiliation:
                  name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
                  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: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:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
            address:
               name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
               type:PostalAddress
            type:Organization
      name:Sonia de Castro
      affiliation:
            name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
            address:
               name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
               type:PostalAddress
            type:Organization
      name:T. Kendall Harden
      affiliation:
            name:University of North Carolina School of Medicine
            address:
               name:Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, USA
               type:PostalAddress
            type:Organization
      name:Hyojin Ko
      affiliation:
            name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
            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:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
      name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
      name:Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, USA
      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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