References
- Bannister A.J., Kouzarides T.: Regulation of chromatin by histone modifications. Cell Res., 2011; 21: 381–395
- Barber M.F., Michishita-Kioi E., Xi Y., Tasselli L., Kioi M., Moqtaderi Z., Tennen R.I., Paredes S., Young N.L., Chen K., Struhl K., Garcia B.A., Gozani O., Li W., Chua K.F.: SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation. Nature, 2012; 487: 114–118
- Bordone L., Motta M.C., Picard F., Robinson A., Jhala U.S., Apfeld J., McDonagh T., Lemieux M., McBurney M., Szilvasi A., Easlon E.J., Lin S.J., Guarente L.: Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic β cells. PLoS Biol., 2006; 4: e31
- Brunet A., Sweeney L.B., Sturgill J.F., Chua K.F., Greer P.L., Lin Y., Tran H., Ross S.E., Mostoslavsky R., Cohen H.Y., Hu L.S., Cheng H.L., Jedrychowski M.P., Gygi S.P., Sinclair D.A. i wsp.: Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science, 2004; 303: 2011–2015
- Chen S., Seiler J., Santiago-Reichelt M., Felbel K., Grummt I., Voit R.: Repression of RNA polymerase I upon stress is caused by inhibition of RNA-dependent deacetylation of PAF53 by SIRT7. Mol. Cell, 2013; 52: 303–313
- Cheng Y., Ren X., Gowda A.S., Shan Y., Zhang L., Yuan Y.S., Patel R., Wu H., Huber-Keener K., Yang J.W., Liu D., Spratt T.E., Yang J.M.: Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress. Cell Death Dis., 2013; 4: e731
- Christovam A.C., Theodoro V., Mendonça F.A., Esquisatto M.A., dos Santos G.M., do Amaral M.E.: Activators of SIRT1 in wound repair: An animal model study. Arch Dermatol Res., 2019; 311: 193–201
- Cimen H., Han M.J., Yang Y., Tong Q., Koc H., Koc E.C.: Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry., 2010; 49: 304–311
- Dominy J.E. Jr, Lee Y., Jedrychowski M.P., Chim H., Jurczak M.J., Camporez J.P., Ruan H.B., Feldman J., Pierce K., Mostoslavsky R., Denu J.M., Clish C.B., Yang X., Shulman G.I., Gygi S.P. i wsp.: The deacetylase Sirt6 activates the acetyltransferase GCN5 and suppresses hepatic gluconeogenesis. Mol. Cell, 2012; 48: 900–913
- Dryden S.C., Nahhas F.A., Nowak J.E., Goustin A.S., Tainsky M.A.: Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol., 2003; 23: 3173–3185
- Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim, J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J. i wsp.: Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science, 2011; 334: 806–809
- Eckschlager T., Plch J., Stiborova M., Hrabeta J.: Histone deacetylase inhibitors as anticancer drugs. Int. J. Mol. Sci., 2017; 18: 1414
- Espenshade P.J.: SREBPs: Sterol-regulated transcription factors. J. Cell Sci., 2006; 119: 973–976
- Fataftah N., Mohr C., Hajirezaei M.R., von Wirén N., Humbeck K.: Changes in nitrogen availability lead to a reprogramming of pyruvate metabolism. BMC Plant Biol., 2018; 18: 77
- Feldman J.L., Dittenhafer-Reed K.E., Denu J.M.: Sirtuin catalysis and regulation. J. Biol. Chem., 2012; 287: 42419–42427
- Finley L.W., Haas W., Desquiret-Dumas V., Wallace D.C., Procaccio V., Gygi S.P., Haigis M.C.: Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity. PLoS One, 2011; 6: e23295
- Flick F., Lüscher B.: Regulation of sirtuin function by posttranslational modifications. Front. Pharmacol., 2012; 3: 29
- Frye R.A.: Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun., 2000; 273: 793–798
- Gao D., Wang H., Xu Y., Zheng D., Zhang Q., Li W.: Protective effect of astaxanthin against contrast-induced acute kidney injury via SIRT1-p53 pathway in rats. Int. Urol. Nephrol., 2019; 51: 351–358
- GeneCards.: https://www.genecards.org (15.06.2020)
- Greiss S., Gartner A.: Sirtuin/Sir2 phylogeny, evolutionary considerations and structural conservation. Mol. Cells, 2009; 28: 407–415
- Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., Christodoulou D.C., Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Karow M., Blander G., Wolberger C., Prolla T.A., Weindruch R., Alt F.W., Guarente L.: SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic β cells. Cell., 2006; 126: 941–954
- Hallows W.C., Yu W., Denu J.M.: Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1 protein-mediated deacetylation. J. Biol. Chem., 2012; 287: 3850–3858
- Hikosaka K., Yaku K., Okabe K., Nakagawa T.: Implications of NAD metabolism in pathophysiology and therapeutics for neurodegenerative diseases. Nutr. Neurosci., 2019; DOI: 10.1080/1028415X.2019.1637504
- Horton J.D., Goldstein J.L., Brown M.S.: SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver. J. Clin. Invest., 2002; 109: 1125–1131
- Houtkooper R.H., Pirinen E., Auwerx J:. Sirtuins as regulators of metabolism and healthspan. Nat. Rev. Mol. Cell Biol., 2012; 13: 225–238
- Hubbi M.E., Hu H., Kshitiz, Gilkes D.M., Semenza G.L.: Sirtuin-7 inhibits the activity of hypoxia-inducible factors. J. Biol. Chem., 2013; 288: 20768–20775
- Jacobs K.M., Pennington J.D., Bisht K.S., Aykin-Burns N., Kim H.S., Mishra M., Sun L., Nguyen P., Ahn B.H., Leclerc J., Deng C.X., Spitz D.R., Gius D.: SIRT3 interacts with the daf-16 homolog FOXO3a in the mitochondria, as well as increases FOXO3a dependent gene expression. Int. J. Biol. Sci., 2008; 4: 291–299
- Jeong J., Juhn K., Lee H., Kim S.H., Min B.H., Lee K.M., Cho M.H., Park G.H., Lee K.H.: SIRT1 promotes DNA repair activity and deacetylation of Ku70. Exp. Mol. Med., 2007; 39: 8–13
- Jęśko H., Strosznajder R.P.: Sirtuins and their interactions with transcription factors and poly(ADP-ribose) polymerases. Folia Neuropathol., 2016; 54: 212–233
- Jiang W., Wang S., Xiao M., Lin Y., Zhou L., Lei Q., Xiong Y., Guan K.L., Zhao S.: Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol Cell., 2011; 43: 33–44
- Jing E., Gesta S., Kahn C.R.: SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab., 2007; 6: 105–114
- Jing H., Lin H.: Sirtuins in epigenetic regulation. Chem Rev., 2015; 115: 2350–2375
- Johnson C.A.: Chromatin modification and disease. J. Med. Genet., 2000; 37: 905–915
- Kahl G.: The dictionary of genomics, transcriptomics and proteomics. Wiley-VCH Verlag GmbH&Co. KGaA, Weinheim 2015; Volume 1 A-D: 2156
- Kaidi A., Weinert B.T., Choudhary C., Jackson S.P.: Human SIRT6 promotes DNA end resection through CtIP deacetylation. Science, 2010; 329: 1348–1353
- Karim M.F., Yoshizawa T., Sobuz S.U., Sato Y., Yamagata K.: Sirtuin 7-dependent deacetylation of DDB1 regulates the expression of nuclear receptor TR4. Biochem. Biophys. Res. Commun., 2017; 490: 423–428
- Kouzarides T.: Chromatin modifications and their function. Cell., 2007; 128: 693–705
- Kozako T., Suzuki T., Yoshimitsu M., Arima N., Honda S., Soeda S.: Anticancer agents targeted to sirtuins. Molecules, 2014; 19: 20295–20313
- Kupis W., Pałyga J., Tomal E., Niewiadomska E.: The role of sirtuins in cellular homeostasis. J. Physiol. Biochem., 2016; 72: 371–380
- Kyrylenko S., Kyrylenko O., Suuronen T., Salminen A.: Differential regulation of the Sir2 histone deacetylase gene family by inhibitors of class I and II histone deacetylases. Cell. Mol. Life Sci., 2003; 60: 1990–1997
- Landry J., Sutton A., Tafrov S.T., Heller R.C., Stebbins J., Pillus L., Sternglanz R.: The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc. Natl. Acad. Sci. USA, 2000; 97: 5807–5811
- Langley E., Pearson M., Faretta M., Bauer U.M., Frye RA., Minucci S., Pelicci P.G., Kouzarides T.: Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J., 2002; 21: 2383–2396
- Laurent G., de Boer V.C., Finley L.W., Sweeney M., Lu H., Schug T.T., Cen Y., Jeong S.M., Li X., Sauve A.A., Haigis M.C.: SIRT4 represses peroxisome proliferator-activated receptor α activity to suppress hepatic fat oxidation. Mol. Cell. Biol., 2013; 33: 4552–4561
- Laurent G., German N.J., Saha A.K., de Boer V.C., Davies M., Koves T.R., Dephoure N., Fischer F., Boanca G., Vaitheesvaran B., Lovitch S.B., Sharpe A.H., Kurland I.J., Steegborn C., Gygi S.P. i wsp: SIRT4 coordinates the balance between lipid synthesis and catabolism by repressing malonyl-CoA decarboxylase. Mol. Cell., 2013; 50: 686–698
- Li L., Shi L., Yang S., Yan R., Zhang D., Yang J., He L., Li W., Yi X., Sun L., Liang J., Cheng Z., Shi L., Shang Y., Yu W.: SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability. Nat. Commun., 2016; 7: 12235
- Li W., Zhang B., Tang J., Cao Q., Wu Y., Wu C., Guo J., Ling E.A., Liang F.: Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin. J. Neurosci., 2007; 27: 2606–2616
- Lipska K., Filip A.A., Gumieniczek A.: Postępy w badaniach nad inhibitorami deacetylaz histonów jako lekami przeciwnowotworowymi. Postępy Hig. Med. Dośw., 2018; 72: 1018–1031
- Liszt G., Ford E., Kurtev M., Guarente L.: Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J. Biol. Chem., 2005; 280: 21313–21320
- Lombard D.B., Alt F.W., Cheng H.L., Bunkenborg J., Streeper R.S., Mostoslavsky R., Kim J., Yancopoulos G., Valenzuela D., Murphy A., Yang Y., Chen Y., Hirschey M.D., Bronson R.T., Haigis M. i wsp.: Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol. Cell. Biol., 2007; 27: 8807–8814
- Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., Gu W.: Negative control of p53 by Sir2α promotes cell survival under stress. Cell., 2001; 107: 137–148
- Luo K., Huang W., Tang S.: Sirt3 enhances glioma cell viability by stabilizing Ku70-BAX interaction. Onco Targets Ther., 2018; 11: 7559–7567
- Mao Z., Hine C., Tian X., Van Meter M., Au M., Vaidya A., Seluanov A., Gorbunova V.: SIRT6 promotes DNA repair under stress by activating PARP1. Science, 2011; 332: 1443–1446
- Mathias R.A., Greco T.M., Cristea I.M.: Identification of sirtuin4 (SIRT4) protein interactions: Uncovering candidate acyl-modified mitochondrial substrates and enzymatic regulators. Methods Mol. Biol., 2016; 1436: 213–239
- Mathias R.A., Greco T.M., Oberstein A., Budayeva H.G., Chakrabarti R., Rowland E.A., Kang Y., Shenk T., Cristea I.M.: Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity. Cell., 2014; 159: 1615–1625
- Matsushita N., Yonashiro R., Ogata Y., Sugiura A., Nagashima S., Fukuda T., Inatome R., Yanagi S.: Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms. Genes Cells, 2011; 16: 190–202
- Maxwell P.H., Pugh C.W., Ratcliffe P.J.: The pVHL-hIF-1 system. A key mediator of oxygen homeostasis. Adv. Exp. Med. Biol., 2001; 502: 365–376
- McCord R.A., Michishita E., Hong T., Berber E., Boxer L.D., Kusumoto R., Guan S., Shi X., Gozani O., Burlingame A.L., Bohr V.A., Chua K.F.: SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair. Aging, 2009; 1: 109–121
- Mei Z., Zhang X., Yi J., Huang J., He J., Tao Y.: Sirtuins in metabolism, DNA repair and cancer. J. Exp. Clin. Cancer Res., 2016; 35: 182
- Meijer A.J., Lamers W.H., Chamuleau R.A.: Nitrogen metabolism and ornithine cycle function. Physiol Rev., 1990; 70: 701–748
- Michan S., Sinclair D.: Sirtuins in mammals: Insights into their biological function. Biochem. J., 2007; 404: 1–13
- Michishita E., McCord R.A., Berber E., Kioi M., Padilla-Nash H., Damian M., Cheung P., Kusumoto R., Kawahara T.L., Barrett J.C., Chang H.Y., Bohr V.A., Ried T., Gozani O., Chua K.F.: SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature, 2008; 452: 492–496
- Muth V., Nadaud S., Grummt I., Voit R.: Acetylation of TAFI68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J., 2001; 20: 1353–1362
- Nakae J., Oki M., Cao Y.: The FoxO transcription factors and metabolic regulation. FEBS Lett., 2008; 582: 54–67
- Nakagawa T., Lomb D.J., Haigis M.C., Guarente L.: SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell, 2009; 137: 560–570
- Nakamura Y., Ogura M., Ogura K., Tanaka D., Inagaki N.: SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice. FEBS Lett., 2012; 586: 4076–4081
- Nishida Y., Rardin M.J., Carrico C., He W., Sahu A.K., Gut P., Najjar R., Fitch M., Hellerstein M., Gibson B.W., Verdin E.: SIRT5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target. Mol. Cell., 2015; 59: 321–332
- North B.J., Marshall B.L., Borra M.T., Denu J.M., Verdin E.: The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell, 2003; 11: 437–444
- Obsil T., Obsilova V.: Structure/function relationships underlying regulation of FOXO transcription factors. Oncogene, 2008; 27: 2263–2275
- Osborne T.F., Espenshade P.J.: Evolutionary conservation and adaptation in the mechanism that regulates SREBP action: What a long, strange tRIP it’s been. Genes Dev., 2009; 23: 2578–2591
- Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.: SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol. Cell, 2013; 50: 919–930
- Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C. i wsp.: The first identification of lysine malonylation substrates and its regulatory enzyme. Mol. Cell Proteomics, 2011; 10: M111.012658
- Picard F., Kurtev M., Chung N., Topark-Ngarm A., Senawong T., Machado de Oliviera R., Leid M., McBurney M.W., Guarente L.: Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ. Nature, 2004; 429: 771–776
- Polletta L., Vernucci E., Carnevale I., Arcangeli T., Rotili D., Palmerio S., Steegborn C., Nowak T., Schutkowski M., Pellegrini L., Sansone L., Villanova L., Runci A., Pucci B., Morgante E. i wsp.: SIRT5 regulation of ammonia-induced autophagy and mitophagy. Autophagy, 2015; 11: 253–270
- Ponugoti B., Kim D.H., Xiao Z., Smith Z., Miao J., Zang M., Wu S.Y., Chiang C.M., Veenstra T.D., Kemper J.K.: SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism. J. Biol. Chem., 2010; 285: 33959–33970
- Ramsey K.M., Mills K.F., Satoh A., Imai S.I.: Age-associated loss of Sirt1-mediated enhancement of glucose-stimulated insulin secretion in beta cell-specific Sirt1-overexpressing (BESTO) mice. Aging Cell, 2008; 7: 78–88
- Rangarajan P., Karthikeyan A., Lu J., Ling E.A., Dheen S.T.: Sirtuin 3 regulates Foxo3a-mediated antioxidant pathway in microglia. Neuroscience, 2015; 311: 398–414
- Rardin M.J., He W., Nishida Y., Newman J.C., Carrico C., Danielson S.R., Guo A., Gut P., Sahu A.K,. Li B., Uppala R., Fitch M., Riiff T., Zhu L., Zhou J. i wsp.: SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. Cell Metab., 2013; 18: 920–933
- Rodgers J.T., Lerin C., Gerhart-Hines Z., Puigserver P.: Metabolic adaptations through the PGC-1α and SIRT1 pathways. FEBS Lett., 2008; 582: 46–53
- Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., Puigserver P.: Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1. Nature, 2005; 434: 113–118
- Rodgers J.T., Puigserver P.: Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1. Proc. Natl. Acad. Sci. USA, 2007; 104: 12861–12866
- Rorbach-Dolata A., Kubis A., Piwowar A.: Modyfikacje epigenetyczne – ważny mechanizm w zaburzeniach cukrzycy. Postępy Hig. Med. Dośw., 2017; 71: 960–974
- Ryu D., Jo Y.S., Lo Sasso G., Stein S., Zhang H., Perino A., Lee J.U., Zeviani M., Romand R., Hottiger M.O., Schoonjans K., Auwerx J.: A SIRT7-dependent acetylation switch of GABPβ1 controls mitochondrial function. Cell. Metab., 2014; 20: 856–869
- Sanders B.D., Jackson B., Marmorstein R.: Structural basis for sirtuin function: What we know and what we don’t. Biochim. Biophys. Acta, 2010; 1804: 1604–1616
- Scher M.B., Vaquero A., Reinberg D.: SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev., 2007; 21: 920–928
- Schiedel M., Robaa D., Rumpf T., Sippl W., Jung M.: The current state of NAD+-dependent histone deacetylases (sirtuins) as novel therapeutic targets. Med. Res. Rev., 2017; 37: 147–200
- Schwer B., North B.J., Frye R.A., Ott M., Verdin E.: The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell. Biol., 2002; 158: 647–657
- Selak M.A., Armour S.M., MacKenzie E.D., Boulahbel H., Watson D.G., Mansfield K.D., Pan Y., Simon M.C., Thompson C.B., Gottlieb E.: Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase. Cancer Cell, 2005; 7: 77–85
- Semenza G.L.: Regulation of oxygen homeostasis by hypoxiainducible factor 1. Physiology, 2009; 24: 97–106
- Shin J., He M., Liu Y., Paredes S., Villanova L., Brown K., Qiu X., Nabavi N., Mohrin M., Wojnoonski K. Li P., Cheng H.L., Murphy A.J., Valenzuela D.M., Luo H. i wsp.: SIRT7 represses Myc activity to suppress ER stress and prevent fatty liver disease. Cell Rep., 2013; 5: 654–665
- Siedlecka K., Bogusławski W.: Sirtuiny – enzymy długowieczności? Gerontol. Pol., 2005; 13: 147–152
- Snyder C.A., Goodson M.L., Schroeder A.C., Privalsky M.L.: Regulation of corepressor alternative mRNA splicing by hormonal and metabolic signaling. Mol. Cell. Endocrinol., 2015; 413: 228–235
- Sundaresan N.R., Samant S.A., Pillai V.B., Rajamohan S.B., Gupta M.P.: SIRT3 is a stress responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol. Cell. Biol., 2008; 28: 6384–6401
- Tan M., Peng C., Anderson K.A., Chhoy P., Xie Z., Dai L., Park J., Chen Y., Huang H., Zhang Y., Ro J., Wagner G.R., Green M.F., Madsen A.S., Schmiesing J. i wsp.: Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell. Metab., 2014; 19: 605–617
- Tavares C.D., Sharabi K., Dominy J.E., Lee Y., Isasa M., Orozco J.M., Jedrychowski M.P., Kamenecka T.M., Griffin P.R., Gygi S.P., Puigserver P.: The methionine transamination pathway controls hepatic glucose metabolism through regulation of the GCN5 acetyltransferase and the PGC-1α transcriptional coactivator. J. Biol. Chem., 2016; 291: 10635–10645
- Tennen R.I., Bua D.J., Wright W.E., Chua K.F.: SIRT6 is required for maintenance of telomere position effect in human cells. Nat. Commun., 2011; 2: 433
- Tsai Y.C., Greco T.M., Cristea I.M.: Sirtuin7 plays a role in ribosome biogenesis and protein synthesis. Mol. Cell. Proteomics, 2014; 13: 73–83
- van der Horst A., Tertoolen L.G., de Vries-Smits L.M., Frye R.A., Medema R.H., Burgering B.M.: FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). J. Biol. Chem., 2004; 279: 28873–28879
- Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P., Reinberg D.: Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell., 2004; 16: 93–105
- Vaquero A., Scher M.B., Lee D.H., Sutton A., Cheng H.L., Alt F.W., Serrano L., Sternglanz R., Reinberg D.: SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev., 2006; 20: 1256–1261
- Vaziri H., Dessain S.K., Ng Eaton E., Imai S.I., Frye R.A., Pandita T.K., Guarente L., Weinberg R.A.: hSIR2 (SIRT1) functions as an NAD-dependent p53 deacetylase. Cell, 2001; 107: 149–159
- Walker A.K., Yang F., Jiang K., Ji J.Y., Watts J.L., Purushotham A,. Boss O., Hirsch M.L., Ribich S., Smith J.J., Israelian K., Westphal C.H., Rodgers J.T., Shioda T., Elson S.L. i wsp.: Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBP. Genes Dev., 2010; 24: 1403–1417
- Wang F., Chan C.H., Chen K., Guan X., Lin H.K., Tong Q.: Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation. Oncogene, 2012; 31: 1546–1557
- Wang F., Nguyen M., Qin F.X., Tong Q.: SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell, 2007; 6: 505–514
- Wang F., Tong Q.: SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1’s repressive interaction with PPARγ. Mol. Biol. Cell, 2009; 20: 801–808
- Webb A.E., Brunet A.: FOXO transcription factors: Key regulators of cellular quality control. Trends Biochem. Sci., 2014; 39: 159–169
- Wiercińska M., Rosołowska-Huszcz D.: Naturalne i syntetyczne modulatory aktywności sirtuin. Kosmos, 2017; 66: 365–377
- Yamamoto H., Schoonjans K., Auwerx J.: Sirtuin functions in health and disease. Mol. Endocrinol., 2007; 21: 1745–1755
- Yang B., Zwaans B.M., Eckersdorff M., Lombard D.B.: The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability. Cell Cycle, 2009; 8: 2662–2663
- Yang S.R., Wright J., Bauter M., Seweryniak K., Kode A., Rahman I.: Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-κB in macrophages in vitro and in rat lungs in vivo: Implications for chronic inflammation and aging. Am. J. Physiol. Lung Cell Mol. Physiol., 2007; 292: L567–L576
- Yeung F., Hoberg J.E., Ramsey C.S., Keller M.D., Jones D.R., Frye R.A., Mayo M.W.: Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J., 2004; 23: 2369–2380
- Zhang M., Pan Y., Dorfman R.G., Yin Y., Zhou Q., Huang S., Liu J., Zhao S.: Sirtinol promotes PEPCK1 degradation and inhibits gluconeogenesis by inhibiting deacetylase SIRT2. Sci Rep., 2017; 7: 7
- Zhang P.Y., Li G., Deng Z.J., Liu L.Y., Chen L., Tang J.Z., Wang Y.Q., Cao S.T., Fang Y.X., Wen F., Xu Y., Chen X., Shi K.Q., Li W.F., Xie C. i wsp.: Dicer interacts with SIRT7 and regulates H3K18 deacetylation in response to DNA damaging agents. Nucleic Acids Res., 2016; 44: 3629–3642
- Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L., Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F. i wsp.: Regulation of cellular metabolism by protein lysine acetylation. Science, 2010; 327: 1000–1004
- Zhao T., Alam H.B., Liu B., Bronson R.T., Nikolian V.C., Wu E., Chong W., Li Y.: Selective inhibition of SIRT2 improves outcomes in a lethal septic model. Curr. Mol. Med., 2015; 15: 634–641
- Zhong L., Mostoslavsky R.: SIRT6: A master epigenetic gate-keeper of glucose metabolism. Transcription, 2010; 1: 17–21
- Zhong L., D’Urso A., Toiber D., Sebastian C., Henry R.E., Vadysirisack D.D., Guimaraes A., Marinelli B., Wikstrom J.D., Nir T., Clish C.B., Vaitheesvaran B., Iliopoulos O., Kurland I., Dor Y. i wsp.: The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1α. Cell, 2010; 140: 280–293