29976-20-3Relevant articles and documents
Inhibition of the histone demethylase JMJD2E by 3-substituted pyridine 2,4-dicarboxylates
Thalhammer, Armin,Mecinovic, Jasmin,Loenarz, Christoph,Tumber, Anthony,Rose, Nathan R.,Heightman, Tom D.,Schofield, Christopher J.
experimental part, p. 127 - 135 (2011/02/24)
Based on structural analysis of the human 2-oxoglutarate (2OG) dependent JMJD2 histone Nε-methyl lysyl demethylase family, 3-substituted pyridine 2,4-dicarboxylic acids were identified as potential inhibitors with possible selectivity over other human 2OG oxygenases. Microwave-assisted palladium-catalysed cross coupling methodology was developed to install a diverse set of substituents on the sterically demanding C-3 position of a pyridine 2,4-dicarboxylate scaffold. The subsequently prepared di-acids were tested for in vitro inhibition of the histone demethylase JMJD2E and another human 2OG oxygenase, prolyl-hydroxylase domain isoform 2 (PHD2, EGLN1). A subset of substitution patterns yielded inhibitors with selectivity for JMJD2E over PHD2, demonstrating that structure-based inhibitor design can enable selective inhibition of histone demethylases over related human 2OG oxygenases.
A Suzuki-Miyaura approach to a series of forensically relevant pyridines
Blachut, Dariusz,Czarnocki, Zbigniew,Wojtasiewicz, Krystyna
, p. 2855 - 2864 (2008/02/07)
A convenient and general method for the preparation of sixteen 3,5-diarylsubstituted 2,4- and 2,6-dimethylpyridines of high forensic importance is described. The Suzuki cross-coupling reaction between a range of ring-substituted phenylboronic acids and 3,
