| Literature DB >> 25847771 |
Torun Ekblad1, Anders E G Lindgren2, C David Andersson2, Rémi Caraballo2, Ann-Gerd Thorsell1, Tobias Karlberg1, Sara Spjut2, Anna Linusson2, Herwig Schüler3, Mikael Elofsson4.
Abstract
Protein ADP-ribosylation is a post-translational modification involved in DNA repair, protein degradation, transcription regulation, and epigenetic events. Intracellular ADP-ribosylation is catalyzed predominantly by ADP-ribosyltransferases with diphtheria toxin homology (ARTDs). The most prominent member of the ARTD family, poly(ADP-ribose) polymerase-1 (ARTD1/PARP1) has been a target for cancer drug development for decades. Current PARP inhibitors are generally non-selective, and inhibit the mono-ADP-ribosyltransferases with low potency. Here we describe the synthesis of acylated amino benzamides and screening against the mono-ADP-ribosyltransferases ARTD7/PARP15, ARTD8/PARP14, ARTD10/PARP10, and the poly-ADP-ribosyltransferase ARTD1/PARP1. The most potent compound inhibits ARTD10 with sub-micromolar IC50.Entities:
Keywords: ARTD inhibitor; Diphtheria toxin-like ADP-ribosyltransferase; Mono-ADP-ribosyltransferase; PARP inhibitor; Poly(ADP-ribose) polymerase; mART
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Year: 2015 PMID： 25847771 DOI： 10.1016/j.ejmech.2015.03.067
Source DB: PubMed Journal: Eur J Med Chem ISSN： 0223-5234 Impact factor: 6.514