Structure-activity relationship study of acridine analogs as haspin and DYRK2 kinase inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 20, Issue 12, 2010, Pages 3491-3494

  Cuny, Gregory D ^a   Robin, Maxime ^b   Ulyanova, Natalia P ^a   Patnaik, Debasis ^a   Pique, Valerie ^b   Casano, Gilles ^b   Liu, Ji Feng ^c   Lin, Xiangjie ^c   Xian, Jun ^a   Glicksman, Marcie A ^a   Stein, Ross L ^a   Higgins, Jonathan M G ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b AIX MARSEILLE UNIVERSITÉ   (France)

^c Aberjona Laboratories Inc   (United States)

Author keywords

Acridine; DYRK2; Haspin; Inhibitor; Kinase; Oncology; Structure activity relationship

Indexed keywords

ACRIDINE DERIVATIVE; ANTINEOPLASTIC AGENT; DUAL SPECIFICITY TYROSINE REGULATED KINASE 2; HAPLOID GERM CELL SPECIFIC NUCLEAR PROTEIN KINASE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN SERINE KINASE; UNCLASSIFIED DRUG;

ANTINEOPLASTIC ACTIVITY; ARTICLE; CELL PROLIFERATION; DRUG TARGETING; HUMAN; IC 50; STRUCTURE ACTIVITY RELATION;

EID: 77954213722     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2010.04.150     Document Type: Article

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26. See Supplementary data for details.
27. 50 = 22 nM for 1. The assay used full-length human haspin fused at the N-terminus to GST and expressed using baculovirus, histone H3 peptide as substrate and [ATP] of 100 μM.
28. Determined by Carna Biosciences. Full-length human DYRK2 fused at the N-terminus to GST and expressed using baculovirus, DYRKtide-F as substrate and [ATP] of 10 μM were used.