Inhibition of the histone demethylase JMJD2E by 3-substituted pyridine 2,4-dicarboxylates.

  title={Inhibition of the histone demethylase JMJD2E by 3-substituted pyridine 2,4-dicarboxylates.},
  author={Armin Thalhammer and Jasmin Mecinovi{\'c} and Christoph Loenarz and Anthony Tumber and Nathan Rose and Tom D Heightman and Christopher J. Schofield},
  journal={Organic & biomolecular chemistry},
  volume={9 1},
Based on structural analysis of the human 2-oxoglutarate (2OG) dependent JMJD2 histone N(ε)-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… CONTINUE READING

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