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1  two were acetylated but not deacetylated by sirtuin.
2 lso an efficient deacetylation substrate for sirtuins.
3 exity in the crosstalk between two different sirtuins.
4  the range of hydrolytic activities of human sirtuins.
5 NAD(+)-dependent deacylase activities of the sirtuins.
6 logical functions regulated by mitochondrial sirtuins.
7 e four amino acids is not conserved in human sirtuins.
8 o increase ER and DAF-12 coactivation by the sirtuins.
9 etylation that is regulated by both Gcn5 and sirtuins.
10                                              Sirtuin 1 (SIRT) mRNA levels were lower in PLAC when com
11  factor 1 (HES1) and the protein deacetylase sirtuin 1 (SIRT1) at the Isl1 gene.
12                                              Sirtuin 1 (SIRT1) binds, deacetylates, and thereby inact
13 und that higher abundance of the deacetylase sirtuin 1 (SIRT1) correlated with lower acetylation occu
14 eptor nuclear translocator-like (Arntl), and sirtuin 1 (Sirt1) expression.
15  of the NAD(+)-dependent lysine deacetylase, sirtuin 1 (SIRT1) in fibrogenesis in the cell culture, a
16                                              Sirtuin 1 (Sirt1) is a NAD(+)-dependent deacetylase capa
17                                              Sirtuin 1 (SIRT1) is a nicotinamide adenine dinucleotide
18                            The class III NAD-sirtuin 1 (SIRT1) is an important negative regulator of
19                                              Sirtuin 1 (SIRT1) is an NAD(+)-dependent deacetylase tha
20             The NAD(+)-dependent deacetylase Sirtuin 1 (SIRT1) is down-regulated in triple-negative b
21                                              Sirtuin 1 (SIRT1) is involved in both aging and circadia
22             The NAD(+)-dependent deacetylase Sirtuin 1 (SIRT1) regulates cell metabolism, proliferati
23                                              Sirtuin 1 (SIRT1) regulates liver regeneration and bile
24    Here, we propose that the nutrient sensor sirtuin 1 (Sirt1) regulates the production of CRH post-t
25 iency, along with significant suppression of sirtuin 1 (SIRT1) signaling pathway in the liver.
26                           In animal studies, sirtuin 1 (SIRT1) was associated with protection against
27                          We investigated how Sirtuin 1 (SIRT1), a conserved mammalian NAD(+)-dependen
28 ed activation of KRAS and over-expression of Sirtuin 1 (SIRT1), a histone deacetylase and gene silenc
29     The NAD(+)-dependent protein deacetylase sirtuin 1 (SIRT1), a key regulator of mammalian metaboli
30 e their known interaction in transactivating Sirtuin 1 (SIRT1), a NAD(+)-dependent histone deacetylas
31                                              Sirtuin 1 (SIRT1), an NAD(+) (nicotinamide adenine dinuc
32 evidence demonstrates the beneficial role of Sirtuin 1 (SIRT1), an NAD(+) dependant deacetylase, in i
33                                              Sirtuin 1 (SIRT1), an NAD(+)-dependent deacetylase, is a
34 leotide (NAD+)-dependent deacetylase enzyme, Sirtuin 1 (SIRT1), can prevent activation of these pathw
35 y several energy sensing pathways, including sirtuin 1 (SIRT1), forkhead box O (FoxO), AMP-activated
36 cers of fatty acid beta-oxidation, including sirtuin 1 (SIRT1), sirtuin 3 (SIRT3), and Nrf-1.
37 how that HAS2 expression can be modulated by sirtuin 1 (SIRT1), the master metabolic sensor of the ce
38  inhibitors and RA reduced HDAC1, HDAC4, and sirtuin 1 (SIRT1), which were involved in chromatin remo
39 eraction with the metabolic sensing protein, Sirtuin 1 (SIRT1).
40 ical and genetic approaches to show that the sirtuin 1 (SIRT1)/FoxO1 signaling pathway in the hypotha
41 ic ischemia-reperfusion and posttreated with sirtuin 1 activator, SRT1720 (20 mg/kg), or vehicle.
42 id hemorrhage injury primarily by increasing sirtuin 1 and inhibiting the Toll-like receptor 4 signal
43                 Pharmacologic stimulation of sirtuin 1 attenuates liver injury after hepatic ischemia
44                            Here we show that sirtuin 1 deacetylase (Sirt1) deacetylates Nav1.5 at lys
45 tly inhibited the TLR4 activation, increased sirtuin 1 expression, and inhibited the subsequent infla
46                                              Sirtuin 1 is an energy-sensing enzyme known to modulate
47 ypothesized that pharmacologic activation of sirtuin 1 is protective after hepatic ischemia-reperfusi
48 in injury after SAH, primarily by increasing sirtuin 1 levels and inhibiting the TLR4 signaling pathw
49                     The inhibitory action on Sirtuin 1 of approximately half of the proposed compound
50                                     However, sirtuin 1 was downregulated and so the accumulation of N
51  in liver PAFR was associated with increased sirtuin 1 while relocalized PAFR expression was limited
52 cade involving AMP-activated protein kinase, sirtuin 1, PGC-1alpha, sirtuin 3, estrogen-related recep
53 arget biomolecule, NAD-dependent deacetylase Sirtuin 1, were identified by a contest-based approach,
54           NAMPT inhibits CXCR4 through a NAD/Sirtuin 1-mediated inactivation of HIF1alpha-driven CXCR
55  neurons, an effect that was reversed by the sirtuin 1-specific inhibitor sirtinol.
56                        We observed that both sirtuins 1 and 7 (SIRT1 and SIRT7) are able to deacetyla
57                                              Sirtuin-1 (Sirt-1) plays a crucial role in various biolo
58 y decreased levels of the histone deactylase Sirtuin-1 (SirT-1) which has been previously shown to fu
59 chloroethylamide inhibited the expression of Sirtuin-1 (Sirt1) and Rictor, a component of mechanistic
60                    NAD-dependent deacetylase sirtuin-1 (SIRT1) is a class III histone deacetylase tha
61 ducer, its role in OLT and interactions with sirtuin-1 (SIRT1), a key autophagy regulator, have not b
62 in states of nutrient and oxygen deprivation-sirtuin-1 (SIRT1), AMP-activated protein kinase (AMPK),
63 s activate low-energy sensors, which include sirtuin-1 (SIRT1), AMP-activated protein kinase (AMPK),
64 ue in response to lipolytic stimulation in a sirtuin-1 (SIRT1)-dependent manner via a mechanism that
65                                              Sirtuin-1 also inhibits cancer metastasis via increasing
66     miR-570 is also involved in reduction of sirtuin-1 and cellular senescence and is activated by p3
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              Loss of key antiaging molecules sirtuin-1 and sirtuin-6 may be important in acceleration
71 ithelial cells, using an antagomir, restores sirtuin-1 and suppresses markers of cellular senescence
72 AP, above 0.001%, enhanced the expression of sirtuin-1 and thermogenic uncoupling protein 1 (UCP-1) i
73 ors, AMP-activated protein kinase (AMPK) and sirtuin-1 are activated.
74 ve stress and nephropathy via stimulation of Sirtuin-1 expression and signaling in diabetes.
75 as to determine whether differences exist in sirtuin-1 expression/activity in old vs. young liver gra
76                                         AMPK/sirtuin-1 inhibit the activity of STAT3 (signal transduc
77     Importantly, treating AAV-NT mice with a sirtuin-1 inhibitor markedly reversed many of the observ
78 iption via hnRNP F-responsive element in the Sirtuin-1 promoter.
79 tudies using inhibitors of PPARbeta/delta or sirtuin-1 showed that the tubulogenic effect of GW0742,
80 ervals, increasing NAD-dependent deacetylase sirtuin-1 signaling important for glucose and lipid meta
81                              Transfection of Sirtuin-1 small interfering RNA prevented hnRNP F stimul
82                           hnRNP F stimulated Sirtuin-1 transcription via hnRNP F-responsive element i
83 esis and ketogenesis is activation of SIRT1 (sirtuin-1) and its downstream mediators: PGC-1alpha (pro
84 roblast growth factor 21 (FGF21), targets of sirtuin-1, and beta-klotho, which can acts as a tumor su
85 C apoptosis and lower expression of hnRNP F, SIRTUIN-1, and FOXO3alpha than nondiabetic kidneys.
86          Instead, triiodothyronine increased sirtuin-1, fibrillin-1, proliferator-activated receptor-
87                                              Sirtuin-1, Foxo3alpha, and catalase expression were sign
88 -570-3p rejuvenates cells via restoration of sirtuin-1, reducing many of the abnormalities associated
89 742, but not VEGF-A, was PPARbeta/delta- and sirtuin-1-dependent.
90 Furthermore, we identified that aging alters Sirtuin-1-hepatic nuclear factor 4alpha circuit in hepat
91 low AGE diets with increased adiponectin and sirtuin-1.
92 ignaling and drives senescence by inhibiting sirtuin-1.
93 nescence by restoring the antiaging molecule sirtuin-1.
94  signaling, plays a pivotal role in reducing sirtuin-1/6, and its inhibition with an antagomir result
95 heat shock proteins, antioxidant enzymes and sirtuin-1/PGC-1 signalling) are central to the protectiv
96 onsive E3 ubiquitin ligases targeting fungal sirtuin 2 (Sir2), an antioxidation regulator required fo
97 , we identified that the protein deacetylase sirtuin 2 (SIRT2) as a novel interactor of LMAN2.
98 rerequisite for its phosphorylation, whereas Sirtuin 2 (SIRT2) deacetylated MARCKS.
99   Derived from our previously reported human sirtuin 2 (SIRT2) inhibitors that were based on a 5-amin
100                                              Sirtuin 2 (SIRT2) is a protein lysine deacylase that has
101                                              Sirtuin 2 (SIRT2) is a sirtuin family deacetylase, which
102 cotinamide phosphoribosyltransferase (NAMPT)/sirtuin 2 (SIRT2) pathway.
103 munoblotting and kinase assays, we show that sirtuin 2 (SIRT2), a member of the NAD-dependent protein
104                                              Sirtuin 2 (SIRT2), one of the mammalian nicotinamide ade
105 dulators, NAD+ dependent histone deacetylase Sirtuin 2 (SIRT2), which upon infection translocate to t
106 esting of synthetic substrates of S. mansoni sirtuin 2 (SmSirt2) and kinetic experiments on a myristo
107 chanistic insight into the interplay between sirtuin 2 and alpha-synuclein, the major component of th
108 nstrating the potential therapeutic value of sirtuin 2 inhibition in synucleinopathies.
109                      Genetic manipulation of sirtuin 2 levels in vitro and in vivo modulates the leve
110                                              Sirtuin 2 was previously shown to modulate proteotoxicit
111  and that these residues are deacetylated by sirtuin 2.
112 and the NAD(+)-dependent tubulin deacetylase sirtuin-2 (SIRT2) play key roles in oligodendrocyte diff
113 cetylation was elevated because of decreased sirtuin-2 expression, thereby promoting loss of PCK1.
114 onal repression of mitochondrial deacetylase sirtuin 3 (SIRT3) by androgen receptor (AR) and its core
115                                              Sirtuin 3 (SIRT3) deacetylates and regulates many mitoch
116                                              Sirtuin 3 (SIRT3) detoxifies mitochondrial reactive oxyg
117 functional significance of the mitochondrial sirtuin 3 (SIRT3) in melanoma.
118                            The mitochondrial sirtuin 3 (SIRT3) is involved in suppressing the onset o
119                The mitochondrial deacetylase sirtuin 3 (SIRT3) is thought to be one of the main contr
120                                              Sirtuin 3 (SIRT3) mediates histone protein post-translat
121 beta-oxidation, including sirtuin 1 (SIRT1), sirtuin 3 (SIRT3), and Nrf-1.
122 ly with oxidative phosphorylation Complex I, sirtuin 3 and succinate dehydrogenase.
123 the NAD(+)-dependent deacetylase activity of sirtuin 3 to inhibit superoxide dismutase 2 (SOD2) activ
124 ALE: Clinical studies have shown that Sirt3 (Sirtuin 3) expression declines by 40% by 65 years of age
125         The mitochondrial deacetylase Sirt3 (Sirtuin 3) is critical in the regulation of metabolic an
126                                       SIRT3 (sirtuin 3) is the major deacetylase within the mitochond
127 rAT (carnitine acetyltransferase) and Sirt3 (sirtuin 3)-enzymes that oppose Kac by buffering the acet
128 vated protein kinase, sirtuin 1, PGC-1alpha, sirtuin 3, estrogen-related receptor-alpha, and Nrf-1; i
129 gnificantly induce mitochondrial deacetylase sirtuin-3 (SIRT3) activity, disrupted mitochondrial stru
130                                  We examined Sirtuin-3 (Sirt3) co-expressed gene sets extracted from
131                                              Sirtuin-3 (Sirt3) is a mitochondrial deacetylase that co
132                          Here, we found that Sirtuin 4 (SIRT4) interacts with PTEN and regulates its
133                                              Sirtuin 5 (SIRT5) is a mitochondrial-localized NAD(+)-de
134 he discovery of the most potent inhibitor of sirtuin 5 (SIRT5) reported to date.
135                                              Sirtuin 5 (Sirt5), which localizes to both mitochondria
136  lysine succinylation, which is regulated by sirtuin 5 (SIRT5).
137  models and biochemical assays, we show that sirtuin 6 (SIRT6) deficiency plays a major role in aging
138                              NAD + dependent Sirtuin 6 (SIRT6) is a glucose homeostasis regulator in
139                                              Sirtuin 6 (SIRT6) is a nuclear NAD(+)-dependent deacetyl
140                                              Sirtuin 6 (SIRT6) is a sirtuin family member involved in
141                                    Mammalian Sirtuin 6 (Sirt6) is an NAD(+)-dependent protein deacyla
142            The class III histone deacetylase sirtuin 6 (SIRT6) modulates numerous functions in the ce
143                      The histone deacetylase sirtuin 6 (SIRT6) regulates numerous biological function
144  by the NAD(+)-dependent histone deacetylase Sirtuin 6 (SIRT6) that is critical for suppression of pa
145                                Inhibition of sirtuin 6 (SIRT6), a histone deacetylase repressor of gl
146                                       SIRT6 (sirtuin 6) is a member of sirtuin family of deacetylases
147                                       SIRT6 (Sirtuin 6) is a nuclear deacetylase involved in DNA dama
148                                              Sirtuin 6, SIRT6, is critical for both glucose and lipid
149 oss of key antiaging molecules sirtuin-1 and sirtuin-6 may be important in acceleration of aging and
150                                              Sirtuin 7 (SIRT7), an NAD(+)-dependent deacetylase, play
151                                              Sirtuins, a family of protein deacetylases, promote cell
152                             Although dietary sirtuin-activating compounds (dSTACs) including resverat
153           Research shows that resveratrol, a sirtuin activator in red wine, improves exercise enduran
154 ther dissect the regulation of both Gcn5 and sirtuin activities in vivo.
155          Our findings suggest that targeting sirtuin activities may offer an avenue in the developmen
156       Although multiple reports suggest that sirtuin activity is regulated by oxidative post-translat
157 ts oxidative damage, maintains mitochondrial sirtuin activity, and prevents metabolic stress-induced
158 erstanding of sirtuin targets, regulation of sirtuin activity, and the relationships between sirtuins
159  and hepatosteatosis by dioxin and increased sirtuin activity, providing a therapeutic approach for p
160 o increased poly(ADP-ribosyl) polymerase and sirtuin activity, suggesting an increased cellular deman
161 ied class of compounds capable of inhibiting sirtuin activity, which is thought to result in increase
162 m of the NAD+ salvage pathway due to reduced sirtuin activity.
163                                The impact of sirtuin and PARP inhibition was also explored.
164 s, programmed cell death, synaptic function, sirtuins and aging, and insulin resistance, all processe
165 ng protein/p300 acetylated FUS, whereas both sirtuins and histone deacetylases families of lysine dea
166  a reduction in antiaging molecules, such as sirtuins and Klotho, which further accelerate the aging
167 dria approximate the Michaelis constants for sirtuins and PARPs in their respective compartments.
168 otide (NAD(+)) is an essential substrate for sirtuins and poly(adenosine diphosphate-ribose) polymera
169 tivity of various enzyme families, including sirtuins and poly(ADP-ribose) polymerases.
170            NAD-dependent signaling (e.g., by sirtuins and poly-adenosine diphosphate [ADP] ribose pol
171    The development of monoclonal antibodies, sirtuins, and cyclopropovir may provide new treatment op
172  enzymes (e.g. poly(ADP-ribose) polymerases, sirtuins, and others).
173                                              Sirtuins are class III histone deacylases that use NAD(+
174  expression is highest in the heart and that sirtuins are commonly stress-response proteins, we used
175                                Modulators of sirtuins are considered promising therapeutic targets fo
176                                     Gcn5 and sirtuins are highly conserved histone acetyltransferase
177                                              Sirtuins are important regulators of lysine acylation, w
178  rapamycin, AMP-activated protein kinase and sirtuins are key regulators of autophagy.
179                                              Sirtuins are NAD(+) dependent protein deacetylases, whic
180                                              Sirtuins are NAD(+)-dependent enzymes universally presen
181                                              Sirtuins are NAD(+)-dependent lysine deacylases, regulat
182                                              Sirtuins are NAD(+)-dependent protein deacylases that cl
183                                              Sirtuins are protein deacylases regulating metabolism an
184                These enzymes, along with the sirtuins, are collectively responsible for reversing lys
185 vo These data suggest a re-evaluation of the sirtuins as direct sensors of the NAD(+)/NADH ratio.
186           Several studies have described the sirtuins as sensors of the NAD(+)/NADH ratio, but it has
187  foundation for future studies investigating sirtuin-based therapies.
188 sttranslational modifications, and show that sirtuins can act as erasers of HibK modified proteins.
189 l significance of lysine fatty acylation and sirtuin-catalyzed protein lysine defatty-acylation.
190 on-redox NAD(+)-dependent enzymes, including sirtuins, CD38 and poly(ADP-ribose) polymerases.
191                               This makes the sirtuin class of enzymes interesting targets for develop
192 nt work indicates that SIRT1 and orthologous sirtuins coactivate the oestrogen receptor/ER and the wo
193                                    Different sirtuins control similar cellular processes, suggesting
194 ematic comparative study of potential direct sirtuin cysteine oxidative modifications has been perfor
195  discrepancies involving effects of sir-2.1 (sirtuin deacetylase) on ageing, and show that in a fln-2
196           Although early studies showed that sirtuins deacetylated lysines in a reaction that consume
197 ARP-enzymes (mono/poly-ADP-ribosylation) and sirtuins (deacetylation).
198                                   All tested sirtuin deacylase activities showed sensitivity to NADH
199       We report 1) modulation of a bacterial sirtuin deacylase activity by acetylation, 2) that the G
200 s in an NAD(+)-dependent manner, and loss of sirtuin deacylase activity correlates with the developme
201  we report that, in Salmonella enterica, the sirtuin deacylase CobB long isoform (CobB(L)) is N-termi
202 ied CoA ligases were under NAD(+) -dependent sirtuin deacylase reversible lysine (de)acetylation cont
203        Here, we investigated the role of the sirtuin deacylase Sirt5 in MCT metabolism by feeding Sir
204                                              Sirtuins (e.g. human Sirt1-7) catalyze the removal of ac
205  results thus provide a structural basis for Sirtuin effects of quercetin-related compounds and helpf
206                                          The sirtuin enzymes are important regulatory deacylases in a
207 nzymatic activity of the histone deacetylase sirtuin family (SIRT1, SIRT2, SIRT3, SIRT5 and SIRT6) us
208 roto member of the proteins in the mammalian sirtuin family and plays multiple roles in aging and dis
209                       Sirtuin 2 (SIRT2) is a sirtuin family deacetylase, which maintains genome integ
210 ial cross-regulatory interactions within the sirtuin family is still limited.
211                       Sirtuin 6 (SIRT6) is a sirtuin family member involved in a wide range of physio
212                        Here we show that the sirtuin family member SIRT7 participates in the epigenet
213             SIRT6 (sirtuin 6) is a member of sirtuin family of deacetylases involved in diverse proce
214 trated that SIRT6, a member of the mammalian sirtuin family of enzymes, can remove the fatty acyl mod
215 ls and highlights how SIRT7, a member of the sirtuin family of protein deacylases and mono-ADP ribosy
216                                          The sirtuin family of proteins catalyze the NAD(+)-dependent
217  In particular, we review the biology of the sirtuin family of proteins, the insulin/insulin-like gro
218     SIRT6 is a chromatin-bound member of the sirtuin family, implicated in regulating many cellular p
219                                    Targeting sirtuins for cancer treatment has been a topic of debate
220                                              Sirtuin genes have been associated with aging and are kn
221                                              Sirtuins have been shown to possess NAD(+)-dependent des
222 3 are robust deacetylases, whereas the other sirtuins have preferences for longer acyl chains.
223  association between class I, II, or IV (non-sirtuin) HDACs and linker histones has been reported.
224             However, the pivotal targets for sirtuins in cancer are mainly unknown.
225 rescent probe (EGFP-K85AcK) that responds to sirtuins in living cells.
226 tify novel nonhistone substrates of Gcn5 and sirtuins in yeast and found a shared target consensus se
227  that the probe can respond to various human sirtuins, including SIRT1, SIRT2, SIRT3 and SIRT5.
228 s may causatively link nuclear and cytosolic sirtuin inhibition to aging-related inflammatory disease
229 e developed a mitochondrial-targeted class I sirtuin inhibitor, YC8-02, which phenocopied the effects
230  siRNA or treated with nicotinamide (NAM), a sirtuin inhibitor.
231           Due to the strong effects of human sirtuin inhibitors on parasite survival and reproduction
232 nowledge of HDACi (both class I/II HDACi and sirtuin inhibitors) targeted to the main human parasitic
233                            This work reveals sirtuin interactions with numerous functional modules wi
234 ding and activity effects on Sirt6 and other Sirtuin isoforms and solved crystal structures of compou
235 ut showing any significant increase in other sirtuin isoforms.
236 on to the well established activities of the sirtuins, "long chain" acyllysine modifications were als
237 rapies that regulate NAD+ and thereby target sirtuins may be beneficial in human diabetic sensory pol
238 olism through histone hyper-acetylation, and Sirtuin-mediated silencing of starvation-induced subtelo
239 an also be added by other enzymes, including sirtuins or bacterial toxins.
240  inhibition was not caused by suppression of sirtuins or PARP1, and 4) phosphorylation of several pro
241                                          The sirtuin pathway may represent a target for intervention
242  and poly(ADP-ribose) polymerase also reduce sirtuin, PGC-1alpha, and AMP-activated protein kinase ac
243 ivated) by the NAD(+) -dependent (class III) sirtuin protein deacetylase (hereafter SaCobB).
244 on proteomics to elucidate the mitochondrial sirtuin protein interaction landscape.
245 together, our results uncover a link between sirtuin proteins and direct control over cellular iron h
246 he combination of the unique features of the sirtuin rearranging ligands (SirReals) as highly potent
247                                          The sirtuin rearranging ligands (SirReals) have recently bee
248 ty of sirtuins with a focus on how different sirtuins recognize distinct substrates and thus carry ou
249 tuin activity, and the relationships between sirtuins remains a key challenge in mitochondrial physio
250                              Moreover, other Sirtuins share some DSB-binding capacity and DDR activat
251 es that use exploitative mimicry to modulate sirtuin signalling through steroid receptors.
252 gly, resveratrol non-monotonically modulates sirtuin signalling, suggesting that it may induce hormes
253 arkedly changes histone acetylation, and the sirtuin Sir2/SIRT1 that deacetylates histones and transc
254  preserving the NAD(+)-dependent deacetylase sirtuin (Sirt) 1 in human macrophages.
255 malian cells, histone deacetylase (HDAC) and Sirtuin (SIRT) are two families responsible for removing
256                       One such factor is the sirtuin (SIRT) family of nicotinamide adenine dinucleoti
257      Acetylation of NAT1 was enhanced by the sirtuin (SIRT) inhibitor nicotinamide but not by the his
258 ivation of the class III histone deacetylase sirtuin (SIRT)-1.
259  NR prevents and reverts NAFLD by inducing a sirtuin (SIRT)1- and SIRT3-dependent mitochondrial unfol
260 , transcription factor A, mitochondrial, and Sirtuin (Sirt)3 and Sirt1 expression in whole lungs and
261  p300/CBP in situ and is deacetylated by the sirtuins SIRT1 and 2.
262           We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytos
263      Small molecule activators for the human sirtuins Sirt1-7 are sought as chemical tools and potent
264                                              Sirtuins (SIRT1-7) are NAD-dependent proteins with the e
265                          Humans encode seven sirtuins (Sirt1-7), and recent studies have suggested th
266 , ADP-ribosyl cyclases (CD38 and CD157), and sirtuins (SIRT1-7).
267                                              Sirtuins (Sirt1-Sirt7) are NAD(+)-dependent protein deac
268                             The best-studied sirtuin, SIRT1, counteracts aging- and obesity-related d
269 te kinase (PKM2) as a critical target of the sirtuin SIRT2 implicated in cancer.
270 nd Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-
271              Surprisingly, the mitochondrial sirtuins Sirt3 and Sirt5 were resistant to inhibition by
272                                Mitochondrial sirtuins, SIRT3-5, are NAD(+)-dependent deacylases and A
273                         In mitochondria, the sirtuin SIRT5 is an NAD(+)-dependent protein deacylase t
274 hts into regulation of the tumor suppressive sirtuin SIRT6 and its implications for the development o
275 riggers degradation of the tumor-suppressive sirtuin SIRT6 in hepatocellular carcinoma.
276                The nuclear and mitochondrial sirtuins, Sirt6 and Sirt3, regulate each other's activit
277      The enzymatic activity of the mammalian sirtuin SIRT7 targets acetylated lysine in the N-termina
278                                              Sirtuins (Sirts) are implicated in regulating a myriad o
279                                              Sirtuins (SIRTs) are NAD(+)-dependent deacylases that pl
280                                              Sirtuins (SIRTs) are NAD-dependent deacylases, known to
281 eacetylases (HDACs) and the NAD(+) dependent sirtuins (SIRTs) in the DNA damage response (DDR).
282                                              Sirtuins (SIRTs), central regulators of the aging proces
283 hat several histone deacetylases (HDACs) and sirtuins (SIRTs), including HDACs 2, 7, 8, and 11 and SI
284 ch as CD38, poly-ADP-ribose polymerases, and sirtuins (SIRTs).
285 d 9, and Silent information regulator genes (sirtuins [SIRTs]) 6 and 7 were significantly high in HBE
286                      However, other reported sirtuin substrate proteins such as cyclophilin D, supero
287  protein structure is a major determinant of sirtuin substrate specificity.
288 es within mitochondria, identifies candidate sirtuin substrates, and uncovers a fundamental role for
289    However, a comprehensive understanding of sirtuin targets, regulation of sirtuin activity, and the
290                       SIRT2 is a cytoplasmic sirtuin that plays a role in various cellular processes,
291 d uncovered the unexpected contribution of a sirtuin to heterochromatin dynamics.
292 lly mimic gonadal steroid hormones, enabling sirtuins to transduce the cognate signals through a cons
293 roach can be used to examine the activity of sirtuins toward additional lysyl posttranslational modif
294 ld not be removed by the histone deacetylase sirtuin type 1.
295 erring the silencing and show it to encode a sirtuin-type histone deacetylase.
296                The activity of mitochondrial sirtuins was reduced in livers of the KO mice.
297 asite survival and reproduction, Schistosoma sirtuins were postulated as potential therapeutic target
298                                     SIRT6, a sirtuin with established tumor suppressor function, regu
299 ure, chemistry, and substrate specificity of sirtuins with a focus on how different sirtuins recogniz
300 underlie the distinct roles of the different sirtuins within a given organism.
301 lated with Zn(2+) release from the conserved sirtuin Zn(2+)-tetrathiolate and a loss of alpha-helical

 
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