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10.1080/15592294.2017.1290032

http://scihub22266oqcxt.onion/10.1080/15592294.2017.1290032
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C5453194!5453194!28277979
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suck abstract from ncbi


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pmid28277979      Epigenetics 2017 ; 12 (5): 340-52
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  • Structural insight into inhibitors of flavin adenine dinucleotide-dependent lysine demethylases #MMPMID28277979
  • Niwa H; Umehara T
  • Epigenetics 2017[]; 12 (5): 340-52 PMID28277979show ga
  • Until 2004, many researchers believed that protein methylation in eukaryotic cells was an irreversible reaction. However, the discovery of lysine-specific demethylase 1 in 2004 drastically changed this view and the concept of chromatin regulation. Since then, the enzymes responsible for lysine demethylation and their cellular substrates, biological significance, and selective regulation have become major research topics in epigenetics and chromatin biology. Many cell-permeable inhibitors for lysine demethylases have been developed, including both target-specific and nonspecific inhibitors. Structural understanding of how these inhibitors bind to lysine demethylases is crucial both for validation of the inhibitors as chemical probes and for the rational design of more potent, target-specific inhibitors. This review focuses on published small-molecule inhibitors targeted at the two flavin adenine dinucleotide-dependent lysine demethylases, lysine-specific demethylases 1 and 2, and how the inhibitors interact with the tertiary structures of the enzymes.
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