Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors.

@article{Hamada2010DesignSE,
  title={Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors.},
  author={Shohei Hamada and Takayoshi Suzuki and Koshiki Mino and Koichi Koseki and Felix Oehme and Ingo Flamme and Hiroki Ozasa and Yukihiro Itoh and Daisuke Ogasawara and Haruka Komaarashi and Aiko Kato and Hiroki Tsumoto and Hidehiko Nakagawa and Makoto Hasegawa and Ryuzo Sasaki and Tamio Mizukami and Naoki Miyata},
  journal={Journal of medicinal chemistry},
  year={2010},
  volume={53 15},
  pages={
          5629-38
        }
}
Selective inhibitors of Jumonji domain-containing protein (JMJD) histone demethylases are candidate anticancer agents as well as potential tools for elucidating the biological functions of JMJDs. On the basis of the crystal structure of JMJD2A and a homology model of JMJD2C, we designed and prepared a series of hydroxamate analogues bearing a tertiary amine. Enzyme assays using JMJD2C, JMJD2A, and prolyl hydroxylases revealed that hydroxamate analogue 8 is a potent and selective JMJD2 inhibitor… Expand
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It is highlighted that overexpression of JMJD2C confers a pro-growth effect on colon cancer cells and, therefore, its inhibition by curcuminoids or other small molecules could be beneficial as an adjuvant therapy for colon cancer patients. Expand
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