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10.1021/jo900578j
165. Bemis JE, Vu CB, Xie R et al (2009) Discovery of oxazolo[4,5-b]pyridines and related
heterocyclic analogs as novel SIRT1 activators. Bioorg Med Chem Lett 19(8):2350–2353.
https://doi.org/10.1016/j.bmcl.2008.11.106
166. Dai H, Kustigian L, Carney A et al (2010) SIRT1 activation by small molecules: kinetic and
biophysical evidence for direct interaction of enzyme and activator. J Biol Chem 285
(43):32695–32703. https://doi.org/10.1074/jbc.M110.133892
167. Dao TT, Tran TL, Kim J et al (2012) Terpenylated coumarins as SIRT1 activators isolated
from Ailanthus altissima. J Nat Prod 75(7):1332–1338. https://doi.org/10.1021/np300258u
168. de Boer VCJ, de Goffau MC, Arts ICW et al (2006) SIRT1 stimulation by polyphenols is
affected by their stability and metabolism. Mech Ageing Dev 127(7):618–627. https://doi.org/
10.1016/j.mad.2006.02.007
169. Hubbard BP, Gomes AP, Dai H et al (2013) Evidence for a common mechanism of SIRT1
regulation by allosteric activators. Science 339:1216–1219. https://doi.org/10.1126/science.
1231097
170. Mai A, Valente S, Meade S et al (2009) Study of 1,4-dihydropyridine structural scaffold:
discovery of novel sirtuin activators and inhibitors. J Med Chem 52(17):5496–5504. https://
doi.org/10.1021/jm9008289
171. Milne JC, Lambert PD, Schenk S et al (2007) Small molecule activators of SIRT1 as
therapeutics for the treatment of type 2 diabetes. Nature 450(7170):712–716. https://doi.org/
10.1038/nature06261
172. Borra MT, Smith BC, Denu JM (2005) Mechanism of human SIRT1 activation by resveratrol.
J Biol Chem 280(17):17187–17195. https://doi.org/10.1074/jbc.M501250200
173. Kaeberlein M, McDonagh T, Heltweg B et al (2005) Substrate-specific activation of sirtuins by
resveratrol. J Biol Chem 280(17):17038–17045. https://doi.org/10.1074/jbc.M500655200
174. Cao D, Wang M, Qiu X et al (2015) Structural basis for allosteric, substrate-dependent
stimulation of SIRT1 activity by resveratrol. Genes Dev 29(12):1316–1325. https://doi.org/
10.1101/gad.265462.115
175. Dai H, Case AW, Riera TV et al (2015) Crystallographic structure of a small molecule SIRT1
activator-enzyme complex. Nat Commun 6:7645. https://doi.org/10.1038/ncomms8645
176. Gertz M, Nguyen GTT, Fischer F et al (2012) A molecular mechanism for direct sirtuin
activation by resveratrol. PLoS One 7(11):e49761. https://doi.org/10.1371/journal.pone.
0049761
177. Dai H, Ellis JL, Sinclair DA et al (2016a) Synthesis and assay of SIRT1-activating compounds. Methods Enzymol 574:213–244. https://doi.org/10.1016/bs.mie.2016.01.012
178. Anderson RM, Bitterman KJ, Wood JG et al (2003) Nicotinamide and PNC1 govern lifespan
extension by calorie restriction in Saccharomyces cerevisiae. Nature 423(6936):181–185.
https://doi.org/10.1038/nature01578
179. Lin SJ, Defossez PA, Guarente L (2000) Requirement of NAD and SIR2 for life-span
extension by calorie restriction in Saccharomyces cerevisiae. Science 289(5487):2126–2128
180. Lin SJ, Kaeberlein M, Andalis AA et al (2002) Calorie restriction extends Saccharomyces
cerevisiae lifespan by increasing respiration. Nature 418(6895):344–348. https://doi.org/10.
1038/nature00829
181. Hubbard BP, Sinclair DA (2014) Small molecule SIRT1 activators for the treatment of aging
and age-related diseases. Trends Pharmacol Sci 35(3):146–154. https://doi.org/10.1016/j.tips.
2013.12.004
182. Rahnasto-Rilla M, Kokkola T, Jarho E et al (2016) N-Acylethanolamines bind to SIRT6.
ChemBioChem 17(1):77–81. https://doi.org/10.1002/cbic.201500482
183. Wang Y, Liang X, Chen Y et al (2016) Screening SIRT1 activators from medicinal plants as
bioactive compounds against oxidative damage in mitochondrial function. Oxid Med Cell
Longev 2016:4206392. https://doi.org/10.1155/2016/4206392
Sirtuin Inhibitors and Activators
91