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Journal Abstract Search

274 related items for PubMed ID: 26141769

  • 1. Discovery of dihydroisoquinolinone derivatives as novel inhibitors of the p53-MDM2 interaction with a distinct binding mode.
    Gessier F, Kallen J, Jacoby E, Chène P, Stachyra-Valat T, Ruetz S, Jeay S, Holzer P, Masuya K, Furet P.
    Bioorg Med Chem Lett; 2015 Sep 01; 25(17):3621-5. PubMed ID: 26141769
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  • 2. Discovery of a novel class of highly potent inhibitors of the p53-MDM2 interaction by structure-based design starting from a conformational argument.
    Furet P, Masuya K, Kallen J, Stachyra-Valat T, Ruetz S, Guagnano V, Holzer P, Mah R, Stutz S, Vaupel A, Chène P, Jeay S, Schlapbach A.
    Bioorg Med Chem Lett; 2016 Oct 01; 26(19):4837-4841. PubMed ID: 27542305
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  • 8. An integrated in silico screening strategy for identifying promising disruptors of p53-MDM2 interaction.
    Sirous H, Chemi G, Campiani G, Brogi S.
    Comput Biol Chem; 2019 Dec 01; 83():107105. PubMed ID: 31473433
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  • 10. The central valine concept provides an entry in a new class of non peptide inhibitors of the p53-MDM2 interaction.
    Furet P, Chène P, De Pover A, Valat TS, Lisztwan JH, Kallen J, Masuya K.
    Bioorg Med Chem Lett; 2012 May 15; 22(10):3498-502. PubMed ID: 22507962
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  • 11. An Effective Virtual Screening Protocol To Identify Promising p53-MDM2 Inhibitors.
    Tortorella P, Laghezza A, Durante M, Gomez-Monterrey I, Bertamino A, Campiglia P, Loiodice F, Daniele S, Martini C, Agamennone M.
    J Chem Inf Model; 2016 Jun 27; 56(6):1216-27. PubMed ID: 27269808
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  • 12. Affinity-based screening of MDM2/MDMX-p53 interaction inhibitors by chemical array: identification of novel peptidic inhibitors.
    Noguchi T, Oishi S, Honda K, Kondoh Y, Saito T, Kubo T, Kaneda M, Ohno H, Osada H, Fujii N.
    Bioorg Med Chem Lett; 2013 Jul 01; 23(13):3802-5. PubMed ID: 23726030
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  • 13. Small-molecule MDM2-p53 inhibitors: recent advances.
    Zhang B, Golding BT, Hardcastle IR.
    Future Med Chem; 2015 Jul 01; 7(5):631-45. PubMed ID: 25921402
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  • 16. Simulation of MDM2 N-terminal domain conformational lability in the presence of imidazoline based inhibitors of MDM2-p53 protein-protein interaction.
    Gureev M, Novikova D, Grigoreva T, Vorona S, Garabadzhiu A, Tribulovich V.
    J Comput Aided Mol Des; 2020 Jan 01; 34(1):55-70. PubMed ID: 31781989
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  • 17. Design, synthesis and biological evaluation of novel 3,4,5-trisubstituted aminothiophenes as inhibitors of p53-MDM2 interaction. Part 2.
    Wang W, Lv D, Qiu N, Zhang L, Hu C, Hu Y.
    Bioorg Med Chem; 2013 Jun 01; 21(11):2886-94. PubMed ID: 23611770
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