Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure-Activity Relationship Study.

@article{Schiedel2016AminothiazolesAP,
  title={Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure-Activity Relationship Study.},
  author={Matthias Schiedel and Tobias Rumpf and Berin Karaman and Attila Lehotzky and Judit Ol{\'a}h and Stefan Gerhardt and Judit Ov{\'a}di and Wolfgang Sippl and Oliver Einsle and Manfred Jung},
  journal={Journal of medicinal chemistry},
  year={2016},
  volume={59 4},
  pages={
          1599-612
        }
}
Sirtuins are NAD(+)-dependent protein deacylases that cleave off acetyl but also other acyl groups from the ε-amino group of lysines in histones and other substrate proteins. Dysregulation of human Sirt2 (hSirt2) activity has been associated with the pathogenesis of cancer, inflammation, and neurodegeneration, which makes the modulation of hSirt2 activity a promising strategy for pharmaceutical intervention. The sirtuin rearranging ligands (SirReals) have recently been discovered by us as… CONTINUE READING
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New chemical tools for probing activity and inhibition of the NAD+-dependent lysine deacylase sirtuin 2.

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