Details of Drug Off-Target (DOT)

General Information of Drug Off-Target (DOT) (ID: OTAYZMOY)

• DOT Name: NAD-dependent protein deacetylase sirtuin-1 (SIRT1)
• Synonyms: hSIRT1; EC 2.3.1.286; NAD-dependent protein deacylase sirtuin-1; EC 2.3.1.-; Regulatory protein SIR2 homolog 1; SIR2-like protein 1; hSIR2
• Gene Name: SIRT1
• UniProt ID: SIR1_HUMAN
• PDB ID: 4I5I; 4IF6; 4IG9; 4KXQ; 4ZZH; 4ZZI; 4ZZJ; 5BTR
• EC Number: 2.3.1.-; 2.3.1.286
• Pfam ID: PF02146
• Sequence:
  MADEAALALQPGGSPSAAGADREAASSPAGEPLRKRPRRDGPGLERSPGEPGGAAPEREV
  PAAARGCPGAAAAALWREAEAEAAAAGGEQEAQATAAAGEGDNGPGLQGPSREPPLADNL
  YDEDDDDEGEEEEEAAAAAIGYRDNLLFGDEIITNGFHSCESDEEDRASHASSSDWTPRP
  RIGPYTFVQQHLMIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDI
  NTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIE
  YFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRII
  QCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPE
  QFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLG
  DCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELAYLSELPPTPLHVSEDSSS
  PERTSPPDSSVIVTLLDQAAKSNDDLDVSESKGCMEEKPQEVQTSRNVESIAEQMENPDL
  KNVGSSTGEKNERTSVAGTVRKCWPNRVAKEQISRRLDGNQYLFLPPNRYIFHGAEVYSD
  SEDDVLSSSSCGSNSDSGTCQSPSLEEPMEDESEIEEFYNGLEDEPDVPERAGGAGFGTD
  GDDQEAINEAISVKQEVTDMNYPSNKS
• Function: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of H1-4. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates p300/EP300 and PRMT1. Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation. Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Promotes DNA double-strand breaks by mediating deacetylation of SIRT6. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacetylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome. Protects cardiomyocytes against palmitate-induced apoptosis. Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity. Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis. Involved in the CCAR2-mediated regulation of PCK1 and NR1D1. Deacetylates CTNB1 at 'Lys-49'. In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling. In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein depropionylation and decrotonylation. Mediates depropionylation of Osterix (SP7). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase. Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity. Involved in the regulation of centrosome duplication. Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly. Deacetylates NDC80/HEC1 ; [Isoform 2]: Deacetylates 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop; [SirtT1 75 kDa fragment]: Catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly; (Microbial infection) In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection.
• Tissue Specificity: Widely expressed.
• KEGG Pathway:
  Nicoti.te and nicoti.mide metabolism (hsa00760)
  Metabolic pathways (hsa01100)
  FoxO sig.ling pathway (hsa04068)
  Efferocytosis (hsa04148)
  AMPK sig.ling pathway (hsa04152)
  Longevity regulating pathway (hsa04211)
  Longevity regulating pathway - multiple species (hsa04213)
  Cellular senescence (hsa04218)
  Wnt sig.ling pathway (hsa04310)
  Glucagon sig.ling pathway (hsa04922)
  Alcoholic liver disease (hsa04936)
  Amphetamine addiction (hsa05031)
  MicroR.s in cancer (hsa05206)
• Reactome Pathway:
  Circadian Clock (R-HSA-400253)
  SIRT1 negatively regulates rRNA expression (R-HSA-427359)
  Regulation of FOXO transcriptional activity by acetylation (R-HSA-9617629)
  Heme signaling (R-HSA-9707616)
  Regulation of HSF1-mediated heat shock response (R-HSA-3371453)
• BioCyc Pathway: MetaCyc:ENSG00000096717-MONOMER

Molecular Interaction Atlas (MIA) of This DOT

This DOT Affected the Drug Response of 3 Drug(s)

Drug Name	Drug ID	Highest Status	Interaction	REF
Troglitazone	DM3VFPD	Approved	NAD-dependent protein deacetylase sirtuin-1 (SIRT1) increases the Obesity ADR of Troglitazone.	[64]
Genistein	DM0JETC	Phase 2/3	NAD-dependent protein deacetylase sirtuin-1 (SIRT1) increases the response to substance of Genistein.	[65]
PJ34	DMXO6YH	Preclinical	NAD-dependent protein deacetylase sirtuin-1 (SIRT1) increases the response to substance of PJ34.	[66]

2 Drug(s) Affected the Post-Translational Modifications of This DOT

Drug Name	Drug ID	Highest Status	Interaction	REF
Valproate	DMCFE9I	Approved	Valproate decreases the methylation of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[1]
Atorvastatin	DMF28YC	Phase 3 Trial	Atorvastatin increases the phosphorylation of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[33]

70 Drug(s) Affected the Gene/Protein Processing of This DOT

Drug Name	Drug ID	Highest Status	Interaction	REF
Ciclosporin	DMAZJFX	Approved	Ciclosporin increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[2]
Acetaminophen	DMUIE76	Approved	Acetaminophen increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[3]
Doxorubicin	DMVP5YE	Approved	Doxorubicin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[4]
Cupric Sulfate	DMP0NFQ	Approved	Cupric Sulfate increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[5]
Cisplatin	DMRHGI9	Approved	Cisplatin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[6]
Estradiol	DMUNTE3	Approved	Estradiol decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[7]
Quercetin	DM3NC4M	Approved	Quercetin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[8]
Temozolomide	DMKECZD	Approved	Temozolomide increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[9]
Arsenic trioxide	DM61TA4	Approved	Arsenic trioxide decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[10]
Hydrogen peroxide	DM1NG5W	Approved	Hydrogen peroxide decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[11]
Testosterone	DM7HUNW	Approved	Testosterone decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[12]
Selenium	DM25CGV	Approved	Selenium decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[13]
Phenobarbital	DMXZOCG	Approved	Phenobarbital affects the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[14]
Dexamethasone	DMMWZET	Approved	Dexamethasone increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[15]
Hydroquinone	DM6AVR4	Approved	Hydroquinone affects the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[16]
Ethanol	DMDRQZU	Approved	Ethanol decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[17]
Paclitaxel	DMLB81S	Approved	Paclitaxel decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[18]
Fenofibrate	DMFKXDY	Approved	Fenofibrate increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[19]
Sulindac	DM2QHZU	Approved	Sulindac increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[20]
Capsaicin	DMGMF6V	Approved	Capsaicin affects the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[21]
Hydrocortisone	DMGEMB7	Approved	Hydrocortisone decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[22]
Dinoprostone	DMTYOPD	Approved	Dinoprostone decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[23]
Melatonin	DMKWFBT	Approved	Melatonin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[24]
Isoniazid	DM5JVS3	Approved	Isoniazid decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[25]
Prasterone	DM67VKL	Approved	Prasterone decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[26]
Nicotinamide	DMUPE07	Approved	Nicotinamide decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[27]
Olaparib	DM8QB1D	Approved	Olaparib increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[28]
Cilostazol	DMZMSCT	Approved	Cilostazol increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[29]
Urethane	DM7NSI0	Phase 4	Urethane increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[30]
Berberine	DMC5Q8X	Phase 4	Berberine decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[31]
Camptothecin	DM6CHNJ	Phase 3	Camptothecin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[32]
Napabucasin	DMDZ6Q3	Phase 3	Napabucasin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[34]
Buparlisib	DM1WEHC	Phase 3	Buparlisib decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[35]
ICARIIN	DMOJQGT	Phase 3	ICARIIN increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[36]
Acadesine	DM1RMF5	Phase 3	Acadesine increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[25]
Phenol	DM1QSM3	Phase 2/3	Phenol increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[37]
Tocopherol	DMBIJZ6	Phase 2	Tocopherol decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[13]
CERC-801	DM3SZ7P	Phase 2	CERC-801 decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[38]
(+)-JQ1	DM1CZSJ	Phase 1	(+)-JQ1 increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[39]
PMID28460551-Compound-2	DM4DOUB	Patented	PMID28460551-Compound-2 increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[40]
PMID28870136-Compound-52	DMFDERP	Patented	PMID28870136-Compound-52 decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[41]
BUTAPROST	DMVYNJZ	Patented	BUTAPROST decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[23]
PMID27998201-Compound-22	DMS9QA7	Patented	PMID27998201-Compound-22 decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[42]
Phenformin	DMQ52JG	Withdrawn from market	Phenformin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[43]
Bisphenol A	DM2ZLD7	Investigative	Bisphenol A decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[44]
Coumestrol	DM40TBU	Investigative	Coumestrol decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[45]
Sulforaphane	DMQY3L0	Investigative	Sulforaphane increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[46]
3R14S-OCHRATOXIN A	DM2KEW6	Investigative	3R14S-OCHRATOXIN A increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[47]
Nickel chloride	DMI12Y8	Investigative	Nickel chloride increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[37]
Hexadecanoic acid	DMWUXDZ	Investigative	Hexadecanoic acid decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[48]
D-glucose	DMMG2TO	Investigative	D-glucose increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[26]
geraniol	DMS3CBD	Investigative	geraniol increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[49]
Chlorpyrifos	DMKPUI6	Investigative	Chlorpyrifos decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[50]
Rapamycin Immunosuppressant Drug	DM678IB	Investigative	Rapamycin Immunosuppressant Drug decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[18]
Cycloheximide	DMGDA3C	Investigative	Cycloheximide decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[51]
U0126	DM31OGF	Investigative	U0126 decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[52]
Cordycepin	DM72Y01	Investigative	Cordycepin affects the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[53]
Lead acetate	DML0GZ2	Investigative	Lead acetate decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[54]
Oleic acid	DM54O1Z	Investigative	Oleic acid decreases the activity of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[55]
Myricetin	DMTV4L0	Investigative	Myricetin increases the activity of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[56]
Piceatannol	DMYOP45	Investigative	Piceatannol increases the activity of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[57]
Dorsomorphin	DMKYXJW	Investigative	Dorsomorphin decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[58]
BAY11-7082	DMQNOFA	Investigative	BAY11-7082 increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[59]
L-thyroxine	DM83HWL	Investigative	L-thyroxine increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[60]
Propanoic Acid	DM9TN2W	Investigative	Propanoic Acid decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[61]
Oxalic Acid	DMLN2GQ	Investigative	Oxalic Acid decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[62]
BUTEIN	DM8E54P	Investigative	BUTEIN increases the activity of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[57]
2-Methylamino-succinic acid(NMDA)	DMKP6BM	Investigative	2-Methylamino-succinic acid(NMDA) decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[63]
Oxindole 94	DMPFD6Y	Investigative	Oxindole 94 decreases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[52]
8-cyclopentyltheophylline	DMMITAJ	Investigative	8-cyclopentyltheophylline increases the expression of NAD-dependent protein deacetylase sirtuin-1 (SIRT1).	[58]

References

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