ライフサイエンスコーパス: sirtuin

1 NAD(+)-dependent deacylase activities of the sirtuins.

2 logical functions regulated by mitochondrial sirtuins.

3 d functional interplay between two mammalian sirtuins.

4 lso an efficient deacetylation substrate for sirtuins.

5 exity in the crosstalk between two different sirtuins.

6 the range of hydrolytic activities of human sirtuins.

7 We show that UnAG rescues sirtuin 1 (SIRT1) activity and superoxide dismutase-2 (S

8 ted genes are the anti-lipogenic deacetylase sirtuin 1 (Sirt1) and the anti-lipogenic transcription f

9 factor 1 (HES1) and the protein deacetylase sirtuin 1 (SIRT1) at the Isl1 gene.

10 und that higher abundance of the deacetylase sirtuin 1 (SIRT1) correlated with lower acetylation occu

11 rmacological activation that the deacetylase Sirtuin 1 (SIRT1) has an anti-inflammatory role in a les

12 of the NAD(+)-dependent lysine deacetylase, sirtuin 1 (SIRT1) in fibrogenesis in the cell culture, a

13 We sought to determine the role of sirtuin 1 (SIRT1) in skin barrier function, FLG expressi

14 dinucleotide (NAD(+))-dependent deacetylase sirtuin 1 (SIRT1) in various tissues.

15 Sirtuin 1 (Sirt1) is a class III histone deacetylase tha

16 Sirtuin 1 (SIRT1) is a nicotinamide adenine dinucleotide

17 Sirtuin 1 (SIRT1) is an NAD(+)-dependent deacetylase tha

18 Sirtuin 1 (SIRT1) is involved in both aging and circadia

19 ximately 7.5 muM) restored the normal TF and sirtuin 1 (SIRT1) levels in MCECs before PGE2 (EC50 appr

20 Here, we propose that the nutrient sensor sirtuin 1 (Sirt1) regulates the production of CRH post-t

21 ulation and Th2 inflammation and blockers of sirtuin 1 (Sirt1) to define its roles in these responses

22 d the target of DLA, the binding affinity of Sirtuin 1 (SIRT1) to DLA and DLA derivatives with replac

23 We investigated how Sirtuin 1 (SIRT1), a conserved mammalian NAD(+)-dependen

24 ed activation of KRAS and over-expression of Sirtuin 1 (SIRT1), a histone deacetylase and gene silenc

25 The NAD(+)-dependent protein deacetylase sirtuin 1 (SIRT1), a key regulator of mammalian metaboli

26 e their known interaction in transactivating Sirtuin 1 (SIRT1), a NAD(+)-dependent histone deacetylas

27 Sirtuin 1 (SIRT1), an NAD(+)-dependent deacetylase, has

28 Sirtuin 1 (SIRT1), an NAD(+)-dependent protein deacetyla

29 Sirtuin 1 (SIRT1), an NAD-dependent deacetylase, partici

30 cers of fatty acid beta-oxidation, including sirtuin 1 (SIRT1), sirtuin 3 (SIRT3), and Nrf-1.

31 Sirtuin 1 (SIRT1), the founding member of Class III hist

32 Sirtuin 1 (SIRT1), the most conserved mammalian oxidized

33 lation of memory-associated genes, including Sirtuin 1 (Sirt1), within the hippocampus, and thus offe

34 gulation of the NAD(+)-dependent deacetylase sirtuin 1 (SIRT1).

35 dinucleotide (NAD(+))-dependent deacetylase Sirtuin 1 (Sirt1).

36 ylation via maintenance of NAD(+) levels and sirtuin 1 activation.

37 ic ischemia-reperfusion and posttreated with sirtuin 1 activator, SRT1720 (20 mg/kg), or vehicle.

38 to determine the effects of a small molecule sirtuin 1 activator, SRT2104, on inflammation and coagul

39 Indeed, when sirtuin 1 activity was rescued by resveratrol pretreatme

40 f stored maternal mRNA transcripts including sirtuin 1 and ubiquitin protein ligase E3a, two genes wi

41 Pharmacologic stimulation of sirtuin 1 attenuates liver injury after hepatic ischemia

42 responses consistent with the activation of sirtuin 1 by a small molecule.

43 Here we show that sirtuin 1 deacetylase (Sirt1) deacetylates Nav1.5 at lys

44 levels by the p300 acetyltransferase and the sirtuin 1 deacetylase controls transcriptional activity,

45 bined ethanol and LPS-mediated inhibition of sirtuin 1 expression and activity in macrophages.

46 d ADH activity through its direct control of sirtuin 1 expression.

47 Sirtuin 1 influences gene expression and other cellular

48 Moreover, miR-217-mediated sirtuin 1 inhibition was accompanied by increased activi

49 Sirtuin 1 is an energy-sensing enzyme involved in regula

50 Sirtuin 1 is an energy-sensing enzyme known to modulate

51 ypothesized that pharmacologic activation of sirtuin 1 is protective after hepatic ischemia-reperfusi

52 histone deacetylase 2 enrichment, but not of sirtuin 1 or sirtuin 2, onto GluA1 and GluA2 gene sequen

53 ng Nnmt expression or MNAM levels stabilizes sirtuin 1 protein, an effect that is required for their

54 However, sirtuin 1 was downregulated and so the accumulation of N

55 activity of the NAD(+) dependent deacetylase sirtuin 1, a ChREBP-negative target, were down-regulated

56 cade involving AMP-activated protein kinase, sirtuin 1, PGC-1alpha, sirtuin 3, estrogen-related recep

57 rations and the AMP-activated protein kinase/sirtuin 1/peroxisome proliferator-activated receptor-gam

58 We observed that both sirtuins 1 and 7 (SIRT1 and SIRT7) are able to deacetyla

59 y decreased levels of the histone deactylase Sirtuin-1 (SirT-1) which has been previously shown to fu

60 FD-induced mitochondrial dysfunction via the sirtuin-1 (SIRT-1)/ peroxisome proliferator-activated re

61 We focused on sirtuin-1 (SIRT1) deacetylase due to its involvement in

62 ducer, its role in OLT and interactions with sirtuin-1 (SIRT1), a key autophagy regulator, have not b

63 Sirtuin-1 (SirT1), a member of the NAD(+)-dependent clas

64 ion by adropin may be mediated by inhibiting Sirtuin-1 (SIRT1), a PGC-1alpha deacetylase.

65 pendent class III histone deactelyase (HDAC) sirtuin-1 (SIRT1).

66 Sirtuin-1 also inhibits cancer metastasis via increasing

67 In summary, activation of hepatic AMPK/sirtuin-1 and FGF21/beta-klotho signaling pathways combi

68 3 expression and prevented downregulation of Sirtuin-1 and Foxo3alpha expression in IRPTCs by high gl

69 In vitro, hnRNP F overexpression stimulated Sirtuin-1 and Foxo3alpha with downregulation of acetylat

70 ors, AMP-activated protein kinase (AMPK) and sirtuin-1 are activated.

71 ve stress and nephropathy via stimulation of Sirtuin-1 expression and signaling in diabetes.

72 AMPK/sirtuin-1 inhibit the activity of STAT3 (signal transduc

73 Importantly, treating AAV-NT mice with a sirtuin-1 inhibitor markedly reversed many of the observ

74 iption via hnRNP F-responsive element in the Sirtuin-1 promoter.

75 Transfection of Sirtuin-1 small interfering RNA prevented hnRNP F stimul

76 hnRNP F stimulated Sirtuin-1 transcription via hnRNP F-responsive element i

77 roblast growth factor 21 (FGF21), targets of sirtuin-1, and beta-klotho, which can acts as a tumor su

78 C apoptosis and lower expression of hnRNP F, SIRTUIN-1, and FOXO3alpha than nondiabetic kidneys.

79 Instead, triiodothyronine increased sirtuin-1, fibrillin-1, proliferator-activated receptor-

80 Sirtuin-1, Foxo3alpha, and catalase expression were sign

81 CAF-mediated acetylation and the deacetylase sirtuin-1-mediated deacetylation coexist to maintain CRE

82 low AGE diets with increased adiponectin and sirtuin-1.

83 heat shock proteins, antioxidant enzymes and sirtuin-1/PGC-1 signalling) are central to the protectiv

84 CBP-associated factor (PCAF) and deacetylase sirtuin 2 (SIRT2) are responsible for regulating the ace

85 Derived from our previously reported human sirtuin 2 (SIRT2) inhibitors that were based on a 5-amin

86 Sirtuin 2 (SIRT2) is a sirtuin family deacetylase, which

87 Sirtuin 2 (SIRT2), a NAD(+)-dependent deacetylase, bound

88 Sirtuin 2 (SIRT2), one of the mammalian nicotinamide ade

89 chanistic insight into the interplay between sirtuin 2 and alpha-synuclein, the major component of th

90 fectively to other lysine deacetylases, like sirtuin 2 and sirtuin 3, which now enables more efficien

91 nstrating the potential therapeutic value of sirtuin 2 inhibition in synucleinopathies.

92 Genetic manipulation of sirtuin 2 levels in vitro and in vivo modulates the leve

93 Sirtuin 2 was previously shown to modulate proteotoxicit

94 tylase 2 enrichment, but not of sirtuin 1 or sirtuin 2, onto GluA1 and GluA2 gene sequences.

95 and that these residues are deacetylated by sirtuin 2.

96 and the NAD(+)-dependent tubulin deacetylase sirtuin-2 (SIRT2) play key roles in oligodendrocyte diff

97 ndependently of uncoupling protein-2 (UCP2), sirtuin-2 (SIRT2), the G protein-coupled receptor GPR109

98 Sirtuin 3 (SIRT3) deacetylates and regulates many mitoch

99 Sirtuin 3 (SIRT3) detoxifies mitochondrial reactive oxyg

100 functional significance of the mitochondrial sirtuin 3 (SIRT3) in melanoma.

101 The mitochondrial sirtuin 3 (SIRT3) is involved in suppressing the onset o

102 Sirtuin 3 (SIRT3) mediates histone protein post-translat

103 Although Sirtuin 3 (SIRT3), a mitochondrially enriched deacetylas

104 beta-oxidation, including sirtuin 1 (SIRT1), sirtuin 3 (SIRT3), and Nrf-1.

105 Sirtuin 3 (SIRT3), the primary mitochondrial deacetylase

106 are associated with reduced levels of renal sirtuin 3 (SIRT3).

107 mediates STC1-induced expression of UCP2 and sirtuin 3 and protection from I/R.

108 the NAD(+)-dependent deacetylase activity of sirtuin 3 to inhibit superoxide dismutase 2 (SOD2) activ

109 ALE: Clinical studies have shown that Sirt3 (Sirtuin 3) expression declines by 40% by 65 years of age

110 SIRT3 (sirtuin 3) is the major deacetylase within the mitochond

111 AMPK, diminished the expression of UCP2 and sirtuin 3, and aggravated kidney injury but did not affe

112 MPK and increased the expression of UCP2 and sirtuin 3, and concomitant treatment with compound C abo

113 vated protein kinase, sirtuin 1, PGC-1alpha, sirtuin 3, estrogen-related receptor-alpha, and Nrf-1; i

114 ther lysine deacetylases, like sirtuin 2 and sirtuin 3, which now enables more efficient development

115 tivity and the expression of STC1, UCP2, and sirtuin 3.

116 Sirtuin-3 (SIRT3) is a class III lysine deacetylase that

117 Sirtuin-3 (Sirt3) is a mitochondrial deacetylase that co

118 5-fold increase in NAD-dependent deacetylase sirtuin-3 expression caused by enhanced PGC-1alpha-estro

119 Sirtuin 5 (SIRT5) is a mitochondrial-localized NAD(+)-de

120 he discovery of the most potent inhibitor of sirtuin 5 (SIRT5) reported to date.

121 lysine succinylation, which is regulated by sirtuin 5 (SIRT5).

122 Here we describe an improved continuous sirtuin 5 assay based on the coupling of the sirtuin rea

123 The role of sirtuin 6 (SIRT6) in atherosclerotic progression of diab

124 NAD + dependent Sirtuin 6 (SIRT6) is a glucose homeostasis regulator in

125 Sirtuin 6 (SIRT6) is a sirtuin family member involved in

126 by the NAD(+)-dependent histone deacetylase Sirtuin 6 (SIRT6) that is critical for suppression of pa

127 Inhibition of sirtuin 6 (SIRT6), a histone deacetylase repressor of gl

128 SIRT6 (sirtuin 6) is a member of sirtuin family of deacetylases

129 on of the NAD+-dependent protein deacetylase sirtuin-6 (SIRT6) and nuclear factor kappa B (NFkappaB),

130 Sirtuins, a family of protein deacetylases, promote cell

131 n and catalytic activation by small molecule sirtuin-activating compounds (STACs).

132 Research shows that resveratrol, a sirtuin activator in red wine, improves exercise enduran

133 lthy volunteers to assess the effects of the sirtuin activator, nicotinamide riboside, on NLRP3 infla

134 Modulators of sirtuin activity are needed as tools for uncovering the

135 We found that diminished sirtuin activity led to the disruption of the DVL1-TIAM1

136 ts oxidative damage, maintains mitochondrial sirtuin activity, and prevents metabolic stress-induced

137 erstanding of sirtuin targets, regulation of sirtuin activity, and the relationships between sirtuins

138 and hepatosteatosis by dioxin and increased sirtuin activity, providing a therapeutic approach for p

139 emotherapeutics as well as tools to modulate sirtuin activity, we previously identified a nonselectiv

140 m of the NAD+ salvage pathway due to reduced sirtuin activity.

141 This sirtuin also plays a role in memory formation by modulat

142 clude poly (ADP-ribose) polymerases (PARPs), sirtuins, AMP-activated protein kinase (AMPK), and mecha

143 the only constitutively chromatin-associated sirtuin and is prominently present at transcriptionally

144 s, programmed cell death, synaptic function, sirtuins and aging, and insulin resistance, all processe

145 or understanding the biological functions of sirtuins and development of potential therapeutics.

146 a reduction in antiaging molecules, such as sirtuins and Klotho, which further accelerate the aging

147 dria approximate the Michaelis constants for sirtuins and PARPs in their respective compartments.

148 otide (NAD(+)) is an essential substrate for sirtuins and poly(adenosine diphosphate-ribose) polymera

149 a cosubstrate for other enzymes such as the sirtuins and poly(adenosine diphosphate-ribose) polymera

150 tivity of various enzyme families, including sirtuins and poly(ADP-ribose) polymerases.

151 Sirtuins are a class of enzymes originally identified as

152 Sirtuins are a family of deacylases and ADP-ribosyltrans

153 Sirtuins are a family of NAD(+)-dependent protein deacet

154 Sirtuins are a highly conserved class of NAD(+)-dependen

155 Sirtuins are an ancient family of NAD(+)-dependent deacy

156 Sirtuins are class III deacetylases that regulate many e

157 Sirtuins are class III histone deacylases that use NAD(+

158 expression is highest in the heart and that sirtuins are commonly stress-response proteins, we used

159 Modulators of sirtuins are considered promising therapeutic targets fo

160 However, whether sirtuins are critical to control ageing and longevity in

161 Sirtuins are evolutionarily conserved NAD(+)-dependent a

162 Sirtuins are important regulators of lysine acylation, w

163 Sirtuins are NAD(+) dependent lysine deacylases involved

164 Sirtuins are NAD(+) dependent protein deacetylases, whic

165 Sirtuins are NAD(+)-dependent enzymes universally presen

166 Sirtuins are NAD(+)-dependent lysine deacylases, regulat

167 Sirtuins are NAD(+)-dependent protein deacylases that cl

168 Sirtuins are protein deacylases regulating metabolism an

169 atus with coordination of metabolic outputs, sirtuins are well poised to play pivotal roles in tumor

170 Our results, for the first time, implicate sirtuins as a central player in the determination of pla

171 acetyltransferases and deacetylases and the sirtuins as a conserved family of a nicotinamide adenine

172 vo These data suggest a re-evaluation of the sirtuins as direct sensors of the NAD(+)/NADH ratio.

173 Several studies have described the sirtuins as sensors of the NAD(+)/NADH ratio, but it has

174 the target protein and can be reversed by a sirtuin-associated macrodomain protein.

175 nhibitor development and selective tools for sirtuin biology.

176 sttranslational modifications, and show that sirtuins can act as erasers of HibK modified proteins.

177 Most previous studies investigated sirtuin-catalyzed deacylation on peptide substrates only

178 l significance of lysine fatty acylation and sirtuin-catalyzed protein lysine defatty-acylation.

179 This makes the sirtuin class of enzymes interesting targets for develop

180 e propofol binding site on SIRT2 contact the sirtuin co-substrate NAD(+) during enzymatic catalysis,

181 reover, this modification is reversed by the sirtuin CobB.

182 le continuous activity assays running at low sirtuin concentrations in microtiter plates.

183 Different sirtuins control similar cellular processes, suggesting

184 at brain with [(3)H]AziPm and identified the sirtuin deacetylase SIRT2 as a target of the anesthetic.

185 ine, depletion of the mitochondrial-enriched sirtuin deacetylase SIRT3 increased NLRP3 inflammasome a

186 associated with hypoacetylated histones or a sirtuin deacetylase that generates heterochromatin in ot

187 Although early studies showed that sirtuins deacetylated lysines in a reaction that consume

188 All tested sirtuin deacylase activities showed sensitivity to NADH

189 Together, our data describe a sirtuin-dependent reversible protein ADP-ribosylation sy

190 The sirtuin enzymes are important regulatory deacylases in a

191 For a number of years, sirtuin enzymes have been appreciated as effective "sens

192 contrast to earlier described classes, these sirtuins exhibit robust protein ADP-ribosylation activit

193 Here, we identify the chromatin regulatory Sirtuin factor SIRT7 as a key regulator of metastatic ph

194 roto member of the proteins in the mammalian sirtuin family and plays multiple roles in aging and dis

195 Sirtuin 2 (SIRT2) is a sirtuin family deacetylase, which maintains genome integ

196 ial cross-regulatory interactions within the sirtuin family is still limited.

197 Sirtuin 6 (SIRT6) is a sirtuin family member involved in a wide range of physio

198 MEK1 is under the regulatory control of the sirtuin family members SIRT1 and SIRT2.

199 SIRT6 is a member of the mammalian sirtuin family of anti-aging genes.

200 SIRT6 (sirtuin 6) is a member of sirtuin family of deacetylases involved in diverse proce

201 trated that SIRT6, a member of the mammalian sirtuin family of enzymes, can remove the fatty acyl mod

202 Sirt6, a member of the sirtuin family of NAD-dependent protein deacetylases, ha

203 The sirtuin family of proteins catalyze the NAD(+)-dependent

204 In particular, we review the biology of the sirtuin family of proteins, the insulin/insulin-like gro

205 p-regulating the level of Sirt3, a member of Sirtuin family protein located in mitochondria, which re

206 eacetylase SIRT1, the founding member of the sirtuin family, contributes to clock function.

207 SIRT6 is a chromatin-bound member of the sirtuin family, implicated in regulating many cellular p

208 The catalytic domain adopts the canonical sirtuin fold.

209 Targeting sirtuins for cancer treatment has been a topic of debate

210 ort to identify small molecule inhibitors of sirtuins for potential use as chemotherapeutics as well

211 the other hand, cancer cells tend to require sirtuins for these same processes to allow them to survi

212 xistence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens.

213 Here, we discuss sirtuin functions in the context of viral infection, whi

214 Sirtuin genes have been associated with aging and are kn

215 3 are robust deacetylases, whereas the other sirtuins have preferences for longer acyl chains.

216 association between class I, II, or IV (non-sirtuin) HDACs and linker histones has been reported.

217 In addition, we identified the sirtuin Hst3 and its histone target as contributors to t

218 ent inhibitors in the presence of only 10 nM sirtuin in microtiter plate format.

219 However, the pivotal targets for sirtuins in cancer are mainly unknown.

220 rescent probe (EGFP-K85AcK) that responds to sirtuins in living cells.

221 Here, we review the multi-faceted duties of sirtuins in tackling the metabolic hurdles in cancer.

222 studies have demonstrated critical roles of sirtuins in the brain, especially the hypothalamus, in g

223 us on both beneficial and adverse effects of sirtuins in the regulation of energetic, biosynthetic an

224 ed roles of SIRT1, and perhaps several other sirtuins, in cancer may be in part a result of the natur

225 that the probe can respond to various human sirtuins, including SIRT1, SIRT2, SIRT3 and SIRT5.

226 es attention on the potential side effect of sirtuin inhibition in delimiting platelet life span and

227 ghts into this unique mechanism of selective sirtuin inhibition provide the basis for further inhibit

228 ity, we previously identified a nonselective sirtuin inhibitor called cambinol (IC50 approximately 50

229 deletion showed that the effects of the pan-sirtuin inhibitor nicotinamide are primarily mediated by

230 siRNA or treated with nicotinamide (NAM), a sirtuin inhibitor.

231 Because sirtuin inhibitors are being evaluated for their antitum

232 nowledge of HDACi (both class I/II HDACi and sirtuin inhibitors) targeted to the main human parasitic

233 iled profiling and kinetic insight regarding sirtuin inhibitors, it is important to have access to ef

234 Treatment of cells with sirtuin inhibitors, or siRNA knockdown of SIRT1 or SIRT2

235 ing the p53-Bax axis in apoptosis induced by sirtuin inhibitors.

236 This work reveals sirtuin interactions with numerous functional modules wi

237 e mammalian family of seven NAD(+)-dependent sirtuins, is composed of 747 amino acids forming a catal

238 In humans, seven sirtuin isoforms (Sirt1 to Sirt7) have been identified.

239 on to the well established activities of the sirtuins, "long chain" acyllysine modifications were als

240 r fasting blunts inflammasome activation via sirtuin-mediated augmentation of mitochondrial integrity

241 Here, we report that a M. oryzae sirtuin, MoSir2, plays an essential role in rice defence

242 an also be added by other enzymes, including sirtuins or bacterial toxins.

243 Sirtuins participate in sensing nutrient availability an

244 and poly(ADP-ribose) polymerase also reduce sirtuin, PGC-1alpha, and AMP-activated protein kinase ac

245 on proteomics to elucidate the mitochondrial sirtuin protein interaction landscape.

246 together, our results uncover a link between sirtuin proteins and direct control over cellular iron h

247 sirtuin 5 assay based on the coupling of the sirtuin reaction to a proteolytic cleavage using interna

248 he combination of the unique features of the sirtuin rearranging ligands (SirReals) as highly potent

249 The sirtuin rearranging ligands (SirReals) have recently bee

250 Application of the most potent Sirtuin-rearranging ligand, termed SirReal2, leads to tu

251 ty of sirtuins with a focus on how different sirtuins recognize distinct substrates and thus carry ou

252 s review, we discuss the mechanisms by which sirtuins regulate Akt activation and how they influence

253 aptive cellular responses, identification of sirtuin-regulated signaling targets remain under-studied

254 we discuss the current understanding of how sirtuins relate to aging.

255 tuin activity, and the relationships between sirtuins remains a key challenge in mitochondrial physio

256 nce the activity and expression of cytosolic sirtuins, resulting in global changes in protein acetyla

257 arkedly changes histone acetylation, and the sirtuin Sir2/SIRT1 that deacetylates histones and transc

258 malian cells, histone deacetylase (HDAC) and Sirtuin (SIRT) are two families responsible for removing

259 One such factor is the sirtuin (SIRT) family of nicotinamide adenine dinucleoti

260 ivation of the class III histone deacetylase sirtuin (SIRT)-1.

261 NR prevents and reverts NAFLD by inducing a sirtuin (SIRT)1- and SIRT3-dependent mitochondrial unfol

262 Small molecule activators for the human sirtuins Sirt1-7 are sought as chemical tools and potent

263 Sirtuins (SIRT1-7) are NAD-dependent proteins with the e

264 Humans encode seven sirtuins (Sirt1-7), and recent studies have suggested th

265 , ADP-ribosyl cyclases (CD38 and CD157), and sirtuins (SIRT1-7).

266 Sirtuins (Sirt1-Sirt7) are NAD(+)-dependent protein deac

267 The best-studied sirtuin, SIRT1, counteracts aging- and obesity-related d

268 Among the seven mammalian sirtuins, SIRT1-7, only SIRT1-3 possess efficient deacet

269 te kinase (PKM2) as a critical target of the sirtuin SIRT2 implicated in cancer.

270 Mitochondrial sirtuins, SIRT3-5, are NAD(+)-dependent deacylases and A

271 Recently, the mitochondrial sirtuin SIRT4 has been reported to function as a tumor s

272 In mitochondria, the sirtuin SIRT5 is an NAD(+)-dependent protein deacylase t

273 hts into regulation of the tumor suppressive sirtuin SIRT6 and its implications for the development o

274 riggers degradation of the tumor-suppressive sirtuin SIRT6 in hepatocellular carcinoma.

275 The enzymatic activity of the mammalian sirtuin SIRT7 targets acetylated lysine in the N-termina

276 Sirtuins (SIRTs) are NAD-dependent deacylases, known to

277 SHV from latency, the role of class III HDAC sirtuins (SIRTs) in KSHV latency remains unclear.

278 eacetylases (HDACs) and the NAD(+) dependent sirtuins (SIRTs) in the DNA damage response (DDR).

279 d 9, and Silent information regulator genes (sirtuins [SIRTs]) 6 and 7 were significantly high in HBE

280 7,000 M(-1) s(-1), which represents the best sirtuin substrate described so far.

281 However, other reported sirtuin substrate proteins such as cyclophilin D, supero

282 protein structure is a major determinant of sirtuin substrate specificity.

283 es within mitochondria, identifies candidate sirtuin substrates, and uncovers a fundamental role for

284 ch now enables more efficient development of sirtuin targeting drugs.

285 However, a comprehensive understanding of sirtuin targets, regulation of sirtuin activity, and the

286 SIRT2 is a cytoplasmic sirtuin that plays a role in various cellular processes,

287 Several sirtuins that exhibit weak deacetylase activity have rec

288 d uncovered the unexpected contribution of a sirtuin to heterochromatin dynamics.

289 roach can be used to examine the activity of sirtuins toward additional lysyl posttranslational modif

290 ld not be removed by the histone deacetylase sirtuin type 1.

291 opsis thaliana) genome encodes two predicted sirtuin-type Lys deacetylases, of which only Silent Info

292 Acetylated SacAcsA was deacetylated by a sirtuin-type NAD(+)-dependent consuming deacetylase (Sac

293 Deacetylation activity of certain sirtuins was detected for two Ran acetylation sites in v

294 The activity of mitochondrial sirtuins was reduced in livers of the KO mice.

295 SIRT6, a sirtuin with established tumor suppressor function, regu

296 ure, chemistry, and substrate specificity of sirtuins with a focus on how different sirtuins recogniz

297 Sirtuins with an extended N-terminal domain (NTD), repre

298 underlie the distinct roles of the different sirtuins within a given organism.

299 by ADP-ribosyltransferases and a subclass of sirtuins (writers), is sensed by proteins that contain b

300 lated with Zn(2+) release from the conserved sirtuin Zn(2+)-tetrathiolate and a loss of alpha-helical