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For active pharmaceutical ingredients (APIs) related to SIRT1 FRET-
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Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 389 349-
Imai, S., Armstrong, C.M., Kaeberlein, M., et al. Transcriptional silencing and longevity protein Sir2 is an NAD-
Tanny, J.C., Moazed, D. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci USA 98(2) 415-
Borra, M.T., Smith, B.C., Denu, J.M. Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 280(17) 17187-
Wood, J.G., Rogina, B., Lavu, S., et al. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 430 686-
Howitz, K.T., Bitterman, K.J., Cohen, H.Y., et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425 191-
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Luo, J., Nikolaev, A.Y., Imai, S., et al. Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107 137-
Frye, R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-
Denu, J.M. The Sir2 family of protein deacetylases. Curr Opin Chem Biol 9 431-
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Kaeberlein, M., McDonagh, T., Heltweg, B., et al. Substrate-
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![]() | Download Material Safety Data Sheet (MSDS) 95 Kb PDF |
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