Discovery of dihydroisoquinolinone derivatives as novel inhibitors of the p53-MDM2 interaction with a distinct binding mode

Bioorganic and Medicinal Chemistry Letters

Volumn 25, Issue 17, 2015, Pages 3621-3625

  Gessier, François ^a   Kallen, Joerg ^a   Jacoby, Edgar ^a   Chène, Patrick ^a   Stachyra Valat, Thérèse ^a   Ruetz, Stephan ^a   Jeay, Sébastien ^a   Holzer, Philipp ^a   Masuya, Keiichi ^a   Furet, Pascal ^a  

^a NOVARTIS PHARMA AG   (Switzerland)

Author keywords

MDM2; p53; Protein protein interaction inhibitors

Indexed keywords

DIHYDROISOQUINOLINONE DERIVATIVE; PROTEIN INHIBITOR; PROTEIN MDM2; PROTEIN P53; UNCLASSIFIED DRUG; ISOQUINOLINE DERIVATIVE; PROTEIN BINDING;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; DERIVATIZATION; DRUG STRUCTURE; PROTEIN PROTEIN INTERACTION; X RAY; ANTAGONISTS AND INHIBITORS; CHEMISTRY; DRUG EFFECTS; HUMAN; METABOLISM; MOLECULAR DOCKING; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; HUMANS; ISOQUINOLINES; MOLECULAR DOCKING SIMULATION; PROTEIN BINDING; PROTEIN INTERACTION MAPS; PROTO-ONCOGENE PROTEINS C-MDM2; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84938420316     PISSN: 0960894X     EISSN: 14643405     Source Type: Journal    
DOI: 10.1016/j.bmcl.2015.06.058     Document Type: Article

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31. The optimization of compound 11 towards a clinical candidate will be reported elsewhere.